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Conserved domains on  [gi|1678550997|gb|QCX89537|]
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plipastatin synthase subunit D [Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 1058-3599 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 2132.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTL--- 1133
Cdd:PRK12467    51 PLSYAQERQWFLWQLDpDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQ-DEEGFRQVIDASLSLTIpld 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1134 --------SKETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR---- 1196
Cdd:PRK12467   130 dlaneqgrARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgr 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 --QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLA 1274
Cdd:PRK12467   210 epSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1275 HKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAY 1354
Cdd:PRK12467   290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1355 EHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQ-----QKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQ 1429
Cdd:PRK12467   370 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATggrdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAA 449

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1430 FEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLfEETGYSmNQTLHYALEQQAEKTPD 1509
Cdd:PRK12467   450 FTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNA-PATEYA-PDCVHQLIEAQARQHPE 527

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1510 QAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLED 1589
Cdd:PRK12467   528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD 607

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1590 SGTNILLLQSAGL-HVPEFTG-EIVYLNQTNSGLAHRLS-NPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNS 1666
Cdd:PRK12467   608 SGVRLLLTQSHLLaQLPVPAGlRSLCLDEPADLLCGYSGhNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV 687

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1667 LQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHiky 1746
Cdd:PRK12467   688 IAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA--- 764

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1747 rSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEK-LERIPIGKPVHHVRLYLLN 1825
Cdd:PRK12467   765 -SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERdFGNVPIGQPLANLGLYILD 843

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1826 QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYP-GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRI 1904
Cdd:PRK12467   844 HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRI 923

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1905 EPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ----------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTP 1974
Cdd:PRK12467   924 ELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAvadgaehqatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1975 SGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKD 2054
Cdd:PRK12467  1004 NGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRT 1083

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2055 VFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQEL 2134
Cdd:PRK12467  1084 LFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDAL 1163

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2135 IKRHESLRTSFEQdEGGDPVQRIHDEVPFTL-QTTVLGARTEQEAAAAFI-----KPFDLSQAPLFRAQIVKVSDERHLL 2208
Cdd:PRK12467  1164 VARHESLRTTFVQ-EDGRTRQVIHPVGSLTLeEPLLLAADKDEAQLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVL 1242

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2209 LVDMHHIISDGVSVNILIQEFGELY------NNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLP 2282
Cdd:PRK12467  1243 VLTLHHIVSDGWSMQVLVDELVALYaaysqgQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELP 1322

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2283 ADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGM 2362
Cdd:PRK12467  1323 TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGF 1402

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2363 FVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLH-LHDLQM 2441
Cdd:PRK12467  1403 FVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAqLPGLSV 1482

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2442 KPAQVSHLVSKFDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNE 2521
Cdd:PRK12467  1483 ESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEG 1562

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2522 FNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASIL 2601
Cdd:PRK12467  1563 WNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLL 1642

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2602 GVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTiNEADLGVLADFEG-EILTIES----VEEDDKSPLPQMSSAHHLA 2676
Cdd:PRK12467  1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT-QSHLQARLPLPDGlRSLVLDQeddwLEGYSDSNPAVNLAPQNLA 1721

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 YIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAI 2756
Cdd:PRK12467  1722 YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQL 1801

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2757 KHQLSRQRITHMIIVPVLYRALLDVV-QPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATT--VM 2833
Cdd:PRK12467  1802 IQLIERQQVTTLHFVPSMLQQLLQMDeQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVThwTC 1881

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 RH--MEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDA 2910
Cdd:PRK12467  1882 RRkdLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDL 1961

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVVTK----------PGLST 2980
Cdd:PRK12467  1962 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGK-QLVAYVVPTdpglvdddeaQVALR 2040

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2981 NAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNhEGERPFLPPSSKMEQILADIWKEVLGAEKIGTAD 3060
Cdd:PRK12467  2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-ELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHD 2119

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3061 SFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSS--QAAVEGDVQWSPVQKWFLSQDIKEKH 3138
Cdd:PRK12467  2120 NFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSidQGPVTGDLPLLPIQQMFFADDIPERH 2199

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3139 HFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQnEQGKWDQYNR-PLSHSDDALYGLQMIDLSApdgtdgnrpY 3217
Cdd:PRK12467  2200 HWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQ-EDGGWSAMHRaPEQERRPLLWQVVVADKEE---------L 2269

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3218 EPLikrhVLDIQQKMDLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSF 3296
Cdd:PRK12467  2270 EAL----CEQAQRSLDLEEGPLLRAVLATLPDGSqRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAF 2345

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3297 KAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEgQRSTISFTLNDKETAALLKDANSAYNTDTQDML 3376
Cdd:PRK12467  2346 KAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRR-HAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLL 2424

                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3377 LASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTAIYPLLIKLNADLPDSeesmvhvLKTTKDTLRRVPDK 3456
Cdd:PRK12467  2425 LTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATS-------IKTIKEQLRAVPNK 2497

                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3457 GFGYGVIKYL-TPPGKKDINFTGAPEISFNYLGQFESGRTAevpEEDAFsFSPLG--AGGDISTTWNREQSLDISAIAAE 3533
Cdd:PRK12467  2498 GLGFGVLRYLgSEAARQTLQALPVPRITFNYLGQFDGSFDA---EKQAL-FVPSGefSGAEQSEEAPLGNWLSINGQVYG 2573

                         2570      2580      2590      2600      2610      2620      2630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 3534 GKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTED-------ALQEIADM 3599
Cdd:PRK12467  2574 GELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEqldrlpvAVGDIEDI 2646
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 476-953 0e+00

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: 895.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  476 TPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYI 555
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 LHDCGCSHVVSQAHLPSSLEDNYIITHPE-DIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFE 634
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEdPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  635 YTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELA 714
Cdd:cd17656    161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  715 NSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQ 794
Cdd:cd17656    241 NRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQ 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  795 LQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEI 874
Cdd:cd17656    321 LQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEI 400

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  875 EVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:cd17656    401 EAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
PRK12316 super family cl36106
peptide synthase; Provisional
 4-1030 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 715.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    4 ANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGkVNPQFFQNSINALVERHDIFRTIFISQ-NVSSPQQVVLR 82
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQgELGRPLQVVHK 4174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   83 ERNVIVLEEDITHLNEAEQSqfIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLH 162
Cdd:PRK12316  4175 QVSLPFAELDWRGRADLQAA--LDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLE 4252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  163 IYASYVNAspitlEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVL----PKQKKTKGKSRQEHVTfSFSKEESS 238
Cdd:PRK12316  4253 RYSGRPPA-----QPGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLaqaiARADLRSANGYGEHVR-ELDATATA 4326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  239 RLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDM 317
Cdd:PRK12316  4327 RLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATpRAQQSVVEWLQQV 4406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  318 QKDRLAAEAYSYHPLYEIQsRSAVKQG--LIDHILVFENYPVQQEIQmlnkQEHASDLfQIHNFTVADETNYSFYLMVAP 395
Cdd:PRK12316  4407 QRQNLALREHEHTPLYEIQ-RWAGQGGeaLFDSLLVFENYPVSEALQ----QGAPGGL-RFGEVTNHEQTNYPLTLAVGL 4480

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  396 GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITtDTEKRQLIGEITDQT----PVYETIHAMFEK 471
Cdd:PRK12316  4481 GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLL-EKAEQQRIVALWNRTdagyPATRCVHQLVAE 4559

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  472 QAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADR 551
Cdd:PRK12316  4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  552 IRYILHDCGCSHVVSQAHLPSSLE-----DNYIITHPEDIESKVDgSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:PRK12316  4640 LAYMMEDSGAALLLTQSHLLQRLPipdglASLALDRDEDWEGFPA-HDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 MANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIkRDVPQLFAFINKHQTNIVFLPTAFIKM 706
Cdd:PRK12316  4719 LVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVYLQQ 4797

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IFSERELANSFPDgVKHLIAAGEQLMiSDLFQDVLRK-RGIHLHNHYGPSETHV-VSTYTIHPGDP-IPELPPIGKPIGC 783
Cdd:PRK12316  4798 LAEHAERDGEPPS-LRVYCFGGEAVA-QASYDLAWRAlKPVYLFNGYGPTETTVtVLLWKARDGDAcGAAYMPIGTPLGN 4875

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDVIMYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:PRK12316  4876 RSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQV 4955

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAaILIWQDQNGEHELCAY----------YCSVQKLNTIDLRSYMASELPEYMIPAK 932
Cdd:PRK12316  4956 KIRGFRIELGEIEARLREHPAVREA-VVIAQEGAVGKQLVGYvvpqdpaladADEAQAELRDELKAALRERLPEYMVPAH 5034

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  933 WIWVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIA 1012
Cdd:PRK12316  5035 LVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQ 5114

                         1050
                   ....*....|....*...
gi 1678550997 1013 KEFHVQVSLKDIFAHPTV 1030
Cdd:PRK12316  5115 LELGLELPLRELFQTPTL 5132
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 1058-3599 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 2132.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTL--- 1133
Cdd:PRK12467    51 PLSYAQERQWFLWQLDpDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQ-DEEGFRQVIDASLSLTIpld 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1134 --------SKETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR---- 1196
Cdd:PRK12467   130 dlaneqgrARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgr 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 --QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLA 1274
Cdd:PRK12467   210 epSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1275 HKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAY 1354
Cdd:PRK12467   290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1355 EHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQ-----QKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQ 1429
Cdd:PRK12467   370 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATggrdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAA 449

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1430 FEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLfEETGYSmNQTLHYALEQQAEKTPD 1509
Cdd:PRK12467   450 FTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNA-PATEYA-PDCVHQLIEAQARQHPE 527

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1510 QAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLED 1589
Cdd:PRK12467   528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD 607

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1590 SGTNILLLQSAGL-HVPEFTG-EIVYLNQTNSGLAHRLS-NPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNS 1666
Cdd:PRK12467   608 SGVRLLLTQSHLLaQLPVPAGlRSLCLDEPADLLCGYSGhNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV 687

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1667 LQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHiky 1746
Cdd:PRK12467   688 IAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA--- 764

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1747 rSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEK-LERIPIGKPVHHVRLYLLN 1825
Cdd:PRK12467   765 -SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERdFGNVPIGQPLANLGLYILD 843

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1826 QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYP-GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRI 1904
Cdd:PRK12467   844 HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRI 923

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1905 EPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ----------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTP 1974
Cdd:PRK12467   924 ELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAvadgaehqatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1975 SGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKD 2054
Cdd:PRK12467  1004 NGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRT 1083

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2055 VFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQEL 2134
Cdd:PRK12467  1084 LFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDAL 1163

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2135 IKRHESLRTSFEQdEGGDPVQRIHDEVPFTL-QTTVLGARTEQEAAAAFI-----KPFDLSQAPLFRAQIVKVSDERHLL 2208
Cdd:PRK12467  1164 VARHESLRTTFVQ-EDGRTRQVIHPVGSLTLeEPLLLAADKDEAQLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVL 1242

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2209 LVDMHHIISDGVSVNILIQEFGELY------NNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLP 2282
Cdd:PRK12467  1243 VLTLHHIVSDGWSMQVLVDELVALYaaysqgQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELP 1322

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2283 ADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGM 2362
Cdd:PRK12467  1323 TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGF 1402

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2363 FVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLH-LHDLQM 2441
Cdd:PRK12467  1403 FVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAqLPGLSV 1482

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2442 KPAQVSHLVSKFDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNE 2521
Cdd:PRK12467  1483 ESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEG 1562

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2522 FNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASIL 2601
Cdd:PRK12467  1563 WNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLL 1642

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2602 GVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTiNEADLGVLADFEG-EILTIES----VEEDDKSPLPQMSSAHHLA 2676
Cdd:PRK12467  1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT-QSHLQARLPLPDGlRSLVLDQeddwLEGYSDSNPAVNLAPQNLA 1721

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 YIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAI 2756
Cdd:PRK12467  1722 YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQL 1801

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2757 KHQLSRQRITHMIIVPVLYRALLDVV-QPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATT--VM 2833
Cdd:PRK12467  1802 IQLIERQQVTTLHFVPSMLQQLLQMDeQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVThwTC 1881

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 RH--MEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDA 2910
Cdd:PRK12467  1882 RRkdLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDL 1961

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVVTK----------PGLST 2980
Cdd:PRK12467  1962 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGK-QLVAYVVPTdpglvdddeaQVALR 2040

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2981 NAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNhEGERPFLPPSSKMEQILADIWKEVLGAEKIGTAD 3060
Cdd:PRK12467  2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-ELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHD 2119

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3061 SFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSS--QAAVEGDVQWSPVQKWFLSQDIKEKH 3138
Cdd:PRK12467  2120 NFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSidQGPVTGDLPLLPIQQMFFADDIPERH 2199

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3139 HFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQnEQGKWDQYNR-PLSHSDDALYGLQMIDLSApdgtdgnrpY 3217
Cdd:PRK12467  2200 HWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQ-EDGGWSAMHRaPEQERRPLLWQVVVADKEE---------L 2269

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3218 EPLikrhVLDIQQKMDLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSF 3296
Cdd:PRK12467  2270 EAL----CEQAQRSLDLEEGPLLRAVLATLPDGSqRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAF 2345

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3297 KAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEgQRSTISFTLNDKETAALLKDANSAYNTDTQDML 3376
Cdd:PRK12467  2346 KAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRR-HAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLL 2424

                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3377 LASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTAIYPLLIKLNADLPDSeesmvhvLKTTKDTLRRVPDK 3456
Cdd:PRK12467  2425 LTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATS-------IKTIKEQLRAVPNK 2497

                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3457 GFGYGVIKYL-TPPGKKDINFTGAPEISFNYLGQFESGRTAevpEEDAFsFSPLG--AGGDISTTWNREQSLDISAIAAE 3533
Cdd:PRK12467  2498 GLGFGVLRYLgSEAARQTLQALPVPRITFNYLGQFDGSFDA---EKQAL-FVPSGefSGAEQSEEAPLGNWLSINGQVYG 2573

                         2570      2580      2590      2600      2610      2620      2630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 3534 GKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTED-------ALQEIADM 3599
Cdd:PRK12467  2574 GELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEqldrlpvAVGDIEDI 2646
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1046-2328 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: 1118.78  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1046 AAIEPAEKRDTYPVSSAQKRIYVLQQLDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRI 1125
Cdd:COG1020      7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1126 HTEVPFTL----------------SKETTIEGFVRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREF 1189
Cdd:COG1020     87 QPVVAAPLpvvvllvdlealaeaaAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1190 TDLY------ANRQLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLD 1263
Cdd:COG1020    167 LRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1264 KEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFL 1343
Cdd:COG1020    247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1344 KEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHD 1423
Cdd:COG1020    327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETG 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1424 SELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESchlFEETG--YSMNQTLHYALE 1501
Cdd:COG1020    407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAE---WNATAapYPADATLHELFE 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1502 QQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEE 1581
Cdd:COG1020    484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1582 RISFLLEDSGTNILLLQSAGL-HVPEFTGEIVYLNQTNSGlAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSA 1660
Cdd:COG1020    564 RLAYMLEDAGARLVLTQSALAaRLPELGVPVLALDALALA-AEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1661 VNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAF 1740
Cdd:COG1020    643 VNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRAL 722

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1741 LEHikyrsVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKL-ERIPIGKPVHHV 1819
Cdd:COG1020    723 LDA-----APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADgGSVPIGRPIANT 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1820 RLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVK 1898
Cdd:COG1020    798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1899 IRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV 1972
Cdd:COG1020    878 IRGFRIELGEIEAALLQHPGVREAVVVAREDaPGDKRLVAYVvpeagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1973 TPSGKLDRNALPAPgGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPL 2052
Cdd:COG1020    958 TGNGKLDRLALPAP-AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2053 KDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQ 2132
Cdd:COG1020   1037 LLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLA 1116

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2133 ELIKRHESLRTSF-----EQDEGGDPVQRIHDEVPFTLQTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHL 2207
Cdd:COG1020   1117 LLLALLAALRARRavrqeGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLL 1196

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2208 LLVDMHHIISDGVSVNILIQEFGELY------NNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDL 2281
Cdd:COG1020   1197 LLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLAL 1276

                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997 2282 PADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAA 2328
Cdd:COG1020   1277 ALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLAL 1323
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 476-953 0e+00

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: 895.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  476 TPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYI 555
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 LHDCGCSHVVSQAHLPSSLEDNYIITHPE-DIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFE 634
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEdPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  635 YTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELA 714
Cdd:cd17656    161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  715 NSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQ 794
Cdd:cd17656    241 NRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQ 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  795 LQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEI 874
Cdd:cd17656    321 LQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEI 400

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  875 EVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:cd17656    401 EAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
PRK12316 PRK12316
peptide synthase; Provisional
 4-1030 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 715.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    4 ANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGkVNPQFFQNSINALVERHDIFRTIFISQ-NVSSPQQVVLR 82
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQgELGRPLQVVHK 4174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   83 ERNVIVLEEDITHLNEAEQSqfIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLH 162
Cdd:PRK12316  4175 QVSLPFAELDWRGRADLQAA--LDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLE 4252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  163 IYASYVNAspitlEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVL----PKQKKTKGKSRQEHVTfSFSKEESS 238
Cdd:PRK12316  4253 RYSGRPPA-----QPGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLaqaiARADLRSANGYGEHVR-ELDATATA 4326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  239 RLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDM 317
Cdd:PRK12316  4327 RLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATpRAQQSVVEWLQQV 4406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  318 QKDRLAAEAYSYHPLYEIQsRSAVKQG--LIDHILVFENYPVQQEIQmlnkQEHASDLfQIHNFTVADETNYSFYLMVAP 395
Cdd:PRK12316  4407 QRQNLALREHEHTPLYEIQ-RWAGQGGeaLFDSLLVFENYPVSEALQ----QGAPGGL-RFGEVTNHEQTNYPLTLAVGL 4480

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  396 GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITtDTEKRQLIGEITDQT----PVYETIHAMFEK 471
Cdd:PRK12316  4481 GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLL-EKAEQQRIVALWNRTdagyPATRCVHQLVAE 4559

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  472 QAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADR 551
Cdd:PRK12316  4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  552 IRYILHDCGCSHVVSQAHLPSSLE-----DNYIITHPEDIESKVDgSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:PRK12316  4640 LAYMMEDSGAALLLTQSHLLQRLPipdglASLALDRDEDWEGFPA-HDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 MANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIkRDVPQLFAFINKHQTNIVFLPTAFIKM 706
Cdd:PRK12316  4719 LVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVYLQQ 4797

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IFSERELANSFPDgVKHLIAAGEQLMiSDLFQDVLRK-RGIHLHNHYGPSETHV-VSTYTIHPGDP-IPELPPIGKPIGC 783
Cdd:PRK12316  4798 LAEHAERDGEPPS-LRVYCFGGEAVA-QASYDLAWRAlKPVYLFNGYGPTETTVtVLLWKARDGDAcGAAYMPIGTPLGN 4875

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDVIMYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:PRK12316  4876 RSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQV 4955

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAaILIWQDQNGEHELCAY----------YCSVQKLNTIDLRSYMASELPEYMIPAK 932
Cdd:PRK12316  4956 KIRGFRIELGEIEARLREHPAVREA-VVIAQEGAVGKQLVGYvvpqdpaladADEAQAELRDELKAALRERLPEYMVPAH 5034

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  933 WIWVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIA 1012
Cdd:PRK12316  5035 LVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQ 5114

                         1050
                   ....*....|....*...
gi 1678550997 1013 KEFHVQVSLKDIFAHPTV 1030
Cdd:PRK12316  5115 LELGLELPLRELFQTPTL 5132
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1508-1983 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: 644.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd05930     81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYR 1747
Cdd:cd05930    126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1748 SVPiktnRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPP-HEKLERIPIGKPVHHVRLYLLNQ 1826
Cdd:cd05930    206 ALP----SLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPdDEEDGRVPIGRPIPNTRVYVLDE 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1827 NQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 1906
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1907 GEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd05930    362 GEIEAALLAHPGVREAAVVAREDgDGEKRLVAYVvpdegGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441


                   ...
gi 1678550997 1981 NAL 1983
Cdd:cd05930    442 KAL 444
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 10-433 0e+00

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: 621.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNVIVL 89
Cdd:cd19543      1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 EEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVN 169
Cdd:cd19543     81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 ASPITLEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKS--RQEHVTFSFSKEESSRLSELAARE 247
Cdd:cd19543    161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGsyEPGEVSFELSAELTARLQELARQH 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  248 EVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQGAK-TPFLQLIKDMQKDRLAAEA 326
Cdd:cd19543    241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPdQTVLELLKDLQAQQLELRE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  327 YSYHPLYEIQSRSAVKQGLIDHILVFENYPVQQEIQMlnkqEHASDLFQIHNFTVADETNYSFYLMVAPGEEIHIKMNYD 406
Cdd:cd19543    321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEE----EQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYD 396

                          410       420
                   ....*....|....*....|....*..
gi 1678550997  407 AEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19543    397 AEVFDEATIERLLGHLRRVLEQVAANP 423
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1521-1924 2.70e-166

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: 519.90  E-value: 2.70e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQS 1599
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 AGLH-VPEFTGEIVYLNQTNSGLAHRLSN---PNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKH 1675
Cdd:TIGR01733   81 ALASrLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1676 SDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEK-EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIkyrsvPIKTN 1754
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERdDAALLAALIAEHPVTVLNLTPSLLALLAAAL-----PPALA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1755 RLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHE--KLERIPIGKPVHHVRLYLLNQNQRMLP 1832
Cdd:TIGR01733  236 SLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDapRESPVPIGRPLANTRLYVLDDDLRPVP 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1833 VGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYP--GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIE 1910
Cdd:TIGR01733  316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395

                          410
                   ....*....|....
gi 1678550997 1911 AALRSIEGVREAAV 1924
Cdd:TIGR01733  396 AALLRHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 2084-2519 6.55e-165

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: 517.66  E-value: 6.55e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2084 KQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPF 2163
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2164 TLQTTVLG---ARTEQEAAAAFI-----KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELY-- 2233
Cdd:pfam00668   81 ELEIIDISdlsESEEEEAIEAFIqrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqq 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2234 --NNRKLPALRIQ-YKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGL 2310
Cdd:pfam00668  161 llKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2311 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 2390
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2391 LEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDY-----EPLHLHDLQMKPAQVSHLVSKFDLTLQASEGDGN 2465
Cdd:pfam00668  321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGqdsqeEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGG 400

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2466 IHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLL 2519
Cdd:pfam00668  401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 490-888 1.67e-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: 440.16  E-value: 1.67e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLR-MKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA 568
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDNYI------ITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDF 642
Cdd:TIGR01733   81 ALASRLAGLVLpvilldPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  643 EADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVP-QLFAFINKHQTNIVFLPTAFIKMIfseRELANSFPDGV 721
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAaLLAALIAEHPVTVLNLTPSLLALL---AAALPPALASL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  722 KHLIAAGEQLMISDLfqDVLRKR--GIHLHNHYGPSETHVVSTYTIHPGDPIP--ELPPIGKPIGCTDLYILNHQKQLQP 797
Cdd:TIGR01733  238 RLVILGGEALTPALV--DRWRARgpGARLINLYGPTETTVWSTATLVDPDDAPreSPVPIGRPLANTRLYVLDDDLRPVP 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  798 CGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDV--IMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:TIGR01733  316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395

                          410
                   ....*....|...
gi 1678550997  876 VTLMNHPDISEAA 888
Cdd:TIGR01733  396 AALLRHPGVREAV 408
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 7-452 1.79e-120

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: 390.16  E-value: 1.79e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    7 IQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNV 86
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   87 IVLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYAS 166
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  167 YVNASPITLEPVQPYGKYIKW----LMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKS--RQEHVTFSFSKEESSRL 240
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRsfKGDRLSFTLDEDTEELL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  241 SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQ--GAKTpFLQLIKDMQ 318
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDpkGGKT-FSELIKRVQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  319 KDRLAAEAYSYHPLYEIQSRSAVKQ-----GLIDHILVFENYPVQQEIQmlnkQEHASDLFQIHNFTVA-DETNYSFYLM 392
Cdd:pfam00668  318 EDLLSAEPHQGYPFGDLVNDLRLPRdlsrhPLFDPMFSFQNYLGQDSQE----EEFQLSELDLSVSSVIeEEAKYDLSLT 393

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  393 VAP-GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLI 452
Cdd:pfam00668  394 ASErGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
AMP-binding pfam00501
AMP-binding enzyme;
469-865 2.27e-111

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 362.40  E-value: 2.27e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAV-IDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHY 547
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  548 PADRIRYILHDCGCSHVVSQAHLP--------SSLEDNYIITH------------PEDIESKVDGSNIKSVNNADDLLYM 607
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVldrdpvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  608 IYTSGTTGKPKGVQFEHRNMANLL----KFEYTHSGIDFEADVLQFATPSFDVCYQ-EIFSALLKGGTLHIVPEAIKRDV 682
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  683 PQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDGVKHLIAAGEQLMiSDLFQDVLRKRGIHLHNHYGPSETHVVST 762
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLP-PELARRFRELFGGALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  763 YTIHPGDPIPELPPIGKPIGCTDLYILN-HQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPfkpdviMYRTG 841
Cdd:pfam00501  320 TPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG------WYRTG 393

                          410       420
                   ....*....|....*....|....
gi 1678550997  842 DLARRLEDGNIEYIGRADNQVKIR 865
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 465-954 2.64e-104

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: 343.33  E-value: 2.64e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVVSqahlpsslednyiithpedieskvdgsniksvnnaddlLYMIYTSGTTGKPKGVQFEH 624
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNMANLLKFEYTHSGIDfEADVLQFATPSFDV--CYQEIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFLPTA 702
Cdd:COG0318    123 RNLLANAAAIAAALGLT-PGDVVLVALPLFHVfgLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPT 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  703 FIKMIFSERELANSFPDGVKHLIAAGEQLMIsDLFQDVLRKRGIHLHNHYGPSETHVVSTYTihPGDPIPELP-PIGKPI 781
Cdd:COG0318    199 MLARLLRHPEFARYDLSSLRLVVSGGAPLPP-ELLERFEERFGVRIVEGYGLTETSPVVTVN--PEDPGERRPgSVGRPL 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  782 GCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSsDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQ 861
Cdd:COG0318    276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGW------LRTGDLGRLDEDGYLYIVGRKKDM 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  862 VKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSV--QKLNTIDLRSYMASELPEYMIPAKWIWVDSI 939
Cdd:COG0318    349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDEL 428

                          490
                   ....*....|....*
gi 1678550997  940 PLTPNGKVDRAALPE 954
Cdd:COG0318    429 PRTASGKIDRRALRE 443
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
469-952 6.29e-80

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 274.85  E-value: 6.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRIRYILHDCGCSHVVSQAHLPSSLEDNYIIThPEDIESKVDGSNIKSVNNA---DDLLYMIYTSGTTGKPKGVQFEHr 625
Cdd:PRK04813    88 AERIEMIIEVAKPSLIIATEELPLEILGIPVIT-LDELKDIFATGNPYDFDHAvkgDDNYYIIFTSGTTGKPKGVQISH- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  626 nmANLLKFeyTHSGI-DFE-ADVLQF---ATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNI-VFL 699
Cdd:PRK04813   166 --DNLVSF--TNWMLeDFAlPEGPQFlnqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVwVST 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  700 PTaFIKMIFSEREL-ANSFPDgVKHLIAAGEQLMISDlfQDVLRKR--GIHLHNHYGPSETHV-VSTYTIHPgDPIPELP 775
Cdd:PRK04813   242 PS-FADMCLLDPSFnEEHLPN-LTHFLFCGEELPHKT--AKKLLERfpSATIYNTYGPTEATVaVTSIEITD-EMLDQYK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  776 --PIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPdviMYRTGDLARrLEDGNIE 853
Cdd:PRK04813   317 rlPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQP---AYHTGDAGY-LEDGLLF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  854 YIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQKLNTID--------LRSYMASELP 925
Cdd:PRK04813   393 YQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYV--VPKEEDFErefeltkaIKKELKERLM 470

                          490       500
                   ....*....|....*....|....*..
gi 1678550997  926 EYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK04813   471 EYMIPRKFIYRDSLPLTPNGKIDRKAL 497
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 13-251 1.61e-49

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 177.54  E-value: 1.61e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   13 LSYMQEGMLFhslLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVIVLEED 92
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   93 ITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNASP 172
Cdd:COG4908     77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  173 ITLEPVQ-PYGKYIKWLMEQ----DKEQAVSYWDHYLSGHEQQTVLPKQKK--TKGKSRQEHVTFSFSKEESSRLSELAA 245
Cdd:COG4908    157 PPLPELPiQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPrpAVQTFRGATLSFTLPAELTEALKALAK 236


                   ....*.
gi 1678550997  246 REEVTL 251
Cdd:COG4908    237 AHGATV 242
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 3033-3106 4.00e-09

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 56.10  E-value: 4.00e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  3033 LPPSSKMEQILADI---WKEVLG---AEKIGTADSFFELGGDSIKALQVSARLHR-IGKQMAVKDLFSHPTIQELAAYIR 3105
Cdd:smart00823    4 LPPAERRRLLLDLVreqVAAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAaTGLRLPATLVFDHPTPAALAEHLA 83


                    .
gi 1678550997  3106 D 3106
Cdd:smart00823   84 A 84
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 988-1034 5.41e-04

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 41.47  E-value: 5.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1678550997   988 IGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLA 1034
Cdd:smart00823   33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 1058-3599 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 2132.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTL--- 1133
Cdd:PRK12467    51 PLSYAQERQWFLWQLDpDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQ-DEEGFRQVIDASLSLTIpld 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1134 --------SKETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR---- 1196
Cdd:PRK12467   130 dlaneqgrARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgr 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 --QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLA 1274
Cdd:PRK12467   210 epSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1275 HKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAY 1354
Cdd:PRK12467   290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1355 EHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQ-----QKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQ 1429
Cdd:PRK12467   370 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATggrdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAA 449

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1430 FEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLfEETGYSmNQTLHYALEQQAEKTPD 1509
Cdd:PRK12467   450 FTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNA-PATEYA-PDCVHQLIEAQARQHPE 527

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1510 QAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLED 1589
Cdd:PRK12467   528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD 607

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1590 SGTNILLLQSAGL-HVPEFTG-EIVYLNQTNSGLAHRLS-NPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNS 1666
Cdd:PRK12467   608 SGVRLLLTQSHLLaQLPVPAGlRSLCLDEPADLLCGYSGhNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV 687

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1667 LQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHiky 1746
Cdd:PRK12467   688 IAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA--- 764

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1747 rSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEK-LERIPIGKPVHHVRLYLLN 1825
Cdd:PRK12467   765 -SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERdFGNVPIGQPLANLGLYILD 843

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1826 QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYP-GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRI 1904
Cdd:PRK12467   844 HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRI 923

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1905 EPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ----------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTP 1974
Cdd:PRK12467   924 ELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAvadgaehqatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1975 SGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKD 2054
Cdd:PRK12467  1004 NGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRT 1083

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2055 VFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQEL 2134
Cdd:PRK12467  1084 LFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDAL 1163

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2135 IKRHESLRTSFEQdEGGDPVQRIHDEVPFTL-QTTVLGARTEQEAAAAFI-----KPFDLSQAPLFRAQIVKVSDERHLL 2208
Cdd:PRK12467  1164 VARHESLRTTFVQ-EDGRTRQVIHPVGSLTLeEPLLLAADKDEAQLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVL 1242

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2209 LVDMHHIISDGVSVNILIQEFGELY------NNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLP 2282
Cdd:PRK12467  1243 VLTLHHIVSDGWSMQVLVDELVALYaaysqgQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELP 1322

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2283 ADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGM 2362
Cdd:PRK12467  1323 TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGF 1402

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2363 FVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLH-LHDLQM 2441
Cdd:PRK12467  1403 FVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAqLPGLSV 1482

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2442 KPAQVSHLVSKFDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNE 2521
Cdd:PRK12467  1483 ESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEG 1562

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2522 FNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASIL 2601
Cdd:PRK12467  1563 WNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLL 1642

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2602 GVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTiNEADLGVLADFEG-EILTIES----VEEDDKSPLPQMSSAHHLA 2676
Cdd:PRK12467  1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT-QSHLQARLPLPDGlRSLVLDQeddwLEGYSDSNPAVNLAPQNLA 1721

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 YIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAI 2756
Cdd:PRK12467  1722 YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQL 1801

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2757 KHQLSRQRITHMIIVPVLYRALLDVV-QPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATT--VM 2833
Cdd:PRK12467  1802 IQLIERQQVTTLHFVPSMLQQLLQMDeQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVThwTC 1881

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 RH--MEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDA 2910
Cdd:PRK12467  1882 RRkdLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDL 1961

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVVTK----------PGLST 2980
Cdd:PRK12467  1962 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGK-QLVAYVVPTdpglvdddeaQVALR 2040

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2981 NAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNhEGERPFLPPSSKMEQILADIWKEVLGAEKIGTAD 3060
Cdd:PRK12467  2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-ELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHD 2119

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3061 SFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSS--QAAVEGDVQWSPVQKWFLSQDIKEKH 3138
Cdd:PRK12467  2120 NFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSidQGPVTGDLPLLPIQQMFFADDIPERH 2199

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3139 HFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQnEQGKWDQYNR-PLSHSDDALYGLQMIDLSApdgtdgnrpY 3217
Cdd:PRK12467  2200 HWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQ-EDGGWSAMHRaPEQERRPLLWQVVVADKEE---------L 2269

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3218 EPLikrhVLDIQQKMDLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSF 3296
Cdd:PRK12467  2270 EAL----CEQAQRSLDLEEGPLLRAVLATLPDGSqRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAF 2345

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3297 KAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEgQRSTISFTLNDKETAALLKDANSAYNTDTQDML 3376
Cdd:PRK12467  2346 KAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRR-HAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLL 2424

                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3377 LASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTAIYPLLIKLNADLPDSeesmvhvLKTTKDTLRRVPDK 3456
Cdd:PRK12467  2425 LTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATS-------IKTIKEQLRAVPNK 2497

                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3457 GFGYGVIKYL-TPPGKKDINFTGAPEISFNYLGQFESGRTAevpEEDAFsFSPLG--AGGDISTTWNREQSLDISAIAAE 3533
Cdd:PRK12467  2498 GLGFGVLRYLgSEAARQTLQALPVPRITFNYLGQFDGSFDA---EKQAL-FVPSGefSGAEQSEEAPLGNWLSINGQVYG 2573

                         2570      2580      2590      2600      2610      2620      2630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 3534 GKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTED-------ALQEIADM 3599
Cdd:PRK12467  2574 GELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEqldrlpvAVGDIEDI 2646
PRK05691 PRK05691
peptide synthase; Validated
 465-3593 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1907.98  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMfEKQAEKTPDAHAVI------DQACSLTYRELNKAANRLARHLRMKGVVRQEPVaIMMERSAAFITGVLGILKAGG 538
Cdd:PRK05691    12 VQAL-QRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  539 AIVPVDP------HYpADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIES-KVDGSNIKSVNN-------ADDL 604
Cdd:PRK05691    90 IAVPAYPpesarrHH-QERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELlCVDTLDPALAEAwqepalqPDDI 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  605 LYMIYTSGTTGKPKGVQFEHRNM-AN--LLKFEYthsGIDFEADvlqfatpsfDVcyqeIFSAL-------LKGGTLhiv 674
Cdd:PRK05691   169 AFLQYTSGSTALPKGVQVSHGNLvANeqLIRHGF---GIDLNPD---------DV----IVSWLplyhdmgLIGGLL--- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  675 pEAIKRDVPQLFafinkhQTNIVFL--PTAFIKMIFSERELANSFPDGVKHLI------AAGEQLMIS------------ 734
Cdd:PRK05691   230 -QPIFSGVPCVL------MSPAYFLerPLRWLEAISEYGGTISGGPDFAYRLCservseSALERLDLSrwrvaysgsepi 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  735 -----DLFQDVLRKRGIHLHNH---YGPSE-THVVSTYTihPGDPIPEL-------------PPIGKPIGCTDLYILNH- 791
Cdd:PRK05691   303 rqdslERFAEKFAACGFDPDSFfasYGLAEaTLFVSGGR--RGQGIPALeldaealarnraePGTGSVLMSCGRSQPGHa 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  792 -------QKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKpdvIMYRTGDLARrLEDGNIEYIGRADNQVKI 864
Cdd:PRK05691   381 vlivdpqSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGR---TWLRTGDLGF-LRDGELFVTGRLKDMLIV 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  865 RGYRIEPQEIEVTLMNHPDISE----AAILIwqDQNGEHEL---CAYYCSVQKLNTID-----LRSYMASELPEymIPAK 932
Cdd:PRK05691   457 RGHNLYPQDIEKTVEREVEVVRkgrvAAFAV--NHQGEEGIgiaAEISRSVQKILPPQaliksIRQAVAEACQE--APSV 532

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  933 WIWVD--SIPLTPNGKVDRAA---------------LPEPDASISGNPYTAPRNLlEAKLSQLFEDVLKNGHIGIQDNFF 995
Cdd:PRK05691   533 VLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDEL-QARIAAIWCEQLKVEQVAADDHFF 611

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  996 DNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLALIIREAEQN---LYAAIEPAEKRDTYPVSSAQKRIYVLQQL 1072
Cdd:PRK05691   612 LLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGggaAQAAIARLPRGQALPQSLAQNRLWLLWQL 691

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1073 D-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTL----------SKETTIEG 1141
Cdd:PRK05691   692 DpQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE-RDGVALQRIDAQGEFALqridlsdlpeAEREARAA 770

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1142 FVR------PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR------QLKPLRIQYKDYA 1209
Cdd:PRK05691   771 QIReeearqPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYG 850

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1210 VWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRSTLYMTLLALY 1289
Cdd:PRK05691   851 AWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAF 930

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1290 SAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLG 1369
Cdd:PRK05691   931 QALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALP 1010

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1370 VQREMSrnpLFDttlVLQNMEQQKLK-------MNDVQLQWNDLEhpiSKFDISLYVTE-HDSELFCQFEYSTALFEKET 1441
Cdd:PRK05691  1011 QAREQG---LFQ---VMFNHQQRDLSalrrlpgLLAEELPWHSRE---AKFDLQLHSEEdRNGRLTLSFDYAAELFDAAT 1081

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1442 IQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLfeeTGYSMNQTLHYALEQQAEKTPDQAAVIFEDGVMT 1521
Cdd:PRK05691  1082 IERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQA---PCAPAQAWLPELLNEQARQTPERIALVWDGGSLD 1158

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1522 YKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAG 1601
Cdd:PRK05691  1159 YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHL 1238

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1602 L-HVPEFTGEIVYLNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM 1680
Cdd:PRK05691  1239 LeRLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLM 1318

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1681 HKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHikyrsvPIKTN--RLKR 1758
Cdd:PRK05691  1319 QKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE------PLAAActSLRR 1392

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1759 VFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKlERIPIGKPVHHVRLYLLNQNQRMLPVGCIGE 1838
Cdd:PRK05691  1393 LFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDG-ERSPIGRPLGNVLCRVLDAELNLLPPGVAGE 1471

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1839 LYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 1917
Cdd:PRK05691  1472 LCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQP 1551

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1918 GVREAAVTVRTDSGEPELCAYVEGL-----QRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGaaDA 1992
Cdd:PRK05691  1552 GVAQAAVLVREGAAGAQLVGYYTGEagqeaEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW--QQ 1629

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1993 ETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKDVFAHPTVEGLATVIR--- 2069
Cdd:PRK05691  1630 REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVAriq 1709

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2070 -EGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQD 2148
Cdd:PRK05691  1710 aAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSV 1789

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2149 eGGDPVQRIHDEVPFTLQTTVLGA--------RTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGV 2220
Cdd:PRK05691  1790 -DGVPVQQVAEDSGLRMDWQDFSAlpadarqqRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGW 1868

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2221 SVNILIQEFGELY----NNRKLP--ALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFA 2294
Cdd:PRK05691  1869 AMDIFARELGALYeaflDDRESPlePLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHR 1948

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2295 GDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPE 2374
Cdd:PRK05691  1949 GELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLD 2028

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2375 GGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEplhlHDLQMKPAQVSHLV---- 2450
Cdd:PRK05691  2029 GQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQ----QSRQLAGMTVEYLVndar 2104

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2451 -SKFDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNEFNTGQANQ 2529
Cdd:PRK05691  2105 aTKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEA 2184

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2530 YGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGC 2609
Cdd:PRK05691  2185 RLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2610 YVPIDPEYPKERKRYILSDSGTKLLmtineadLGVLADFE--GEI---LTIESVEED-------DKSPLPQMSSAHHLAY 2677
Cdd:PRK05691  2265 YVPLDPEYPLERLHYMIEDSGIGLL-------LSDRALFEalGELpagVARWCLEDDaaalaaySDAPLPFLSLPQHQAY 2337

                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEE--AKDILa 2755
Cdd:PRK05691  2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQwgAEEIC- 2416

                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2756 ikhQLSR-QRITHMIIVPVLYRALLD-VVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTEnsvaTTVM 2833
Cdd:PRK05691  2417 ---QLIReQQVSILGFTPSYGSQLAQwLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTE----TVVM 2489

                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 --------RHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEA-RM 2904
Cdd:PRK05691  2490 placlapeQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGgRL 2569

                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2905 YRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVVTKPGLSTN--- 2981
Cdd:PRK05691  2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGK-QLAGYLVSAVAGQDDeaq 2648

                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2982 -----AVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPvyNHEGERP-FLPPSSKMEQILADIWKEVLGAEK 3055
Cdd:PRK05691  2649 aalreALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAP--DPELNRQaYQAPRSELEQQLAQIWREVLNVER 2726

                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3056 IGTADSFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSS-QAAVEGDVQWSPVQKWFLSQDI 3134
Cdd:PRK05691  2727 VGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAeQGPLQGASGLTPIQHWFFDSPV 2806

                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3135 KEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEqGKWDQYNRPLshSDDALyglqMIDLSAPDGTDGN 3214
Cdd:PRK05691  2807 PQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQAD-GRWQAEYRAV--TAQEL----LWQVTVADFAECA 2879

                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3215 RPYEplikrhvlDIQQKMDLKNGPLLQAGLFHTIDG-DFLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKT 3293
Cdd:PRK05691  2880 ALFA--------DAQRSLDLQQGPLLRALLVDGPQGqQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKT 2951

                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3294 SSFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEgQRSTISFTLNDKETAALLKDANSAYNTDTQ 3373
Cdd:PRK05691  2952 SAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNR-HAQTVSVRLDAERTRQLLQQAPAAYRTQVN 3030

                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3374 DMLLASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTAIYPL-LIKLNADLPDSEESmvhvLKTTKDTLRR 3452
Cdd:PRK05691  3031 DLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLrLTPAPGDDAARGES----IKAIKEQLRA 3106

                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3453 VPDKGFGYGVIKYL-TPPGKKDINFTGAPEISFNYLGQFESGRtaevpEEDAFsFSPL----GAGGDISTTWNREQSLDI 3527
Cdd:PRK05691  3107 VPHKGLGYGVLRYLaDAAVREAMAALPQAPITFNYLGQFDQSF-----ASDAL-FRPLdepaGPAHDPDAPLPNELSVDG 3180

                         3290      3300      3310      3320      3330      3340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 3528 SAIAaeGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTE---DAL 3593
Cdd:PRK05691  3181 QVYG--GELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQaqlDAL 3247
PRK12316 PRK12316
peptide synthase; Provisional
 1048-3593 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1760.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1048 IEPAEKRDTYPVSSAQKRIY---VLQQldEGVAYNMPAVLELEGaLDVAKLSAVCKELISRHEPLRTSFVSGAD-DEPVQ 1123
Cdd:PRK12316  1548 LPAGEIADIYPLSPMQQGMLfhsLYEQ--EAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGlEQPLQ 1624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1124 RIHTEV--PFTLSKETTIEGFV------------RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREF 1189
Cdd:PRK12316  1625 VIHKQVelPFAELDWRGREDLGqaldalaqaerqKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEV 1704

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1190 TDLYANRQLKPLRIQYKDYAVWQQKFKKGDSyqkqETYWQQQfsgdLPILELPT----DKRRPAERQfiGGKVTFQ-LDK 1264
Cdd:PRK12316  1705 LQRYAGQPVAAPGGRYRDYIAWLQRQDAAAS----EAFWKEQ----LAALEEPTrlaqAARTEDGQV--GYGDHQQlLDP 1774

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1265 EITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPhADL---EAVLGMFVNTLALRTRPAGNKTFEE 1341
Cdd:PRK12316  1775 AQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRP-AELpgiEQQIGLFINTLPVIAAPRPDQSVAD 1853

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1342 FLKEVRQTALEAYEHQDYPFEELVDKLGVQREmsrnPLFDTTLVLQNME-QQKLKMN-DVQLQWNDL-EHPISKFDISLY 1418
Cdd:PRK12316  1854 WLQEVQALNLALREHEHTPLYDIQRWAGQGGE----ALFDSLLVFENYPvAEALKQGaPAGLVFGRVsNHEQTNYPLTLA 1929

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1419 VTEHDSeLFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLFEEtGYSMNQTLHY 1498
Cdd:PRK12316  1930 VTLGET-LSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPE-AYPRGPGVHQ 2007

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:PRK12316  2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSG-LAHRLS-NPNVDVLPQSLAYVIYTSGSTGMPKGVEIE 1656
Cdd:PRK12316  2088 PAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDtAPAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1657 HRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVyLLPQGGEKEPEVIAKAIEEQKITAMHFVPSM 1736
Cdd:PRK12316  2168 HGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVY 2246

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1737 LHAFLEHIKYRSVPIKtnrLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEK--LERIPIGK 1814
Cdd:PRK12316  2247 LQQLAEHAERDGRPPA---VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPcgAAYVPIGR 2323

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1815 PVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRT 1893
Cdd:PRK12316  2324 ALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRI 2403

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1894 DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEG-----LQRNEVRAQLERLLPGYMVPAYMIEME 1968
Cdd:PRK12316  2404 DHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPddaaeDLLAELRAWLAARLPAYMVPAHWVVLE 2483

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1969 QWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDV 2048
Cdd:PRK12316  2484 RLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGL 2563

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2049 QVPLKDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMD 2128
Cdd:PRK12316  2564 EVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALE 2643

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2129 RAFQELIKRHESLRTSFEQDeGGDPVQRIHDEVPFTLQ----TTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDE 2204
Cdd:PRK12316  2644 QAFDALVLRHETLRTRFVEV-GEQTRQVILPNMSLRIVledcAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQ 2722

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2205 RHLLLVDMHHIISDGVSVNILIQEFGELYNNRK------LPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPV 2278
Cdd:PRK12316  2723 EHVLVITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPV 2802

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2279 LDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEP 2358
Cdd:PRK12316  2803 LELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETER 2882

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2359 ILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHD 2438
Cdd:PRK12316  2883 LIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPG 2962

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2439 LQMKPAQVSHLVSKFDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQL 2518
Cdd:PRK12316  2963 LHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQL 3042

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2519 LNEFNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIA 2598
Cdd:PRK12316  3043 LEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVV 3122

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2599 SILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEADLGVLADFegEILTIESVEEDDKSPLPQM-SSAHHLAY 2677
Cdd:PRK12316  3123 GLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGV--QVLDLDRGDENYAEANPAIrTMPENLAY 3200

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIK 2757
Cdd:PRK12316  3201 VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLV 3280

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2758 HQLSRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPhteLANEYGPTENSVATTVMRHME 2837
Cdd:PRK12316  3281 ELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVE 3357

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2838 K-QAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMAD 2916
Cdd:PRK12316  3358 EgKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRAD 3437

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2917 GTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVahvtASGQTELSAYVVTKPGLST--NAVRSELQNKLPVF 2994
Cdd:PRK12316  3438 GVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDlrEALKAHLKASLPEY 3513

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2995 MHPAFIEKLDSLPLSPNGKLDRGALPKPVYNhEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELGGDSIKALQ 3074
Cdd:PRK12316  3514 MVPAHLLFLERMPLTPNGKLDRKALPRPDAA-LLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQ 3592

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3075 VSARLHRIGKQMAVKDLFSHPTIQELAAYIR-DSDTSSSQAAVEGDVQWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQ 3153
Cdd:PRK12316  3593 VVSRARQAGIRFTPKDLFQHQTIQGLARVARvGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALD 3672

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3154 EDALRKTLKAITCHHDALRMVFTQNEqGKWDQYNRPLSHSDDALYGLQMIDLSApdgtdgnrpyeplIKRHVLDIQQKMD 3233
Cdd:PRK12316  3673 AAALEAALQALVEHHDALRLRFVEDA-GGWTAEHLPVELGGALLWRAELDDAEE-------------LERLGEEAQRSLD 3738

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3234 LKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYAKKLSDYAESQQL 3312
Cdd:PRK12316  3739 LADGPLLRALLATLADGSqRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEAL 3818

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3313 MKQLKYWREAEEYQTEALPFDQIDGTRAHEGQRSTISfTLNDKETAALLKDANSAYNTDTQDMLLASVILALRHWTNQSA 3392
Cdd:PRK12316  3819 KAELAYWQEQLQGVSSELPCDHPQGALQNRHAASVQT-RLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEAS 3897

                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3393 FKLSLEGHGREDVLKGIDVSRTIGWFTAIYPLLIKLNADLPDSeesmvhvLKTTKDTLRRVPDKGFGYGVIKYL-TPPGK 3471
Cdd:PRK12316  3898 ALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVEDLGAS-------IKAIKEQLRAIPNKGIGFGLLRYLgDEESR 3970

                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3472 KDINFTGAPEISFNYLGQFESGRTAEvpeedAFSFSPLG--AGGDISTTWNREQSLDISAIAAEGKLTVNMTYDNARFQR 3549
Cdd:PRK12316  3971 RTLAGLPVPRITFNYLGQFDGSFDEE-----MALFVPAGesAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEE 4045

                         2570      2580      2590      2600
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 3550 KTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTEDAL 3593
Cdd:PRK12316  4046 ATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQARL 4089
PRK12316 PRK12316
peptide synthase; Provisional
 4-2373 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1588.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    4 ANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGkVNPQFFQNSINALVERHDIFRTIFISQN-VSSPQQVVLR 82
Cdd:PRK12316  1550 AGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDgLEQPLQVIHK 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   83 ERNVIVLEEDITHLNEAEQSqfIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLH 162
Cdd:PRK12316  1629 QVELPFAELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQ 1706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  163 IYASYVNASPitlepVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKT--KGKSRQEHVTfSFSKEESSRL 240
Cdd:PRK12316  1707 RYAGQPVAAP-----GGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAARTedGQVGYGDHQQ-LLDPAQTRAL 1780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  241 SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVrvQGAKTPFLQL---IKDM 317
Cdd:PRK12316  1781 AEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPV--IAAPRPDQSVadwLQEV 1858

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  318 QKDRLAAEAYSYHPLYEIQsRSAVKQG--LIDHILVFENYPVQQEiqmLNKQEHASDLF-QIHNFtvaDETNYSFYLMVA 394
Cdd:PRK12316  1859 QALNLALREHEHTPLYDIQ-RWAGQGGeaLFDSLLVFENYPVAEA---LKQGAPAGLVFgRVSNH---EQTNYPLTLAVT 1931

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  395 PGEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITtDTEKRQLIGEITDQT----PVYETIHAMFE 470
Cdd:PRK12316  1932 LGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALL-DAGERQRILADWDRTpeayPRGPGVHQRIA 2010

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  471 KQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPAD 550
Cdd:PRK12316  2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  551 RIRYILHDCGCSHVVSQAHL------PSSLEdNYIITHPEDIESKVDGSNIKSVNnADDLLYMIYTSGTTGKPKGVQFEH 624
Cdd:PRK12316  2091 RLAYMLEDSGAALLLTQRHLlerlplPAGVA-RLPLDRDAEWADYPDTAPAVQLA-GENLAYVIYTSGSTGLPKGVAVSH 2168

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIkRDVPQLFAFINKHQTNIVFLPTAFI 704
Cdd:PRK12316  2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLYDEMERHGVTILDFPPVYL 2247

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  705 KMIFSERELANSfPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVST-YTIHPGDPI-PELPPIGKPIG 782
Cdd:PRK12316  2248 QQLAEHAERDGR-PPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLlWKCRPQDPCgAAYVPIGRALG 2326

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  783 CTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDVIMYRTGDLARRLEDGNIEYIGRADNQ 861
Cdd:PRK12316  2327 NRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQ 2406

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  862 VKIRGYRIEPQEIEVTLMNHPDISEAAIlIWQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSI 939
Cdd:PRK12316  2407 VKIRGFRIELGEIEARLQAHPAVREAVV-VAQDGASGKQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERL 2485

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  940 PLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQV 1019
Cdd:PRK12316  2486 PLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEV 2565

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1020 SLKDIFAHPTVEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAV 1098
Cdd:PRK12316  2566 PLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEpESAAYHLPSALHLRGVLDQAALEQA 2645

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1099 CKELISRHEPLRTSFVSGADD-----------EPVQRIHTEVPFTLSKETTIEGFVRPFDLSQAPLFRAGLIEVSNEKHV 1167
Cdd:PRK12316  2646 FDALVLRHETLRTRFVEVGEQtrqvilpnmslRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV 2725

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1168 LLVDMHHIISDGVSVQLLIREFTDLYANR------QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILEL 1241
Cdd:PRK12316  2726 LVITQHHIVSDGWSMQVMVDELVQAYAGArrgeqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLEL 2805

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1242 PTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLG 1321
Cdd:PRK12316  2806 PLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIG 2885

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1322 MFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQL 1401
Cdd:PRK12316  2886 FFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHI 2965

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1402 QWNDLEHPISKFDISLYVTEHDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIES 1481
Cdd:PRK12316  2966 ESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEA 3045

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1482 CHlFEETGYSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGI 1561
Cdd:PRK12316  3046 WN-ATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGL 3124

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1562 YGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAgLHVPEFTG-EIVYLNQTNSGLAHrlSNPNVDVLPQSLAYV 1640
Cdd:PRK12316  3125 LAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH-LRLPLAQGvQVLDLDRGDENYAE--ANPAIRTMPENLAYV 3201

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1641 IYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAK 1720
Cdd:PRK12316  3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVE 3281

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1721 AIEEQKITAMHFVPSMLHAFLEHIKYRSVPIktnrLKRVFSGGEQLGTHLVSRFYELLPnvsITNSYGPTEATVEAAFFD 1800
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQAFLEEEDAHRCTS----LKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQ 3354

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1801 CpPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVAR 1880
Cdd:PRK12316  3355 C-VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLAR 3433

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1881 WLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVtvrTDSGEPELCAYV-----EGLQRNEVRAQLERLL 1955
Cdd:PRK12316  3434 YRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVV---LAVDGRQLVAYVvpedeAGDLREALKAHLKASL 3510

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1956 PGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKA 2035
Cdd:PRK12316  3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2036 TALVSRItKEFDVQVPLKDVFAHPTVEGLATVIREGT-----DSPYEAIKP--AEKQETYPVSSAQKRIYVLQQLedggt 2108
Cdd:PRK12316  3591 LQVVSRA-RQAGIRFTPKDLFQHQTIQGLARVARVGGgvavdQGPVSGETLllPIQQQFFEEPVPERHHWNQSLL----- 3664

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2109 gynmpavLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPFTL--QTTVLGARTEQEAAAAFIKPF 2186
Cdd:PRK12316  3665 -------LKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALlwRAELDDAEELERLGEEAQRSL 3737

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2187 DLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR------KLPALRIQYKDYAVWQEGFKTGDA 2260
Cdd:PRK12316  3738 DLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLlqgeapRLPAKTSSFKAWAERLQEHARGEA 3817

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2261 YKMQEAYWLKQLEGELPvlDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGST-LYMVLLAAYTAFLSRLSGQ 2339
Cdd:PRK12316  3818 LKAELAYWQEQLQGVSS--ELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTqVNDLLLTALARVVCRWTGE 3895

                         2410      2420      2430
                   ....*....|....*....|....*....|....*...
gi 1678550997 2340 EDIIVGSPIAGRPHK----DLEPILGMFVNTLALRTRP 2373
Cdd:PRK12316  3896 ASALVQLEGHGREDLfadiDLSRTVGWFTSLFPVRLSP 3933
PRK12467 PRK12467
peptide synthase; Provisional
 12-2373 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1576.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVIVLEE 91
Cdd:PRK12467    51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDE-EGFRQVIDASLSLTIPLD 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   92 DITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNAS 171
Cdd:PRK12467   130 DLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGR 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  172 PITLE--PVQpYGKYI----KWLMEQDKEQAVSYWDHYLSGheQQTVL--------PKQKKTKGKSRQehvtFSFSKEES 237
Cdd:PRK12467   210 EPSLPalPIQ-YADYAiwqrSWLEAGERERQLAYWQEQLGG--EHTVLelptdrprPAVPSYRGARLR----VDLPQALS 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  238 SRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRP-AEIEGiehMVGLFINTMPVRVQ-GAKTPFLQLIK 315
Cdd:PRK12467   283 AGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNrVETER---LIGFFVNTQVLKAEvDPQASFLELLQ 359

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  316 DMQKDRLAAEAYSYHPLYEI---------QSRSAVKQGLIDHilvfenypvQQEIQMLNKQEhASDL--FQIHNFTVADE 384
Cdd:PRK12467   360 QVKRTALGAQAHQDLPFEQLvealqpersLSHSPLFQVMFNH---------QNTATGGRDRE-GAQLpgLTVEELSWARH 429

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  385 TNYsFYLMVAPGEE---IHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLI--GEITDQT 459
Cdd:PRK12467   430 TAQ-FDLALDTYESaqgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELvrWNAPATE 508

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  460 PVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGA 539
Cdd:PRK12467   509 YAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGA 588

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  540 IVPVDPHYPADRIRYILHDCGCSHVVSQAH------LPSSLEdNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGT 613
Cdd:PRK12467   589 YVPLDPEYPQDRLAYMLDDSGVRLLLTQSHllaqlpVPAGLR-SLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGS 667

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  614 TGKPKGVQFEHRNMANLlkFEYTHSGIDFEAD--VLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINK 691
Cdd:PRK12467   668 TGQPKGVAISHGALANY--VCVIAERLQLAADdsMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMAD 745

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  692 HQTNIVFLPTAFIKMIFSERELANsfPDGVKHLIAAGEQLMIsDLFQDVLRKR-GIHLHNHYGPSETHV-VSTYTIHPGD 769
Cdd:PRK12467   746 QGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQV-DLLARVRALGpGARLINHYGPTETTVgVSTYELSDEE 822

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  770 PIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPD-VIMYRTGDLARRLE 848
Cdd:PRK12467   823 RDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADgGRLYRTGDLARYRA 902

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  849 DGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIwQDQNGEHELCAYYCSVQKLNT-------IDLRSYMA 921
Cdd:PRK12467   903 DGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVPAAVADGaehqatrDELKAQLR 981

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  922 SELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHS 1001
Cdd:PRK12467   982 QVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHS 1061

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1002 LKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLDEG-VAYNM 1080
Cdd:PRK12467  1062 LLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGsAAYHI 1141

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1081 PAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTLSKET---------TIEGFV-----RPF 1146
Cdd:PRK12467  1142 PQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTLEEPLllaadkdeaQLKVYVeaearQPF 1220

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1147 DLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR------QLKPLRIQYKDYAVWQQKFKKGDS 1220
Cdd:PRK12467  1221 DLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGE 1300

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1221 YQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQD 1300
Cdd:PRK12467  1301 RARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQD 1380

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1301 DIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLF 1380
Cdd:PRK12467  1381 DIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLF 1460

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1381 DTTLVLQNMEQQKL-KMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAAS 1459
Cdd:PRK12467  1461 QVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVAD 1540

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1460 PETELDNIPILTKEEERDFIESCHLfEETGYSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGR 1539
Cdd:PRK12467  1541 PERRLGELDLLDEAERRQILEGWNA-THTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL 1619

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1540 GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGL-HVPEFTG-EIVYLNQT 1617
Cdd:PRK12467  1620 GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQaRLPLPDGlRSLVLDQE 1699

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1618 NSGLA-HRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFW 1696
Cdd:PRK12467  1700 DDWLEgYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFW 1779

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1697 WPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKtnrLKRVFSGGEQLGTHLVSRFYE 1776
Cdd:PRK12467  1780 PLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS---LRRVVCGGEALEVEALRPWLE 1856

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1777 LLPNVSITNSYGPTEATVEAAFFDCPPHEKLER--IPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRP 1854
Cdd:PRK12467  1857 RLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRP 1936

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1855 ALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEP 1933
Cdd:PRK12467  1937 ALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGK 2016

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1934 ELCAYV-------------EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRN 2000
Cdd:PRK12467  2017 QLVAYVvptdpglvdddeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQS 2096

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2001 VTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRiTKEFDVQVPLKDVFAHPTVEGLATVIREGTDSPyeAIK 2080
Cdd:PRK12467  2097 ELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTV--SID 2173

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2081 PAEKQETYPVSSAQKRIYVLQQLEDggTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGG------DPV 2154
Cdd:PRK12467  2174 QGPVTGDLPLLPIQQMFFADDIPER--HHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGwsamhrAPE 2251

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2155 QrihDEVPFTLQTTVL-GARTEQEAAAAfIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELY 2233
Cdd:PRK12467  2252 Q---ERRPLLWQVVVAdKEELEALCEQA-QRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAY 2327

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2234 NNR------KLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEG---ELPVLDLPADHARPPVRSfagdkVSFTLEP 2304
Cdd:PRK12467  2328 RQLqggqpvKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGastELPCDHPQGGLQRRHAAS-----VTTHLDS 2402

                         2410      2420      2430      2440      2450      2460      2470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2305 EVASGLHKLA-RENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGR----PHKDLEPILGMFVNTLALRTRP 2373
Cdd:PRK12467  2403 EWTRRLLQEApAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGRedlfDEIDLTRTVGWFTSLYPVKLSP 2476
PRK05691 PRK05691
peptide synthase; Validated
 12-2376 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1311.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVIVLEE 91
Cdd:PRK05691   677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERD-GVALQRIDAQGEFALQRI 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   92 DITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNAS 171
Cdd:PRK05691   756 DLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQ 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  172 PITLEPVQ-PYGKYI----KWLMEQDKEQAVSYWDHYLSGheQQTVLPKQKKTKGKSRQEHVTFSFSKEESSRLSE---- 242
Cdd:PRK05691   836 TAELAPLPlGYADYGawqrQWLAQGEAARQLAYWKAQLGD--EQPVLELATDHPRSARQAHSAARYSLRVDASLSEalrg 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  243 LAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRP-AEIEGiehMVGLFINTMPVRVQ-GAKTPFLQLIKDMQKD 320
Cdd:PRK05691   914 LAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPrLETQG---LVGFFINTQVLRAQlDGRLPFTALLAQVRQA 990

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  321 RLAAEAYSYHPLYEiqsrsavkqglidhilVFENYPVQQEIQ----MLNKQEHasDLFQIHNF--TVADETNY-----SF 389
Cdd:PRK05691   991 TLGAQAHQDLPFEQ----------------LVEALPQAREQGlfqvMFNHQQR--DLSALRRLpgLLAEELPWhsreaKF 1052

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  390 YLMVAPGEE----IHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLIG-EITDQTPVYET 464
Cdd:PRK05691  1053 DLQLHSEEDrngrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQwGQAPCAPAQAW 1132

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:PRK05691  1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIIT-------HPEDIESKVDGSNIksvnNADDLLYMIYTSGTTGKP 617
Cdd:PRK05691  1213 PDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSaialdslHLDSWPSQAPGLHL----HGDNLAYVIYTSGSTGQP 1288

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  618 KGVQFEHRNMANLLKFEYTHSGIDfEADVL-QFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQ-TN 695
Cdd:PRK05691  1289 KGVGNTHAALAERLQWMQATYALD-DSDVLmQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGvTT 1367

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  696 IVFLPtAFIKMIFSERELANSfpDGVKHLIAAGEQLMiSDLFQDVL-RKRGIHLHNHYGPSETHVVSTYTiHPGDPIPEL 774
Cdd:PRK05691  1368 LHFVP-PLLQLFIDEPLAAAC--TSLRRLFSGGEALP-AELRNRVLqRLPQVQLHNRYGPTETAINVTHW-QCQAEDGER 1442

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  775 PPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPD-VIMYRTGDLARRLEDGNIE 853
Cdd:PRK05691  1443 SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDgARLYRTGDRARWNADGALE 1522

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  854 YIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEhELCAYYCSV--QKLNTIDLRSYMASELPEYMIPA 931
Cdd:PRK05691  1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA-QLVGYYTGEagQEAEAERLKAALAAELPEYMVPA 1601

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  932 KWIWVDSIPLTPNGKVDRAALPEPDASIsgNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRI 1011
Cdd:PRK05691  1602 QLIRLDQMPLGPSGKLDRRALPEPVWQQ--REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRT 1679

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1012 AKEFHVQVSLKDIFAHPT----VEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLD-EGVAYNMPAVLEL 1086
Cdd:PRK05691  1680 RQACDVELPLRALFEASElgafAEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEpDSPAYNVGGMARL 1759

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1087 EGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTLSKE--TTIEGFVR--------------PFDLSQ 1150
Cdd:PRK05691  1760 SGVLDVDRFEAALQALILRHETLRTTFPS-VDGVPVQQVAEDSGLRMDWQdfSALPADARqqrlqqladseahqPFDLER 1838

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1151 APLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLY----ANRQ--LKPLRIQYKDYAVWQQKFKKGDSYQKQ 1224
Cdd:PRK05691  1839 GPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYeaflDDREspLEPLPVQYLDYSVWQRQWLESGERQRQ 1918

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1225 ETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVI 1304
Cdd:PRK05691  1919 LDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRI 1998

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1305 GSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTL 1384
Cdd:PRK05691  1999 GAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMC 2078

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1385 VLQNME-QQKLKMNDVQLQW--NDLEhpISKFDISLYVTEHDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPE 1461
Cdd:PRK05691  2079 NVQRWEfQQSRQLAGMTVEYlvNDAR--ATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ 2156

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1462 TELDNIPILTKEEERDFIESchLFEETG-YSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRG 1540
Cdd:PRK05691  2157 QRLAELPLLAAAEQQQLLDS--LAGEAGeARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERG 2234

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1541 VKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLhvpEFTGEIVY------L 1614
Cdd:PRK05691  2235 VGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALF---EALGELPAgvarwcL 2311

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1615 NQTNSGLAHRLSNPNVDV-LPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWE 1693
Cdd:PRK05691  2312 EDDAAALAAYSDAPLPFLsLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASER 2391

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1694 LFWWPYAGASVYLLPQgGEKEPEVIAKAIEEQKITAMHFVP---SMLHAFLEHiKYRSVPIKTnrlkrVFSGGEQL-GTH 1769
Cdd:PRK05691  2392 LLVPLLCGARVVLRAQ-GQWGAEEICQLIREQQVSILGFTPsygSQLAQWLAG-QGEQLPVRM-----CITGGEALtGEH 2464

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1770 LvSRFYELLPNVSITNSYGPTEATVEAafFDCPPHEKLER----IPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAG 1845
Cdd:PRK05691  2465 L-QRIRQAFAPQLFFNAYGPTETVVMP--LACLAPEQLEEgaasVPIGRVVGARVAYILDADLALVPQGATGELYVGGAG 2541

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1846 VARGYLNRPALTEERFLEDPFYP-GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:PRK05691  2542 LAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVV 2621

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1925 TVRTDSGEPELCAYVEGLQ-----------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAE 1993
Cdd:PRK05691  2622 LALDTPSGKQLAGYLVSAVagqddeaqaalREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQ 2701

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1994 TYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRiTKEFDVQVPLKDVFAHPTVEGLATVIregTD 2073
Cdd:PRK05691  2702 AYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVA---TH 2777

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2074 SPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDggTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdp 2153
Cdd:PRK05691  2778 SEAAQAEQGPLQGASGLTPIQHWFFDSPVPQP--QHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGR-- 2853

                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2154 VQRIHDEV---PFTLQTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFG 2230
Cdd:PRK05691  2854 WQAEYRAVtaqELLWQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQ 2933

                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2231 ELYNNR------KLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGelPVLDLPADHARPPVRSFAGDKVSFTLEP 2304
Cdd:PRK05691  2934 ALYRQLsagaepALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDA 3011

                         2410      2420      2430      2440      2450      2460      2470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2305 EVASGLHKLARENGST-LYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHK----DLEPILGMFVNTLALRTRPEGG 2376
Cdd:PRK05691  3012 ERTRQLLQQAPAAYRTqVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTPAPG 3088
PRK12316 PRK12316
peptide synthase; Provisional
 2064-3599 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1187.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2064 LATVIREGTD----SPYEAIKPAEKQetyPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHE 2139
Cdd:PRK12316    25 LATLRGEGVDfslfPIPAGVSSAERD---RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2140 SLRTSFEQdEGGDPVQRIHDEVPFTLQ--------TTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVD 2211
Cdd:PRK12316   102 TLRTVFPR-GADDSLAQVPLDRPLEVEfedcsglpEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLT 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2212 MHHIISDGVSVNILIQEFGELYNNR------KLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADH 2285
Cdd:PRK12316   181 LHHIVSDGWSMNVLIEEFSRFYSAYatgaepGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDH 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2286 ARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVN 2365
Cdd:PRK12316   261 PRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVN 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2366 TLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQN--NDYEPL-HLHDLQMK 2442
Cdd:PRK12316   341 TQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPlvADIEALdTVAGLEFG 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2443 PAQVSHLVSKFDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNEF 2522
Cdd:PRK12316   421 QLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGW 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2523 NTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILG 2602
Cdd:PRK12316   501 NATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLA 580

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2603 VWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTinEADLGVLADFEGEILTIE------SVEEDDKSPLPQMSSAHHLA 2676
Cdd:PRK12316   581 ILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS--QSHLGRKLPLAAGVQVLDldrpaaWLEGYSEENPGTELNPENLA 658

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 YIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAI 2756
Cdd:PRK12316   659 YVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKL 738

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2757 KHQLSRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSV-ATTVMRH 2835
Cdd:PRK12316   739 VELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIdVTHWTCV 818

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2836 MEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMA 2915
Cdd:PRK12316   819 EEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRA 898

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2916 DGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhvtASGQtELSAYVV-TKPGLST-NAVRSELQNKLPV 2993
Cdd:PRK12316   899 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGK-QLVGYVVlESEGGDWrEALKAHLAASLPE 974

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2994 FMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNhEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELGGDSIKAL 3073
Cdd:PRK12316   975 YMVPAQWLALERLPLTPNGKLDRKALPAPEAS-VAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSI 1053

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3074 QVSARLHRIGKQMAVKDLFSHPTIQELA-AYIRDSDTSSSQAAVEGDVQWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSV 3152
Cdd:PRK12316  1054 QVVSRARQAGIQLSPRDLFQHQTIRSLAlVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPL 1133

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3153 QEDALRKTLKAITCHHDALRMVFTQnEQGKWDQ-YNRPlsHSDDALYGLQMIDLSApdgtdgnrpyeplIKRHVLDIQQK 3231
Cdd:PRK12316  1134 DPDRLGRALERLVAHHDALRLRFRE-EDGGWQQaYAAP--QAGEVLWQRQAASEEE-------------LLALCEEAQRS 1197

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3232 MDLKNGPLLQAGLFHTIDG-DFLFLSAHHLVVDGISWRVLLEDLALGYRQAaggeDIKLPPKTSSFKAYAKKLSDYAESq 3310
Cdd:PRK12316  1198 LDLEQGPLLRALLVDMADGsQRLLLVIHHLVVDGVSWRILLEDLQRAYADL----DADLPARTSSYQAWARRLHEHAGA- 1272

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3311 qLMKQLKYWREAEEYQTEALPFDQIDGTRAHEGQRsTISFTLNDKETAALLKDANSAYNTDTQDMLLASVILALRHWTNQ 3390
Cdd:PRK12316  1273 -RAEELDYWQAQLEDAPHELPCENPDGALENRHER-KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQ 1350

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3391 SAFKLSLEGHGREDVLKGIDVSRTIGWFTAIYPLLIKLNADLPDSeesmvhvLKTTKDTLRRVPDKGFGYGVIKYL-TPP 3469
Cdd:PRK12316  1351 ASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGES-------IKAIKEQLRAVPDKGIGYGLLRYLaGEE 1423

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3470 GKKDINFTGAPEISFNYLGQF--------------ESGRTAEVPEedafsfSPLGAggdisttWnreqsLDISAIAAEGK 3535
Cdd:PRK12316  1424 AAARLAALPQPRITFNYLGQFdrqfdeaalfvpatESAGAAQDPC------APLAN-------W-----LSIEGQVYGGE 1485

                         1530      1540      1550      1560      1570      1580      1590
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 3536 LTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTE---DAL----QEIADM 3599
Cdd:PRK12316  1486 LSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLAGLSQaqlDALplpaGEIADI 1556
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1046-2328 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: 1118.78  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1046 AAIEPAEKRDTYPVSSAQKRIYVLQQLDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRI 1125
Cdd:COG1020      7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1126 HTEVPFTL----------------SKETTIEGFVRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREF 1189
Cdd:COG1020     87 QPVVAAPLpvvvllvdlealaeaaAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1190 TDLY------ANRQLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLD 1263
Cdd:COG1020    167 LRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1264 KEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFL 1343
Cdd:COG1020    247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1344 KEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHD 1423
Cdd:COG1020    327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETG 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1424 SELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESchlFEETG--YSMNQTLHYALE 1501
Cdd:COG1020    407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAE---WNATAapYPADATLHELFE 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1502 QQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEE 1581
Cdd:COG1020    484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1582 RISFLLEDSGTNILLLQSAGL-HVPEFTGEIVYLNQTNSGlAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSA 1660
Cdd:COG1020    564 RLAYMLEDAGARLVLTQSALAaRLPELGVPVLALDALALA-AEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1661 VNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAF 1740
Cdd:COG1020    643 VNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRAL 722

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1741 LEHikyrsVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKL-ERIPIGKPVHHV 1819
Cdd:COG1020    723 LDA-----APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADgGSVPIGRPIANT 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1820 RLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVK 1898
Cdd:COG1020    798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1899 IRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV 1972
Cdd:COG1020    878 IRGFRIELGEIEAALLQHPGVREAVVVAREDaPGDKRLVAYVvpeagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1973 TPSGKLDRNALPAPgGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPL 2052
Cdd:COG1020    958 TGNGKLDRLALPAP-AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2053 KDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQ 2132
Cdd:COG1020   1037 LLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLA 1116

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2133 ELIKRHESLRTSF-----EQDEGGDPVQRIHDEVPFTLQTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHL 2207
Cdd:COG1020   1117 LLLALLAALRARRavrqeGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLL 1196

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2208 LLVDMHHIISDGVSVNILIQEFGELY------NNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDL 2281
Cdd:COG1020   1197 LLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLAL 1276

                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997 2282 PADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAA 2328
Cdd:COG1020   1277 ALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLAL 1323
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 2077-3386 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: 1089.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2077 EAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGgDPVQR 2156
Cdd:COG1020      7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG-RPVQV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2157 IHDEVPFTLQTTVL--------GARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQE 2228
Cdd:COG1020     86 IQPVVAAPLPVVVLlvdlealaEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2229 FGELYN------NRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTL 2302
Cdd:COG1020    166 LLRLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2303 EPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQY 2382
Cdd:COG1020    246 PAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAEL 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2383 LQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQASEG 2462
Cdd:COG1020    326 LARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2463 DGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNEFNTGQANQYGVQTISQLFEQQ 2542
Cdd:COG1020    406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQ 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERK 2622
Cdd:COG1020    486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 RYILSDSGTKLLMTiNEADLGVLADFEGEILTIESVE--EDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIAN 2700
Cdd:COG1020    566 AYMLEDAGARLVLT-QSALAARLPELGVPVLALDALAlaAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2701 TLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLD 2780
Cdd:COG1020    645 LLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD 724

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2781 VVqPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMR---HMEKQAYVSIGQPIDGTQVLILN 2857
Cdd:COG1020    725 AA-PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtpPDADGGSVPIGRPIANTRVYVLD 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2858 SNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFK-PEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRV 2936
Cdd:COG1020    804 AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRI 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2937 ETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNA--VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:COG1020    884 ELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAalLRLALALLLPPYMVPAAVVLLLPLPLTGNGKL 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3015 DRGALPKPVYNHEGERPFLPPSSkmEQILADIWKEVLGAEKIGTADSFFELGGDSIKALQVSARLHRIGKQMAVKDLFSH 3094
Cdd:COG1020    964 DRLALPAPAAAAAAAAAAPPAEE--EEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFL 1041

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3095 PTIQELAAYIRDSDTSSSQAAVEGDVQWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMV 3174
Cdd:COG1020   1042 AAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLAL 1121

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3175 FTQNEQGKWDQYNRPLSHSDDALYGLQMIDLSAPDGTDGNRPYEPLIKRHVLDIQQKMDLKNGPLLQAGLFHTIDgdfLF 3254
Cdd:COG1020   1122 LAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLL---LL 1198

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3255 LSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQ 3334
Cdd:COG1020   1199 LLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALAL 1278

                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 3335 IDGTRAHEGQRSTiSFTLNDKETAALLKDANSAYNTDTQDMLLASVILALRH 3386
Cdd:COG1020   1279 LLPALARARAART-ARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
PRK12316 PRK12316
peptide synthase; Provisional
 1047-2375 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 969.43  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1047 AIEPAEKRDtyPVSSAQKRIYVLQQLDEGV-AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEpVQRI 1125
Cdd:PRK12316    42 AGVSSAERD--RLSYAQQRMWFLWQLEPQSgAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDS-LAQV 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1126 HTEVPFTLSK-------ETTIEGFVR---------PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREF 1189
Cdd:PRK12316   119 PLDRPLEVEFedcsglpEAEQEARLRdeaqreslqPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEF 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1190 TDLY------ANRQLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLD 1263
Cdd:PRK12316   199 SRFYsayatgAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSID 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1264 KEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFL 1343
Cdd:PRK12316   279 PALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLL 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1344 KEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNM--EQQKLK----MNDVQLQWNDlehPISKFDISL 1417
Cdd:PRK12316   359 AGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLvaDIEALDtvagLEFGQLEWKS---RTTQFDLTL 435

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1418 YVTEHDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLFEEtGYSMNQTLH 1497
Cdd:PRK12316   436 DTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAA-EYPLQRGVH 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1498 YALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPD 1577
Cdd:PRK12316   515 RLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1578 YPEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSGL---AHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVE 1654
Cdd:PRK12316   595 YPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAwleGYSEENPGTELNPENLAYVIYTSGSTGKPKGAG 674

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 IEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVP 1734
Cdd:PRK12316   675 NRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 754

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHAFLEHIKYRSVpiktNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCpPHEKLERIPIGK 1814
Cdd:PRK12316   755 SMLQAFLQDEDVASC----TSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC-VEEGGDSVPIGR 829

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1815 PVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTD 1894
Cdd:PRK12316   830 PIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRID 909

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1895 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVrtdSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQ 1969
Cdd:PRK12316   910 HQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGKQLVGYVvleseGGDWREALKAHLAASLPEYMVPAQWLALER 986

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1970 WPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRiTKEFDVQ 2049
Cdd:PRK12316   987 LPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQAGIQ 1065

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2050 VPLKDVFAHPTVEGLATVIREGTDSPYEAiKPAEKQetYPVSSAQKRIYvlQQLEDGGTGYNMPAVLELEGKLNPERMDR 2129
Cdd:PRK12316  1066 LSPRDLFQHQTIRSLALVAKAGQATAADQ-GPASGE--VALAPVQRWFF--EQAIPQRQHWNQSLLLQARQPLDPDRLGR 1140

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2130 AFQELIKRHESLRTSFEQDEGGdpVQRIHDEvpfTLQTTVLGART--EQEAAAAFI----KPFDLSQAPLFRAQIVKVSD 2203
Cdd:PRK12316  1141 ALERLVAHHDALRLRFREEDGG--WQQAYAA---PQAGEVLWQRQaaSEEELLALCeeaqRSLDLEQGPLLRALLVDMAD 1215

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2204 ERHLLLVDMHHIISDGVSVNILIQEFGELYNNR--KLPALRIQYKDYAVWQEGFKTGDAykMQEAYWLKQLEGELPvlDL 2281
Cdd:PRK12316  1216 GSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLdaDLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPH--EL 1291

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2282 PADHARPPVRSFAGDKVSFTLEPEVASGLHKLA----RENGSTLymvLLAAYTAFLSRLSGQEDIIVGSPIAGRPHK--- 2354
Cdd:PRK12316  1292 PCENPDGALENRHERKLELRLDAERTRQLLQEApaayRTQVNDL---LLTALARVTCRWSGQASVLVQLEGHGREDLfed 1368

                         1370      1380
                   ....*....|....*....|..
gi 1678550997 2355 -DLEPILGMFVNTLALRTRPEG 2375
Cdd:PRK12316  1369 iDLSRTVGWFTSLFPVRLTPAA 1390
PRK05691 PRK05691
peptide synthase; Validated
 1490-3386 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 927.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1490 YSMNQTLHYALEQQAEKTPDQAAVIF------EDGVMTYKELNEQANRIAWELIGRGVKPETTVaIIGKRSPEMLLGIYG 1563
Cdd:PRK05691     5 FELPLTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1564 ILKAGGAYLPIDPdyPE-------ERISFLLEDSGTNiLLLQSAGLHVP-----EFTG----EIVYLNQTNSGLAHRLSN 1627
Cdd:PRK05691    84 CLYAGVIAVPAYP--PEsarrhhqERLLSIIADAEPR-LLLTVADLRDSllqmeELAAanapELLCVDTLDPALAEAWQE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1628 PNVDvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNflNSLQSRY----QLKHSDMIMHKTSYSFDAS-IWELFWWPYAGA 1702
Cdd:PRK05691   161 PALQ--PDDIAFLQYTSGSTALPKGVQVSHGNLVA--NEQLIRHgfgiDLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGV 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1703 SVYLL-PQGGEKEPEVIAKAIEEQKIT---AMHFVPSMLHAFLEHIKYRSVPIktNRLKRVFSGGEQLGTHLVSRFYELL 1778
Cdd:PRK05691   237 PCVLMsPAYFLERPLRWLEAISEYGGTisgGPDFAYRLCSERVSESALERLDL--SRWRVAYSGSEPIRQDSLERFAEKF 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1779 PNVSITN-----SYGPTEAT----------------VEAAFFDCPPHEKLERIPI-----GKPVHHVRLyLLNQNQRMLP 1832
Cdd:PRK05691   315 AACGFDPdsffaSYGLAEATlfvsggrrgqgipaleLDAEALARNRAEPGTGSVLmscgrSQPGHAVLI-VDPQSLEVLG 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1833 VGCIGELYIAGAGVARGYLNRPALTEERFLEdpfYPGERMYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAA 1912
Cdd:PRK05691   394 DNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKT 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1913 L-RSIEGVREAAVTV--RTDSGEPELCAYVE---GLQR-----------NEVRAQLERLLPGYMVpayMIEMEQWPVTPS 1975
Cdd:PRK05691   470 VeREVEVVRKGRVAAfaVNHQGEEGIGIAAEisrSVQKilppqaliksiRQAVAEACQEAPSVVL---LLNPGALPKTSS 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1976 GKLDRNA---------------LPAPGGAADAETYTAPRNVTEMkLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVS 2040
Cdd:PRK05691   547 GKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQAR-IAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVA 625

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2041 RITKEFDVQVPLKDVFAHPTVEG----LATVIREGTDSPyEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVL 2116
Cdd:PRK05691   626 RLRDELGIDLNLRQLFEAPTLAAfsaaVARQLAGGGAAQ-AAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGL 704

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2117 ELEGKLNPERMDRAFQELIKRHESLRTSF-EQDegGDPVQRIHDEVPFTLQTTVLGA--RTEQEAAAAFIK------PFD 2187
Cdd:PRK05691   705 HLRGELDEAALRASFQRLVERHESLRTRFyERD--GVALQRIDAQGEFALQRIDLSDlpEAEREARAAQIReeearqPFD 782

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2188 LSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR------KLPALRIQYKDYAVWQEGFKTGDAY 2261
Cdd:PRK05691   783 LEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQRQWLAQGEA 862

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2262 KMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQED 2341
Cdd:PRK05691   863 ARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGD 942

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2342 IIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSrnpVFD 2421
Cdd:PRK05691   943 IRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG---LFQ 1019

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2422 AMLVVQNNDYEPL-HLHDLQMKPAQVSHLVSKFDLTLQASEG-DGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKN 2499
Cdd:PRK05691  1020 VMFNHQQRDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDrNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCED 1099

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2500 PKVTLNHIDILTQEERHQLLnefNTGQANQYGVQ-TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR 2578
Cdd:PRK05691  1100 PQRALGDVQLLDAAERAQLA---QWGQAPCAPAQaWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDK 1176

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2579 GVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTiNEADLGVLADFEGEI-LTIES 2657
Cdd:PRK05691  1177 GVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT-QSHLLERLPQAEGVSaIALDS 1255

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2658 VEEDD-KSPLPQMS-SAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTP 2735
Cdd:PRK05691  1256 LHLDSwPSQAPGLHlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWP 1335

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2736 LLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHT 2815
Cdd:PRK05691  1336 LITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQV 1415

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2816 ELANEYGPTENSVATTVMR-HMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFT 2894
Cdd:PRK05691  1416 QLHNRYGPTETAINVTHWQcQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFV 1495

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2895 QNPF-KPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVV 2973
Cdd:PRK05691  1496 PDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTG 1575

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2974 TK-PGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNhegERPFLPPSSKMEQILADIWKEVLG 3052
Cdd:PRK05691  1576 EAgQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ---QREHVEPRTELQQQIAAIWREVLG 1652

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3053 AEKIGTADSFFELGGDSIKALQVSARL-HRIGKQMAVKDLFSHPTIQELA---AYIRDSDTSSSQAAVEGDVQWSPV--- 3125
Cdd:PRK05691  1653 LPRVGLRDDFFALGGHSLLATQIVSRTrQACDVELPLRALFEASELGAFAeqvARIQAAGERNSQGAIARVDRSQPVpls 1732

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3126 ----QKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQYnrplsHSDDALYgLQ 3201
Cdd:PRK05691  1733 ysqqRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQV-----AEDSGLR-MD 1806

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3202 MIDLSAPDGTDGNRPYEPLIKRHVldiQQKMDLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQ 3280
Cdd:PRK05691  1807 WQDFSALPADARQQRLQQLADSEA---HQPFDLERGPLLRACLVKAAEREhYFVLTLHHIVTEGWAMDIFARELGALYEA 1883

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3281 AAGGEDIKLPPKTSSFKAYAKKLSDYAESQQLMKQLKYWRE--AEEYQTEALPFDQI-DGTRAHEGQrsTISFTLNDkET 3357
Cdd:PRK05691  1884 FLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAqlGNEHPLLELPADRPrPPVQSHRGE--LYRFDLSP-EL 1960

                         2010      2020
                   ....*....|....*....|....*....
gi 1678550997 3358 AALLKDANSAYNTdTQDMLLASVILALRH 3386
Cdd:PRK05691  1961 AARVRAFNAQRGL-TLFMTMTATLAALLY 1988
PRK12467 PRK12467
peptide synthase; Provisional
 2086-3391 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 927.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2086 ETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPFTL 2165
Cdd:PRK12467    48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEG-FRQVIDASLSLTI 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2166 QTTVLGA---RTEQEAAAAFI-----KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELY---- 2233
Cdd:PRK12467   127 PLDDLANeqgRARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYsays 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2234 NNRK--LPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLH 2311
Cdd:PRK12467   207 QGREpsLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLK 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2312 KLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETAL 2391
Cdd:PRK12467   287 ALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTAL 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2392 EAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQN-----NDYEPLHLHDLQMKPAQVSHLVSKFDLTLQASEGDGNI 2466
Cdd:PRK12467   367 GAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNtatggRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGL 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2467 HFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNEFNTgQANQYGVQTISQLFEQQAART 2546
Cdd:PRK12467   447 WAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNA-PATEYAPDCVHQLIEAQARQH 525

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:PRK12467   526 PERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTINE--ADLGVLADfegeiltIESVEEDDKSPLPQMSSAHH---------LAYIIYTSGTTGRPKGVMVEH 2695
Cdd:PRK12467   606 DDSGVRLLLTQSHllAQLPVPAG-------LRSLCLDEPADLLCGYSGHNpevaldpdnLAYVIYTSGSTGQPKGVAISH 678

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2696 KGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLY 2775
Cdd:PRK12467   679 GALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHL 758

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2776 RALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMRHMEKQA---YVSIGQPIDGTQ 2852
Cdd:PRK12467   759 QALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERdfgNVPIGQPLANLG 838

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2853 VLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPE-ARMYRTGDAARWMADGTLEYLGRIDDQVKI 2931
Cdd:PRK12467   839 LYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKI 918

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2932 RGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELSAYVV-------TKPGLSTNAVRSELQNKLPVFMHPAFIEKLD 3004
Cdd:PRK12467   919 RGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLD 997

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3005 SLPLSPNGKLDRGALPKPVYNhEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELGGDSIKALQVSARL-HRIG 3083
Cdd:PRK12467   998 SLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVrQRLG 1076

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3084 KQMAVKDLFSHPTIQELAAYIRDSDTSSSQAAVEGDVQWSPV------QKWFLSQDIKEKHHFNQSVMLHRSTSVQEDAL 3157
Cdd:PRK12467  1077 IQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPlsyaqeRQWFLWQLEPGSAAYHIPQALRLKGPLDIEAL 1156

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3158 RKTLKAITCHHDALRMVFTQNEqgkwdqyNRPLSHSDDALYGLQMIDLSAPDGTDgnrpyEPLIKRHV-LDIQQKMDLKN 3236
Cdd:PRK12467  1157 ERSFDALVARHESLRTTFVQED-------GRTRQVIHPVGSLTLEEPLLLAADKD-----EAQLKVYVeAEARQPFDLEQ 1224

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3237 GPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYAKKLSDYAESQQLMKQ 3315
Cdd:PRK12467  1225 GPLLRVGLLRLAADEhVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQ 1304

                         1290      1300      1310      1320      1330      1340      1350
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 3316 LKYWRE--AEEYQTEALPFDQI-DGTRAHEGQRstISFTLnDKETAALLKDANSAYNTDTQDMLLASVILALRHWTNQS 3391
Cdd:PRK12467  1305 LAYWKAqlGGEQPVLELPTDRPrPAVQSHRGAR--LAFEL-PPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQD 1380
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 476-953 0e+00

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: 895.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  476 TPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYI 555
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 LHDCGCSHVVSQAHLPSSLEDNYIITHPE-DIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFE 634
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEdPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  635 YTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELA 714
Cdd:cd17656    161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  715 NSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQ 794
Cdd:cd17656    241 NRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQ 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  795 LQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEI 874
Cdd:cd17656    321 LQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEI 400

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  875 EVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:cd17656    401 EAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 8-1288 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: 796.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    8 QDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSsPQQVVLRERNVI 87
Cdd:COG1020     15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGR-PVQVIQPVVAAP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   88 VLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASY 167
Cdd:COG1020     94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  168 VNASPITLEPVQPYGK-----YIKWLMEQDKEQAVSYWDHYLSGHEQQTVLP--KQKKTKGKSRQEHVTFSFSKEESSRL 240
Cdd:COG1020    174 YAGAPLPLPPLPIQYAdyalwQREWLQGEELARQLAYWRQQLAGLPPLLELPtdRPRPAVQSYRGARVSFRLPAELTAAL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  241 SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEieGIEHMVGLFINTMPVRVQGAKTP-FLQLIKDMQK 319
Cdd:COG1020    254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPsFAELLARVRE 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  320 DRLAAEAYSYHPLYEIQ-----SRSAVKQGLIDHILVFENYPVQQEiqmlnkqeHASDLfQIHNFTVADET-NYSFYLMV 393
Cdd:COG1020    332 TLLAAYAHQDLPFERLVeelqpERDLSRNPLFQVMFVLQNAPADEL--------ELPGL-TLEPLELDSGTaKFDLTLTV 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  394 AP-GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLIGEITD---QTPVYETIHAMF 469
Cdd:COG1020    403 VEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNAtaaPYPADATLHELF 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA 549
Cdd:COG1020    483 EAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPA 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  550 DRIRYILHDCGCSHVVSQAHLPSSLEDN--YIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNM 627
Cdd:COG1020    563 ERLAYMLEDAGARLVLTQSALAARLPELgvPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  628 ANLLkfEYTHSGIDFEAD--VLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIK 705
Cdd:COG1020    643 VNLL--AWMQRRYGLGPGdrVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLR 720

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  706 MIFserELANSFPDGVKHLIAAGEQLMIsDLFQDVLRK-RGIHLHNHYGPSETHVVST-YTIHPGDPIPELPPIGKPIGC 783
Cdd:COG1020    721 ALL---DAAPEALPSLRLVLVGGEALPP-ELVRRWRARlPGARLVNLYGPTETTVDSTyYEVTPPDADGGSVPIGRPIAN 796

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFK-PDVIMYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:COG1020    797 TRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADDQV 876

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTID--LRSYMASELPEYMIPAKWIWVDSIP 940
Cdd:COG1020    877 KIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAalLRLALALLLPPYMVPAAVVLLLPLP 956

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  941 LTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVS 1020
Cdd:COG1020    957 LTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1021 LKDIFAHPTVEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLDEGVAYNMPAVLELEGALDVAKLSAVCK 1100
Cdd:COG1020   1037 LLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLA 1116

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1101 ELISRHEPLRTSFVSGADDEPVQRIHTEVPFTLS-------------KETTIEGFVRPFDLSQAPLFRAGLIEVSNEKHV 1167
Cdd:COG1020   1117 LLLALLAALRARRAVRQEGPRLRLLVALAAALALaallalllaaaaaAAELLAAAALLLLLALLLLALLLLLLLLLLLLL 1196

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1168 LLVDMHHIISDGVSVQLLIREFTDLYA------NRQLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILEL 1241
Cdd:COG1020   1197 LLLLLLLLLLLLLLLLLLLLLLLLLLLlaaaaaALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLAL 1276

                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997 1242 PTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRSTLYMTLLAL 1288
Cdd:COG1020   1277 ALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLAL 1323
PRK12467 PRK12467
peptide synthase; Provisional
 4-1346 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 765.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    4 ANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGkVNPQFFQNSINALVERHDIFRTIFISQ-NVSSPQQVVLR 82
Cdd:PRK12467  2640 VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDgELEEPLQVVYK 2718

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   83 ERNVIVLEEDIThlNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLH 162
Cdd:PRK12467  2719 QARLPFSRLDWR--DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQ 2796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  163 IYASYVNASPITLepvqpYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLP---KQKKTKGKSRQEHVTFSFSKEESSR 239
Cdd:PRK12467  2797 RYFGQPPPAREGR-----YRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLAralYPAPAEAVAGHGAHYLHLDATQTRQ 2871

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  240 LSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVrVQG--AKTPFLQLIKDM 317
Cdd:PRK12467  2872 LIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPV-IASprAEQTVSDWLQQV 2950

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  318 QKDRLAAEAYSYHPLYEIQSRSA-VKQGLIDHILVFENYPVQQEIQmlnkQEHASDLfQIHNFTVADETNYSFYLMVAPG 396
Cdd:PRK12467  2951 QAQNLALREFEHTPLADIQRWAGqGGEALFDSILVFENYPISEALK----QGAPSGL-RFGAVSSREQTNYPLTLAVGLG 3025

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  397 EEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLIGEITDQTPVY---ETIHAMFEKQA 473
Cdd:PRK12467  3026 DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYpseRLVHQLIEAQV 3105

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  474 EKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIR 553
Cdd:PRK12467  3106 ARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLA 3185

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  554 YILHDCGCSHVVSQAH----LPSSLEDNYIITHPEDIESKVDgSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMAN 629
Cdd:PRK12467  3186 YMIEDSGVKLLLTQAHlleqLPAPAGDTALTLDRLDLNGYSE-NNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALAN 3264

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  630 LLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIkRDVPQLFAFINKHQTNIVFLPTAFIKMIFS 709
Cdd:PRK12467  3265 HLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAE 3343

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  710 ERELANSFPdgVKHLIAAGEQlMISDLFQDVLRK-RGIHLHNHYGPSETHVVSTYTIHPGDPIPELP--PIGKPIGCTDL 786
Cdd:PRK12467  3344 DAGGADCAS--LDIYVFGGEA-VPPAAFEQVKRKlKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPyaPIGRPVAGRSI 3420

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  787 YILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPD-VIMYRTGDLARRLEDGNIEYIGRADNQVKIR 865
Cdd:PRK12467  3421 YVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSgGRLYRTGDLARYRADGVIEYLGRIDHQVKIR 3500

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  866 GYRIEPQEIEVTLMNHPDISEAAILIwQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTP 943
Cdd:PRK12467  3501 GFRIELGEIEARLLQHPSVREAVVLA-RDGAGGKQLVAYVVpaDPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGP 3579

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  944 NGKVDRAALPEPDASISGNpYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVSLKD 1023
Cdd:PRK12467  3580 NGKVDRKALPDPDAKGSRE-YVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRD 3658

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1024 IFAHPTVEGLAliireaeqnlyaaiepaekrdtypvssaqkriyvlqqldegvAYNMPAVLELEGALDVAKLSAVCKELI 1103
Cdd:PRK12467  3659 LMSAPTIAELA------------------------------------------GYSPLGDVPVNLLLDLNRLETGFPALF 3696

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1104 SRHEPLRTSFvsgaDDEPVQRIhtevpftlskettiegfvrpfdlsqaplfraglieVSNEKHVLLVDMHHIISDGvsvq 1183
Cdd:PRK12467  3697 CRHEGLGTVF----DYEPLAVI-----------------------------------LEGDRHVLGLTCRHLLDDG---- 3733

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1184 llireftdlYANRQLKPLRIQYKDYAVWQQkfkkgdsyqkqetywqqqfsgdlpilelptdkrrPAERQFIGGkvtFQLD 1263
Cdd:PRK12467  3734 ---------WQDTSLQAMAVQYADYILWQQ----------------------------------AKGPYGLLG---WSLG 3767

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1264 KEITARIKRLAHKNRSTlymtllalysaflsrlsgqddivigspiagrphadlEAVLGMFVNTLALRTRPAGNKTFEEFL 1343
Cdd:PRK12467  3768 GTLARLVAELLEREGES------------------------------------EAFLGLFDNTLPLPDEFVPQAEFLELL 3811


                   ...
gi 1678550997 1344 KEV 1346
Cdd:PRK12467  3812 RQL 3814
PRK12316 PRK12316
peptide synthase; Provisional
 1050-2061 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 753.72  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1050 PAEKRDTYPVSSAQKRIYVLQQLDEGVA-YNMPAVLELEGaLDVAKLSAVCKELISRHEPLRTSFV-SGADDEPVQRIH- 1126
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGdYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVwQGELGRPLQVVHk 4174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1127 -TEVPFT---LSKETTIEGFV---------RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLY 1193
Cdd:PRK12316  4175 qVSLPFAeldWRGRADLQAALdalaaaereRGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1194 ANRQLKPLRIQYKDYAVWQQKFKKGDSyqkqETYWQQQfsgdLPILELPT----DKRRPAERQFIG-GKVTFQLDKEITA 1268
Cdd:PRK12316  4255 SGRPPAQPGGRYRDYIAWLQRQDAAAS----EAFWREQ----LAALDEPTrlaqAIARADLRSANGyGEHVRELDATATA 4326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1269 RIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPhADL---EAVLGMFVNTLALRTRPAGNKTFEEFLKE 1345
Cdd:PRK12316  4327 RLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRP-AELpgiEGQIGLFINTLPVIATPRAQQSVVEWLQQ 4405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1346 VRQTALEAYEHQDYPFEELvdklgvQRE--MSRNPLFDTTLVLQN------MEQQK---LKMNDVqLQWNDLEHPiskFD 1414
Cdd:PRK12316  4406 VQRQNLALREHEHTPLYEI------QRWagQGGEALFDSLLVFENypvseaLQQGApggLRFGEV-TNHEQTNYP---LT 4475

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1415 ISLYVTEhdsELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLfEETGYSMNQ 1494
Cdd:PRK12316  4476 LAVGLGE---TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNR-TDAGYPATR 4551

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI 1574
Cdd:PRK12316  4552 CVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL 4631

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1575 DPDYPEERISFLLEDSGTNILLLQS---AGLHVPEFTGEIVyLNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPK 1651
Cdd:PRK12316  4632 DPEYPRERLAYMMEDSGAALLLTQShllQRLPIPDGLASLA-LDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPK 4710

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1652 GVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVyLLPQGGEKEPEVIAKAIEEQKITAMH 1731
Cdd:PRK12316  4711 GVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV-VIRDDSLWDPERLYAEIHEHRVTVLV 4789

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1732 FVPSMLHAFLEHIKYRSVPIktnRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPH--EKLER 1809
Cdd:PRK12316  4790 FPPVYLQQLAEHAERDGEPP---SLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGdaCGAAY 4866

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1810 IPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVE 1888
Cdd:PRK12316  4867 MPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVID 4946

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1889 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV-------------EGLQRNEVRAQLERLL 1955
Cdd:PRK12316  4947 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVvpqdpaladadeaQAELRDELKAALRERL 5026

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1956 PGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKA 2035
Cdd:PRK12316  5027 PEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLA 5106

                         1050      1060
                   ....*....|....*....|....*.
gi 1678550997 2036 TALVSRITKEFDVQVPLKDVFAHPTV 2061
Cdd:PRK12316  5107 IQVTSRIQLELGLELPLRELFQTPTL 5132
PRK12467 PRK12467
peptide synthase; Provisional
 1047-2253 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 730.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1047 AIEPAEKRDTYPVSSAQKRI--YVLQQLDEGVAYNMPAVLeLEGaLDVAKLSAVCKELISRHEPLRTSFVS-GADDEPVQ 1123
Cdd:PRK12467  2637 PVAVGDIEDIYPLSPMQQGMlfHTLYEGGAGDYINQMRVD-VEG-LDVERFRTAWQAVIDRHEILRSGFLWdGELEEPLQ 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1124 RIH--TEVPFTL-------SKETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREF 1189
Cdd:PRK12467  2715 VVYkqARLPFSRldwrdraDLEQALDALAaadrqQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEV 2794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1190 TDLYANRQLKPLRIQYKDYAVWQQKfkkgDSYQKQETYWQQQFsGDL--PILELPTDKRRPAERQFIGGKVTFQLDKEIT 1267
Cdd:PRK12467  2795 LQRYFGQPPPAREGRYRDYIAWLQA----QDAEASEAFWKEQL-AALeePTRLARALYPAPAEAVAGHGAHYLHLDATQT 2869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1268 ARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPhADL---EAVLGMFVNTLALRTRPAGNKTFEEFLK 1344
Cdd:PRK12467  2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRP-AQLrgaEQQLGLFINTLPVIASPRAEQTVSDWLQ 2948

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1345 EVRQTALEAYEHQDYPFEElvdklgVQREMSR--NPLFDTTLVLQNME-QQKLKMN-DVQLQWNDLE-HPISKFDISLYV 1419
Cdd:PRK12467  2949 QVQAQNLALREFEHTPLAD------IQRWAGQggEALFDSILVFENYPiSEALKQGaPSGLRFGAVSsREQTNYPLTLAV 3022

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1420 TEHDSeLFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEeRDFIESCHLFEETGYSMNQTLHYA 1499
Cdd:PRK12467  3023 GLGDT-LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHE-RRQVLHAWNATAAAYPSERLVHQL 3100

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PRK12467  3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSAGL-HVPEFTGEIVYLNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHR 1658
Cdd:PRK12467  3181 RERLAYMIEDSGVKLLLTQAHLLeQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG 3260

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1659 SAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPqGGEKEPEVIAKAIEEQKITAMHFVPSMLH 1738
Cdd:PRK12467  3261 ALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQ 3339

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1739 AFLEHIKYRSVPiktnRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKLE--RIPIGKPV 1816
Cdd:PRK12467  3340 QFAEDAGGADCA----SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEapYAPIGRPV 3415

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1817 HHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDD 1895
Cdd:PRK12467  3416 AGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDH 3495

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1896 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQW 1970
Cdd:PRK12467  3496 QVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVvpadpQGDWRETLRDHLAASLPDYMVPAQLLVLAAM 3575

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1971 PVTPSGKLDRNALPAPgGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQV 2050
Cdd:PRK12467  3576 PLGPNGKVDRKALPDP-DAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKL 3654

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2051 PLKDVFAHPTVEGLATVIREGTdspyeaikpaekqetypvssaqkriyvlqqledggtgynmpavLELEGKLNPERMDRA 2130
Cdd:PRK12467  3655 SLRDLMSAPTIAELAGYSPLGD-------------------------------------------VPVNLLLDLNRLETG 3691

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2131 FQELIKRHESLRTSFEqdegGDPVQRIhdevpftlqttvlgarteqeaaaafikpfdlsqaplfraqivkVSDERHLLLV 2210
Cdd:PRK12467  3692 FPALFCRHEGLGTVFD----YEPLAVI-------------------------------------------LEGDRHVLGL 3724

                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 2211 DMHHIISDGvsvniliqefgelYNNRKLPALRIQYKDYAVWQE 2253
Cdd:PRK12467  3725 TCRHLLDDG-------------WQDTSLQAMAVQYADYILWQQ 3754
PRK12316 PRK12316
peptide synthase; Provisional
 4-1030 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 715.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    4 ANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGkVNPQFFQNSINALVERHDIFRTIFISQ-NVSSPQQVVLR 82
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQgELGRPLQVVHK 4174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   83 ERNVIVLEEDITHLNEAEQSqfIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLH 162
Cdd:PRK12316  4175 QVSLPFAELDWRGRADLQAA--LDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLE 4252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  163 IYASYVNAspitlEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVL----PKQKKTKGKSRQEHVTfSFSKEESS 238
Cdd:PRK12316  4253 RYSGRPPA-----QPGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLaqaiARADLRSANGYGEHVR-ELDATATA 4326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  239 RLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDM 317
Cdd:PRK12316  4327 RLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATpRAQQSVVEWLQQV 4406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  318 QKDRLAAEAYSYHPLYEIQsRSAVKQG--LIDHILVFENYPVQQEIQmlnkQEHASDLfQIHNFTVADETNYSFYLMVAP 395
Cdd:PRK12316  4407 QRQNLALREHEHTPLYEIQ-RWAGQGGeaLFDSLLVFENYPVSEALQ----QGAPGGL-RFGEVTNHEQTNYPLTLAVGL 4480

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  396 GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITtDTEKRQLIGEITDQT----PVYETIHAMFEK 471
Cdd:PRK12316  4481 GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLL-EKAEQQRIVALWNRTdagyPATRCVHQLVAE 4559

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  472 QAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADR 551
Cdd:PRK12316  4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  552 IRYILHDCGCSHVVSQAHLPSSLE-----DNYIITHPEDIESKVDgSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:PRK12316  4640 LAYMMEDSGAALLLTQSHLLQRLPipdglASLALDRDEDWEGFPA-HDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 MANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIkRDVPQLFAFINKHQTNIVFLPTAFIKM 706
Cdd:PRK12316  4719 LVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVYLQQ 4797

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IFSERELANSFPDgVKHLIAAGEQLMiSDLFQDVLRK-RGIHLHNHYGPSETHV-VSTYTIHPGDP-IPELPPIGKPIGC 783
Cdd:PRK12316  4798 LAEHAERDGEPPS-LRVYCFGGEAVA-QASYDLAWRAlKPVYLFNGYGPTETTVtVLLWKARDGDAcGAAYMPIGTPLGN 4875

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDVIMYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:PRK12316  4876 RSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQV 4955

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAaILIWQDQNGEHELCAY----------YCSVQKLNTIDLRSYMASELPEYMIPAK 932
Cdd:PRK12316  4956 KIRGFRIELGEIEARLREHPAVREA-VVIAQEGAVGKQLVGYvvpqdpaladADEAQAELRDELKAALRERLPEYMVPAH 5034

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  933 WIWVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIA 1012
Cdd:PRK12316  5035 LVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQ 5114

                         1050
                   ....*....|....*...
gi 1678550997 1013 KEFHVQVSLKDIFAHPTV 1030
Cdd:PRK12316  5115 LELGLELPLRELFQTPTL 5132
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1058-2073 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 689.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGaDDEPVQRIHTEVPFT---- 1132
Cdd:PRK10252     9 PLVAAQPGIWMAEKLSpLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQWVDPALTFPlpei 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1133 --LSKETTIEGFVRPF---DLSQA-------PLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQ--- 1197
Cdd:PRK10252    88 idLRTQPDPHAAAQALmqaDLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLrge 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1198 ------LKPLRIQYKDYAVWQQkfkkGDSYQKQETYWQQQFSGDLPILEL---PTDKRRPAERqFIggKVTFQLDKEITA 1268
Cdd:PRK10252   168 ptpaspFTPFADVVEEYQRYRA----SEAWQRDAAFWAEQRRQLPPPASLspaPLPGRSASAD-IL--RLKLEFTDGAFR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1269 RIKRLAHKNRstLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQ 1348
Cdd:PRK10252   241 QLAAQASGVQ--RPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1349 TALEAYEHQDYPFEELVDKLGvqREMSRNPLFDTTLVLQNMEQQkLKMNDVQLQWNDLEH-PISKFDISLYVTEhDSELF 1427
Cdd:PRK10252   319 QLKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDYQ-LDFPGVQAQTHTLATgPVNDLELALFPDE-HGGLS 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1428 CQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEerdfIESCHLFEETGYSM-NQTLHYALEQQAEK 1506
Cdd:PRK10252   395 IEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGE----YAQLAQVNATAVEIpETTLSALVAQQAAK 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1507 TPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFL 1586
Cdd:PRK10252   471 TPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1587 LEDSgTNILLLQSAGLhVPEFTG-EIVYLNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLN 1665
Cdd:PRK10252   551 LEDA-RPSLLITTADQ-LPRFADvPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1666 SLQSRYQLKHSDMIMHKTSYSFDASIWElFWWPY-AGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHI 1744
Cdd:PRK10252   629 WMQNHYPLTADDVVLQKTPCSFDVSVWE-FFWPFiAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASL 707

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1745 KYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAFFDCPPHEKLER----IPIGKPVHHVR 1820
Cdd:PRK10252   708 TPEGARQSCASLRQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYPAFGEELAAVrgssVPIGYPVWNTG 786

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1821 LYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIR 1900
Cdd:PRK10252   787 LRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIR 866

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1901 GYRIEPGEIEAALRSIEGVREAAV-------TVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEME 1968
Cdd:PRK10252   867 GQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLvsqsgLPLDTSALQAQLRERLPPHMVPVVLLQLD 946

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1969 QWPVTPSGKLDRNALPAPGGAADAETyTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDV 2048
Cdd:PRK10252   947 QLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFAR 1025

                         1050      1060
                   ....*....|....*....|....*
gi 1678550997 2049 QVPLKDVFAHPTVEGLATVIREGTD 2073
Cdd:PRK10252  1026 QVTPGQVMVASTVAKLATLLDAEED 1050
PRK12316 PRK12316
peptide synthase; Provisional
 2081-3101 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 687.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2081 PAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGkLNPERMDRAFQELIKRHESLRTSF-EQDEGGDPVQRIHD 2159
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRPLQVVHK 4174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2160 --EVPFTLQ----TTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELY 2233
Cdd:PRK12316  4175 qvSLPFAELdwrgRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2234 NNRKLPALRIQYKDYAVWqegFKTGDAyKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAG-DKVSFTLEPEVASGLHK 2312
Cdd:PRK12316  4255 SGRPPAQPGGRYRDYIAW---LQRQDA-AASEAFWREQLAALDEPTRLAQAIARADLRSANGyGEHVRELDATATARLRE 4330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2313 LARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 2390
Cdd:PRK12316  4331 FARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQN 4410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2391 LEAFEHQNYPFEELvdklELTRDMSRNPVFDAMLVVQNNdyePLHLHDLQMKPAQV------SHLVSKFDLTLQASEGDg 2464
Cdd:PRK12316  4411 LALREHEHTPLYEI----QRWAGQGGEALFDSLLVFENY---PVSEALQQGAPGGLrfgevtNHEQTNYPLTLAVGLGE- 4482

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2465 NIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNEFNTGQANQYGVQTISQLFEQQAA 2544
Cdd:PRK12316  4483 TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERAR 4562

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2545 RTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRY 2624
Cdd:PRK12316  4563 MTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY 4642

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2625 ILSDSGTKLLMTINEAdLGVLADFEG-EILTIESVEEDDKSPL--PQMS-SAHHLAYIIYTSGTTGRPKGVMVEHKGIAN 2700
Cdd:PRK12316  4643 MMEDSGAALLLTQSHL-LQRLPIPDGlASLALDRDEDWEGFPAhdPAVRlHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN 4721

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2701 TLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAkAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALL- 2779
Cdd:PRK12316  4722 HLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGA-SVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAe 4800

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2780 DVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMR----HMEKQAYVSIGQPIDGTQVLI 2855
Cdd:PRK12316  4801 HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKardgDACGAAYMPIGTPLGNRSGYV 4880

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2856 LNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGY 2934
Cdd:PRK12316  4881 LDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGF 4960

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2935 RVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVV--TKPGLSTNAVRSELQNKL--------PVFMHPAFIEKLD 3004
Cdd:PRK12316  4961 RIELGEIEARLREHPAVREAVVIAQEGAVGK-QLVGYVVpqDPALADADEAQAELRDELkaalrerlPEYMVPAHLVFLA 5039

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3005 SLPLSPNGKLDRGALPKPVYNHEgERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELGGDSIKALQVSARLH-RIG 3083
Cdd:PRK12316  5040 RMPLTPNGKLDRKALPQPDASLL-QQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQlELG 5118

                         1050
                   ....*....|....*...
gi 1678550997 3084 KQMAVKDLFSHPTIQELA 3101
Cdd:PRK12316  5119 LELPLRELFQTPTLAAFV 5136
PRK12316 PRK12316
peptide synthase; Provisional
 12-1535 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 677.83  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLrERNVIVLEE 91
Cdd:PRK12316    51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPL-DRPLEVEFE 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   92 DITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNAS 171
Cdd:PRK12316   130 DCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGA 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  172 PITLE--PVQpYGKYI----KWLMEQDKEQAVSYWDHYLSghEQQTVL--------PKQKKTKGKSRQehvtFSFSKEES 237
Cdd:PRK12316   210 EPGLPalPIQ-YADYAlwqrSWLEAGEQERQLEYWRAQLG--EEHPVLelptdhprPAVPSYRGSRYE----FSIDPALA 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  238 SRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRP-AEIEGiehMVGLFINTMPVRVQ-GAKTPFLQLIK 315
Cdd:PRK12316   283 EALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNrAEVEG---LIGFFVNTQVLRSVfDGRTRVATLLA 359

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  316 DMQKDRLAAEAYSYHPLYEIQSRSAVKQGLiDHILVFEnypvqqeiQMLNKQEHASD---LFQIHNFTVAD------ETN 386
Cdd:PRK12316   360 GVKDTVLGAQAHQDLPFERLVEALKVERSL-SHSPLFQ--------VMYNHQPLVADieaLDTVAGLEFGQlewksrTTQ 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  387 YSFYL-MVAPGEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLI---GEITDQTPVY 462
Cdd:PRK12316   431 FDLTLdTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVegwNATAAEYPLQ 510

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVP 542
Cdd:PRK12316   511 RGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  543 VDPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHP--EDIESKVDG---SNIKSVNNADDLLYMIYTSGTTGKP 617
Cdd:PRK12316   591 LDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLdlDRPAAWLEGyseENPGTELNPENLAYVIYTSGSTGKP 670

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  618 KGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIV 697
Cdd:PRK12316   671 KGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTL 750

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  698 FLPTAFIKMIFSERELANSFPdgVKHLIAAGEQLMiSDLFQDVLRKRGI-HLHNHYGPSETHVVSTYTIHPgDPIPELPP 776
Cdd:PRK12316   751 HFVPSMLQAFLQDEDVASCTS--LRRIVCSGEALP-ADAQEQVFAKLPQaGLYNLYGPTEAAIDVTHWTCV-EEGGDSVP 826

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  777 IGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIG 856
Cdd:PRK12316   827 IGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAG 906

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  857 RADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIwqdQNGEhELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKWI 934
Cdd:PRK12316   907 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGK-QLVGYVVleSEGGDWREALKAHLAASLPEYMVPAQWL 982

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  935 WVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRiAKE 1014
Cdd:PRK12316   983 ALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQ 1061

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1015 FHVQVSLKDIFAHPTVEGLALIIREAEQnlyAAIEPAEKRDTYPVSSAQKRIYVlQQLDEGVAYNMPAVLELEGALDVAK 1094
Cdd:PRK12316  1062 AGIQLSPRDLFQHQTIRSLALVAKAGQA---TAADQGPASGEVALAPVQRWFFE-QAIPQRQHWNQSLLLQARQPLDPDR 1137

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1095 LSAVCKELISRHEPLRTSFVSGAD-----------DEPVQRIHTEVPFTLskETTIEGFVRPFDLSQAPLFRAGLIEVSN 1163
Cdd:PRK12316  1138 LGRALERLVAHHDALRLRFREEDGgwqqayaapqaGEVLWQRQAASEEEL--LALCEEAQRSLDLEQGPLLRALLVDMAD 1215

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1164 EKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKpLRIQYKDYAVWQQKFKK-GDSYQKQETYWQQQFsGDLPiLELP 1242
Cdd:PRK12316  1216 GSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDAD-LPARTSSYQAWARRLHEhAGARAEELDYWQAQL-EDAP-HELP 1292

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1243 TDKRRPAERQFIGGKVTFQLDKEITARIKRLA-HKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPH----ADLE 1317
Cdd:PRK12316  1293 CENPDGALENRHERKLELRLDAERTRQLLQEApAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDlfedIDLS 1372

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1318 AVLGMFVNTLALRTRPAGNktFEEFLKEVRQTaLEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMN 1397
Cdd:PRK12316  1373 RTVGWFTSLFPVRLTPAAD--LGESIKAIKEQ-LRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNYLGQFDRQFD 1449

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1398 DVQL---------QWNDLEHPISKFdISLYVTEHDSELFCQFEYSTALFEKETIQRWASLFT----TLVEHTAASP---- 1460
Cdd:PRK12316  1450 EAALfvpatesagAAQDPCAPLANW-LSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYArelqALIEHCCDERnrgv 1528

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1461 -----------ETELDNIPILTKEEERDFIESchlfeetgySMNQTL--HYALEQQAEKTPDQAAVIFEDgvmtykeLNE 1527
Cdd:PRK12316  1529 tpsdfplaglsQAQLDALPLPAGEIADIYPLS---------PMQQGMlfHSLYEQEAGDYINQLRVDVQG-------LDP 1592


                   ....*...
gi 1678550997 1528 QANRIAWE 1535
Cdd:PRK12316  1593 DRFRAAWQ 1600
PRK12316 PRK12316
peptide synthase; Provisional
 12-1460 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 668.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNVIVLEE 91
Cdd:PRK12316  2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLED 2683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   92 DITHLNEAeqsqfIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNAS 171
Cdd:PRK12316  2684 CAGVADAA-----IRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGE 2758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  172 PITLEPVQ-PYGKYIKWLME----QDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKS--RQEHVTFSFSKEESSRLSELA 244
Cdd:PRK12316  2759 QPTLPPLPlQYADYAAWQRAwmdsGEGARQLDYWRERLGGEQPVLELPLDRPRPALQshRGARLDVALDVALSRELLALA 2838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  245 AREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRpaEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDMQKDRLA 323
Cdd:PRK12316  2839 RREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFVNTQVLRAQvDAQLAFRDLLGQVKEQALG 2916

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  324 AEAYSYHPLYEIQS-----RSAVKQGLIDHILVFENYPVQQeiqmlnKQEHASDLFQIHNFTVADETNYSFYLMVAPgEE 398
Cdd:PRK12316  2917 AQAHQDLPFEQLVEalqpeRSLSHSPLFQVMYNHQSGERAA------AQLPGLHIESFAWDGAATQFDLALDTWESA-EG 2989

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  399 IHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLIGEITDQTPVYET---IHAMFEKQAEK 475
Cdd:PRK12316  2990 LGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLergVHRLFEEQVER 3069

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  476 TPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYI 555
Cdd:PRK12316  3070 TPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYM 3149

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 LHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEY 635
Cdd:PRK12316  3150 LEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  636 THSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNivfLPTAFIKMIFSERELAN 715
Cdd:PRK12316  3230 QAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD---VLHAYPSMLQAFLEEED 3306

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 SFPDGVKHLIAAGEQLMISDLFQDVLrkRGIHLHNHYGPSETHVVSTyTIHPGDPIPELPPIGKPIGCTDLYILNHQKQL 795
Cdd:PRK12316  3307 AHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVT-HWQCVEEGKDAVPIGRPIANRACYILDGSLEP 3383

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  796 QPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:PRK12316  3384 VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE 3463

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  876 VTLMNHPDISEAAILiwqDQNGEhELCAYYCSVQKLNTI--DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:PRK12316  3464 ARLLEHPWVREAVVL---AVDGR-QLVAYVVPEDEAGDLreALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP 3539

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  954 EPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRiAKEFHVQVSLKDIFAHPTVEGL 1033
Cdd:PRK12316  3540 RPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSR-ARQAGIRFTPKDLFQHQTIQGL 3618

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1034 ALIIReaeqnlyaaIEPAEKRDTYPVSSAQKRIYVLQQ-LDEGVA----YNMPAVLELEGALDVAKLSAVCKELISRHEP 1108
Cdd:PRK12316  3619 ARVAR---------VGGGVAVDQGPVSGETLLLPIQQQfFEEPVPerhhWNQSLLLKPREALDAAALEAALQALVEHHDA 3689

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1109 LRTSFVSGADDEPVQRIHTEVPFTL----------SKETTIEGFVRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISD 1178
Cdd:PRK12316  3690 LRLRFVEDAGGWTAEHLPVELGGALlwraelddaeELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVD 3769

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1179 GVSVQLLIREFTDLYANR------QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPilELPTDKRRPAERQ 1252
Cdd:PRK12316  3770 GVSWRILLEDLQQAYQQLlqgeapRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSS--ELPCDHPQGALQN 3847

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1253 FIGGKVTFQLDKEITARIKRLA-HKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPH----ADLEAVLGMFVNTL 1327
Cdd:PRK12316  3848 RHAASVQTRLDRELTRRLLQQApAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfadIDLSRTVGWFTSLF 3927

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1328 ALRTRPAGN-----KTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGV--QREMSRNPL--FDTTLvlqNMEQQKL-KMN 1397
Cdd:PRK12316  3928 PVRLSPVEDlgasiKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGlpVPRITFNYLgqFDGSF---DEEMALFvPAG 4004

                         1450      1460      1470      1480      1490      1500
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1398 DVQLQWNDLEHPISKFdISLYVTEHDSELFCQFEYSTALFEKETIQR----WASLFTTLVEHTAASP 1460
Cdd:PRK12316  4005 ESAGAEQSPDAPLDNW-LSLNGRVYGGELSLDWTFSREMFEEATIQRladdYAAELTALVEHCCDAE 4070
PRK12467 PRK12467
peptide synthase; Provisional
 2078-3112 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 650.69  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2078 AIKPAEKQETYPVSSAQKRIyVLQQLEDGGTG-YNMPAVLELEGkLNPERMDRAFQELIKRHESLRTSF-EQDEGGDPVQ 2155
Cdd:PRK12467  2637 PVAVGDIEDIYPLSPMQQGM-LFHTLYEGGAGdYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEEPLQ 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2156 RIHD--EVPFTLQTTVLGARTEQE----AAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEF 2229
Cdd:PRK12467  2715 VVYKqaRLPFSRLDWRDRADLEQAldalAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEV 2794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2230 GELYNNRKLPALRIQYKDYAVWqegFKTGDAyKMQEAYWLKQL----EGELPVLDLPADHARPpvRSFAGDKvSFTLEPE 2305
Cdd:PRK12467  2795 LQRYFGQPPPAREGRYRDYIAW---LQAQDA-EASEAFWKEQLaaleEPTRLARALYPAPAEA--VAGHGAH-YLHLDAT 2867

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2306 VASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYL 2383
Cdd:PRK12467  2868 QTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlRGAEQQLGLFINTLPVIASPRAEQTVSDWL 2947

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2384 QEVRETALEAFEHQNYPFeelvdkLELTRDMSR--NPVFDAMLVVQNndYePLHLHDLQMKPAQV------SHLVSKFDL 2455
Cdd:PRK12467  2948 QQVQAQNLALREFEHTPL------ADIQRWAGQggEALFDSILVFEN--Y-PISEALKQGAPSGLrfgavsSREQTNYPL 3018

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2456 TLQASEGDG-NIHFLfeYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNEFNTGQANQYGVQT 2534
Cdd:PRK12467  3019 TLAVGLGDTlELEFS--YDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERL 3096

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:PRK12467  3097 VHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLD 3176

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMTINE--ADLGVLADfeGEILTIESVEEDDKSP-LPQMSS-AHHLAYIIYTSGTTGRPKG 2690
Cdd:PRK12467  3177 PEYPRERLAYMIEDSGVKLLLTQAHllEQLPAPAG--DTALTLDRLDLNGYSEnNPSTRVmGENLAYVIYTSGSTGKPKG 3254

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2691 VMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAkAVLLHEEEAKDILAIKHQLSRQRITHMII 2770
Cdd:PRK12467  3255 VGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGG-CLVVRDNDLWDPEELWQAIHAHRISIACF 3333

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2771 VPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVA----TTVMRHMEKQAYVSIGQ 2846
Cdd:PRK12467  3334 PPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTvtlwKCGGDAVCEAPYAPIGR 3413

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2847 PIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEA-RMYRTGDAARWMADGTLEYLGRI 2925
Cdd:PRK12467  3414 PVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGgRLYRTGDLARYRADGVIEYLGRI 3493

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2926 DDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVVTK--PGLSTNAVRSELQNKLPVFMHPAFIEKL 3003
Cdd:PRK12467  3494 DHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGK-QLVAYVVPAdpQGDWRETLRDHLAASLPDYMVPAQLLVL 3572

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3004 DSLPLSPNGKLDRGALPKPvyNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELGGDSIKALQVSARLHR-I 3082
Cdd:PRK12467  3573 AAMPLGPNGKVDRKALPDP--DAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQsL 3650

                         1050      1060      1070
                   ....*....|....*....|....*....|
gi 1678550997 3083 GKQMAVKDLFSHPTIQELAAYIRDSDTSSS 3112
Cdd:PRK12467  3651 GLKLSLRDLMSAPTIAELAGYSPLGDVPVN 3680
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1508-1983 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: 644.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd05930     81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYR 1747
Cdd:cd05930    126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1748 SVPiktnRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPP-HEKLERIPIGKPVHHVRLYLLNQ 1826
Cdd:cd05930    206 ALP----SLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPdDEEDGRVPIGRPIPNTRVYVLDE 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1827 NQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 1906
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1907 GEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd05930    362 GEIEAALLAHPGVREAAVVAREDgDGEKRLVAYVvpdegGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441


                   ...
gi 1678550997 1981 NAL 1983
Cdd:cd05930    442 KAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 2547-3019 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: 637.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRR 2706
Cdd:cd05930     81 EDSGAKLVLT----------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2707 NAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQPED 2786
Cdd:cd05930    127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2787 VKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMR---HMEKQAYVSIGQPIDGTQVLILNSNHQLQ 2863
Cdd:cd05930    207 LPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRvppDDEEDGRVPIGRPIPNTRVYVLDENLRPV 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2864 PIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIES 2943
Cdd:cd05930    287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2944 VIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05930    367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGgeLDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2089-3118 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 623.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2089 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPF-TLQT 2167
Cdd:PRK10252     9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGE-VWQWVDPALTFpLPEI 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2168 TVLGARTEQEAAAAFIKPFDLSQA-------PLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRK--- 2237
Cdd:PRK10252    88 IDLRTQPDPHAAAQALMQADLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLrge 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2238 ------LPALRIQYKDYAVWQEGfktgDAYKMQEAYWLKQLEGELPVLDLPAdhARPPVRSFAGDKVSFTLEPEVASGLH 2311
Cdd:PRK10252   168 ptpaspFTPFADVVEEYQRYRAS----EAWQRDAAFWAEQRRQLPPPASLSP--APLPGRSASADILRLKLEFTDGAFRQ 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2312 KLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETAL 2391
Cdd:PRK10252   242 LAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLK 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2392 EAFEHQNYPFEELVdkleltRDMSR----NPVFDAMLVVQNNDYePLHLHDLQmkpAQVSHLVSK--FDLTLQAS-EGDG 2464
Cdd:PRK10252   322 KMRRHQRYDAEQIV------RDSGRaagdEPLFGPVLNIKVFDY-QLDFPGVQ---AQTHTLATGpvNDLELALFpDEHG 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2465 NIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEErHQLLNEFNtgqANQYGV--QTISQLFEQQ 2542
Cdd:PRK10252   392 GLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGE-YAQLAQVN---ATAVEIpeTTLSALVAQQ 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERK 2622
Cdd:PRK10252   468 AAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 RYILSDSGTKLLMTiNEADLGVLADFEG-EILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANT 2701
Cdd:PRK10252   548 KMMLEDARPSLLIT-TADQLPRFADVPDlTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNR 626

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2702 LQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDV 2781
Cdd:PRK10252   627 LLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVAS 706

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2782 VQPED----VKTLRVVTLAGEAADRELIAR--SLAicpHTELANEYGPTENSV------ATTVMRHMEKQAYVSIGQPID 2849
Cdd:PRK10252   707 LTPEGarqsCASLRQVFCSGEALPADLCREwqQLT---GAPLHNLYGPTEAAVdvswypAFGEELAAVRGSSVPIGYPVW 783

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2850 GTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQV 2929
Cdd:PRK10252   784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2930 KIRGYRVETKEIESVIRCIKGVKDAAVVAHV------TASGQTELSAYVVTKPGLS--TNAVRSELQNKLPVFMHPAFIE 3001
Cdd:PRK10252   864 KIRGQRIELGEIDRAMQALPDVEQAVTHACVinqaaaTGGDARQLVGYLVSQSGLPldTSALQAQLRERLPPHMVPVVLL 943

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3002 KLDSLPLSPNGKLDRGALPKPvyNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELGGDSIKALQVSARLHR 3081
Cdd:PRK10252   944 QLDQLPLSANGKLDRKALPLP--ELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSR 1021

                         1050      1060      1070
                   ....*....|....*....|....*....|....*...
gi 1678550997 3082 I-GKQMAVKDLFSHPTIQELAAYIrdsDTSSSQAAVEG 3118
Cdd:PRK10252  1022 QfARQVTPGQVMVASTVAKLATLL---DAEEDESRRLG 1056
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 10-433 0e+00

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: 621.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNVIVL 89
Cdd:cd19543      1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 EEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVN 169
Cdd:cd19543     81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 ASPITLEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKS--RQEHVTFSFSKEESSRLSELAARE 247
Cdd:cd19543    161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGsyEPGEVSFELSAELTARLQELARQH 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  248 EVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQGAK-TPFLQLIKDMQKDRLAAEA 326
Cdd:cd19543    241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPdQTVLELLKDLQAQQLELRE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  327 YSYHPLYEIQSRSAVKQGLIDHILVFENYPVQQEIQMlnkqEHASDLFQIHNFTVADETNYSFYLMVAPGEEIHIKMNYD 406
Cdd:cd19543    321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEE----EQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYD 396

                          410       420
                   ....*....|....*....|....*..
gi 1678550997  407 AEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19543    397 AEVFDEATIERLLGHLRRVLEQVAANP 423
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 2087-2500 0e+00

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: 599.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2087 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPFTLQ 2166
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGE-PVQVILPPLPLPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2167 TTVLGARTE-------QEAAAAFI-KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR-- 2236
Cdd:cd19531     80 VVDLSGLPEaereaeaQRLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFla 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2237 ----KLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHK 2312
Cdd:cd19531    160 grpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2313 LARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALE 2392
Cdd:cd19531    240 LARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2393 AFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQASEGDGNIHFLFEY 2472
Cdd:cd19531    320 AYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEY 399

                          410       420
                   ....*....|....*....|....*...
gi 1678550997 2473 STALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19531    400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1497-1983 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: 592.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1497 HYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDP 1576
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1577 DYPEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSGlAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIE 1656
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALA-APPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1657 HRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSM 1736
Cdd:cd17646    160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1737 LHAFLEHIKYRSVPiktnRLKRVFSGGEQLGTHLVSRFYELlPNVSITNSYGPTEATVEAAFFDCPPHEKLERIPIGKPV 1816
Cdd:cd17646    240 LRVFLAEPAAGSCA----SLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPV 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1817 HHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQ 1896
Cdd:cd17646    315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1897 VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV------EGLQRNEVRAQLERLLPGYMVPAYMIEMEQ 1969
Cdd:cd17646    395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApAGAARLVGYVvpaagaAGPDTAALRAHLAERLPEYMVPAAFVVLDA 474

                          490
                   ....*....|....
gi 1678550997 1970 WPVTPSGKLDRNAL 1983
Cdd:cd17646    475 LPLTANGKLDRAAL 488
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1501-1986 0e+00

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: 590.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1501 EQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPE 1580
Cdd:cd17655      4 EEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1581 ERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSGLAHRlSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSA 1660
Cdd:cd17655     84 ERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEES-ENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGV 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1661 VNFLNSLQSR-YQLKHSDMIMHkTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITamhfVPSMLHA 1739
Cdd:cd17655    163 VNLVEWANKViYQGEHLRVALF-ASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRIT----IIDLTPA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1740 FLEHIKYRSVPIKTNrLKRVFSGGEQLGTHLVSRFYELL-PNVSITNSYGPTEATVEAAFFDC-PPHEKLERIPIGKPVH 1817
Cdd:cd17655    238 HLKLLDAADDSEGLS-LKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYePETDQQVSVPIGKPLG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1818 HVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQV 1897
Cdd:cd17655    317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1898 KIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVT 1973
Cdd:cd17655    397 KIRGYRIELGEIEARLLQHPDIKEAVVIARKDeQGQNYLCAYIvseKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476

                          490
                   ....*....|...
gi 1678550997 1974 PSGKLDRNALPAP 1986
Cdd:cd17655    477 PNGKVDRKALPEP 489
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1056-1460 0e+00

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: 580.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1056 TYPVSSAQKRIYVLQQLDEG-VAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTLS 1134
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGsAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE-VDGEPVQVILPPLPLPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1135 -----------KETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR-- 1196
Cdd:cd19531     80 vvdlsglpeaeREAEAQRLAreearRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFla 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 ----QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKR 1272
Cdd:cd19531    160 grpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1273 LAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALE 1352
Cdd:cd19531    240 LARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1353 AYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQFEY 1432
Cdd:cd19531    320 AYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEY 399

                          410       420
                   ....*....|....*....|....*...
gi 1678550997 1433 STALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19531    400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 477-952 1.66e-179

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: 559.45  E-value: 1.66e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVSQAhlpsslednyiithpedieskvdgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYT 636
Cdd:cd05930     81 EDSGAKLVLTDP---------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANs 716
Cdd:cd05930    128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA- 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  717 fPDGVKHLIAAGEQLMiSDLFQDVLRK-RGIHLHNHYGPSETHVVST-YTIHPGDPIPELPPIGKPIGCTDLYILNHQKQ 794
Cdd:cd05930    207 -LPSLRLVLVGGEALP-PDLVRRWRELlPGARLVNLYGPTEATVDATyYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLR 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  795 LQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEI 874
Cdd:cd05930    285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  875 EVTLMNHPDISEAAILIWQDQNGEHELCAYY--CSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05930    365 EAALLAHPGVREAAVVAREDGDGEKRLVAYVvpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 468-956 8.49e-178

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: 556.56  E-value: 8.49e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  468 MFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHY 547
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  548 PADRIRYILHDCGCSHVVSQAHLPSSLEDNYIIT--HPEDIESKvDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHR 625
Cdd:cd17655     82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDllDEDTIYHE-ESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  626 NMANLLKFeYTHSGIDFEAD-VLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFI 704
Cdd:cd17655    161 GVVNLVEW-ANKVIYQGEHLrVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  705 KMIFSERELANSfpdGVKHLIAAGEQL------MISDLFQDvlrkrGIHLHNHYGPSETHV-VSTYTIHPGDPIPELPPI 777
Cdd:cd17655    240 KLLDAADDSEGL---SLKHLIVGGEALstelakKIIELFGT-----NPTITNAYGPTETTVdASIYQYEPETDQQVSVPI 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  778 GKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGR 857
Cdd:cd17655    312 GKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  858 ADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVD 937
Cdd:cd17655    392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLD 471

                          490
                   ....*....|....*....
gi 1678550997  938 SIPLTPNGKVDRAALPEPD 956
Cdd:cd17655    472 EIPLTPNGKVDRKALPEPD 490
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 2537-3022 1.35e-177

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: 555.79  E-value: 1.35e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2537 QLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPE 2616
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2617 YPKERKRYILSDSGTKLLMTinEADLGVLADFEGEILTIE--SVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVE 2694
Cdd:cd17655     81 YPEERIQYILEDSGADILLT--QSHLQPPIAFIGLIDLLDedTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPvl 2774
Cdd:cd17655    159 HRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTP-- 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2775 yrALLDVVQPEDVKT---LRVVTLAGEAADRELIARSLAICPHT-ELANEYGPTENSVATTVMRHME---KQAYVSIGQP 2847
Cdd:cd17655    237 --AHLKLLDAADDSEglsLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVDASIYQYEPetdQQVSVPIGKP 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2848 IDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDD 2927
Cdd:cd17655    315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDH 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2928 QVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLP 3007
Cdd:cd17655    395 QVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIP 474

                          490
                   ....*....|....*
gi 1678550997 3008 LSPNGKLDRGALPKP 3022
Cdd:cd17655    475 LTPNGKVDRKALPEP 489
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 3119-3570 1.84e-174

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: 544.15  E-value: 1.84e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3119 DVQWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEqGKWDQYNRPLshsDDALY 3198
Cdd:cd19534      1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRED-GGWQQRIRGD---VEELF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3199 GLQMIDLSApdgtdgnRPYEPLIKRHVLDIQQKMDLKNGPLLQAGLFH-TIDGDFLFLSAHHLVVDGISWRVLLEDLALG 3277
Cdd:cd19534     77 RLEVVDLSS-------LAQAAAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3278 YRQAAGGEDIKLPPKTSsFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIdgtrAHEGQRSTISFTLNDKET 3357
Cdd:cd19534    150 YEQALAGEPIPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPE----QTYGDARTVSFTLDEEET 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3358 AALLKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTAIYPLLIKlnadlPDSEE 3437
Cdd:cd19534    225 EALLQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLD-----LEASE 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3438 SMVHVLKTTKDTLRRVPDKGFGYGVIKYLTPPGKKDINFTGAPEISFNYLGQFESGRTaevpeEDAFSFSPLGAGG-DIS 3516
Cdd:cd19534    300 DLGDTLKRVKEQLRRIPNKGIGYGILRYLTPEGTKRLAFHPQPEISFNYLGQFDQGER-----DDALFVSAVGGGGsDIG 374

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 3517 TTWNREQSLDISAIAAEGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHC 3570
Cdd:cd19534    375 PDTPRFALLDINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 2537-3019 2.68e-174

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: 546.03  E-value: 2.68e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2537 QLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPE 2616
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2617 YPKERKRYILSDSGTKLLMTiNEADLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHK 2696
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLT-DRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2697 GIAnTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYR 2776
Cdd:cd12117    160 GVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFN 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2777 ALLDVVqPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATT---VMRHMEKQAYVSIGQPIDGTQV 2853
Cdd:cd12117    239 QLADED-PECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTshvVTELDEVAGSIPIGRPIANTRV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2854 LILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRG 2933
Cdd:cd12117    318 YVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRG 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2934 YRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGK 3013
Cdd:cd12117    398 FRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGK 477


                   ....*.
gi 1678550997 3014 LDRGAL 3019
Cdd:cd12117    478 VDRRAL 483
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 469-953 2.29e-171

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: 538.08  E-value: 2.29e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSV--NNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDpaLDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 MANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKM 706
Cdd:cd17651    161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IFSERELANSFPDGVKHLIAAGEQLMISDLFQDVLRKR-GIHLHNHYGPSETHVVSTYTIhPGDPI--PELPPIGKPIGC 783
Cdd:cd17651    241 LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLpGLRLHNHYGPTETHVVTALSL-PGDPAawPAPPPIGRPIDN 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVK 863
Cdd:cd17651    320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  864 IRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQ--KLNTIDLRSYMASELPEYMIPAKWIWVDSIPL 941
Cdd:cd17651    400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPeaPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479

                          490
                   ....*....|..
gi 1678550997  942 TPNGKVDRAALP 953
Cdd:cd17651    480 TPNGKLDRRALP 491
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1501-1983 3.77e-169

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: 531.39  E-value: 3.77e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1501 EQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPE 1580
Cdd:cd12117      4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1581 ERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSglAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSA 1660
Cdd:cd12117     84 ERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALD--AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1661 VNFLnsLQSRY-QLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHA 1739
Cdd:cd12117    162 VRLV--KNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1740 FLEHikyrsVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKLER-IPIGKPVHH 1818
Cdd:cd12117    240 LADE-----DPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGsIPIGRPIAN 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1819 VRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVK 1898
Cdd:cd12117    315 TRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVK 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1899 IRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTP 1974
Cdd:cd12117    395 IRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLVAYVvaeGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTA 474


                   ....*....
gi 1678550997 1975 SGKLDRNAL 1983
Cdd:cd12117    475 NGKVDRRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 467-952 5.05e-168

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: 527.92  E-value: 5.05e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  467 AMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPH 546
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  547 YPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 MANLLKfeyTHSGIDFEAD--VLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFi 704
Cdd:cd12117    161 VVRLVK---NTNYVTLGPDdrVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL- 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  705 kmiFseRELANSFPD---GVKHLIAAGEQLMISdLFQDVLRKR-GIHLHNHYGPSETHVVST-YTIHPGDPIPELPPIGK 779
Cdd:cd12117    237 ---F--NQLADEDPEcfaGLRELLTGGEVVSPP-HVRRVLAACpGLRLVNGYGPTENTTFTTsHVVTELDEVAGSIPIGR 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  780 PIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRAD 859
Cdd:cd12117    311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRID 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  860 NQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSI 939
Cdd:cd12117    391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDEL 470

                          490
                   ....*....|...
gi 1678550997  940 PLTPNGKVDRAAL 952
Cdd:cd12117    471 PLTANGKVDRRAL 483
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1500-1984 1.14e-167

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: 527.30  E-value: 1.14e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSAglHVPEFTGEIVYLNQTNSGLAHRL--SNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEH 1657
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPA--LAGELAVELVAVTLLDQPGAAAGadAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1658 RSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELfwWPY--AGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPS 1735
Cdd:cd17651    159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEI--FSTlcAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTV 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1736 MLHAFLEHIKYRSVPIKtnRLKRVFSGGEQLG-THLVSRFYELLPNVSITNSYGPTEATVEAAF-FDCPPHEKLERIPIG 1813
Cdd:cd17651    237 ALRALAEHGRPLGVRLA--ALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVTALsLPGDPAAWPAPPPIG 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1814 KPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRT 1893
Cdd:cd17651    315 RPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRA 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1894 DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYVEGLQRN-----EVRAQLERLLPGYMVPAYMIEM 1967
Cdd:cd17651    395 DDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDrPGEKRLVAYVVGDPEApvdaaELRAALATHLPEYMVPSAFVLL 474

                          490
                   ....*....|....*..
gi 1678550997 1968 EQWPVTPSGKLDRNALP 1984
Cdd:cd17651    475 DALPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1521-1924 2.70e-166

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: 519.90  E-value: 2.70e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQS 1599
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 AGLH-VPEFTGEIVYLNQTNSGLAHRLSN---PNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKH 1675
Cdd:TIGR01733   81 ALASrLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1676 SDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEK-EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIkyrsvPIKTN 1754
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERdDAALLAALIAEHPVTVLNLTPSLLALLAAAL-----PPALA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1755 RLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHE--KLERIPIGKPVHHVRLYLLNQNQRMLP 1832
Cdd:TIGR01733  236 SLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDapRESPVPIGRPLANTRLYVLDDDLRPVP 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1833 VGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYP--GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIE 1910
Cdd:TIGR01733  316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395

                          410
                   ....*....|....
gi 1678550997 1911 AALRSIEGVREAAV 1924
Cdd:TIGR01733  396 AALLRHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 2084-2519 6.55e-165

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: 517.66  E-value: 6.55e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2084 KQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPF 2163
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2164 TLQTTVLG---ARTEQEAAAAFI-----KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELY-- 2233
Cdd:pfam00668   81 ELEIIDISdlsESEEEEAIEAFIqrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqq 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2234 --NNRKLPALRIQ-YKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGL 2310
Cdd:pfam00668  161 llKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2311 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 2390
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2391 LEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDY-----EPLHLHDLQMKPAQVSHLVSKFDLTLQASEGDGN 2465
Cdd:pfam00668  321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGqdsqeEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGG 400

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2466 IHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLL 2519
Cdd:pfam00668  401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 2560-2956 3.74e-162

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: 507.96  E-value: 3.74e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2560 TYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTIN 2638
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 EADLG----VLADFEGEILTIESVEEDDKSPLPQMSSAH-HLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNE 2713
Cdd:TIGR01733   81 ALASRlaglVLPVILLDPLELAALDDAPAPPPPDAPSGPdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2714 TDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQR-ITHMIIVPVLYRALLDvVQPEDVKTLRV 2792
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAA-ALPPALASLRL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2793 VTLAGEAADRELIARSLAICPHTELANEYGPTENSVATT---VMRHMEKQAY-VSIGQPIDGTQVLILNSNHQLQPIGVA 2868
Cdd:TIGR01733  240 VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTatlVDPDDAPRESpVPIGRPLANTRLYVLDDDLRPVPVGVV 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2869 GELCIAGTGLARGYVNLPELTERAFTQNPF--KPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIR 2946
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399

                          410
                   ....*....|
gi 1678550997 2947 CIKGVKDAAV 2956
Cdd:TIGR01733  400 RHPGVREAVV 409
PRK05691 PRK05691
peptide synthase; Validated
 4-1038 2.28e-161

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 565.95  E-value: 2.28e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    4 ANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFiSQNVSSPQ-QVVLR 82
Cdd:PRK05691  3251 AAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASF-SWNAGETMlQVIHK 3329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   83 ERNVIVLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLH 162
Cdd:PRK05691  3330 PGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFE 3409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  163 IYASYVNASPITLEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTkgksRQEHVTFS----------- 231
Cdd:PRK05691  3410 IYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPIPSDRPF----LREHAGDSggmvvgdcytr 3485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  232 FSKEESSRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ----GAK 307
Cdd:PRK05691  3486 LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQlpaaGQR 3565

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  308 TPFLQLIKDMQKDRLAAEAYSYHPLYEIQSRSAVKQG--LIDHILVFENYPVqqEIQMLNKQEH---ASDLFQIHnftva 382
Cdd:PRK05691  3566 CSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGqpLFDSLFVFENAPV--EVSVLDRAQSlnaSSDSGRTH----- 3638

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  383 deTNYSFYLMVAPGEEIHIKMNYDAEQHDRSFV---LSVKEHLLNAVSQILNNPnlpPEEIDITTDTEKRQLIGEiTDQT 459
Cdd:PRK05691  3639 --TNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVerlLGEFKRLLLALVQGFHGD---LSELPLLGEQERDFLLDG-CNRS 3712

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  460 ----PVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILK 535
Cdd:PRK05691  3713 erdyPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFK 3792

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  536 AGGAIVPVDPHYPADRIRYILHDCG-----CSHV-VSQAHlpSSLEDNYIITHP-----EDIE-SKVDGSNIKSVNNADD 603
Cdd:PRK05691  3793 AGAGYLPLDPGLPAQRLQRIIELSRtpvlvCSAAcREQAR--ALLDELGCANRPrllvwEEVQaGEVASHNPGIYSGPDN 3870

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  604 LLYMIYTSGTTGKPKGVQFEHRNMAN--LLKFEYTHSGidfEADVL-QFATPSFDVCYQEIFSALLKGGTLHIVPEAIKR 680
Cdd:PRK05691  3871 LAYVIYTSGSTGLPKGVMVEQRGMLNnqLSKVPYLALS---EADVIaQTASQSFDISVWQFLAAPLFGARVEIVPNAIAH 3947

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  681 DVPQLFAFInkHQTNIVFL---PTAFIKMIFSERELAnsfpDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSE- 756
Cdd:PRK05691  3948 DPQGLLAHV--QAQGITVLesvPSLIQGMLAEDRQAL----DGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAEc 4021

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  757 THVVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDV 835
Cdd:PRK05691  4022 SDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGE 4101

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  836 IMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHeLCAYYCSVQKLNTID 915
Cdd:PRK05691  4102 RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH-LVGYLVPHQTVLAQG 4180

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  916 -----LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDAS-ISGNPYTAPRNLLEAKLSQLFEDVLKNGHIG 989
Cdd:PRK05691  4181 allerIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGqLQSQAYLAPRNELEQTLATIWADVLKVERVG 4260

                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997  990 IQDNFFDNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLALIIR 1038
Cdd:PRK05691  4261 VHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1508-1984 2.41e-157

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: 495.74  E-value: 2.41e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQSaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd17649     81 EDSGAGLLLTHH----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHI--K 1745
Cdd:cd17649    127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEAdrT 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1746 YRSVPIktnRLKRVFSGGEQLGTHLVSRFyeLLPNVSITNSYGPTEATVEAAFFDCPPHEKL--ERIPIGKPVHHVRLYL 1823
Cdd:cd17649    207 GDGRPP---SLRLYIFGGEALSPELLRRW--LKAPVRLFNAYGPTEATVTPLVWKCEAGAARagASMPIGRPLGGRSAYI 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1824 LNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGY 1902
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1903 RIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ-------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPS 1975
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAaaaqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441


                   ....*....
gi 1678550997 1976 GKLDRNALP 1984
Cdd:cd17649    442 GKLDRKALP 450
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 2539-3020 5.06e-157

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: 496.87  E-value: 5.06e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2539 FEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYP 2618
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2619 KERKRYILSDSGTKLLMTINEA--DLGVLADFEGEILTIESVEEDDKSPLPQMSsAHHLAYIIYTSGTTGRPKGVMVEHK 2696
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALagELAVELVAVTLLDQPGAAAGADAEPDPALD-ADDLAYVIYTSGSTGRPKGVVMPHR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2697 GIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYR 2776
Cdd:cd17651    160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2777 ALLDVVQPEDVK--TLRVVTLAGEAA-DRELIARSLAICPHTELANEYGPTENSVAT------TVMRHMEKqayVSIGQP 2847
Cdd:cd17651    240 ALAEHGRPLGVRlaALRYLLTGGEQLvLTEDLREFCAGLPGLRLHNHYGPTETHVVTalslpgDPAAWPAP---PPIGRP 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2848 IDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDD 2927
Cdd:cd17651    317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADD 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2928 QVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDS 3005
Cdd:cd17651    397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSAFVLLDA 476

                          490
                   ....*....|....*
gi 1678550997 3006 LPLSPNGKLDRGALP 3020
Cdd:cd17651    477 LPLTPNGKLDRRALP 491
PRK05691 PRK05691
peptide synthase; Validated
 12-1455 4.15e-155

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 545.15  E-value: 4.15e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVIVLEE 91
Cdd:PRK05691  1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPVQQVAEDSGLRMDWQ 1808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   92 DITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNA- 170
Cdd:PRK05691  1809 DFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDr 1888

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  171 -SPITLEPVQpYGKYI----KWLMEQDKEQAVSYWDHYLSGHEQQTVLP--KQKKTKGKSRQEHVTFSFSKEESSRLSEL 243
Cdd:PRK05691  1889 eSPLEPLPVQ-YLDYSvwqrQWLESGERQRQLDYWKAQLGNEHPLLELPadRPRPPVQSHRGELYRFDLSPELAARVRAF 1967

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  244 AAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGR-PAEIEGiehMVGLFINTMPVRVQ--GAKT------------ 308
Cdd:PRK05691  1968 NAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRiRPESEG---LIGAFLNTQVLRCQldGQMSvselleqvrqtv 2044

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  309 ---------PFLQLIKDMQKDRLAAeaysYHPLYEIqsrsavkqglidhilvfenypvqqeiqMLNKQEHAsdlFQ---- 375
Cdd:PRK05691  2045 iegqshqdlPFDHLVEALQPPRSAA----YNPLFQV---------------------------MCNVQRWE---FQqsrq 2090

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  376 IHNFTV------ADETNYSFYLMVAP-GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEK 448
Cdd:PRK05691  2091 LAGMTVeylvndARATKFDLNLEVTDlDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQ 2170

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  449 RQLI----GEITDQtPVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSA 524
Cdd:PRK05691  2171 QQLLdslaGEAGEA-RLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSL 2249

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  525 AFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA-------HLPS-----SLEDNYIIThpedieSKVDG 592
Cdd:PRK05691  2250 EMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRalfealgELPAgvarwCLEDDAAAL------AAYSD 2323

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  593 SNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLH 672
Cdd:PRK05691  2324 APLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVV 2403

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  673 IVPEAiKRDVPQLFAFINKHQTNIV-FLP---TAFIKMIFSERElanSFPdgVKHLIAAGEQLM------ISDLFQDVLr 742
Cdd:PRK05691  2404 LRAQG-QWGAEEICQLIREQQVSILgFTPsygSQLAQWLAGQGE---QLP--VRMCITGGEALTgehlqrIRQAFAPQL- 2476

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  743 krgihLHNHYGPSETHVVSTYTIHPgDPIPE---LPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHD 819
Cdd:PRK05691  2477 -----FFNAYGPTETVVMPLACLAP-EQLEEgaaSVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRP 2550

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  820 KLTSDKFSSDPFKPDV-IMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIwQDQNGE 898
Cdd:PRK05691  2551 GLTAERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA-LDTPSG 2629

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  899 HELCAYYCSVQKLNTID--------LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRNL 970
Cdd:PRK05691  2630 KQLAGYLVSAVAGQDDEaqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSE 2709

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  971 LEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRiAKEFHVQVSLKDIFAHPTVEGLALIIREAEQnlyAAIEP 1050
Cdd:PRK05691  2710 LEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVATHSEA---AQAEQ 2785

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1051 AEKRDTYPVSSAQKRIYVlQQLDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFvSGADDEpVQRIHTEVP 1130
Cdd:PRK05691  2786 GPLQGASGLTPIQHWFFD-SPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRF-SQADGR-WQAEYRAVT 2862

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1131 F-TLSKETTIEGFV----------RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYanRQLK 1199
Cdd:PRK05691  2863 AqELLWQVTVADFAecaalfadaqRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALY--RQLS 2940

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1200 PLRIQ--------YKDYAVWQQKFKKGDSYQKQETYWQQQFSGdlPILELPTDKRRPAERQFIGGKVTFQLDKEITARIK 1271
Cdd:PRK05691  2941 AGAEPalpaktsaFRDWAARLQAYAGSESLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLL 3018

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1272 RLA----HKNRSTLYMTLLAlysAFLSRLSGQDDIVIGSPIAGRPHA----DLEAVLGMFVNTLALRTRPAGNKTFE--E 1341
Cdd:PRK05691  3019 QQApaayRTQVNDLLLTALA---RVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTPAPGDDAArgE 3095

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1342 FLKEVRQTaLEAYEH--QDY-PFEELVDKLGVQReMSRNPLFDTTL-VLQNMEQQklKMNDVQLQW--------NDLEHP 1409
Cdd:PRK05691  3096 SIKAIKEQ-LRAVPHkgLGYgVLRYLADAAVREA-MAALPQAPITFnYLGQFDQS--FASDALFRPldepagpaHDPDAP 3171

                         1530      1540      1550      1560      1570
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1410 ISKfDISLYVTEHDSELFCQFEYSTALFEKETIQRWASLF----TTLVEH 1455
Cdd:PRK05691  3172 LPN-ELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYlaelQALIAH 3220
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1508-1984 6.33e-155

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: 488.30  E-value: 6.33e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd17652     81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAflehIKYR 1747
Cdd:cd17652    126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA----LPPD 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1748 SVPiktnRLKRVFSGGEQLGTHLVSRFyelLPNVSITNSYGPTEATVEAAFFDCPPHEklERIPIGKPVHHVRLYLLNQN 1827
Cdd:cd17652    202 DLP----DLRTLVVAGEACPAELVDRW---APGRRMINAYGPTETTVCATMAGPLPGG--GVPPIGRPVPGTRVYVLDAR 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1828 QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 1906
Cdd:cd17652    273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1907 GEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd17652    353 GEVEAALTEHPGVAEAVVVVRDDrPGDKRLVAYVvpapgAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432


                   ....
gi 1678550997 1981 NALP 1984
Cdd:cd17652    433 RALP 436
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 2538-3019 5.08e-154

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: 487.94  E-value: 5.08e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2538 LFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEY 2617
Cdd:cd17646      3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2618 PKERKRYILSDSGTKLLMTINE-----ADLGVLADFEGEILTIESVEEDDKSPLPqmssaHHLAYIIYTSGTTGRPKGVM 2692
Cdd:cd17646     83 PADRLAYMLADAGPAVVLTTADlaarlPAGGDVALLGDEALAAPPATPPLVPPRP-----DNLAYVIYTSGSTGRPKGVM 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2693 VEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVP 2772
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2773 VLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAIcPHTELANEYGPTENSVATT--VMRHMEKQAYVSIGQPIDG 2850
Cdd:cd17646    238 SMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVThwPVRGPAETPSVPIGRPVPN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2851 TQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVK 2930
Cdd:cd17646    317 TRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVK 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2931 IRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVV---TKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLP 3007
Cdd:cd17646    397 IRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALP 476

                          490
                   ....*....|..
gi 1678550997 3008 LSPNGKLDRGAL 3019
Cdd:cd17646    477 LTANGKLDRAAL 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 2547-3019 5.66e-151

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: 478.32  E-value: 5.66e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTINEADLGVLADFEGEILTIESVEEDDKSPLPQMSSaHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRR 2706
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSP-DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2707 NAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDvVQPED 2786
Cdd:cd12116    160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD-AGWQG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2787 VKTLRVVTlAGEAADRELIARSLAicPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIG 2866
Cdd:cd12116    239 RAGLTALC-GGEALPPDLAARLLS--RVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2867 VAGELCIAGTGLARGYVNLPELTERAFTQNPFKPE-ARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVI 2945
Cdd:cd12116    316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAAL 395

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 2946 RCIKGVKDAAVVAHvTASGQTELSAYVVTK--PGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd12116    396 AAHPGVAQAAVVVR-EDGGDRRLVAYVVLKagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
PRK05691 PRK05691
peptide synthase; Validated
 1047-2069 1.91e-150

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 529.74  E-value: 1.91e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1047 AIEPAEKRDTYPVSSAQKRIYVLQQLDEGVA-YNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRI 1125
Cdd:PRK05691  3248 PVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVI 3327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1126 HT------------EVPFTlSKETTIEGFVRP-----FDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIRE 1188
Cdd:PRK05691  3328 HKpgrtpidyldwrGLPED-GQEQRLQALHKQereagFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMND 3406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1189 FTDLYA----NRQLK-PLRIQYKDYAVWQQKFKKGDSYQkqetYWQQQFSGDLPILELPTDkrRPAERQFIG-------G 1256
Cdd:PRK05691  3407 FFEIYTalgeGREAQlPVPPRYRDYIGWLQRQDLAQARQ----WWQDNLRGFERPTPIPSD--RPFLREHAGdsggmvvG 3480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1257 KVTFQLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRP--HADLEAVLGMFVNTLALRTR-P 1333
Cdd:PRK05691  3481 DCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMPQMQRTVGLFINSIALRVQlP 3560

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1334 AGNK--TFEEFLKEVRQTALEAYEHQDYPfeeLVDkLGVQREMSR-NPLFDTTLVLQNMEQQKLKMNDVQlQWN---DLE 1407
Cdd:PRK05691  3561 AAGQrcSVRQWLQGLLDSNMELREYEYLP---LVA-IQECSELPKgQPLFDSLFVFENAPVEVSVLDRAQ-SLNassDSG 3635

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1408 HPISKFDISLYVTEHDsELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLfEE 1487
Cdd:PRK05691  3636 RTHTNFPLTAVCYPGD-DLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNR-SE 3713

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1488 TGYSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKA 1567
Cdd:PRK05691  3714 RDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKA 3793

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1568 GGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLH-----VPEFTGE-----IVYLNQTNSGLAHrlSNPNVDVLPQSL 1637
Cdd:PRK05691  3794 GAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREqaralLDELGCAnrprlLVWEEVQAGEVAS--HNPGIYSGPDNL 3871

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1638 AYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEV 1717
Cdd:PRK05691  3872 AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQG 3951

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1718 IAKAIEEQKITAMHFVPSMLHAFLEHIKyrsvpIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAA 1797
Cdd:PRK05691  3952 LLAHVQAQGITVLESVPSLIQGMLAEDR-----QALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVA 4026

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1798 FFdcPPHEKLER---IPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMY 1873
Cdd:PRK05691  4027 FF--RVDLASTRgsyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLY 4104

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1874 KTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV--------EGLQRN 1945
Cdd:PRK05691  4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLvphqtvlaQGALLE 4184

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1946 EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPG-GAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDN 2024
Cdd:PRK05691  4185 RIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDiGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDN 4264

                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*
gi 1678550997 2025 FFDRGGHSLKATALVSRITKEFDVQVPLKDVFAHPTVEGLATVIR 2069
Cdd:PRK05691  4265 FFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1508-1983 3.78e-150

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: 476.01  E-value: 3.78e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSGLAHrlSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAP--AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEhikyr 1747
Cdd:cd12116    159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD----- 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1748 SVPIKTNRLkRVFSGGEQLGTHLVSRFyeLLPNVSITNSYGPTEATVEAAFfdCPPHEKLERIPIGKPVHHVRLYLLNQN 1827
Cdd:cd12116    234 AGWQGRAGL-TALCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTA--ARVTAAAGPIPIGRPLANTQVYVLDAA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1828 QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 1906
Cdd:cd12116    309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1907 GEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEG-----LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 1981
Cdd:cd12116    389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLkagaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468


                   ..
gi 1678550997 1982 AL 1983
Cdd:cd12116    469 AL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 2547-3020 1.09e-149

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: 473.28  E-value: 1.09e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRR 2706
Cdd:cd17652     81 ADARPALLLT----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2707 NAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPvlyrALLDVVQPED 2786
Cdd:cd17652    127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPP----AALAALPPDD 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2787 VKTLRVVTLAGEAADRELIARslaICPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIG 2866
Cdd:cd17652    203 LPDLRTLVVAGEACPAELVDR---WAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPG 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2867 VAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVI 2945
Cdd:cd17652    280 VPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAAL 359

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2946 RCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALP 3020
Cdd:cd17652    360 TEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1508-1983 3.46e-147

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: 466.78  E-value: 3.46e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd17643     81 ADSGPSLLLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSYSFDASIWELfWWPYA-GASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIky 1746
Cdd:cd17643    126 QRWFGFNEDDVWTLFHSYAFDFSVWEI-WGALLhGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAA-- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1747 RSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVS--ITNSYGPTEATVEAAFF-----DCPPHEkleRIPIGKPVHHV 1819
Cdd:cd17643    203 DRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTVHVTFRpldaaDLPAAA---ASPIGRPLPGL 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1820 RLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDDQVK 1898
Cdd:cd17643    280 RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVK 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1899 IRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV 1972
Cdd:cd17643    360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEpGDTRLVAYVvaddgAAADIAELRALLKELLPDYMVPARYVPLDALPL 439

                          490
                   ....*....|.
gi 1678550997 1973 TPSGKLDRNAL 1983
Cdd:cd17643    440 TVNGKLDRAAL 450
PRK05691 PRK05691
peptide synthase; Validated
 2078-3105 9.84e-147

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 517.80  E-value: 9.84e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2078 AIKPAEKQETYPVSSAQKRIyVLQQLEDGGTG-YNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQR 2156
Cdd:PRK05691  3248 PVPAAEIEDVYPLTPMQEGL-LLHTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQV 3326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2157 IHD------------EVPFTLQTTVLGARTEQEAAAAFikpfDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNI 2224
Cdd:PRK05691  3327 IHKpgrtpidyldwrGLPEDGQEQRLQALHKQEREAGF----DLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSL 3402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2225 LIQEFGELYN------NRKLPALRiQYKDYAVWQEGFKTGDAykmqEAYWLKQLEG-ELPVLdLPADhaRPPVRSFAGDK 2297
Cdd:PRK05691  3403 LMNDFFEIYTalgegrEAQLPVPP-RYRDYIGWLQRQDLAQA----RQWWQDNLRGfERPTP-IPSD--RPFLREHAGDS 3474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2298 VSFT-------LEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRP--HKDLEPILGMFVNTLA 2368
Cdd:PRK05691  3475 GGMVvgdcytrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMPQMQRTVGLFINSIA 3554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2369 LRTR-PEGGKP--FVQYLQEVRETALEAFEHQNYPfeeLVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQ 2445
Cdd:PRK05691  3555 LRVQlPAAGQRcsVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNAS 3631

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2446 V----SHlvSKFDLTLQASEGDgNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLNE 2521
Cdd:PRK05691  3632 SdsgrTH--TNFPLTAVCYPGD-DLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDG 3708

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2522 FNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASIL 2601
Cdd:PRK05691  3709 CNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIV 3788

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2602 GVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLM---TINEADLGVLADFEG----EILTIESVEEDD-KSPLPQM-SSA 2672
Cdd:PRK05691  3789 GSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcsaACREQARALLDELGCanrpRLLVWEEVQAGEvASHNPGIySGP 3868

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2673 HHLAYIIYTSGTTGRPKGVMVEHKGIANTlQWRRNAY-AFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAK 2751
Cdd:PRK05691  3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLNN-QLSKVPYlALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAH 3947

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2752 DILAIKHQLSRQRITHMIIVPVLYRALLdvVQPED-VKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVAT 2830
Cdd:PRK05691  3948 DPQGLLAHVQAQGITVLESVPSLIQGML--AEDRQaLDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDV 4025

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2831 TVMR---HMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYR 2906
Cdd:PRK05691  4026 AFFRvdlASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYR 4105

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2907 TGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtELSAYVVTKPGLSTNA---- 2982
Cdd:PRK05691  4106 TGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK-HLVGYLVPHQTVLAQGalle 4184

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2983 -VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADS 3061
Cdd:PRK05691  4185 rIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDN 4264

                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*
gi 1678550997 3062 FFELGGDSIKALQVSARLHR-IGKQMAVKDLFSHPTIQELAAYIR 3105
Cdd:PRK05691  4265 FFELGGHSLLATQIASRVQKaLQRNVPLRAMFECSTVEELAEYIE 4309
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 2535-3019 2.16e-145

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: 461.40  E-value: 2.16e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVE 2694
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLT----------------------------------DPDDLAYVIYTSGSTGRPKGVAIE 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLlheeeAKDILAIKHQLSRQRITHMIIVPVL 2774
Cdd:cd12115    127 HRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVL-----ADNVLALPDLPAAAEVTLINTVPSA 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2775 YRALLDV-VQPedvKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTEN---SVATTVMRHMEKQayVSIGQPIDG 2850
Cdd:cd12115    202 AAELLRHdALP---ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDttySTVAPVPPGASGE--VSIGRPLAN 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2851 TQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVK 2930
Cdd:cd12115    277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVK 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2931 IRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLS--TNAVRSELQNKLPVFMHPAFIEKLDSLPL 3008
Cdd:cd12115    357 VRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAglVEDLRRHLGTRLPAYMVPSRFVRLDALPL 436

                          490
                   ....*....|.
gi 1678550997 3009 SPNGKLDRGAL 3019
Cdd:cd12115    437 TPNGKIDRSAL 447
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1053-1477 1.06e-144

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: 459.88  E-value: 1.06e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1053 KRDTYPVSSAQKRIYVLQQLDEG-VAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPF 1131
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHsSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1132 TL-----------SKETTIEGFVR-----PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYA- 1194
Cdd:pfam00668   81 ELeiidisdlsesEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQq 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1195 ---NRQLKPLRIQ-YKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARI 1270
Cdd:pfam00668  161 llkGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1271 KRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTA 1350
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1351 LEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDL-----EHPISKFDISLYVTEHDSE 1425
Cdd:pfam00668  321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLsvssvIEEEAKYDLSLTASERGGG 400

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1426 LFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETELDNIPILTKEEERD 1477
Cdd:pfam00668  401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQK 452
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1495-1984 1.42e-144

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: 459.98  E-value: 1.42e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI 1574
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1575 DPDYPEERISFLLEDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVE 1654
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ-----------------------------------PENLAYVIYTSGSTGKPKGVM 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 IEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVP 1734
Cdd:cd17644    126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHAFLEHIKYRSVPIkTNRLKRVFSGGEQLGTHLVSRFYELL-PNVSITNSYGPTEATVEAAFFDC--PPHEKLERIP 1811
Cdd:cd17644    206 AYWHLLVLELLLSTIDL-PSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEATIAATVCRLtqLTERNITSVP 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1812 IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY--PGERMYKTGDVARWLPDGNVEF 1889
Cdd:cd17644    285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEY 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1890 LGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAY 1963
Cdd:cd17644    365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqPGNKRLVAYIvphyeESPSTVELRQFLKAKLPDYMIPSA 444

                          490       500
                   ....*....|....*....|.
gi 1678550997 1964 MIEMEQWPVTPSGKLDRNALP 1984
Cdd:cd17644    445 FVVLEELPLTPNGKIDRRALP 465
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1496-1983 1.51e-144

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: 459.09  E-value: 1.51e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPID 1575
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPEERISFLLEDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEI 1655
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVAI 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1656 EHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLpqggEKEPEVIAKAIEEQkITAMHFVPS 1735
Cdd:cd12115    126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA----DNVLALPDLPAAAE-VTLINTVPS 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1736 MLHAFLEHikyRSVPiktNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKlERIPIGKP 1815
Cdd:cd12115    201 AAAELLRH---DALP---ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGAS-GEVSIGRP 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1816 VHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDD 1895
Cdd:cd12115    274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADN 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1896 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQ 1969
Cdd:cd12115    354 QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAaGERRLVAYIvaepgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDA 433

                          490
                   ....*....|....
gi 1678550997 1970 WPVTPSGKLDRNAL 1983
Cdd:cd12115    434 LPLTPNGKIDRSAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1508-1983 4.55e-144

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: 457.70  E-value: 4.55e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd17650     81 EDSGAKLLLTQ-----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQL-KHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKY 1746
Cdd:cd17650    126 RREYELdSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1747 RSVPIKTNRLKRVFSGGEQLG--THLVSRFyelLPNVSITNSYGPTEATVEAAFF--DCPPHEKLERIPIGKPVHHVRLY 1822
Cdd:cd17650    206 NGLDLSAMRLLIVGSDGCKAQdfKTLAARF---GQGMRIINSYGVTEATIDSTYYeeGRDPLGDSANVPIGRPLPNTAMY 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1823 LLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGY 1902
Cdd:cd17650    283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1903 RIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:cd17650    363 RIELGEIESQLARHPAIDEAVVAVREDKgGEARLCAYVvaaATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442


                   ....*
gi 1678550997 1979 DRNAL 1983
Cdd:cd17650    443 DRRAL 447
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 466-952 5.65e-141

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: 450.57  E-value: 5.65e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  466 HAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDP 545
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  546 HYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIE-SKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEH 624
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEAlAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIV-FLPT-- 701
Cdd:cd17646    161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTChFVPSml 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  702 -AFIkmifseRELANSFPDGVKHLIAAGEQLMIsDLFQDVLRKRGIHLHNHYGPSETHV-VSTYTIHPGDPIPELPpIGK 779
Cdd:cd17646    241 rVFL------AEPAAGSCASLRRVFCSGEALPP-ELAARFLALPGAELHNLYGPTEAAIdVTHWPVRGPAETPSVP-IGR 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  780 PIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRAD 859
Cdd:cd17646    313 PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSD 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  860 NQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSV---QKLNTIDLRSYMASELPEYMIPAKWIWV 936
Cdd:cd17646    393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAagaAGPDTAALRAHLAERLPEYMVPAAFVVL 472

                          490
                   ....*....|....*.
gi 1678550997  937 DSIPLTPNGKVDRAAL 952
Cdd:cd17646    473 DALPLTANGKLDRAAL 488
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 477-953 6.96e-139

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: 442.08  E-value: 6.96e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVSQAhlpsslednyiithpedieskvdgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYT 636
Cdd:cd17652     81 ADARPALLLTTP---------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIfSERELans 716
Cdd:cd17652    128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL-PPDDL--- 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  717 fPDGVkHLIAAGEQLMISdlfqdvLRKR---GIHLHNHYGPSETHVVSTYtiHPGDPIPELPPIGKPIGCTDLYILNHQK 793
Cdd:cd17652    204 -PDLR-TLVVAGEACPAE------LVDRwapGRRMINAYGPTETTVCATM--AGPLPGGGVPPIGRPVPGTRVYVLDARL 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  794 QLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQ 872
Cdd:cd17652    274 RPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELG 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  873 EIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTI--DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRA 950
Cdd:cd17652    354 EVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTaaELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRR 433


                   ...
gi 1678550997  951 ALP 953
Cdd:cd17652    434 ALP 436
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 490-888 1.67e-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: 440.16  E-value: 1.67e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLR-MKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA 568
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDNYI------ITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDF 642
Cdd:TIGR01733   81 ALASRLAGLVLpvilldPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  643 EADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVP-QLFAFINKHQTNIVFLPTAFIKMIfseRELANSFPDGV 721
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAaLLAALIAEHPVTVLNLTPSLLALL---AAALPPALASL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  722 KHLIAAGEQLMISDLfqDVLRKR--GIHLHNHYGPSETHVVSTYTIHPGDPIP--ELPPIGKPIGCTDLYILNHQKQLQP 797
Cdd:TIGR01733  238 RLVILGGEALTPALV--DRWRARgpGARLINLYGPTETTVWSTATLVDPDDAPreSPVPIGRPLANTRLYVLDDDLRPVP 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  798 CGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDV--IMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:TIGR01733  316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395

                          410
                   ....*....|...
gi 1678550997  876 VTLMNHPDISEAA 888
Cdd:TIGR01733  396 AALLRHPGVREAV 408
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1507-1984 5.09e-138

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: 441.53  E-value: 5.09e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1507 TPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFL 1586
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1587 LEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNsgLAHRL-SNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLN 1665
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPS--ISQEDtSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1666 SLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMhFVPSMLHAFLEHIK 1745
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSER 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1746 YRSVPIKTNrLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKLERIPIGKPVHHVRLYLLN 1825
Cdd:cd17656    238 EFINRFPTC-VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1826 QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIE 1905
Cdd:cd17656    317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1906 PGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYVEGLQR---NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 1981
Cdd:cd17656    397 LGEIEAQLLNHPGVSEAVVLDKADDkGEKYLCAYFVMEQElniSQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476


                   ...
gi 1678550997 1982 ALP 1984
Cdd:cd17656    477 ALP 479
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1497-1984 1.37e-135

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: 433.13  E-value: 1.37e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1497 HYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDP 1576
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1577 DYPEERISFLLEDSGTNILLLQsaglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIE 1656
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN-----------------------------------PDDLAYVIYTSGSTGLPKGVMIE 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1657 HRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITaMHFVPSM 1736
Cdd:cd17645    126 HHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTG 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1737 L-HAFLEhikyrsvpIKTNRLKRVFSGGEQLgTHLVSRFYELLpnvsitNSYGPTEATVEAAFFdcPPHEKLERIPIGKP 1815
Cdd:cd17645    205 AaEQFMQ--------LDNQSLRVLLTGGDKL-KKIERKGYKLV------NNYGPTENTVVATSF--EIDKPYANIPIGKP 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1816 VHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDD 1895
Cdd:cd17645    268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQ 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1896 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWP 1971
Cdd:cd17645    348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAdGRKYLVAYVtapEEIPHEELREWLKNDLPDYMIPTYFVHLKALP 427

                          490
                   ....*....|...
gi 1678550997 1972 VTPSGKLDRNALP 1984
Cdd:cd17645    428 LTANGKVDRKALP 440
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 2547-3019 8.20e-135

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: 430.96  E-value: 8.20e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRR 2706
Cdd:cd17643     81 ADSGPSLLLT----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2707 NAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQ--P 2784
Cdd:cd17643    127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADrdG 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2785 EDVKTLRVVTLAGEAADRELIARSLA--ICPHTELANEYGPTENSVATTVMR----HMEKQAYVSIGQPIDGTQVLILNS 2858
Cdd:cd17643    207 RDPLALRYVIFGGEALEAAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPldaaDLPAAAASPIGRPLPGLRVYVLDA 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2859 NHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPE-ARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVE 2937
Cdd:cd17643    287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPgSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIE 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2938 TKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTN--AVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:cd17643    367 LGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADiaELRALLKELLPDYMVPARYVPLDALPLTVNGKLD 446


                   ....
gi 1678550997 3016 RGAL 3019
Cdd:cd17643    447 RAAL 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 466-953 1.79e-134

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: 429.67  E-value: 1.79e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  466 HAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDP 545
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  546 HYPADRIRYILHDCGCSHVVSqahlpsslednyiithpedieskvdgsniksvnNADDLLYMIYTSGTTGKPKGVQFEHR 625
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLT---------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHH 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  626 NMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIK 705
Cdd:cd17645    128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAE 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  706 MIFserELANSfpdGVKHLIAAGEQLmisdlfqDVLRKRGIHLHNHYGPSETHVVSTytIHPGDPIPELPPIGKPIGCTD 785
Cdd:cd17645    208 QFM---QLDNQ---SLRVLLTGGDKL-------KKIERKGYKLVNNYGPTENTVVAT--SFEIDKPYANIPIGKPIDNTR 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  786 LYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIR 865
Cdd:cd17645    273 VYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  866 GYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNG 945
Cdd:cd17645    353 GYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANG 432


                   ....*...
gi 1678550997  946 KVDRAALP 953
Cdd:cd17645    433 KVDRKALP 440
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 477-952 1.95e-134

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: 430.94  E-value: 1.95e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLkfeyt 636
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL----- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HS-----GIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSER 711
Cdd:cd12116    156 HSmrerlGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAG 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  712 ELANsfpDGVkHLIAAGEQLmISDLFQDVLRkRGIHLHNHYGPSETHVVStyTIHPGDPIPELPPIGKPIGCTDLYILNH 791
Cdd:cd12116    236 WQGR---AGL-TALCGGEAL-PPDLAARLLS-RVGSLWNLYGPTETTIWS--TAARVTAAAGPIPIGRPLANTQVYVLDA 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  792 QKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFK-PDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIE 870
Cdd:cd12116    308 ALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  871 PQEIEVTLMNHPDISEAAILIWQDQNGEHeLCAYY--CSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd12116    388 LGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVvlKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466


                   ....
gi 1678550997  949 RAAL 952
Cdd:cd12116    467 RKAL 470
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 2537-3020 7.18e-134

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: 428.13  E-value: 7.18e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2537 QLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPE 2616
Cdd:cd17645      2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2617 YPKERKRYILSDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVEHK 2696
Cdd:cd17645     82 YPGERIAYMLADSSAKILLT----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHH 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2697 GIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAikhqLSRQRITHMIIVPVLYR 2776
Cdd:cd17645    128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDA----LNDYFNQEGITISFLPT 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2777 ALLDVVQPEDVKTLRVVTLAGEAADRelIARSlaicPHTeLANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLIL 2856
Cdd:cd17645    204 GAAEQFMQLDNQSLRVLLTGGDKLKK--IERK----GYK-LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYIL 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRV 2936
Cdd:cd17645    277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRI 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2937 ETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd17645    357 EPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDR 436


                   ....
gi 1678550997 3017 GALP 3020
Cdd:cd17645    437 KALP 440
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 465-952 1.52e-133

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: 427.50  E-value: 1.52e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVVSQAhlpsslednyiithpedieskvdgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEH 624
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTDP---------------------------------DDLAYVIYTSGSTGRPKGVAIEH 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNMANLLKFEYTHSGIDFEADVLQfATP-SFDVCYQEIFSALLKGGTLHIVpeaikRDVPQLFAF-INKHQTNIVFLPTA 702
Cdd:cd12115    128 RNAAAFLQWAAAAFSAEELAGVLA-STSiCFDLSVFELFGPLATGGKVVLA-----DNVLALPDLpAAAEVTLINTVPSA 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  703 FikmifseREL--ANSFPDGVKHLIAAGEQLMiSDLFQDVLRK-RGIHLHNHYGPSETHVVSTYT-IHPGDPipELPPIG 778
Cdd:cd12115    202 A-------AELlrHDALPASVRVVNLAGEPLP-RDLVQRLYARlQVERVVNLYGPSEDTTYSTVApVPPGAS--GEVSIG 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  779 KPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRA 858
Cdd:cd12115    272 RPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRA 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  859 DNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCS--VQKLNTIDLRSYMASELPEYMIPAKWIWV 936
Cdd:cd12115    352 DNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAepGAAGLVEDLRRHLGTRLPAYMVPSRFVRL 431

                          490
                   ....*....|....*.
gi 1678550997  937 DSIPLTPNGKVDRAAL 952
Cdd:cd12115    432 DALPLTPNGKIDRSAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 2534-3020 1.61e-133

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: 428.01  E-value: 1.61e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI 2613
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 DPEYPKERKRYILSDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMV 2693
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLT----------------------------------QPENLAYVIYTSGSTGKPKGVMI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2694 EHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPV 2773
Cdd:cd17644    127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2774 LYRALLDVVQPED---VKTLRVVTLAGEAADRELIAR-SLAICPHTELANEYGPTENSVATTVMR----HMEKQAYVSIG 2845
Cdd:cd17644    207 YWHLLVLELLLSTidlPSSLRLVIVGGEAVQPELVRQwQKNVGNFIQLINVYGPTEATIAATVCRltqlTERNITSVPIG 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2846 QPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF--KPEARMYRTGDAARWMADGTLEYLG 2923
Cdd:cd17644    287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLG 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2924 RIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTK--PGLSTNAVRSELQNKLPVFMHPAFIE 3001
Cdd:cd17644    367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHyeESPSTVELRQFLKAKLPDYMIPSAFV 446

                          490
                   ....*....|....*....
gi 1678550997 3002 KLDSLPLSPNGKLDRGALP 3020
Cdd:cd17644    447 VLEELPLTPNGKIDRRALP 465
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 2547-3020 4.50e-133

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: 426.01  E-value: 4.50e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmssaHH---LAYIIYTSGTTGRPKGVMVEHKGIANTLQ 2703
Cdd:cd17649     81 EDSGAGLLLT------------------------------------HHprqLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2704 WRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDV-- 2781
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEad 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2782 -VQPEDVKTLRVVTLAGEAADRELIARSLAIcpHTELANEYGPTENSVATTVM----RHMEKQAYVSIGQPIDGTQVLIL 2856
Cdd:cd17649    205 rTGDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWkceaGAARAGASMPIGRPLGGRSAYIL 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYR 2935
Cdd:cd17649    283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFR 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2936 VETKEIESVIRCIKGVKDAAVVAhVTASGQTELSAYVVTKPGLSTNA----VRSELQNKLPVFMHPAFIEKLDSLPLSPN 3011
Cdd:cd17649    363 IELGEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLARLPLTPN 441


                   ....*....
gi 1678550997 3012 GKLDRGALP 3020
Cdd:cd17649    442 GKLDRKALP 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 2546-3020 1.80e-132

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: 425.73  E-value: 1.80e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2546 TPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYI 2625
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2626 LSDSGTKLLMTINEadLGVLADFEGEILTIE--SVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQ 2703
Cdd:cd17656     81 MLDSGVRVVLTQRH--LKSKLSFNKSTILLEdpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2704 WRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQ 2783
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSERE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2784 -----PEDVKTLrvvTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMRH--MEKQAYVSIGQPIDGTQVLIL 2856
Cdd:cd17656    239 finrfPTCVKHI---ITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINpeAEIPELPPIGKPISNTWIYIL 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRV 2936
Cdd:cd17656    316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2937 ETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd17656    396 ELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475


                   ....
gi 1678550997 3017 GALP 3020
Cdd:cd17656    476 KALP 479
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 464-953 2.69e-132

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: 424.54  E-value: 2.69e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPV 543
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 DPHYPADRIRYILHDCGCSHVVSQAHlpsslednyiithpedieskvdgsniksvnnadDLLYMIYTSGTTGKPKGVQFE 623
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQPE---------------------------------NLAYVIYTSGSTGKPKGVMIE 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  624 HRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAF 703
Cdd:cd17644    128 HQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  704 IKMIFSERELAN-SFPDGVKHLIAAGEQLMIS--DLFQDVLRKRgIHLHNHYGPSETHVVSTYTiHPGDPIPEL---PPI 777
Cdd:cd17644    208 WHLLVLELLLSTiDLPSSLRLVIVGGEAVQPElvRQWQKNVGNF-IQLINVYGPTEATIAATVC-RLTQLTERNitsVPI 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  778 GKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF--KPDVIMYRTGDLARRLEDGNIEYI 855
Cdd:cd17644    286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYL 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  856 GRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKW 933
Cdd:cd17644    366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVphYEESPSTVELRQFLKAKLPDYMIPSAF 445

                          490       500
                   ....*....|....*....|
gi 1678550997  934 IWVDSIPLTPNGKVDRAALP 953
Cdd:cd17644    446 VVLEELPLTPNGKIDRRALP 465
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 477-952 2.87e-132

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: 423.80  E-value: 2.87e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVSQahlpsslednyiithpedieskvdgsniksvnnADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYT 636
Cdd:cd17650     81 EDSGAKLLLTQ---------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HSGID-FEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNI-VFLPTAFIK-MIFSEREL 713
Cdd:cd17650    128 EYELDsFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLmESTPALIRPvMAYVYRNG 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  714 ANsfPDGVKHLIAAGEQLMISDlFQDVLRKRGIHLH--NHYGPSETHVVSTYTIHPGDPIPE--LPPIGKPIGCTDLYIL 789
Cdd:cd17650    208 LD--LSAMRLLIVGSDGCKAQD-FKTLAARFGQGMRiiNSYGVTEATIDSTYYEEGRDPLGDsaNVPIGRPLPNTAMYVL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  790 NHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRI 869
Cdd:cd17650    285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  870 EPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd17650    365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444


                   ...
gi 1678550997  950 AAL 952
Cdd:cd17650    445 RAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 2547-3019 8.86e-132

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: 422.26  E-value: 8.86e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTineadlgvladfegeiltiesvEEDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHKGIANT-LQWR 2705
Cdd:cd17650     81 EDSGAKLLLT----------------------QPED------------LAYVIYTSGTTGKPKGVMVEHRNVAHAaHAWR 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2706 RNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVV--- 2782
Cdd:cd17650    127 REYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVyrn 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2783 --QPEDVKTLRVVTLAGEAAD-RELIARSLAicpHTELANEYGPTENSVATTV----MRHMEKQAYVSIGQPIDGTQVLI 2855
Cdd:cd17650    207 glDLSAMRLLIVGSDGCKAQDfKTLAARFGQ---GMRIINSYGVTEATIDSTYyeegRDPLGDSANVPIGRPLPNTAMYV 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2856 LNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYR 2935
Cdd:cd17650    284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2936 VETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:cd17650    364 IELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443


                   ....
gi 1678550997 3016 RGAL 3019
Cdd:cd17650    444 RRAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 2535-3019 1.47e-131

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: 423.11  E-value: 1.47e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmSSAHHLAYIIYTSGTTGRPKGVMVE 2694
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLT---------------------------------SSPSDAAYVIFTSGSTGKPKGVVIE 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAikHQLSRQRITHMIIVPvl 2774
Cdd:cd05918    128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLA--GFINRLRVTWAFLTP-- 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2775 yrALLDVVQPEDVKTLRVVTLAGEAADRELIARslaICPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQ-V 2853
Cdd:cd05918    204 --SVARLLDPEDVPSLRTLVLGGEALTQSDVDT---WADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCwV 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2854 LILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNP-------FKPEARMYRTGDAARWMADGTLEYLGRID 2926
Cdd:cd05918    279 VDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKD 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2927 DQVKIRGYRVETKEIESVIR-CIKGVKD--AAVVAHVTASGQTELSAYVVTKPGLSTN-------------------AVR 2984
Cdd:cd05918    359 TQVKIRGQRVELGEIEHHLRqSLPGAKEvvVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsdefralvaELR 438

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997 2985 SELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05918    439 SKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
12-1042 1.99e-131

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 449.49  E-value: 1.99e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVlrERNVIVLEE 91
Cdd:PRK10252     9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDN-GEVWQWV--DPALTFPLP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   92 DITHLNEAEQSQFIEQ-WKEKDRDRGFHL-QKDVLMRIALIQTGESQYscIW--TFHHIMMDGWCLSIVLKEFLHIYASY 167
Cdd:PRK10252    86 EIIDLRTQPDPHAAAQaLMQADLQQDLRVdSGKPLVFHQLIQLGDNRW--YWyqRYHHLLVDGFSFPAITRRIAAIYCAW 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  168 VNASPITLEPVQPYG----KYIKWLMEQDKEQAVSYWdhylsgHEQQTVLPK-----QKKTKGKSRQEH---VTFSFSKE 235
Cdd:PRK10252   164 LRGEPTPASPFTPFAdvveEYQRYRASEAWQRDAAFW------AEQRRQLPPpaslsPAPLPGRSASADilrLKLEFTDG 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  236 ESSRLseLAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGR--------PAeiegiehMVglfINTMPVRVQGAK 307
Cdd:PRK10252   238 AFRQL--AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgsaaltaTG-------PV---LNVLPLRVHIAA 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  308 TpflQLIKDMQKdRLAAEAYSY--HPLYEIQ------SRSAVKQ---GLIDHILVFENYPVQQEIQMlnkqehasdlfQI 376
Cdd:PRK10252   306 Q---ETLPELAT-RLAAQLKKMrrHQRYDAEqivrdsGRAAGDEplfGPVLNIKVFDYQLDFPGVQA-----------QT 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  377 HNFTVADETNYSFYLMVAPGEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLI-GEI 455
Cdd:PRK10252   371 HTLATGPVNDLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAqVNA 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  456 TDQTPVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILK 535
Cdd:PRK10252   451 TAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  536 AGGAIVPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPE-DIESKVDGSNIKSVNNADDLLYMIYTSGTT 614
Cdd:PRK10252   531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCyNAPLAPQGAAPLQLSQPHHTAYIIFTSGST 610

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  615 GKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQfATP-SFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQ 693
Cdd:PRK10252   611 GRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQ-KTPcSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYG 689

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  694 -TNIVFLPT---AFIKMIFSERelANSFPDGVKHLIAAGEQLMIS--DLFQdvlRKRGIHLHNHYGPSETHV-VSTY--- 763
Cdd:PRK10252   690 vTTTHFVPSmlaAFVASLTPEG--ARQSCASLRQVFCSGEALPADlcREWQ---QLTGAPLHNLYGPTEAAVdVSWYpaf 764

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  764 ----TIHPGDPIPelppIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYR 839
Cdd:PRK10252   765 geelAAVRGSSVP----IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYR 840

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  840 TGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEA---AILIWQDQ---NGEHELCAYYCSVQ--KL 911
Cdd:PRK10252   841 TGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAatgGDARQLVGYLVSQSglPL 920

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  912 NTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDaSISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQ 991
Cdd:PRK10252   921 DTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPE-LKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDAD 999

                         1050      1060      1070      1080      1090
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  992 DNFFDNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLALIIREAEQ 1042
Cdd:PRK10252  1000 ADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEED 1050
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1508-1983 2.49e-130

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: 419.37  E-value: 2.49e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLLQsaglHVPEFTGEIVYLNQTNSGLAHRLS--NPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLN 1665
Cdd:cd12114     81 ADAGARLVLTD----GPDAQLDVAVFDVLILDLDALAAPapPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1666 SLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHik 1745
Cdd:cd12114    157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDV-- 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1746 YRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDC-PPHEKLERIPIGKPVHHVRLYLL 1824
Cdd:cd12114    235 LEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIdEVPPDWRSIPYGRPLANQRYRVL 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1825 NQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRI 1904
Cdd:cd12114    315 DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRI 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1905 EPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVE------GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:cd12114    393 ELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVpdndgtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472


                   ....*
gi 1678550997 1979 DRNAL 1983
Cdd:cd12114    473 DRAAL 477
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 477-952 4.02e-129

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: 414.78  E-value: 4.02e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGcshvvsqahlPSSLednyiithpedieskvdgsniksVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLlkFEYT 636
Cdd:cd17643     81 ADSG----------PSLL-----------------------LTDPDDLAYVIYTSGSTGRPKGVVVSHANVLAL--FAAT 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HSGIDFEAD--VLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDvPQLFAFINKHQTNIVF--LPTAFIKMIFSERE 712
Cdd:cd17643    126 QRWFGFNEDdvWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARS-PEDFARLLRDEGVTVLnqTPSAFYQLVEAADR 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  713 lANSFPDGVKHLIAAGEQL---MISDLFQDVLRKRGiHLHNHYGPSETHVVSTYtiHPGDPiPELP-----PIGKPIGCT 784
Cdd:cd17643    205 -DGRDPLALRYVIFGGEALeaaMLRPWAGRFGLDRP-QLVNMYGITETTVHVTF--RPLDA-ADLPaaaasPIGRPLPGL 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  785 DLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFK-PDVIMYRTGDLARRLEDGNIEYIGRADNQVK 863
Cdd:cd17643    280 RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVK 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  864 IRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPL 941
Cdd:cd17643    360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVPLDALPL 439

                          490
                   ....*....|.
gi 1678550997  942 TPNGKVDRAAL 952
Cdd:cd17643    440 TVNGKLDRAAL 450
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1508-1984 2.81e-128

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: 412.56  E-value: 2.81e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRG-VKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFL 1586
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1587 LEDSGTNILLlqsaglhvpeftgeivylnqTNsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNS 1666
Cdd:cd17648     81 LEDTGARVVI--------------------TN---------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1667 LQSRYQLKHSD--MIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLhaflEHI 1744
Cdd:cd17648    126 LSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL----QQY 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1745 KYRSVPiktnRLKRVFSGGEQLGT----HLVSRFYELlpnvsITNSYGPTEATVEAAFFDCPPHEKLERiPIGKPVHHVR 1820
Cdd:cd17648    202 DLARLP----HLKRVDAAGEEFTApvfeKLRSRFAGL-----IINAYGPTETTVTNHKRFFPGDQRFDK-SLGRPVRNTK 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1821 LYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGE-------RMYKTGDVARWLPDGNVEFLGR 1892
Cdd:cd17648    272 CYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQtEQErargrnaRLYKTGDLVRWLPSGELEYLGR 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVR---TDSGEPE----LCAYV---EGLQRNEVRAQLERLLPGYMVPA 1962
Cdd:cd17648    352 NDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedaSQAQSRIqkylVGYYLpepGHVPESDLLSFLRAKLPRYMVPA 431

                          490       500
                   ....*....|....*....|..
gi 1678550997 1963 YMIEMEQWPVTPSGKLDRNALP 1984
Cdd:cd17648    432 RLVRLEGIPVTINGKLDVRALP 453
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 2089-2493 1.32e-125

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: 403.73  E-value: 1.32e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2089 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHD--EVPFTLQ 2166
Cdd:cd19540      3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGG-PYQVVLPaaEARPDLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2167 TTVLGARTEQEAAAAFI-KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR------KLP 2239
Cdd:cd19540     82 VVDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARragrapDWA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2240 ALRIQYKDYAVWQ------EGFKTGDAYKmQEAYWLKQLEGeLP-VLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHK 2312
Cdd:cd19540    162 PLPVQYADYALWQrellgdEDDPDSLAAR-QLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2313 LARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALE 2392
Cdd:cd19540    240 LAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLA 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2393 AFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQASE------GDGNI 2466
Cdd:cd19540    320 AFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGL 399

                          410       420
                   ....*....|....*....|....*..
gi 1678550997 2467 HFLFEYSTALFEKTTIERWASHLTNVL 2493
Cdd:cd19540    400 TGELEYATDLFDRSTAERLADRFVRVL 426
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1058-1460 2.59e-125

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: 402.96  E-value: 2.59e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIH--TEVPFTLS 1134
Cdd:cd19540      3 PLSFAQQRLWFLNRLDgPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPE-DDGGPYQVVLpaAEARPDLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1135 KETTIEGFV---------RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR------QLK 1199
Cdd:cd19540     82 VVDVTEDELaarlaeaarRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARragrapDWA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1200 PLRIQYKDYAVWQQKF----KKGDS-YQKQETYWQQQFSGdLP-ILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRL 1273
Cdd:cd19540    162 PLPVQYADYALWQRELlgdeDDPDSlAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAAL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1274 AHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEA 1353
Cdd:cd19540    241 AREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1354 YEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSE------LF 1427
Cdd:cd19540    321 FAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDAdgapagLT 400

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1678550997 1428 CQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19540    401 GELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 477-953 6.28e-124

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: 399.82  E-value: 6.28e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVSQahlpsslednyiitHPedieskvdgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYT 636
Cdd:cd17649     81 EDSGAGLLLTH--------------HP------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSE-RELAN 715
Cdd:cd17649    129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDRTGD 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 SFPDGVKHLIAAGEQLMISDLFQdvLRKRGIHLHNHYGPSETHVVST-YTIHPGDP-IPELPPIGKPIGCTDLYILNHQK 793
Cdd:cd17649    209 GRPPSLRLYIFGGEALSPELLRR--WLKAPVRLFNAYGPTEATVTPLvWKCEAGAArAGASMPIGRPLGGRSAYILDADL 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  794 QLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPF-KPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQ 872
Cdd:cd17649    287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  873 EIEVTLMNHPDISEAAILIwQDQNGEHELCAYYCSVQKLNTID----LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd17649    367 EIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445


                   ....*
gi 1678550997  949 RAALP 953
Cdd:cd17649    446 RKALP 450
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 7-452 1.79e-120

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: 390.16  E-value: 1.79e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997    7 IQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNV 86
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   87 IVLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYAS 166
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  167 YVNASPITLEPVQPYGKYIKW----LMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKS--RQEHVTFSFSKEESSRL 240
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRsfKGDRLSFTLDEDTEELL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  241 SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQ--GAKTpFLQLIKDMQ 318
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDpkGGKT-FSELIKRVQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  319 KDRLAAEAYSYHPLYEIQSRSAVKQ-----GLIDHILVFENYPVQQEIQmlnkQEHASDLFQIHNFTVA-DETNYSFYLM 392
Cdd:pfam00668  318 EDLLSAEPHQGYPFGDLVNDLRLPRdlsrhPLFDPMFSFQNYLGQDSQE----EEFQLSELDLSVSSVIeEEAKYDLSLT 393

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  393 VAP-GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLI 452
Cdd:pfam00668  394 ASErGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1496-1983 1.33e-119

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: 388.44  E-value: 1.33e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPID 1575
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPEERISFLLEDSGTNILLlqsaglhvpeftgeivylnqtnsglAHRlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEI 1655
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVL-------------------------TSS---------PSDAAYVIFTSGSTGKPKGVVI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1656 EHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPqggEKE-PEVIAKAIEEQKITAMHFVP 1734
Cdd:cd05918    127 EHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPS---EEDrLNDLAGFINRLRVTWAFLTP 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHafleHIKYRSVPiktnRLKRVFSGGEQLGTHLVSRFyelLPNVSITNSYGPTEATVEAAFFDCPPHEKLERIpiGK 1814
Cdd:cd05918    204 SVAR----LLDPEDVP----SLRTLVLGGEALTQSDVDTW---ADRVRLINAYGPAECTIAATVSPVVPSTDPRNI--GR 270

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1815 PVHhVRLYLLNQN--QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY-------PGERMYKTGDVARWLPDG 1885
Cdd:cd05918    271 PLG-ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWlkqegsgRGRRLYRTGDLVRYNPDG 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1886 NVEFLGRTDDQVKIRGYRIEPGEIEAALRS-IEGVREAAVTV---RTDSGEPELCAYVEG-------------------- 1941
Cdd:cd05918    350 SLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVvkpKDGSSSPQLVAFVVLdgsssgsgdgdslflepsde 429

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 1942 LQRN--EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05918    430 FRALvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 465-952 2.23e-119

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: 388.05  E-value: 2.23e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVVsqahlpsslednyiithpedieskvdgsniksVNNADDLLYMIYTSGTTGKPKGVQFEH 624
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVL--------------------------------TSSPSDAAYVIFTSGSTGKPKGVVIEH 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDvpQLFAFINKHQTNIVFLPTAFI 704
Cdd:cd05918    129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPSVA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  705 KMIFSErelanSFPDgVKHLIAAGEQLMisdlfQDVLRK--RGIHLHNHYGPSETHVVSTYtihpGDPIPELPP--IGKP 780
Cdd:cd05918    207 RLLDPE-----DVPS-LRTLVLGGEALT-----QSDVDTwaDRVRLINAYGPAECTIAATV----SPVVPSTDPrnIGRP 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  781 IGCTdLYIL---NHQkQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDP-------FKPDVIMYRTGDLARRLEDG 850
Cdd:cd05918    272 LGAT-CWVVdpdNHD-RLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDG 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  851 NIEYIGRADNQVKIRGYRIEPQEIE--------------VTLMNHPDISEAAILI--------WQDQNGEHELCAYYCSV 908
Cdd:cd05918    350 SLEYVGRKDTQVKIRGQRVELGEIEhhlrqslpgakevvVEVVKPKDGSSSPQLVafvvldgsSSGSGDGDSLFLEPSDE 429

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1678550997  909 QKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05918    430 FRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 2537-3019 5.14e-118

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: 382.04  E-value: 5.14e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2537 QLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPE 2616
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2617 YPKERKRYILSDSGTKLLMTINeadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVEHK 2696
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTD--------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHR 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2697 GIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLlhEEEAKDILAIKhqlsrQRITHMIIVPvlyr 2776
Cdd:cd17653    129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL--ADPSDPFAHVA-----RTVDALMSTP---- 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2777 ALLDVVQPEDVKTLRVVTLAGEAADRELIARSLaicPHTELANEYGPTENSVATTvMRHMEKQAYVSIGQPIDGTQVLIL 2856
Cdd:cd17653    198 SILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECTISST-MTELLPGQPVTIGKPIPNSTCYIL 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRV 2936
Cdd:cd17653    274 DADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2937 ETKEIESVIRCI-KGVKDAAVVAHvtasgQTELSAYvVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:cd17653    354 NLEEIEEVVLQSqPEVTQAAAIVV-----NGRLVAF-VTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427


                   ....
gi 1678550997 3016 RGAL 3019
Cdd:cd17653    428 RKAL 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 2535-3030 5.21e-117

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: 379.92  E-value: 5.21e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmssahhlAYIIYTSGTTGRPKGVMVE 2694
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKGI-ANTLQWRRnAYAFNETDTILQLFSFSFD-GFITSMFTPLLSGAKAVLLHEEEAKDILAikhQLSRQRITHMIIVP 2772
Cdd:COG0318    122 HRNLlANAAAIAA-ALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPRFDPERVLE---LIERERVTVLFGVP 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2773 VLYRALLDVVQ--PEDVKTLRVVTLAGEAADRELIARSLAICpHTELANEYGPTENSVATTVMRHMEKQAY-VSIGQPID 2849
Cdd:COG0318    198 TMLARLLRHPEfaRYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRpGSVGRPLP 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2850 GTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFtqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQV 2929
Cdd:COG0318    277 GVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------RDGWLRTGDLGRLDEDGYLYIVGRKKDMI 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2930 KIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLP 3007
Cdd:COG0318    350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGaeLDAEELRAFLRERLARYKVPRRVEFVDELP 429

                          490       500
                   ....*....|....*....|...
gi 1678550997 3008 LSPNGKLDRGALPKPVYNHEGER 3030
Cdd:COG0318    430 RTASGKIDRRALRERYAAGALEA 452
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 469-952 8.07e-117

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: 378.58  E-value: 8.07e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:cd17653      3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRIRYILHDCGCSHVVSQahlpsslednyiithpedieskvdgsniksvNNADDLLYMIYTSGTTGKPKGVQFEHRNMA 628
Cdd:cd17653     83 SARIQAILRTSGATLLLTT-------------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  629 NLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLhivpeaIKRDVPQLFAFINKHQTNIVFLPTAFIKMif 708
Cdd:cd17653    132 NYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL------VLADPSDPFAHVARTVDALMSTPSILSTL-- 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  709 sereLANSFPDgVKHLIAAGEQLMisdlfQDVLRK--RGIHLHNHYGPSETHVVSTYT-IHPGDPIPelppIGKPIGCTD 785
Cdd:cd17653    204 ----SPQDFPN-LKTIFLGGEAVP-----PSLLDRwsPGRRLYNAYGPTECTISSTMTeLLPGQPVT----IGKPIPNST 269

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  786 LYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIR 865
Cdd:cd17653    270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  866 GYRIEPQEIEVTLM-NHPDISEAAILIWQDQngeheLCAYYcSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPN 944
Cdd:cd17653    350 GFRINLEEIEEVVLqSQPEVTQAAAIVVNGR-----LVAFV-TPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTAN 423


                   ....*...
gi 1678550997  945 GKVDRAAL 952
Cdd:cd17653    424 GKVDRKAL 431
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1499-1983 4.79e-115

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: 373.57  E-value: 4.79e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:cd17653      2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSAglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHR 1658
Cdd:cd17653     82 PSARIQAILRTSGATLLLTTDS---------------------------------PDDLAYIIFTSGSTGIPKGVMVPHR 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1659 SAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLlpqggeKEPE--VIAKAieeQKITAMHFVPSm 1736
Cdd:cd17653    129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSdpFAHVA---RTVDALMSTPS- 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1737 lhaFLEHIKYRSVPiktnRLKRVFSGGEQLGTHLVSRFyelLPNVSITNSYGPTEATVEAAFFDCPPHEkleRIPIGKPV 1816
Cdd:cd17653    199 ---ILSTLSPQDFP----NLKTIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTECTISSTMTELLPGQ---PVTIGKPI 265

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1817 HHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQ 1896
Cdd:cd17653    266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1897 VKIRGYRIEPGEIEA-ALRSIEGVREAAVTVRTDSgepeLCAYV--EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVT 1973
Cdd:cd17653    346 VKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGR----LVAFVtpETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLT 421

                          490
                   ....*....|
gi 1678550997 1974 PSGKLDRNAL 1983
Cdd:cd17653    422 ANGKVDRKAL 431
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 2547-3019 1.23e-112

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: 368.52  E-value: 1.23e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYIL 2626
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2627 SDSGTKLLMTINEADLGVLADFegeILTIESVEEDDKS--PLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQW 2704
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVF---DVLILDLDALAAPapPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2705 RRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVV-- 2782
Cdd:cd12114    158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLea 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2783 QPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMR-HMEKQAYVSI--GQPIDGTQVLILNSN 2859
Cdd:cd12114    238 AQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPiDEVPPDWRSIpyGRPLANQRYRVLDPR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2860 HQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPfkPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETK 2939
Cdd:cd12114    318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELG 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2940 EIESVIRCIKGVKDAAVVAhVTASGQTELSAYVVTKPGLST---NAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd12114    396 EIEAALQAHPGVARAVVVV-LGDPGGKRLAAFVVPDNDGTPiapDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474


                   ...
gi 1678550997 3017 GAL 3019
Cdd:cd12114    475 AAL 477
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 2543-3019 1.28e-112

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: 367.34  E-value: 1.28e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERK 2622
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 RYILSDSGTKLLMtineadlgvladfegeiltiesVEEDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHKGIANTL 2702
Cdd:cd05945     81 REILDAAKPALLI----------------------ADGDD------------NAYIIFTSGSTGRPKGVQISHDNLVSFT 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2703 QWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALL--D 2780
Cdd:cd05945    127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLlsP 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2781 VVQPEDVKTLRVVTLAGEA----ADRELIARSlaicPHTELANEYGPTENSVATTVMRHMEKQAY----VSIGQPIDGTQ 2852
Cdd:cd05945    207 TFTPESLPSLRHFLFCGEVlphkTARALQQRF----PDARIYNTYGPTEATVAVTYIEVTPEVLDgydrLPIGYAKPGAK 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2853 VLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKpeaRMYRTGDAARWMADGTLEYLGRIDDQVKIR 2932
Cdd:cd05945    283 LVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ---RAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2933 GYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLS---TNAVRSELQNKLPVFMHPAFIEKLDSLPLS 3009
Cdd:cd05945    360 GYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEaglTKAIKAELAERLPPYMIPRRFVYLDELPLN 439

                          490
                   ....*....|
gi 1678550997 3010 PNGKLDRGAL 3019
Cdd:cd05945    440 ANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
1500-1900 1.59e-112

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 365.48  E-value: 1.59e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAV-IFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSAGL-----------------HVPEFTGEIVYLNQ-TNSGLAHRLSNPNVDVLPQSLAYV 1640
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealgklevvklvLVLDRDPVLKEEPLpEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1641 IYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQ----LKHSDMIMHKTSYSFDAS-IWELFWWPYAGASVYLLPQGGEKEP 1715
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1716 EVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRsvPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPTEATVe 1795
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPK--RALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTG- 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1796 AAFFDCPPHEKLERIP-IGKPVHHVRLYLLNQN-QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDpfypgeRMY 1873
Cdd:pfam00501  317 VVTTPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GWY 390

                          410       420
                   ....*....|....*....|....*..
gi 1678550997 1874 KTGDVARWLPDGNVEFLGRTDDQVKIR 1900
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1496-1994 1.75e-112

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: 366.83  E-value: 1.75e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPID 1575
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPEERISFLLEDSGTNILLLqsaglhvpeftgeivylnqtnsglahrlsnpnvdvlpqslAYVIYTSGSTGMPKGVEI 1655
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1656 EHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWP-YAGASVYLLPqggEKEPEVIAKAIEEQKITAMHFVP 1734
Cdd:COG0318    121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLVLLP---RFDPERVLELIERERVTVLFGVP 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHAFLEHIKYRsvPIKTNRLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAffdCPPHEKLERIP--I 1812
Cdd:COG0318    198 TMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVT---VNPEDPGERRPgsV 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1813 GKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFlEDPFYpgermyKTGDVARWLPDGNVEFLGR 1892
Cdd:COG0318    272 GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWL------RTGDLGRLDEDGYLYIVGR 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEpELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMI 1965
Cdd:COG0318    345 KKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDekWGE-RVVAFVvlrpgAELDAEELRAFLRERLARYKVPRRVE 423

                          490       500
                   ....*....|....*....|....*....
gi 1678550997 1966 EMEQWPVTPSGKLDRNALPAPGGAADAET 1994
Cdd:COG0318    424 FVDELPRTASGKIDRRALRERYAAGALEA 452
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 2547-3020 1.03e-111

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: 364.80  E-value: 1.03e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKTLTYQELDEWSNGIARALRSRG-VKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYI 2625
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2626 LSDSGTKLLMTineadlgvladfegeiltiesveeddksplpqmsSAHHLAYIIYTSGTTGRPKGVMVEHKGIAN--TLQ 2703
Cdd:cd17648     81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNlrTSL 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2704 WRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPvlyrallDVVQ 2783
Cdd:cd17648    127 SERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTP-------SVLQ 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2784 PEDVK---TLRVVTLAGE---AADRELIARSLAicphTELANEYGPTENSVATTVMRHMEKQAY-VSIGQPIDGTQVLIL 2856
Cdd:cd17648    200 QYDLArlpHLKRVDAAGEeftAPVFEKLRSRFA----GLIINAYGPTETTVTNHKRFFPGDQRFdKSLGRPVRNTKCYVL 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKPE--------ARMYRTGDAARWMADGTLEYLGRIDDQ 2928
Cdd:cd17648    276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQ 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2929 VKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS-----GQTELSAYVVTKPG-LSTNAVRSELQNKLPVFMHPAFIEK 3002
Cdd:cd17648    356 VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVR 435

                          490
                   ....*....|....*...
gi 1678550997 3003 LDSLPLSPNGKLDRGALP 3020
Cdd:cd17648    436 LEGIPVTINGKLDVRALP 453
AMP-binding pfam00501
AMP-binding enzyme;
469-865 2.27e-111

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 362.40  E-value: 2.27e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAV-IDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHY 547
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  548 PADRIRYILHDCGCSHVVSQAHLP--------SSLEDNYIITH------------PEDIESKVDGSNIKSVNNADDLLYM 607
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVldrdpvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  608 IYTSGTTGKPKGVQFEHRNMANLL----KFEYTHSGIDFEADVLQFATPSFDVCYQ-EIFSALLKGGTLHIVPEAIKRDV 682
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  683 PQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDGVKHLIAAGEQLMiSDLFQDVLRKRGIHLHNHYGPSETHVVST 762
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLP-PELARRFRELFGGALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  763 YTIHPGDPIPELPPIGKPIGCTDLYILN-HQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPfkpdviMYRTG 841
Cdd:pfam00501  320 TPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG------WYRTG 393

                          410       420
                   ....*....|....*....|....
gi 1678550997  842 DLARRLEDGNIEYIGRADNQVKIR 865
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 2089-2500 2.90e-111

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: 362.74  E-value: 2.90e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2089 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFeQDEGGDPVQRIHDEVPFTL--- 2165
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF-PEEDGVPYQLILEEDEATPkle 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2166 QTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR------KLP 2239
Cdd:cd19538     82 IKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2240 ALRIQYKDYAVWQEGF---KTGDAYKM--QEAYWLKQLEGeLPV-LDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKL 2313
Cdd:cd19538    162 PLPVQYADYALWQQELlgdESDPDSLIarQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2314 ARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEA 2393
Cdd:cd19538    241 AKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2394 FEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQ-----ASEGDGNIHF 2468
Cdd:cd19538    321 YEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFElreqyNDGTPNGIEG 400

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1678550997 2469 LFEYSTALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19538    401 FIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
AMP-binding pfam00501
AMP-binding enzyme;
2539-2932 6.37e-111

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 360.86  E-value: 6.37e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2539 FEQQAARTPKASALVSGD-KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEY 2617
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2618 PKERKRYILSDSGTKLLMTINEADLGVLADFEG-------------------EILTIESVEEDDKSPLPQMSSAHHLAYI 2678
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGklevvklvlvldrdpvlkeEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2679 IYTSGTTGRPKGVMVEHKGIANTLQW----RRNAYAFNETDTILQLFSFSFD-GFITSMFTPLLSGAKAVLLHEEEAKDI 2753
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDfGLSLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2754 LAIKHQLSRQRITHMIIVPVLYRALLDV--VQPEDVKTLRVVTLAGEAADRELIARSLAICPHtELANEYGPTENS-VAT 2830
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgaPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTgVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2831 TVMRHMEKQAYV-SIGQPIDGTQVLILNSNH-QLQPIGVAGELCIAGTGLARGYVNLPELTERAFTqnpfkpEARMYRTG 2908
Cdd:pfam00501  320 TPLPLDEDLRSLgSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD------EDGWYRTG 393

                          410       420
                   ....*....|....*....|....
gi 1678550997 2909 DAARWMADGTLEYLGRIDDQVKIR 2932
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1058-1460 2.28e-110

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: 360.04  E-value: 2.28e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLdEGV--AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTE----VPF 1131
Cdd:cd19538      3 PLSFAQRRLWFLHQL-EGPsaTYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPE-EDGVPYQLILEEdeatPKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1132 TLSK------ETTIEGFVR-PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR------QL 1198
Cdd:cd19538     81 EIKEvdeeelESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapEL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1199 KPLRIQYKDYAVWQQKFKKGDSYQ-----KQETYWQQQFSGdLP-ILELPTDKRRPAERQFIGGKVTFQLDKEITARIKR 1272
Cdd:cd19538    161 APLPVQYADYALWQQELLGDESDPdsliaRQLAYWKKQLAG-LPdEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1273 LAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALE 1352
Cdd:cd19538    240 LAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1353 AYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEH-----DSELF 1427
Cdd:cd19538    320 AYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQyndgtPNGIE 399

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1678550997 1428 CQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19538    400 GFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1504-1983 1.46e-108

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: 355.40  E-value: 1.46e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLlqsaglhvpeftgeivylnqtnsglahrlsnpnvdVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNF 1663
Cdd:cd05945     81 REILDAAKPALLI-----------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1664 LNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEH 1743
Cdd:cd05945    126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLS 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1744 IKYrsVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPH--EKLERIPIGKPVHHVRL 1821
Cdd:cd05945    206 PTF--TPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEvlDGYDRLPIGYAKPGAKL 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1822 YLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRG 1901
Cdd:cd05945    284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNG 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1902 YRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYVEG------LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTP 1974
Cdd:cd05945    361 YRIELEEIEAALRQVPGVKEAVVVPKYKGeKVTELIAFVVPkpgaeaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNA 440


                   ....*....
gi 1678550997 1975 SGKLDRNAL 1983
Cdd:cd05945    441 NGKIDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 473-952 1.83e-107

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: 352.32  E-value: 1.83e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVsqahlpsslednyiithpedieskVDGsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNMANLLK 632
Cdd:cd05945     81 REILDAAKPALLI------------------------ADG---------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTN 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  633 FEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERE 712
Cdd:cd05945    128 WMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPT 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  713 LANSFPDGVKHLIAAGEQLMISDLfqDVLRKR--GIHLHNHYGPSETHVVSTYTIHPGDPIPELP--PIGKPIGCTDLYI 788
Cdd:cd05945    208 FTPESLPSLRHFLFCGEVLPHKTA--RALQQRfpDARIYNTYGPTEATVAVTYIEVTPEVLDGYDrlPIGYAKPGAKLVI 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  789 LNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYR 868
Cdd:cd05945    286 LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQR---AYRTGDLVRLEADGLLFYRGRLDFQVKLNGYR 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  869 IEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYC---SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNG 945
Cdd:cd05945    363 IELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkpGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANG 442


                   ....*..
gi 1678550997  946 KVDRAAL 952
Cdd:cd05945    443 KIDRKAL 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 477-953 1.60e-106

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: 349.78  E-value: 1.60e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVR-QEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYI 555
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 LHDcgcshvvSQAHLpsslednyIITHPEdieskvdgsniksvnnadDLLYMIYTSGTTGKPKGVQFEHRNMANL---LK 632
Cdd:cd17648     81 LED-------TGARV--------VITNST------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLrtsLS 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  633 FEYTHSGIDFEAdVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQ-TNIVFLPTafikmIFSER 711
Cdd:cd17648    128 ERYFGRDNGDEA-VLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKvTYLSGTPS-----VLQQY 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  712 ELANSfpDGVKHLIAAGEQLMISDLfqDVLRKR-GIHLHNHYGPSETHVVSTYTIHPGDPiPELPPIGKPIGCTDLYILN 790
Cdd:cd17648    202 DLARL--PHLKRVDAAGEEFTAPVF--EKLRSRfAGLIINAYGPTETTVTNHKRFFPGDQ-RFDKSLGRPVRNTKCYVLN 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  791 HQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPD--------VIMYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:cd17648    277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQV 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHE-----LCAYY-CSVQKLNTIDLRSYMASELPEYMIPAKWIWV 936
Cdd:cd17648    357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYlPEPGHVPESDLLSFLRAKLPRYMVPARLVRL 436

                          490
                   ....*....|....*..
gi 1678550997  937 DSIPLTPNGKVDRAALP 953
Cdd:cd17648    437 EGIPVTINGKLDVRALP 453
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 465-954 2.64e-104

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: 343.33  E-value: 2.64e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVVSqahlpsslednyiithpedieskvdgsniksvnnaddlLYMIYTSGTTGKPKGVQFEH 624
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNMANLLKFEYTHSGIDfEADVLQFATPSFDV--CYQEIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFLPTA 702
Cdd:COG0318    123 RNLLANAAAIAAALGLT-PGDVVLVALPLFHVfgLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPT 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  703 FIKMIFSERELANSFPDGVKHLIAAGEQLMIsDLFQDVLRKRGIHLHNHYGPSETHVVSTYTihPGDPIPELP-PIGKPI 781
Cdd:COG0318    199 MLARLLRHPEFARYDLSSLRLVVSGGAPLPP-ELLERFEERFGVRIVEGYGLTETSPVVTVN--PEDPGERRPgSVGRPL 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  782 GCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSsDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQ 861
Cdd:COG0318    276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGW------LRTGDLGRLDEDGYLYIVGRKKDM 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  862 VKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSV--QKLNTIDLRSYMASELPEYMIPAKWIWVDSI 939
Cdd:COG0318    349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDEL 428

                          490
                   ....*....|....*
gi 1678550997  940 PLTPNGKVDRAALPE 954
Cdd:COG0318    429 PRTASGKIDRRALRE 443
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 477-952 7.49e-104

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: 343.10  E-value: 7.49e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYT 636
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  637 HSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNI-VFLPtAFIKMIFSERELAN 715
Cdd:cd12114    161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLwNSVP-ALLEMLLDVLEAAQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 SFPDGVKhliaageQLMIS------DLfQDVLRKR--GIHLHNHYGPSETHVVSTYtiHP-GDPIPELPPI--GKPIGCT 784
Cdd:cd12114    240 ALLPSLR-------LVLLSgdwiplDL-PARLRALapDARLISLGGATEASIWSIY--HPiDEVPPDWRSIpyGRPLANQ 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  785 DLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPfkPDVIMYRTGDLARRLEDGNIEYIGRADNQVKI 864
Cdd:cd12114    310 RYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKV 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  865 RGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHeLCAYYCSVQKLNTI---DLRSYMASELPEYMIPAKWIWVDSIPL 941
Cdd:cd12114    388 RGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKR-LAAFVVPDNDGTPIapdALRAFLAQTLPAYMIPSRVIALEALPL 466

                          490
                   ....*....|.
gi 1678550997  942 TPNGKVDRAAL 952
Cdd:cd12114    467 TANGKVDRAAL 477
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1228-2085 4.43e-102

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: 362.85  E-value: 4.43e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1228 WQQQFSgDLPILELPTDKRRPAERQFIGGKVTFQLDKEitarikRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIG-- 1305
Cdd:TIGR03443    2 WSERLD-NPTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGts 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1306 SPIAGRPhadleavlgmfvntLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNP-LFDTTL 1384
Cdd:TIGR03443   75 SNKSGRP--------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAF 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1385 VLQNMEQQKlkmndvqlqwNDLEHPISkfDISLYVTEHDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASPETEL 1464
Cdd:TIGR03443  141 QDAPDNQQT----------TYSTGSTT--DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPI 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1465 DNIPILTkEEERDFIE--SCHLfEETGYsmNQTLHYALEQQAEKTPDQAAVI----FEDG-----VMTYKELNEQANRIA 1533
Cdd:TIGR03443  209 GKVSLIT-PSQKSLLPdpTKDL-DWSGF--RGAIHDIFADNAEKHPDRTCVVetpsFLDPssktrSFTYKQINEASNILA 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1534 WELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILL-LQSAGLHVP------- 1605
Cdd:TIGR03443  285 HYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIvIEKAGTLDQlvrdyid 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1606 ---EFTGEIVYLNQTNSG--LAHRLSNPNVDVLPQSLAY------VI----------YTSGSTGMPKGVEIEHRSAVNFL 1664
Cdd:TIGR03443  365 kelELRTEIPALALQDDGslVGGSLEGGETDVLAPYQALkdtptgVVvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYF 444

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1665 NSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSM---LHAfl 1741
Cdd:TIGR03443  445 PWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMgqlLSA-- 522

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1742 ehikYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPH-------EKLER-IPIG 1813
Cdd:TIGR03443  523 ----QATTPIPS--LHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRssdstflKNLKDvMPAG 596

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1814 KPVHHVRLYLLNQNQRMLP--VGCIGELYIAGAGVARGYLNRPALTEERFL--------------------EDPFY--PG 1869
Cdd:TIGR03443  597 KGMKNVQLLVVNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkennkpEREFWlgPR 676

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1870 ERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAY---------- 1938
Cdd:TIGR03443  677 DRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDkDEEPTLVSYivpqdksdel 756

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1939 ----------------VEGLQR-----NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALP----------APG 1987
Cdd:TIGR03443  757 eefksevddeessdpvVKGLIKyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdtaqlaavAKN 836

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1988 GAADAETYTAprNVTEMKLSQLWEDVLKNGP--VGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKDVFAHPTVEGLA 2065
Cdd:TIGR03443  837 RSASAADEEF--TETEREIRDLWLELLPNRPatISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFA 914

                          970       980
                   ....*....|....*....|....*
gi 1678550997 2066 TVIR-----EGTDSPYEAIKPAEKQ 2085
Cdd:TIGR03443  915 KEVDrlkkgEELADEGDSEIEEEET 939
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 3116-3589 6.93e-96

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: 319.28  E-value: 6.93e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3116 VEGDVQWSPVQK--WFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQYNRPLSHS 3193
Cdd:pfam00668    1 VQDEYPLSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3194 DdalygLQMIDLSAPDGTDGNRPYEPLIKRhvlDIQQKMDLKNGPLLQAGLF-HTIDGDFLFLSAHHLVVDGISWRVLLE 3272
Cdd:pfam00668   81 E-----LEIIDISDLSESEEEEAIEAFIQR---DLQSPFDLEKGPLFRAGLFrIAENRHHLLLSMHHIIVDGVSLGILLR 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3273 DLALGYRQAAGGEDIKLPPKTSsFKAYAKKLSDYAESQQLMKQLKYWRE--AEEYQTEALPFDQIDgTRAHEGQRSTISF 3350
Cdd:pfam00668  153 DLADLYQQLLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEqlEGELPVLQLPKDYAR-PADRSFKGDRLSF 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3351 TLnDKETAALLKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREdvlkGIDVSRTIGWFTAIYPLLIKLNA 3430
Cdd:pfam00668  231 TL-DEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP----SPDIERMVGMFVNTLPLRIDPKG 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3431 DlpdseESMVHVLKTTKDTLRRV-PDKGFGYGVIKYLTP-PGKKDINFTGAPEISF-NYLGQFEsgrtaevpEEDAFSFS 3507
Cdd:pfam00668  306 G-----KTFSELIKRVQEDLLSAePHQGYPFGDLVNDLRlPRDLSRHPLFDPMFSFqNYLGQDS--------QEEEFQLS 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3508 PLGAGGDISTTWNREQSLDISAIAAEGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQE 3587
Cdd:pfam00668  373 ELDLSVSSVIEEEAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQK 452


                   ..
gi 1678550997 3588 LT 3589
Cdd:pfam00668  453 LL 454
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1058-1460 1.67e-94

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: 314.32  E-value: 1.67e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQLDEG-VAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRI---------HT 1127
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGgPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEIlppgpapleVR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1128 EVPFTLSK-ETTIEGFVR-----PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQ---- 1197
Cdd:cd19539     83 DLSDPDSDrERRLEELLReresrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1198 --LKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGdLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAH 1275
Cdd:cd19539    163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1276 KNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYE 1355
Cdd:cd19539    242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1356 HQDYPFEELVDKLGVQREMSRNPLFDTTLVLQN---MEQQKLKMNDVQLQWndLEHPISKFDISLYVTEHDSELFCQFEY 1432
Cdd:cd19539    322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNapaGELELAGGLSYTEGS--DIPDGAKFDLNLTVTEEGTGLRGSLGY 399

                          410       420
                   ....*....|....*....|....*...
gi 1678550997 1433 STALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19539    400 ATSLFDEETIQGFLADYLQVLRQLLANP 427
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 2089-2493 1.38e-91

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: 305.84  E-value: 1.38e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2089 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPFTLQTT 2168
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2169 VLGARTEQEAAAAFI-------KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRK---- 2237
Cdd:cd19539     83 DLSDPDSDRERRLEEllreresRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2238 --LPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGeLPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLAR 2315
Cdd:cd19539    163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2316 ENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFE 2395
Cdd:cd19539    242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2396 HQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLH-DLQMKPAQVSHLVSKFDLTLQASEGDGNIHFLFEYST 2474
Cdd:cd19539    322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAgGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYAT 401

                          410
                   ....*....|....*....
gi 1678550997 2475 ALFEKTTIERWASHLTNVL 2493
Cdd:cd19539    402 SLFDEETIQGFLADYLQVL 420
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 10-433 2.95e-91

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: 304.37  E-value: 2.95e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNVIVL 89
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 EEDITHLNEAEQSqfIEQWKEKDRDRGFHLQKDVLMRIALI-QTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYV 168
Cdd:cd19536     81 ELDLTPLEEQLDP--LRAYKEETKIRRFDLGRAPLVRAALVrKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  169 NASPITLEPVQPYGKYIKWLMEQ-DKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKSRQEHVTFsFSKEESSRLSELAARE 247
Cdd:cd19536    159 EYKPLSLPPAQPYRDFVAHERASiQQAASERYWREYLAGATLATLPALSEAVGGGPEQDSELL-VSVPLPVRSRSLAKRS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  248 EVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQGAKTPFLQLIKDMQKDRLAAEAY 327
Cdd:cd19536    238 GIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETVEDLLKRAQEQELESLSH 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  328 SYHPLYEIQSRSAvKQGLIDHILVFENYPVQQEIQmLNKQEHASDLFQIHNFTVadeTNYSFYLMVAP-GEEIHIKMNYD 406
Cdd:cd19536    318 EQVPLADIQRCSE-GEPLFDSIVNFRHFDLDFGLP-EWGSDEGMRRGLLFSEFK---SNYDVNLSVLPkQDRLELKLAYN 392

                          410       420
                   ....*....|....*....|....*..
gi 1678550997  407 AEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19536    393 SQVLDEEQAQRLAAYYKSAIAELATAP 419
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 2090-2322 1.97e-81

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 269.22  E-value: 1.97e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2090 VSSAQKRIYVLqqlEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPFTLQTTV 2169
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE-PVQRIDPDADLPLEVVD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2170 LG--------ARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR----- 2236
Cdd:COG4908     77 LSalpepereAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALlegep 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2237 -KLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLAR 2315
Cdd:COG4908    157 pPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236


                   ....*..
gi 1678550997 2316 ENGSTLY 2322
Cdd:COG4908    237 AHGATVN 243
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 2088-2500 2.28e-80

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: 273.52  E-value: 2.28e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2088 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQdEGGDPVQRIHDEVPFTL-- 2165
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCE-EAGRYEQVVLDKTVRFRie 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2166 -----QTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYN-----N 2235
Cdd:cd19066     81 iidlrNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDaaerqK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2236 RKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLAR 2315
Cdd:cd19066    161 PTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVAR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2316 ENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFE 2395
Cdd:cd19066    241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2396 HQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNdYEPLHLHDLQMKPAQVSHLV--SKFDLTLQASEG-DGNIHFLFEY 2472
Cdd:cd19066    321 HQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNN-QQQLGKTGGFIFTTPVYTSSegTVFDLDLEASEDpDGDLLLRLEY 399

                          410       420
                   ....*....|....*....|....*...
gi 1678550997 2473 STALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19066    400 SRGVYDERTIDRFAERYMTALRQLIENP 427
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
469-952 6.29e-80

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 274.85  E-value: 6.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRIRYILHDCGCSHVVSQAHLPSSLEDNYIIThPEDIESKVDGSNIKSVNNA---DDLLYMIYTSGTTGKPKGVQFEHr 625
Cdd:PRK04813    88 AERIEMIIEVAKPSLIIATEELPLEILGIPVIT-LDELKDIFATGNPYDFDHAvkgDDNYYIIFTSGTTGKPKGVQISH- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  626 nmANLLKFeyTHSGI-DFE-ADVLQF---ATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNI-VFL 699
Cdd:PRK04813   166 --DNLVSF--TNWMLeDFAlPEGPQFlnqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVwVST 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  700 PTaFIKMIFSEREL-ANSFPDgVKHLIAAGEQLMISDlfQDVLRKR--GIHLHNHYGPSETHV-VSTYTIHPgDPIPELP 775
Cdd:PRK04813   242 PS-FADMCLLDPSFnEEHLPN-LTHFLFCGEELPHKT--AKKLLERfpSATIYNTYGPTEATVaVTSIEITD-EMLDQYK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  776 --PIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPdviMYRTGDLARrLEDGNIE 853
Cdd:PRK04813   317 rlPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQP---AYHTGDAGY-LEDGLLF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  854 YIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQKLNTID--------LRSYMASELP 925
Cdd:PRK04813   393 YQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYV--VPKEEDFErefeltkaIKKELKERLM 470

                          490       500
                   ....*....|....*....|....*..
gi 1678550997  926 EYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK04813   471 EYMIPRKFIYRDSLPLTPNGKIDRKAL 497
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 465-954 1.64e-79

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


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 273.56  E-value: 1.64e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEkQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:TIGR01734    3 IEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHP--EDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQF 622
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSalEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  623 EHrnmANLLKFeyTHSGI-DF----EADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIV 697
Cdd:TIGR01734  162 SH---DNLVSF--TNWMLaDFplseGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVW 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  698 FLPTAFIKMI-----FSERELANsfpdgVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIP 772
Cdd:TIGR01734  237 VSTPSFVDMClldpnFNQENYPH-----LTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILD 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  773 ELP--PIG--KPIgcTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPdviMYRTGDLARrLE 848
Cdd:TIGR01734  312 QYPrlPIGfaKPD--MNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHEGQP---AYRTGDAGT-IT 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  849 DGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEHELCAYycSVQKLN--------TIDLRSY 919
Cdd:TIGR01734  386 DGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVpKYNKDHKVEYLIAA--IVPETEdfekefqlTKAIKKE 463

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997  920 MASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:TIGR01734  464 LKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1056-1460 4.49e-78

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: 266.87  E-value: 4.49e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1056 TYPVSSAQKRIYVLQQLDEGV-AYNMPAVLELEGALDVAKLSAVCKELISRHePLRTSFVSGADDEPVQRIHTEVPFTLS 1134
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMsAYNVPLCFRFSSKLDVEKFKQACQFVLEQH-PILKSVIEEEDGVPFQKIEPSKPLSFQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1135 -------KETTIEGFVR-----PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYanRQL---K 1199
Cdd:cd20484     80 eedisslKESEIIAYLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAY--QALlqgK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1200 PLRIQ-----YKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLA 1274
Cdd:cd20484    158 QPTLAsspasYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1275 HKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAY 1354
Cdd:cd20484    238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1355 EHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMeQQKLKMNDVQLQWND---LE-----HPISKFDISLYVTEHDSEL 1426
Cdd:cd20484    318 DHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF-LQSTSLQQFLAEYQDvlsIEfvegiHQEGEYELVLEVYEQEDRF 396

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1678550997 1427 FCQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd20484    397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1057-1460 4.90e-78

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: 266.58  E-value: 4.90e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1057 YPVSSAQKRIYVLQQLDEG-VAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADD------EPVQRIHTEV 1129
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDpSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRyeqvvlDKTVRFRIEI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1130 pFTLSKETTIEGFV---------RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLY--ANRQL 1198
Cdd:cd19066     82 -IDLRNLADPEARLlelidqiqqTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYdaAERQK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1199 K---PLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAH 1275
Cdd:cd19066    161 PtlpPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVAR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1276 KNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYE 1355
Cdd:cd19066    241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1356 HQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDLEHPI-SKFDISLYVTEH-DSELFCQFEYS 1433
Cdd:cd19066    321 HQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEgTVFDLDLEASEDpDGDLLLRLEYS 400

                          410       420
                   ....*....|....*....|....*..
gi 1678550997 1434 TALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19066    401 RGVYDERTIDRFAERYMTALRQLIENP 427
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1499-1983 1.22e-76

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 265.22  E-value: 1.22e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:PRK04813     7 TIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILL----LQSAGLHVPEFTGEIVylnqTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVE 1654
Cdd:PRK04813    87 PAERIEMIIEVAKPSLIIateeLPLEILGIPVITLDEL----KDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQ 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 IEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIweLFWWP--YAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHF 1732
Cdd:PRK04813   163 ISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSV--MDLYPtlASGGTLVALPKDMTANFKQLFETLPQLPINVWVS 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1733 VPS------MLHAFLEHikyrsvpiKTNRLKRVFSGGEQLgTH-----LVSRFyellPNVSITNSYGPTEATV------- 1794
Cdd:PRK04813   241 TPSfadmclLDPSFNEE--------HLPNLTHFLFCGEEL-PHktakkLLERF----PSATIYNTYGPTEATVavtsiei 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1795 --EAAffdcpphEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEdpfYPGERM 1872
Cdd:PRK04813   308 tdEML-------DQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPA 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1873 YKTGDVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA-AVTVRTDSGEPELCAYV---EGLQRNE-- 1946
Cdd:PRK04813   378 YHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAvVVPYNKDHKVQYLIAYVvpkEEDFEREfe 456

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1678550997 1947 ----VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK04813   457 ltkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 1499-1983 1.64e-76

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


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 264.70  E-value: 1.64e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:TIGR01734    5 AIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNiLLLQSAGLHVPEFTGEIVYLNQT----NSGLAHRLSNPnvdVLPQSLAYVIYTSGSTGMPKGVE 1654
Cdd:TIGR01734   85 PSERIEMIIEAAGPE-LVIHTAELSIDAVGTQIITLSALeqaeTSGGPVSFDHA---VKGDDNYYIIYTSGSTGNPKGVQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 IEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVP 1734
Cdd:TIGR01734  161 ISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHAFL--EHIKYRSVPiktnRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEA-------AFFDcpphe 1805
Cdd:TIGR01734  241 SFVDMCLldPNFNQENYP----HLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVtsvkitqEILD----- 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1806 KLERIPIG--KPvhHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLedpFYPGERMYKTGDVARwLP 1883
Cdd:TIGR01734  312 QYPRLPIGfaKP--DMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-IT 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1884 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEP--ELCAYV---------EGLQRNEVRAQLE 1952
Cdd:TIGR01734  386 DGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKveYLIAAIvpetedfekEFQLTKAIKKELK 465

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1678550997 1953 RLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:TIGR01734  466 KSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2539-3023 5.60e-76

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 263.29  E-value: 5.60e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2539 FEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYP 2618
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2619 KERKRYILSDSGTKLLMTINEADLGVLadfEGEILTIESVEED---DKSPLPQMS-SAHHLAYIIYTSGTTGRPKGVMVE 2694
Cdd:PRK04813    88 AERIEMIIEVAKPSLIIATEELPLEIL---GIPVITLDELKDIfatGNPYDFDHAvKGDDNYYIIFTSGTTGKPKGVQIS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVL 2774
Cdd:PRK04813   165 HDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSF 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2775 YR-ALLDvvqP----EDVKTLRVVTLAGEA----ADRELIARSlaicPHTELANEYGPTENSVATT---VMRHM-EKQAY 2841
Cdd:PRK04813   245 ADmCLLD---PsfneEHLPNLTHFLFCGEElphkTAKKLLERF----PSATIYNTYGPTEATVAVTsieITDEMlDQYKR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2842 VSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQnpFKPEaRMYRTGDAARwMADGTLEY 2921
Cdd:PRK04813   318 LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT--FDGQ-PAYHTGDAGY-LEDGLLFY 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2922 LGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGL------STNAVRSELQNKLPVFM 2995
Cdd:PRK04813   394 QGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDferefeLTKAIKKELKERLMEYM 473

                          490       500
                   ....*....|....*....|....*...
gi 1678550997 2996 HPAFIEKLDSLPLSPNGKLDRGALPKPV 3023
Cdd:PRK04813   474 IPRKFIYRDSLPLTPNGKIDRKALIEEV 501
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1056-1460 8.10e-76

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: 260.08  E-value: 8.10e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1056 TYPVSSAQKRIYVLQQ-LDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSF-VSGADDEPVQRIHTEVPFTL 1133
Cdd:cd19532      1 TEPMSFGQSRFWFLQQyLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLASSPLRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1134 ------SKETTIEGF----VRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKPLRI 1203
Cdd:cd19532     81 ehvqisDEAEVEEEFerlkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1204 QYKDYAVWQQKFKKGDSYQKQETYWQQQFSGD---LPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRST 1280
Cdd:cd19532    161 QYLDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1281 ---LYmtlLALYSAFLSRLSGQDDIVIGspI--AGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYE 1355
Cdd:cd19532    241 pfhFY---LAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1356 HQDYPFEELVDKLGVQREMSRNPLFDTTL--VLQNMEQQKL---KMNDVqlQWNDLEHPiskFDISLYVTEHDS-----E 1425
Cdd:cd19532    316 HSRVPFDVLLDELGVPRSATHSPLFQVFInyRQGVAESRPFgdcELEGE--EFEDARTP---YDLSLDIIDNPDgdcllT 390

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1678550997 1426 LFCQfeysTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19532    391 LKVQ----SSLYSEEDAELLLDSYVNLLEAFARDP 421
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1637-1979 1.26e-75

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: 256.06  E-value: 1.26e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1637 LAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGgekEPE 1716
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1717 VIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIktNRLKRVFSGGEQLGTHLVSRFYELlPNVSITNSYGPTEATVEA 1796
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDL--SSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1797 AFfdCPPHEKLERIP-IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFledpfypGERMYKT 1875
Cdd:cd04433    156 AT--GPPDDDARKPGsVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRT 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1876 GDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVE-----GLQRNEVR 1948
Cdd:cd04433    227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPewGE-RVVAVVVlrpgaDLDAEELR 305

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1678550997 1949 AQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 1979
Cdd:cd04433    306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 2674-3015 2.13e-75

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: 255.67  E-value: 2.13e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 HLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDI 2753
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2754 LAIkhqLSRQRITHMIIVPVLYRALLDV--VQPEDVKTLRVVTLAGEAADRELIARSLAIcPHTELANEYGPTENSVATT 2831
Cdd:cd04433     81 LEL---IEREKVTILLGVPTLLARLLKApeSAGYDLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTVA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2832 VMR-HMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFtqnpfkpEARMYRTGDA 2910
Cdd:cd04433    157 TGPpDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDL 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQ 2988
Cdd:cd04433    230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGadLDAEELRAHVR 309

                          330       340
                   ....*....|....*....|....*..
gi 1678550997 2989 NKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:cd04433    310 ERLAPYKVPRRVVFVDALPRTASGKID 336
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1058-1455 2.74e-74

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: 255.65  E-value: 2.74e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRIYVLQQ-LDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGaDDEPVQRIHTEVPFTLSK- 1135
Cdd:cd20483      3 PMSTFQRRLWFLHNfLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEG-DDFGEQQVLDDPSFHLIVi 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1136 --------ETTIEGFVR-----PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLY---ANRQ-- 1197
Cdd:cd20483     82 dlseaadpEAALDQLVRnlrrqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalRAGRdl 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1198 --LKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSG--DLPILeLPTDKR-RPAERQFIGGKVTFQLDKEITARIKR 1272
Cdd:cd20483    162 atVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipDASKL-LPFAKAeRPPVKDYERSTVEATLDKELLARMKR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1273 LAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALE 1352
Cdd:cd20483    241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1353 AYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQ------NMEQQKLKMNDVqlqwnDLEHPISKFDISLYVTEH-DSE 1425
Cdd:cd20483    321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgkfpEYDTGDFKFTDY-----DHYDIPTACDIALEAEEDpDGG 395

                          410       420       430
                   ....*....|....*....|....*....|
gi 1678550997 1426 LFCQFEYSTALFEKETIQRWASLFTTLVEH 1455
Cdd:cd20483    396 LDLRLEFSTTLYDSADMERFLDNFVTFLTS 425
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 2534-3021 5.00e-74

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: 258.17  E-value: 5.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI 2613
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 DPEYPKERKRYILSDSGTKLLMT------INEADLGVLADFEGEILTIESVEEDDKSPLPQMSS------------AH-- 2673
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTsserldLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASwpkllalgdadpPHpv 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 ---HLAYIIYTSGTTGRPKGVMVEHK----GIANTLQWRRNayafNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLH 2746
Cdd:TIGR03098  161 idsDMAAILYTSGSTGRPKGVVLSHRnlvaGAQSVATYLEN----RPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2747 EEEAKDILAIkhqLSRQRITHMIIVPVLYRAL--LDvVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPT 2824
Cdd:TIGR03098  237 YLLPRDVLKA---LEKHGITGLAAVPPLWAQLaqLD-WPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLT 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2825 ENSVATT-----VMRHMEkqayvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNP-F 2898
Cdd:TIGR03098  313 EAFRSTYlppeeVDRRPD-----SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpF 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2899 KPEARMYRT----GDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV--VAHVTaSGQTelSAYV 2972
Cdd:TIGR03098  388 PGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfgVPDPT-LGQA--IVLV 464

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 2973 VTKPG---LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPK 3021
Cdd:TIGR03098  465 VTPPGgeeLDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1059-1282 5.27e-74

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 247.64  E-value: 5.27e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1059 VSSAQKRIYVLQQldEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPFTLS---- 1134
Cdd:COG4908      1 LSPAQKRFLFLEP--GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVE-EDGEPVQRIDPDADLPLEvvdl 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1135 -------KETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR------ 1196
Cdd:COG4908     78 salpepeREAELEELVaeeasRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALlegepp 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 QLKPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIKRLAHK 1276
Cdd:COG4908    158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237


                   ....*.
gi 1678550997 1277 NRSTLY 1282
Cdd:COG4908    238 HGATVN 243
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 2088-2500 6.50e-74

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: 254.44  E-value: 6.50e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2088 YPVSSAQKRIYvLQQLEDGGTG-YNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPFTLQ 2166
Cdd:cd19543      2 YPLSPMQEGML-FHSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2167 TTVLGARTEQEAAAAF--------IKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYN---- 2234
Cdd:cd19543     81 ELDLSHLSEAEQEAELealaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalge 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2235 --NRKLPALRiQYKDYAVWQEGFKTGDAykmqEAYWLKQLEG--ELPVldLPADHARPPVRSFAGDKVSFTLEPEVASGL 2310
Cdd:cd19543    161 gqPPSLPPVR-PYRDYIAWLQRQDKEAA----EAYWREYLAGfeEPTP--LPKELPADADGSYEPGEVSFELSAELTARL 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2311 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRE 2388
Cdd:cd19543    234 QELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQA 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2389 TALEAFEHQNYPFEELvdkleLTRDMSRNPVFDAMLVVQN----------NDYEPLHLHDLQMkpAQVSHlvskFDLTLQ 2458
Cdd:cd19543    314 QQLELREHEYVPLYEI-----QAWSEGKQALFDHLLVFENypvdesleeeQDEDGLRITDVSA--EEQTN----YPLTVV 382

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 2459 ASEGDGnIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19543    383 AIPGEE-LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 2535-3019 6.76e-74

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: 255.95  E-value: 6.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMTInEADLGVLADFEGEILTIESVEEDdksplpqmssahhLAYIIYTSGTTGRPKGVMVE 2694
Cdd:cd05936     81 PLYTPRELEHILNDSGAKALIVA-VSFTDLLAAGAPLGERVALTPED-------------VAVLQYTSGTTGVPKGAMLT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKGI-ANTLQWRRNAYAFNETD----TILQLF-SFsfdGFITSMFTPLLSGAKAVLLHEEEAKDILaikHQLSRQRITHM 2768
Cdd:cd05936    147 HRNLvANALQIKAWLEDLLEGDdvvlAALPLFhVF---GLTVALLLPLALGATIVLIPRFRPIGVL---KEIRKHRVTIF 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2769 IIVPVLYRALLDV--VQPEDVKTLRVVTLAGEAADRELIARSLAI--CPhteLANEYGPTENSVATTVMRHMEKQAYVSI 2844
Cdd:cd05936    221 PGVPTMYIALLNApeFKKRDFSSLRLCISGGAPLPVEVAERFEELtgVP---IVEGYGLTETSPVVAVNPLDGPRKPGSI 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2845 GQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmyRTGDAARWMADGTLEYLGR 2924
Cdd:cd05936    298 GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVDR 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2925 IDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEK 3002
Cdd:cd05936    371 KKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGasLTEEEIIAFCREQLAGYKVPRQVEF 450

                          490
                   ....*....|....*..
gi 1678550997 3003 LDSLPLSPNGKLDRGAL 3019
Cdd:cd05936    451 RDELPKSAVGKILRREL 467
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 2268-3119 2.07e-73

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: 273.09  E-value: 2.07e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2268 WLKQLEGeLPVLDLPADHARPPVRSFAGDKVSFTLEPEVAsglhklARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSp 2347
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2348 iagRPHKDLEPilgmfvntLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVq 2427
Cdd:TIGR03443   74 ---SSNKSGRP--------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFRLAFQ- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2428 nndyeplHLHDLQMKPAQVSHLVskfDLTLQASEGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHI 2507
Cdd:TIGR03443  142 -------DAPDNQQTTYSTGSTT---DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKV 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2508 DILTQEERHQLLNEfnTGQANQYG-VQTISQLFEQQAAR---------TPKASALVSGDKTLTYQELDEWSNGIARALRS 2577
Cdd:TIGR03443  212 SLITPSQKSLLPDP--TKDLDWSGfRGAIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNILAHYLLK 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2578 RGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEAdlGVLADF-------EG 2650
Cdd:TIGR03443  290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKA--GTLDQLvrdyidkEL 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2651 EILT-IESVE-EDDKS----PLPQMSS---AHHLAY----------------IIYTSGTTGRPKGVMVEHKGIANTLQWR 2705
Cdd:TIGR03443  368 ELRTeIPALAlQDDGSlvggSLEGGETdvlAPYQALkdtptgvvvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFPWM 447

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2706 RNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKavlLHEEEAKDI-----LAIKHQLSRQRITHMI----------- 2769
Cdd:TIGR03443  448 AKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQ---LLVPTADDIgtpgrLAEWMAKYGATVTHLTpamgqllsaqa 524

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2770 --IVPVLYRALL--DVVQPEDVktLRVVTLAgeaadreliarslaicPHTELANEYGPTENSVAT---TVMRHMEKQAYV 2842
Cdd:TIGR03443  525 ttPIPSLHHAFFvgDILTKRDC--LRLQTLA----------------ENVCIVNMYGTTETQRAVsyfEIPSRSSDSTFL 586

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2843 S-------IGQPIDGTQVLILNSNHQLQPIGVA--GELCIAGTGLARGYVNLPELTERAFTQNPF--------------- 2898
Cdd:TIGR03443  587 KnlkdvmpAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennk 666

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2899 -------KPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEI-----------ESV--IRCIKGVKDAAVVA 2958
Cdd:TIGR03443  667 perefwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIdthlsqhplvrENVtlVRRDKDEEPTLVSY 746

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2959 HVTASGQTELSAYVVTKPGLSTNA---------------VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKP- 3022
Cdd:TIGR03443  747 IVPQDKSDELEEFKSEVDDEESSDpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPd 826

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3023 ------VYNHEGERPFLPPSSKMEQILADIWKEVL--GAEKIGTADSFFELGGDSIKALQVsarLHRIGKQMAVK----D 3090
Cdd:TIGR03443  827 taqlaaVAKNRSASAADEEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRM---IFELRKKLNVElplgL 903

                          970       980
                   ....*....|....*....|....*....
gi 1678550997 3091 LFSHPTIQELAAYIrDSDTSSSQAAVEGD 3119
Cdd:TIGR03443  904 IFKSPTIKGFAKEV-DRLKKGEELADEGD 931
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2087-2431 7.09e-73

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: 251.22  E-value: 7.09e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2087 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEG-GDPVQRIHDEVPFTL 2165
Cdd:cd19532      1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdGEPMQGVLASSPLRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2166 QTtvLGARTEQEAAAAFIK----PFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRKLPAL 2241
Cdd:cd19532     81 EH--VQISDEAEVEEEFERlknhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2242 RIQYKDYAVWQ-EGFKTGdayKMQE--AYWLKQLEGE---LPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLAR 2315
Cdd:cd19532    159 PLQYLDFAARQrQDYESG---ALDEdlAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASR 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2316 ENGSTLYMVLLAAYTAFLSRLSGQEDIIVGspI--AGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEA 2393
Cdd:cd19532    236 KLRVTPFHFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAA 313

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1678550997 2394 FEHQNYPFEELVDKLELTRDMSRNPVFDAMLvvqnnDY 2431
Cdd:cd19532    314 LAHSRVPFDVLLDELGVPRSATHSPLFQVFI-----NY 346
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2087-2500 5.20e-72

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: 249.16  E-value: 5.20e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2087 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPFTLQ 2166
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV-PFQKIEPSKPLSFQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2167 TTVLGARTEQEAAAaFI-----KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELY-------N 2234
Cdd:cd20484     80 EEDISSLKESEIIA-YLrekakEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallqgkQ 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2235 NRKLPALRIqYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKLA 2314
Cdd:cd20484    159 PTLASSPAS-YYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2315 RENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAF 2394
Cdd:cd20484    238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2395 EHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNNdYEPLHLHDLQMKPAQVSH--LVSK------FDLTLQASEGDGNI 2466
Cdd:cd20484    318 DHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF-LQSTSLQQFLAEYQDVLSieFVEGihqegeYELVLEVYEQEDRF 396

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1678550997 2467 HFLFEYSTALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd20484    397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2089-2486 1.16e-69

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: 242.55  E-value: 1.16e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2089 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDeGGDPVQRIHDEVPFTLqtT 2168
Cdd:cd20483      3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEG-DDFGEQQVLDDPSFHL--I 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2169 VLGARTEQEAAAAF--------IKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRK--- 2237
Cdd:cd20483     80 VIDLSEAADPEAALdqlvrnlrRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRagr 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2238 ----LPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLD-LP-ADHARPPVRSFAGDKVSFTLEPEVASGLH 2311
Cdd:cd20483    160 dlatVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKlLPfAKAERPPVKDYERSTVEATLDKELLARMK 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2312 KLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETAL 2391
Cdd:cd20483    240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2392 EAFEHQNYPFEELVDKLELTRDMSRNPVFD---------AMLVVQNNDYEPLHLHDLQMKPAqvshlvskFDLTLQASE- 2461
Cdd:cd20483    320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQiavnyqvhgKFPEYDTGDFKFTDYDHYDIPTA--------CDIALEAEEd 391

                          410       420
                   ....*....|....*....|....*
gi 1678550997 2462 GDGNIHFLFEYSTALFEKTTIERWA 2486
Cdd:cd20483    392 PDGGLDLRLEFSTTLYDSADMERFL 416
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 236-1117 1.57e-69

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


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 260.38  E-value: 1.57e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  236 ESSRLSElAAREEVTLSTIFH---TIWGILLQKYNNNDDAVFGSvisgrPAEIEGIEHMVGLFINtmpvrvqgAKTPFLQ 312
Cdd:TIGR03443   31 YSLQLPS-AEVTAGGGSTPFIillAAFAALVYRLTGDEDIVLGT-----SSNKSGRPFVLRLNIT--------PELSFLQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  313 LIKDMQKDRLAAEAYSYHPLYEIQSRSAVKQGLidhilvfENYPVQQEIQMLNKQEhasdlFQIHNFTVADETNYSFYLM 392
Cdd:TIGR03443   97 LYAKVSEEEKEGASDIGVPFDELSEHIQAAKKL-------ERTPPLFRLAFQDAPD-----NQQTTYSTGSTTDLTVFLT 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  393 VAPGE-EIHIKMNYDAEQHDRsfVLSVKEHLLNAVSQILNNPNLPPEEIDITTDTEKRQLigeiTDQTPVYE------TI 465
Cdd:TIGR03443  165 PSSPElELSIYYNSLLFSSDR--ITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLL----PDPTKDLDwsgfrgAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  466 HAMFEKQAEKTPDAHAVIDQACSL---------TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKA 536
Cdd:TIGR03443  239 HDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  537 GGAIVPVDPHYPADRIRYILhdcGCSH-----VVSQAHLPSSLEDNYI------ITHPEDIESKVDGSNI--KSVNNADD 603
Cdd:TIGR03443  319 GATFSVIDPAYPPARQTIYL---SVAKpraliVIEKAGTLDQLVRDYIdkelelRTEIPALALQDDGSLVggSLEGGETD 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  604 LL---------------------YMIYTSGTTGKPKGVQFEHRNMA----------NLLKFE-YTH-SGIdfEADVLQfa 650
Cdd:TIGR03443  396 VLapyqalkdtptgvvvgpdsnpTLSFTSGSEGIPKGVLGRHFSLAyyfpwmakrfGLSENDkFTMlSGI--AHDPIQ-- 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  651 tpsfdvcyQEIFSALLKGGTLHiVPEAIKRDVP-QLFAFINKHQTNIVFLPTAfikmifserelansfpdgVKHLIAAGE 729
Cdd:TIGR03443  472 --------RDMFTPLFLGAQLL-VPTADDIGTPgRLAEWMAKYGATVTHLTPA------------------MGQLLSAQA 524

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  730 QLMISDLFQ-----DVLRKR----------GIHLHNHYGPSETH-VVSTYTIHP--GDP-----IPELPPIGKPIGCTDL 786
Cdd:TIGR03443  525 TTPIPSLHHaffvgDILTKRdclrlqtlaeNVCIVNMYGTTETQrAVSYFEIPSrsSDStflknLKDVMPAGKGMKNVQL 604

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  787 YILNHQKQLQPCGVP--GELYISGASVARGYVNHDKLTSDKFSSDPFKPDVI----------------------MYRTGD 842
Cdd:TIGR03443  605 LVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkperefwlgprdrLYRTGD 684

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  843 LARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQKLNTI-------- 914
Cdd:TIGR03443  685 LGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYI--VPQDKSDeleefkse 762

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  915 ----------------------DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPD------ASISGNPYTA 966
Cdd:TIGR03443  763 vddeessdpvvkglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaqlaaVAKNRSASAA 842

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  967 PRNL--LEAKLSQLFEDVLKN--GHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLAliiREAEQ 1042
Cdd:TIGR03443  843 DEEFteTEREIRDLWLELLPNrpATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFA---KEVDR 919

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1043 nLYAAIEPAEKRDTYPVSSAQkriyvlqqldegvaynmpaVLELEGALDVAKLSA-VCKELISRHEPL----RTSFVSGA 1117
Cdd:TIGR03443  920 -LKKGEELADEGDSEIEEEET-------------------VLELDYAKDAKTLVDsLPKSYPSRKELDastpITVFLTGA 979
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 1495-1985 2.00e-69

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: 244.69  E-value: 2.00e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI 1574
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1575 DPDYPEERISFLLEDSGTNILLLQSAGL-----------------HVPEFTGEIVYLNQTNSGLAHRL-----SNPNVDV 1632
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLdllhpalpgchdlrtliIVGDPAHASEGHPGEEPASWPKLlalgdADPPHPV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1633 LPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASV----YLLP 1708
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLLP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1709 QggekepEVIaKAIEEQKITAMHFVPSmLHAFLEHIKYRsvPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYG 1788
Cdd:TIGR03098  241 R------DVL-KALEKHGITGLAAVPP-LWAQLAQLDWP--ESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYG 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1789 PTEAtVEAAFFdcPPhEKLERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF 1866
Cdd:TIGR03098  311 LTEA-FRSTYL--PP-EEVDRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPP 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1867 YPG-----ERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA--------------VTVR 1927
Cdd:TIGR03098  387 FPGelhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVafgvpdptlgqaivLVVT 466

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 1928 TDSGEPelcayvegLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:TIGR03098  467 PPGGEE--------LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 2535-3019 4.88e-68

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


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 240.05  E-value: 4.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQqAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:TIGR01734    3 IEAIQAF-AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMTINEADLGVLadfEGEILTIESVE--EDDKSPLPQMS--SAHHLAYIIYTSGTTGRPKG 2690
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAELSIDAV---GTQIITLSALEqaETSGGPVSFDHavKGDDNYYIIYTSGSTGNPKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2691 VMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMII 2770
Cdd:TIGR01734  159 VQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2771 VPVLYR-ALLD-VVQPEDVKTLRVVTLAGE----AADRELIARslaiCPHTELANEYGPTENSVATT---VMRHMEKQ-A 2840
Cdd:TIGR01734  239 TPSFVDmCLLDpNFNQENYPHLTHFLFCGEelpvKTAKALLER----FPKATIYNTYGPTEATVAVTsvkITQEILDQyP 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2841 YVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFtqnpFKPEA-RMYRTGDAARwMADGTL 2919
Cdd:TIGR01734  315 RLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEGqPAYRTGDAGT-ITDGQL 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2920 EYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTE-LSAYVVTKPG------LSTNAVRSELQNKLP 2992
Cdd:TIGR01734  390 FYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKVEyLIAAIVPETEdfekefQLTKAIKKELKKSLP 469

                          490       500
                   ....*....|....*....|....*..
gi 1678550997 2993 VFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:TIGR01734  470 AYMIPRKFIYRDQLPLTANGKIDRKAL 496
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1057-1460 9.88e-67

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: 233.63  E-value: 9.88e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1057 YPVSSAQKRIYVLQQLDEGV-AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPFTL-- 1133
Cdd:cd19543      2 YPLSPMQEGMLFHSLLDPGSgAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWre 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1134 ---------SKETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYA----- 1194
Cdd:cd19543     82 ldlshlseaEQEAELEALAeedreRGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgeg 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1195 -NRQLKPLRiQYKDYAVWQQKFKKGDSyqkqETYWQQQFSG--DLPilELPTDKRRPAERQFIGGKVTFQLDKEITARIK 1271
Cdd:cd19543    162 qPPSLPPVR-PYRDYIAWLQRQDKEAA----EAYWREYLAGfeEPT--PLPKELPADADGSYEPGEVSFELSAELTARLQ 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1272 RLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPhADL---EAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQ 1348
Cdd:cd19543    235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELpgiETMVGLFINTLPVRVRLDPDQTVLELLKDLQA 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1349 TALEAYEHQDYPfeeLVDklgVQR-EMSRNPLFDTTLVLQN----------MEQQKLKMNDVQLQwndlEHpiSKFDISL 1417
Cdd:cd19543    314 QQLELREHEYVP---LYE---IQAwSEGKQALFDHLLVFENypvdesleeeQDEDGLRITDVSAE----EQ--TNYPLTV 381

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 1418 YVTEhDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19543    382 VAIP-GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1521-1986 3.60e-66

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: 235.49  E-value: 3.60e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERisflledsgtnilllQSA 1600
Cdd:cd17647     22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR---------------QNI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 GLHVPEFTGEIVylnqtnsglahrLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM 1680
Cdd:cd17647     87 YLGVAKPRGLIV------------IRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1681 HKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHikyRSVPIKTnrLKRVF 1760
Cdd:cd17647    155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQ---ATTPFPK--LHHAF 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1761 SGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCP-----PH--EKLER-IPIGKPVHHVRLYLLNQNQR--M 1830
Cdd:cd17647    230 FVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPsrssdPTflKNLKDvMPAGRGMLNVQLLVVNRNDRtqI 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1831 LPVGCIGELYIAGAGVARGYLNRPALTEERFLED--------------------PFY--PGERMYKTGDVARWLPDGNVE 1888
Cdd:cd17647    310 CGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWlgPRDRLYRTGDLGRYLPNGDCE 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1889 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAY---------------------------VE 1940
Cdd:cd17647    390 CCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDkDEEPTLVSYivprfdkpddesfaqedvpkevstdpiVK 469

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 1941 GLQR-----NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAP 1986
Cdd:cd17647    470 GLIGyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 2539-3016 1.40e-64

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: 227.88  E-value: 1.40e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2539 FEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYP 2618
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2619 KERKRYILSDSGTKLLMtineadlgvladfegeiltiesveeDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHKGI 2698
Cdd:cd17631     81 PPEVAYILADSGAKVLF-------------------------DD------------LALLMYTSGTTGRPKGAMLTHRNL 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2699 -ANTLQWRrNAYAFNETDTILQLFSFsFDGFITSMFTP--LLSGAKAVLLHEEEAKDILAikhQLSRQRITHMIIVPVLY 2775
Cdd:cd17631    124 lWNAVNAL-AALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVILRKFDPETVLD---LIERHRVTSFFLVPTMI 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2776 RALLDVVQPE--DVKTLRVVTLAGEAADRELIARSLAIcpHTELANEYGPTENSVATTVMR---HMEKQAyvSIGQPIDG 2850
Cdd:cd17631    199 QALLQHPRFAttDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSpedHRRKLG--SAGRPVFF 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2851 TQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmyRTGDAARWMADGTLEYLGRIDDQVK 2930
Cdd:cd17631    275 VEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMII 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2931 IRGYRVETKEIESVIRCIKGVKDAAVVA--------HVTasgqtelsAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFI 3000
Cdd:cd17631    348 SGGENVYPAEVEDVLYEHPAVAEVAVIGvpdekwgeAVV--------AVVVPRPGaeLDEDELIAHCRERLARYKIPKSV 419

                          490
                   ....*....|....*.
gi 1678550997 3001 EKLDSLPLSPNGKLDR 3016
Cdd:cd17631    420 EFVDALPRNATGKILK 435
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 603-948 1.14e-63

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: 221.78  E-value: 1.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  603 DLLYMIYTSGTTGKPKGVQFEHRNMANLLKFeYTHSGIDFEADVLQFATPSFDVCYQ-EIFSALLKGGTLHIVPeaiKRD 681
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHIGGLfGLLGALLAGGTVVLLP---KFD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  682 VPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDGVKHLIAAGEQlMISDLFQDVLRKRGIHLHNHYGPSETHVVS 761
Cdd:cd04433     77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAP-LPPELLERFEEAPGIKLVNGYGLTETGGTV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  762 TyTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTsdkfssDPFKPDvIMYRTG 841
Cdd:cd04433    156 A-TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEAT------AAVDED-GWYRTG 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  842 DLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAY--YCSVQKLNTIDLRSY 919
Cdd:cd04433    228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVvvLRPGADLDAEELRAH 307

                          330       340
                   ....*....|....*....|....*....
gi 1678550997  920 MASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd04433    308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
2557-3019 1.86e-63

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 228.84  E-value: 1.86e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:COG0365     38 RTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 ----------------INEA--------------DLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTG 2686
Cdd:COG0365    118 adgglrggkvidlkekVDEAleelpslehvivvgRTGADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTG 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2687 RPKGVMVEHKGIANTLQWR-RNAYAFNETDTIlqlFSFSfD-GFIT----SMFTPLLSGAkAVLLHEE-----EAKDILA 2755
Cdd:COG0365    198 KPKGVVHTHGGYLVHAATTaKYVLDLKPGDVF---WCTA-DiGWATghsyIVYGPLLNGA-TVVLYEGrpdfpDPGRLWE 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2756 IkhqLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAADRELIARSLAI--CPhteLANEYGPTE---- 2825
Cdd:COG0365    273 L---IEKYGVTVFFTAPTAIRALMkagdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAvgVP---IVDGWGQTEtggi 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2826 --NSVATTVMRhmekqaYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAG--TGLARGYVNLPELTERAFtqnpFKPE 2901
Cdd:COG0365    347 fiSNLPGLPVK------PGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETY----FGRF 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2902 ARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLS-T 2980
Cdd:COG0365    417 PGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEpS 496

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 2981 NAVRSELQN----KLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:COG0365    497 DELAKELQAhvreELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1500-1983 5.29e-63

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: 224.36  E-value: 5.29e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:cd05936      5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSAGLHV---PEFTGEIVYLNqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIE 1656
Cdd:cd05936     85 PRELEHILNDSGAKALIVAVSFTDLlaaGAPLGERVALT------------------PEDVAVLQYTSGTTGVPKGAMLT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1657 HRsavNFL-NSLQSRYQLKHS----DMIM------HktSYSFDASiweLFWWPYAGASVYLLPQggeKEPEVIAKAIEEQ 1725
Cdd:cd05936    147 HR---NLVaNALQIKAWLEDLlegdDVVLaalplfH--VFGLTVA---LLLPLALGATIVLIPR---FRPIGVLKEIRKH 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1726 KITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAFfdCPPHE 1805
Cdd:cd05936    216 RVTIFPGVPTMYIALLNAPEFKKRDFSS--LRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAV--NPLDG 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1806 klERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLP 1883
Cdd:cd05936    291 --PRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDE 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1884 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT--VRTDSGEpELCAYV-----EGLQRNEVRAQLERLLP 1956
Cdd:cd05936    362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvPDPYSGE-AVKAFVvlkegASLTEEEIIAFCREQLA 440

                          490       500
                   ....*....|....*....|....*..
gi 1678550997 1957 GYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05936    441 GYKVPRQVEFRDELPKSAVGKILRREL 467
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 2087-2500 6.28e-63

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: 222.63  E-value: 6.28e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2087 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPFTLQ 2166
Cdd:cd19533      1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGE-PYQWIDPYTPVPIR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2167 -TTVLGARTEQEAA-----AAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRK--- 2237
Cdd:cd19533     80 hIDLSGDPDPEGAAqqwmqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLkgr 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2238 -------LPALRIQYKDYAvwqegFKTGDAYKMQEAYWLKQLEGELPVLDLpADhaRPPVRSFAGDKVSFTLEPEVASGL 2310
Cdd:cd19533    160 pappapfGSFLDLVEEEQA-----YRQSERFERDRAFWTEQFEDLPEPVSL-AR--RAPGRSLAFLRRTAELPPELTRTL 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2311 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 2390
Cdd:cd19533    232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2391 LEAFEHQNYPFEELVDKLELTRDmsRNPVFDAMLVVQNNDYePLHLHDLQMKPAQVSHLVSKfDLTLQASE--GDGNIHF 2468
Cdd:cd19533    312 RSLLRHQRYRYEDLRRDLGLTGE--LHPLFGPTVNYMPFDY-GLDFGGVVGLTHNLSSGPTN-DLSIFVYDrdDESGLRI 387

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1678550997 2469 LFEYSTALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19533    388 DFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1490-1983 3.57e-61

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 220.83  E-value: 3.57e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1490 YSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGG 1569
Cdd:PRK06187     2 QDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1570 AYLPIDPDYPEERISFLLEDSGTNILLLQSAglHVPEFTG---------EIVYLNQT----NSGLAHRLSN--------- 1627
Cdd:PRK06187    82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSE--FVPLLAAilpqlptvrTVIVEGDGpaapLAPEVGEYEEllaaasdtf 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1628 PNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAvnFLNSLQSRYQLK--HSDMIMHKTSYsFDASIWelfWWPY----AG 1701
Cdd:PRK06187   160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL--FLHSLAVCAWLKlsRDDVYLVIVPM-FHVHAW---GLPYlalmAG 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1702 AS-VYLlpqgGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIkyRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLpN 1780
Cdd:PRK06187   234 AKqVIP----RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAP--RAYFVDFSSLRLVIYGGAALPPALLREFKEKF-G 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1781 VSITNSYGPTEA--TVEAAFfdcPPHEKLERIPI----GKPVHHVRLYLLNQNQRMLPV--GCIGELYIAGAGVARGYLN 1852
Cdd:PRK06187   307 IDLVQGYGMTETspVVSVLP---PEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWN 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1853 RPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGE 1932
Cdd:PRK06187   384 RPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI-----GV 451

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1933 P------ELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK06187   452 PdekwgeRPVAVVvlkpgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 467-952 1.45e-60

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: 217.43  E-value: 1.45e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  467 AMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPH 546
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  547 YPADRIRYILHDCGCSHVVSQAHLPSSLEDnyiithPEDIESKVdgsniksVNNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:cd05936     83 YTPRELEHILNDSGAKALIVAVSFTDLLAA------GAPLGERV-------ALTPEDVAVLQYTSGTTGVPKGAMLTHRN 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 M-ANLLKFEYTHSGIDFEADVLQFATP-----SFDVCYqeiFSALLKGGTLHIVPEAikrDVPQLFAFINKHQ-TNIVFL 699
Cdd:cd05936    150 LvANALQIKAWLEDLLEGDDVVLAALPlfhvfGLTVAL---LLPLALGATIVLIPRF---RPIGVLKEIRKHRvTIFPGV 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  700 PTAFIKMI-FSERELANsfPDGVKHLIAAGEQLMIsDLFQDVLRKRGIHLHNHYGPSETHVVSTYT-----IHPGDpipe 773
Cdd:cd05936    224 PTMYIALLnAPEFKKRD--FSSLRLCISGGAPLPV-EVAERFEELTGVPIVEGYGLTETSPVVAVNpldgpRKPGS---- 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  774 lppIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimyRTGDLARRLEDGNIE 853
Cdd:cd05936    297 ---IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFF 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  854 YIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYycsV-----QKLNTIDLRSYMASELPEYM 928
Cdd:cd05936    367 IVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAF---VvlkegASLTEEEIIAFCREQLAGYK 443

                          490       500
                   ....*....|....*....|....
gi 1678550997  929 IPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05936    444 VPRQVEFRDELPKSAVGKILRREL 467
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1500-1980 1.14e-59

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: 213.63  E-value: 1.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLlqsaglhvpeftgeivylnqtnsglahrlsnpnvdvlpQSLAYVIYTSGSTGMPKGVEIEHRs 1659
Cdd:cd17631     81 PPEVAYILADSGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHR- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1660 avNFLNSLQSryQLKHSDMIMHKTSYS----FDASIWELFWWP--YAGASVYLLPqggEKEPEVIAKAIEEQKITAMHFV 1733
Cdd:cd17631    122 --NLLWNAVN--ALAALDLGPDDVLLVvaplFHIGGLGVFTLPtlLRGGTVVILR---KFDPETVLDLIERHRVTSFFLV 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1734 PSMLHAFLEHIKYRSVpiKTNRLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTEATVEAAFFdcPPHEKLERI-PI 1812
Cdd:cd17631    195 PTMIQALLQHPRFATT--DLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFL--SPEDHRRKLgSA 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1813 GKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGR 1892
Cdd:cd17631    269 GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDR 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRAQLERLLPGYMVPAYMI 1965
Cdd:cd17631    342 KKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEkwGE-AVVAVVvprPGaeLDEDELIAHCRERLARYKIPKSVE 420

                          490
                   ....*....|....*
gi 1678550997 1966 EMEQWPVTPSGKLDR 1980
Cdd:cd17631    421 FVDALPRNATGKILK 435
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1056-1460 4.56e-58

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: 208.38  E-value: 4.56e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1056 TYPVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIHTEVPF--- 1131
Cdd:cd19533      1 RLPLTSAQRGVWFAEQLDpEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTE-EEGEPYQWIDPYTPVpir 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1132 --TLSKETTIEGFVR---------PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLY----ANR 1196
Cdd:cd19533     80 hiDLSGDPDPEGAAQqwmqedlrkPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 QLKP------LRIQYKDyavwqQKFKKGDSYQKQETYWQQQFsGDLPilELPTDKRRPAERQFIGGKVTFQLDKEITARI 1270
Cdd:cd19533    160 PAPPapfgsfLDLVEEE-----QAYRQSERFERDRAFWTEQF-EDLP--EPVSLARRAPGRSLAFLRRTAELPPELTRTL 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1271 KRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTA 1350
Cdd:cd19533    232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1351 LEAYEHQDYPFEELVDKLGvqREMSRNPLFDTTLVLQNMEQQkLKMNDVQLQWNDLEHPISKfDISLYVTEHD--SELFC 1428
Cdd:cd19533    312 RSLLRHQRYRYEDLRRDLG--LTGELHPLFGPTVNYMPFDYG-LDFGGVVGLTHNLSSGPTN-DLSIFVYDRDdeSGLRI 387

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1678550997 1429 QFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19533    388 DFDANPALYSGEDLARHQERLLRLLEEAAADP 419
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1055-1460 5.85e-58

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


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 208.87  E-value: 5.85e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1055 DTYPVSSAQKRIYVLQQLDEGV-AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDePVQRIH------T 1127
Cdd:cd19546      3 DEVPATAGQLRTWLLARLDEETrGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGD-VHQRILdadaarP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1128 EVPFTLSKETTIEGFV-----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR------ 1196
Cdd:cd19546     82 ELPVVPATEEELPALLadraaHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrap 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 QLKPLRIQYKDYAVWQQKFKKGDSYQK-----QETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTFQLDKEITARIK 1271
Cdd:cd19546    162 ERAPLPLQFADYALWERELLAGEDDRDsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1272 RLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRP-HADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTA 1350
Cdd:cd19546    242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1351 LEAYEHQDYPFEELVDKLGVQREMSRNPLFDTTLVLQNMEQQK--------LKMNDVqlqwnDLEHPISKFDISLYVTEH 1422
Cdd:cd19546    322 REARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPwdapelpgLRTSPV-----PLGTEAMELDLSLALTER 396

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 1423 DSE------LFCQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19546    397 RNDdgdpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2560-3020 2.20e-57

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: 206.37  E-value: 2.20e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2560 TYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLlmtine 2639
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL------ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2640 adlgVLADfegeiltiesveeddksplpqmssahhLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTIL- 2718
Cdd:cd05934     79 ----VVVD---------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLt 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2719 QLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAikhQLSRQRITHMIIVPVLYRALLdvVQPEDVK----TLRVVT 2794
Cdd:cd05934    128 VLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWS---DVRRYGATVTNYLGAMLSYLL--AQPPSPDdrahRLRAAY 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2795 LAGEAAD--RELIARSlaicpHTELANEYGPTENSVATTVMRHmEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELC 2872
Cdd:cd05934    203 GAPNPPElhEEFEERF-----GVRLLEGYGMTETIVGVIGPRD-EPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELV 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2873 I---AGTGLARGYVNLPELTERAFtqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIK 2949
Cdd:cd05934    277 IrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHP 349

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 2950 GVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALP 3020
Cdd:cd05934    350 AVREAAVVAVPDEVGEDEVKAVVVLRPGetLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 2089-2500 2.39e-57

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


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 206.95  E-value: 2.39e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2089 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDeGGDPVQRIHDEVPFTLQTT 2168
Cdd:cd19546      6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGD-GGDVHQRILDADAARPELP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2169 VLGArTEQEA----AAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNR---KLP-- 2239
Cdd:cd19546     85 VVPA-TEEELpallADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregRAPer 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2240 -ALRIQYKDYAVWQEGFKTG--DAYKM---QEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLEPEVASGLHKL 2313
Cdd:cd19546    164 aPLPLQFADYALWERELLAGedDRDSLigdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEA 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2314 ARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHK-DLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALE 2392
Cdd:cd19546    244 AESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVRE 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2393 AFEHQNYPFEELVDKLELTRDMSRNPVFDAMLVVQNND---YEPLHLHDLQMKPAQVSHLVSKFDLTLQASEG------- 2462
Cdd:cd19546    324 ARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDndpWDAPELPGLRTSPVPLGTEAMELDLSLALTERrnddgdp 403

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1678550997 2463 ---DGNIHflfeYSTALFEKTTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19546    404 dglDGSLR----YAADLFDRATAAALARRLVRVLEQVAADP 440
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 10-432 1.06e-56

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: 203.69  E-value: 1.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLlqKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSP-QQVVLRErnviv 88
Cdd:cd19542      1 IYPCTPMQEGMLLSQL--RSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKS----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   89 LEEDITHLNEAEQSQFIEQWKEKDRDRGFhlqKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLhiyASYV 168
Cdd:cd19542     74 LDPPIEEVETDEDSLDALTRDLLDDPTLF---GQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLA---AAYN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  169 NASPitlEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGHEQqTVLPKQKKTKGKSRQEHVTFSFSKEessrLSELAAREE 248
Cdd:cd19542    148 GQLL---PPAPPFSDYISYLQSQSQEESLQYWRKYLQGASP-CAFPSLSPKRPAERSLSSTRRSLAK----LEAFCASLG 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  249 VTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDMQKDRLAAEAY 327
Cdd:cd19542    220 VTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKlDPDWTVLDLLRQLQQQYLRSLPH 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  328 SYHPLYEIQ--SRSAVKQGLIDHILVFENYPVQQEiqmlnkqehaSDLFQIHNFTVADETNYSFYLM----VAPGEEIHI 401
Cdd:cd19542    300 QHLSLREIQraLGLWPSGTLFNTLVSYQNFEASPE----------SELSGSSVFELSAAEDPTEYPVavevEPSGDSLKV 369

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1678550997  402 KMNYDaeqhdrSFVLSVK--EHLLNAVSQILNN 432
Cdd:cd19542    370 SLAYS------TSVLSEEqaEELLEQFDDILEA 396
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 2532-3019 2.09e-56

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 206.29  E-value: 2.09e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2532 VQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYV 2611
Cdd:PRK07656     4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPEYPKERKRYILSDSGTKLLMTINEAdLGVLADFEGEILTIESV----EEDDKSPLPQMSS-----AHH-------- 2674
Cdd:PRK07656    84 PLNTRYTADEAAYILARGDAKALFVLGLF-LGVDYSATTRLPALEHVviceTEEDDPHTEKMKTftdflAAGdpaerape 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 -----LAYIIYTSGTTGRPKGVMVEHKgiaNTLqwrRNAYAF------NETDTILQL--FSFSFdGFITSMFTPLLSGAK 2741
Cdd:PRK07656   163 vdpddVADILFTSGTTGRPKGAMLTHR---QLL---SNAADWaeylglTEGDRYLAAnpFFHVF-GYKAGVNAPLMRGAT 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2742 AVLLHEEEAKDILAIkhqLSRQRITHMIIVPVLYRALLDVVQ--PEDVKTLRVVTLAGEAADRELIARSLAICPHTELAN 2819
Cdd:PRK07656   236 ILPLPVFDPDEVFRL---IETERITVLPGPPTMYNSLLQHPDrsAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLT 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2820 EYGPTENSVATTVMRHMEKQAYV--SIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAftqnp 2897
Cdd:PRK07656   313 GYGLSEASGVTTFNRLDDDRKTVagTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA----- 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2898 FKPEARMYrTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhV--TASGQTeLSAYVVTK 2975
Cdd:PRK07656   388 IDADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG-VpdERLGEV-GKAYVVLK 464

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1678550997 2976 PG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK07656   465 PGaeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 2529-3019 2.52e-56

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 206.58  E-value: 2.52e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2529 QYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGG 2608
Cdd:PRK06187     2 QDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2609 CYVPIDPEYPKERKRYILSDSGTKLLMtINEADLGVLADFEGEILTIESV---EEDDKSPLPQMSSAHH----------- 2674
Cdd:PRK06187    82 VLHPINIRLKPEEIAYILNDAEDRVVL-VDSEFVPLLAAILPQLPTVRTViveGDGPAAPLAPEVGEYEellaaasdtfd 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 --------LAYIIYTSGTTGRPKGVMVEHKGI-ANTLQ---WRRnayaFNETDTILQlfsfsfdgfITSMF--------- 2733
Cdd:PRK06187   161 fpdidendAAAMLYTSGTTGHPKGVVLSHRNLfLHSLAvcaWLK----LSRDDVYLV---------IVPMFhvhawglpy 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2734 TPLLSGAKAVLLHEEEAKDILaikHQLSRQRITHMIIVPVLYRALLD--VVQPEDVKTLRVVTLAGEAADRELIARSLAI 2811
Cdd:PRK06187   228 LALMAGAKQVIPRRFDPENLL---DLIETERVTFFFAVPTIWQMLLKapRAYFVDFSSLRLVIYGGAALPPALLREFKEK 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2812 CpHTELANEYGPTENSVATTVMR---HMEKQAYV--SIGQPIDGTQVLILNSNHQLQP--IGVAGELCIAGTGLARGYVN 2884
Cdd:PRK06187   305 F-GIDLVQGYGMTETSPVVSVLPpedQLPGQWTKrrSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWN 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2885 LPELTERAFtqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhV--TA 2962
Cdd:PRK06187   384 RPEATAETI-------DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIG-VpdEK 455

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2963 SGQTELsAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06187   456 WGERPV-AVVVLKPGatLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 11-433 3.10e-56

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: 203.41  E-value: 3.10e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   11 YPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFIsQNVSSPQQVVLRERNVIVLE 90
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVVLDKTVRFRIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   91 E-DITHLNEAEQSqfIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVN 169
Cdd:cd19066     81 IiDLRNLADPEAR--LLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 ASPITLEPVQPYGKYIKWLMEQDKEQA----VSYWDHYLSGHEQQTVLPKQKKTKGKSRQE--HVTFSFSKEESSRLSEL 243
Cdd:cd19066    159 QKPTLPPPVGSYADYAAWLEKQLESEAaqadLAYWTSYLHGLPPPLPLPKAKRPSQVASYEvlTLEFFLRSEETKRLREV 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  244 AAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQGAKTP-FLQLIKDMQKDRL 322
Cdd:cd19066    239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDAtFPELLKRTKEQSR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  323 AAEAYSYHPLYEIQSRSAVKQG-----LIDHILVFENYPvqqeiQMLNKQEHASDLFQIHnfTVADETNYSFYLMVAPGE 397
Cdd:cd19066    317 EAIEHQRVPFIELVRHLGVVPEapkhpLFEPVFTFKNNQ-----QQLGKTGGFIFTTPVY--TSSEGTVFDLDLEASEDP 389

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1678550997  398 --EIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19066    390 dgDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
PRK05691 PRK05691
peptide synthase; Validated
 2533-3402 4.50e-56

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 218.50  E-value: 4.50e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALV------SGDKTLTYQELDEWSNGIARALRSRGVKPDTPVgIMMHRSFSMIASILGVWKA 2606
Cdd:PRK05691     9 LTLVQALQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDP-----EYPKERKRYILSDSGTKLLMTIneadlgvlADFEGEILTIESVEEDDKSPL--------------- 2666
Cdd:PRK05691    88 GVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTV--------ADLRDSLLQMEELAAANAPELlcvdtldpalaeawq 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2667 -PQMSsAHHLAYIIYTSGTTGRPKGVMVEHKG-IANTLQWRRN-AYAFNETDTILQLFSFSFD-GFITSMFTPLLSGAKA 2742
Cdd:PRK05691   160 ePALQ-PDDIAFLQYTSGSTALPKGVQVSHGNlVANEQLIRHGfGIDLNPDDVIVSWLPLYHDmGLIGGLLQPIFSGVPC 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2743 VLLH-----EEEAKDILAIKH-------------QLSRQRITHmiivpvlyrallDVVQPEDVKTLRVVTLAGEAADR-- 2802
Cdd:PRK05691   239 VLMSpayflERPLRWLEAISEyggtisggpdfayRLCSERVSE------------SALERLDLSRWRVAYSGSEPIRQds 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2803 -ELIARSLAIC---PHTELANeYGPTENSVATTVMR--------HMEKQAY-------------VSIGQPIDGTQVLILN 2857
Cdd:PRK05691   307 lERFAEKFAACgfdPDSFFAS-YGLAEATLFVSGGRrgqgipalELDAEALarnraepgtgsvlMSCGRSQPGHAVLIVD 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2858 SNH-QLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNpfkpEARMY-RTGDAArWMADGTLEYLGRIDDQVKIRGYR 2935
Cdd:PRK05691   386 PQSlEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGRTWlRTGDLG-FLRDGELFVTGRLKDMLIVRGHN 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2936 VETKEIESVI-RCIKGVKDAAVVAH-VTASGQ------TELSAYV--VTKPGLSTNAVR---SELQNKLP---VFMHPAf 2999
Cdd:PRK05691   461 LYPQDIEKTVeREVEVVRKGRVAAFaVNHQGEegigiaAEISRSVqkILPPQALIKSIRqavAEACQEAPsvvLLLNPG- 539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3000 iekldSLPLSPNGKLDRGALPK-------------PVYNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTADSFFELG 3066
Cdd:PRK05691   540 -----ALPKTSSGKLQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLG 614

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3067 GDSIKALQVSARLH-RIGKQMAVKDLFSHPTIQELAAYIRD--SDTSSSQAAV-----EGDVQWSPVQK--WFLSQDIKE 3136
Cdd:PRK05691   615 GNSIAATQVVARLRdELGIDLNLRQLFEAPTLAAFSAAVARqlAGGGAAQAAIarlprGQALPQSLAQNrlWLLWQLDPQ 694

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3137 KHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQnEQGKwdQYNRPLSHSDdalYGLQMIDLSAPDGTDgnRP 3216
Cdd:PRK05691   695 SAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE-RDGV--ALQRIDAQGE---FALQRIDLSDLPEAE--RE 766

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3217 YEPLIKRHVlDIQQKMDLKNGPLLQAGLFHTIDGDF-LFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSS 3295
Cdd:PRK05691   767 ARAAQIREE-EARQPFDLEKGPLLRVTLVRLDDEEHqLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLG 845

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3296 FKAYAKKLSDYAESQQLMKQLKYWRE--AEEYQTEALPFDQidgTRAHEGQRSTISFTLN-DKETAALLKDANSAYNTDT 3372
Cdd:PRK05691   846 YADYGAWQRQWLAQGEAARQLAYWKAqlGDEQPVLELATDH---PRSARQAHSAARYSLRvDASLSEALRGLAQAHQATL 922

                          970       980       990
                   ....*....|....*....|....*....|
gi 1678550997 3373 QDMLLASVILALRHWTNQSAFKLSLEGHGR 3402
Cdd:PRK05691   923 FMVLLAAFQALLHRYSGQGDIRIGVPNANR 952
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 2550-3019 9.36e-56

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: 202.31  E-value: 9.36e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2550 SALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDS 2629
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2630 GTKLLMTineadlgvladfegeiltiesvEEDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHKGIANTLQ-WRRNA 2708
Cdd:cd05919     82 EARLVVT----------------------SADD------------IAYLLYSSGTTGPPKGVMHAHRDPLLFADaMAREA 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2709 YAFNETDTIL---QLFsFSFdGFITSMFTPLLSGAKAVLlhEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLD--VVQ 2783
Cdd:cd05919    128 LGLTPGDRVFssaKMF-FGY-GLGNSLWFPLAVGASAVL--NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDscAGS 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2784 PEDVKTLRVVTLAGEAADRELIARSLAicpHT--ELANEYGPTENsVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQ 2861
Cdd:cd05919    204 PDALRSLRLCVSAGEALPRGLGERWME---HFggPILDGIGATEV-GHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2862 LQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEI 2941
Cdd:cd05919    280 TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2942 ESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSE-----LQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd05919    353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARdihrhLLERLSAHKVPRRIAFVDELPRTATGKLQR 432


                   ...
gi 1678550997 3017 GAL 3019
Cdd:cd05919    433 FKL 435
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 10-415 1.40e-55

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: 201.39  E-value: 1.40e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNVIVL 89
Cdd:cd19547      1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 EEDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVN 169
Cdd:cd19547     81 LLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 ASPITLEPVQPYGKYIKWLMEQ--DKEQAVSYWDHYLSgheqqTVLPKQKKTKGKSRQ---EHVTFSFSKEESSRLSELA 244
Cdd:cd19547    161 GREPQLSPCRPYRDYVRWIRARtaQSEESERFWREYLR-----DLTPSPFSTAPADREgefDTVVHEFPEQLTRLVNEAA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  245 AREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDMQKDRLA 323
Cdd:cd19547    236 RGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRlDPDQTVTGLLETIHRDLAT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  324 AEAYSYHPLYEIQSRSAVKQ----GLIDHILVFENYPVQQeiqmLNKQEHASDLFQIHnftVADETNYSFYLMVAPGEEI 399
Cdd:cd19547    316 TAAHGHVPLAQIKSWASGERlsggRVFDNLVAFENYPEDN----LPGDDLSIQIIDLH---AQEKTEYPIGLIVLPLQKL 388

                          410
                   ....*....|....*.
gi 1678550997  400 HIKMNYDAEQHDRSFV 415
Cdd:cd19547    389 AFHFNYDTTHFTRAQV 404
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 469-949 3.37e-55

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: 200.53  E-value: 3.37e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRIRYILHDCGcSHVVsqahlpsslednyiithpedieskvdgsniksvnnADDLLYMIYTSGTTGKPKGVQFEHRNMA 628
Cdd:cd17631     81 PPEVAYILADSG-AKVL-----------------------------------FDDLALLMYTSGTTGRPKGAMLTHRNLL 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  629 nllkFEYTHSGIDFEA---DVLQFATPSFDV----CYqeIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFL-P 700
Cdd:cd17631    125 ----WNAVNALAALDLgpdDVLLVVAPLFHIgglgVF--TLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLvP 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  701 TAFIKMI----FSERELANsfpdgVKHLIAAGEQlMISDLFQdVLRKRGIHLHNHYGPSETHVVSTyTIHPGDPIPELPP 776
Cdd:cd17631    196 TMIQALLqhprFATTDLSS-----LRAVIYGGAP-MPERLLR-ALQARGVKFVQGYGMTETSPGVT-FLSPEDHRRKLGS 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  777 IGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimyRTGDLARRLEDGNIEYIG 856
Cdd:cd17631    268 AGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVD 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  857 RADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEhELCAyYCSVQKLNTID---LRSYMASELPEYMIPAK 932
Cdd:cd17631    341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGE-AVVA-VVVPRPGAELDedeLIAHCRERLARYKIPKS 418

                          490
                   ....*....|....*..
gi 1678550997  933 WIWVDSIPLTPNGKVDR 949
Cdd:cd17631    419 VEFVDALPRNATGKILK 435
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 1519-1924 3.67e-55

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: 202.06  E-value: 3.67e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1519 VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQ 1598
Cdd:cd05911     10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1599 SAGLHV-------PEFTGEIVYLNQTNSGLAHR---LSNPNVD----------VLPQSLAYVIYTSGSTGMPKGVEIEHR 1658
Cdd:cd05911     90 PDGLEKvkeaakeLGPKDKIIVLDDKPDGVLSIedlLSPTLGEededlppplkDGKDDTAAILYSSGTTGLPKGVCLSHR 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1659 SAVNflNSLQSRYQLKHSDmIMHKTSYSFD-----ASIWELFWWPYAGASVYLLPQGgekEPEVIAKAIEEQKITAMHFV 1733
Cdd:cd05911    170 NLIA--NLSQVQTFLYGND-GSNDVILGFLplyhiYGLFTTLASLLNGATVIIMPKF---DSELFLDLIEKYKITFLYLV 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1734 PSMLHAFLEHIKYRSvpIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAffdCPPHEKLERIPIG 1813
Cdd:cd05911    244 PPIAAALAKSPLLDK--YDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT---VNPDGDDKPGSVG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1814 KPVHHVRLYLLN-QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGR 1892
Cdd:cd05911    319 RLLPNVEAKIVDdDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL------HTGDIGYFDEDGYLYIVDR 392

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:cd05911    393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAV 424
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 2551-3014 5.78e-55

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: 201.29  E-value: 5.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2551 ALVSGD--KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSD 2628
Cdd:cd05911      1 AQIDADtgKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2629 SGTKLL-----------------------MTINEADLGVLadFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTT 2685
Cdd:cd05911     81 SKPKVIftdpdglekvkeaakelgpkdkiIVLDDKPDGVL--SIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2686 GRPKGVMVEHKG-IANTLQWRRNAYAFNETDTILQLFSfSFD---GFITSMFTPLLsGAKAVLLHEEEAKDILAIkhqLS 2761
Cdd:cd05911    159 GLPKGVCLSHRNlIANLSQVQTFLYGNDGSNDVILGFL-PLYhiyGLFTTLASLLN-GATVIIMPKFDSELFLDL---IE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2762 RQRITHMIIVPVLYRALLD--VVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVMRHMEKQ 2839
Cdd:cd05911    234 KYKITFLYLVPPIAAALAKspLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDK 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2840 aYVSIGQPIDGTQVLILNSN-HQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGT 2918
Cdd:cd05911    314 -PGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGY 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2919 LEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTEL-SAYVVTKPG--LSTNAVRSELQNKLP--- 2992
Cdd:cd05911    387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIG-IPDEVSGELpRAYVVRKPGekLTEKEVKDYVAKKVAsyk 465

                          490       500
                   ....*....|....*....|....*..
gi 1678550997 2993 -----VFmhpaFIeklDSLPLSPNGKL 3014
Cdd:cd05911    466 qlrggVV----FV---DEIPKSASGKI 485
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 2551-3019 9.78e-55

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: 201.44  E-value: 9.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2551 ALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSG 2630
Cdd:cd05959     22 AFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2631 TK-------LLMTINEADLGVLADFEGEILTiESVEEDDKSPL-------------PQMSSAHHLAYIIYTSGTTGRPKG 2690
Cdd:cd05959    102 ARvvvvsgeLAPVLAAALTKSEHTLVVLIVS-GGAGPEAGALLlaelvaaeaeqlkPAATHADDPAFWLYSSGSTGRPKG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2691 VMVEHKGIANTLQ-WRRNAYAFNETDTIL---QLFsFSFdGFITSMFTPLLSGAKAVLLHEEEAKDilAIKHQLSRQRIT 2766
Cdd:cd05959    181 VVHLHADIYWTAElYARNVLGIREDDVCFsaaKLF-FAY-GLGNSLTFPLSVGATTVLMPERPTPA--AVFKRIRRYRPT 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2767 HMIIVPVLYRALL--DVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELaneygpteNSVATTVMRHM------EK 2838
Cdd:cd05959    257 VFFGVPTLYAAMLaaPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDIL--------DGIGSTEMLHIflsnrpGR 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2839 QAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFtqnpfkpEARMYRTGDAARWMADGT 2918
Cdd:cd05959    329 VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-------QGEWTRTGDKYVRDDDGF 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2919 LEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAV-RSELQ----NKLPV 2993
Cdd:cd05959    402 YTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAlEEELKefvkDRLAP 481

                          490       500
                   ....*....|....*....|....*.
gi 1678550997 2994 FMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05959    482 YKYPRWIVFVDELPKTATGKIQRFKL 507
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1497-1983 1.42e-54

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 202.65  E-value: 1.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1497 HYALEQQAEKTPDQAAVIFED-----GVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAY 1571
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1572 LPIDPDYPEERISFLLEDSGTNILLLQSAGLhvpeFTGEIVYLNQTNSGLAHRLSNP-NVDVLPQSL------------- 1637
Cdd:COG0365     92 SPVFPGFGAEALADRIEDAEAKVLITADGGL----RGGKVIDLKEKVDEALEELPSLeHVIVVGRTGadvpmegdldwde 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1638 -------------------AYVIYTSGSTGMPKGVEIEHRS-AVNFLNSLQSRYQLKHSDmimhktsysfdasiweLFWW 1697
Cdd:COG0365    168 llaaasaefepeptdaddpLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGD----------------VFWC 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1698 P-----------------YAGASVYLLPQGGE-KEPEVIAKAIEEQKITAMHFVPSMLHAFlehIKYRSVPIKT---NRL 1756
Cdd:COG0365    232 TadigwatghsyivygplLNGATVVLYEGRPDfPDPGRLWELIEKYGVTVFFTAPTAIRAL---MKAGDEPLKKydlSSL 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1757 KRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATveAAFFDCPPHEKLERIPIGKPV--HHVRLylLNQNQRMLPVG 1834
Cdd:COG0365    309 RLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTETG--GIFISNLPGLPVKPGSMGKPVpgYDVAV--VDEDGNPVPPG 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1835 CIGELYIAGA--GVARGYLNRPALTEERFLEDpfYPGerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAA 1912
Cdd:COG0365    384 EEGELVIKGPwpGMFRGYWNDPERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESA 459

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1913 LRSIEGVREAAVTVRTDS--GEpELCAYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNA 1982
Cdd:COG0365    460 LVSHPAVAEAAVVGVPDEirGQ-VVKAFVvlkPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRL 538


                   .
gi 1678550997 1983 L 1983
Cdd:COG0365    539 L 539
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2568-3019 1.20e-53

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: 196.89  E-value: 1.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2568 SNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGC----YVPIDPEYPKERKRYILSDSGTKL------LMTI 2637
Cdd:cd05922      3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIvladagAADR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2638 NEADLGVLADfEGEILTIESVEeDDKSPLPQMSSAHH-LAYIIYTSGTTGRPKGVMVEHKGIantlqwRRNAYAFNE--- 2713
Cdd:cd05922     83 LRDALPASPD-PGTVLDADGIR-AARASAPAHEVSHEdLALLLYTSGSTGSPKLVRLSHQNL------LANARSIAEylg 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2714 ---TDTILQLFSFSFDGFITSMFTPLLSGAKAVLlHEEEAKDILAIKhQLSRQRITHMIIVPVLYrALLDVV--QPEDVK 2788
Cdd:cd05922    155 itaDDRALTVLPLSYDYGLSVLNTHLLRGATLVL-TNDGVLDDAFWE-DLREHGATGLAGVPSTY-AMLTRLgfDPAKLP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2789 TLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVM-RHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGV 2867
Cdd:cd05922    232 SLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLpPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGE 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2868 AGELCIAGTGLARGYVNLPelterAFTQNPFKPEARMYrTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRC 2947
Cdd:cd05922    312 PGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 2948 IKGVKDAAVVAHVTASGQtELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05922    386 IGLIIEAAAVGLPDPLGE-KLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 2551-3019 1.32e-53

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: 195.97  E-value: 1.32e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2551 ALVSGDKTLTYQELDEWSNGIARAL-RSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDS 2629
Cdd:cd05941      4 AIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2630 GTKLLMtineadlgvladfegeiltiesveeddksplpqmssahHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAY 2709
Cdd:cd05941     84 EPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2710 AFNETDTILQ-LFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQlsrQRITHMIIVPVLYRALLDVVQpEDVK 2788
Cdd:cd05941    126 RWTEDDVLLHvLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLM---PSITVFMGVPTIYTRLLQYYE-AHFT 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2789 TLRVVTLAGEAADRELIARSLAICPHT--ELAN--------EYGPTENSVATTVMRHMEKQAYvSIGQPIDGTQVLIL-N 2857
Cdd:cd05941    202 DPQFARAAAAERLRLMVSGSAALPVPTleEWEAitghtlleRYGMTEIGMALSNPLDGERRPG-TVGMPLPGVQARIVdE 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2858 SNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRI-DDQVKIRGYRV 2936
Cdd:cd05941    281 ETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKV 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2937 ETKEIESVIRCIKGVKDAAVV--AHVTAsGQtELSAYVVTKPG---LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPN 3011
Cdd:cd05941    355 SALEIERVLLAHPGVSECAVIgvPDPDW-GE-RVVAVVVLRAGaaaLSLEELKEWAKQRLAPYKRPRRLILVDELPRNAM 432


                   ....*...
gi 1678550997 3012 GKLDRGAL 3019
Cdd:cd05941    433 GKVNKKEL 440
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 10-433 2.54e-53

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: 193.67  E-value: 2.54e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLlqKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRErnvivl 89
Cdd:cd19545      1 IYPCTPLQEGLMALTA--RQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKE------ 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 eEDITHlneaEQSQFIEQWKEKDRDRGFHLQKDvLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYvn 169
Cdd:cd19545     73 -SPISW----TESTSLDEYLEEDRAAPMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGE-- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 aspiTLEPVQPYGKYIKWLMEQDKEQAVSYWDHYLSGhEQQTVLP-----KQKKTKGKSRQEHVTFSFSkeessrlsela 244
Cdd:cd19545    145 ----PVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAG-LDPAVFPplpssRYQPRPDATLEHSISLPSS----------- 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  245 AREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDMQKDRLA 323
Cdd:cd19545    209 ASSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRiDPEQSVEDFLQTVQKDLLD 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  324 AEAYSYHPLYEIQSRS--AVKQGLIDHILVFEnYPVQQEiqmlnkqEHASDLFQIHNFTVADETNYSFYLMV---APGEE 398
Cdd:cd19545    289 MIPFEHTGLQNIRRLGpdARAACNFQTLLVVQ-PALPSS-------TSESLELGIEEESEDLEDFSSYGLTLecqLSGSG 360

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1678550997  399 IHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19545    361 LRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 464-952 5.85e-53

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: 196.54  E-value: 5.85e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPV 543
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 DPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDN----------YIITHPEDIESKVDGSNIKSVNNA------------ 601
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPAlpgchdlrtlIIVGDPAHASEGHPGEEPASWPKLlalgdadpphpv 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 --DDLLYMIYTSGTTGKPKGVQFEHRNM-------ANLLKFEythsgidfEADVLQFATP-SFDVCYQEIFSALLKGGTL 671
Cdd:TIGR03098  161 idSDMAAILYTSGSTGRPKGVVLSHRNLvagaqsvATYLENR--------PDDRLLAVLPlSFDYGFNQLTTAFYVGATV 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  672 HIVPEAIKRDVPQLfafINKHQ-TNIVFLPTAFIKMifSERELANSFPDGVKHLIAAGEQL---MISDLFQDVLRKRgih 747
Cdd:TIGR03098  233 VLHDYLLPRDVLKA---LEKHGiTGLAAVPPLWAQL--AQLDWPESAAPSLRYLTNSGGAMpraTLSRLRSFLPNAR--- 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  748 LHNHYGPSEThVVSTYtihpgdpipeLPP---------IGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNH 818
Cdd:TIGR03098  305 LFLMYGLTEA-FRSTY----------LPPeevdrrpdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWND 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  819 DKLTSDKFSSDPFKPDV-----IMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQ 893
Cdd:TIGR03098  374 PEKTAERFRPLPPFPGElhlpeLAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVP 453

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  894 DQNGEHELCAYYCSVQK--LNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:TIGR03098  454 DPTLGQAIVLVVTPPGGeeLDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
466-952 1.01e-52

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 196.87  E-value: 1.01e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  466 HAMFEKQAEKTPDAHAVI-----DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI 540
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  541 VPVDPHYPADRIRYILHDCGCSHVVS--------------------QAHLPSsLEdNYIITHPEDIESKVDGSN-----I 595
Cdd:COG0365     92 SPVFPGFGAEALADRIEDAEAKVLITadgglrggkvidlkekvdeaLEELPS-LE-HVIVVGRTGADVPMEGDLdwdelL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  596 KSVN--------NADDLLYMIYTSGTTGKPKGVQFEHRNManLLKFEYTHSGI-DFEAD--VLQFATPSF-----DVCYq 659
Cdd:COG0365    170 AAASaefepeptDADDPLFILYTSGTTGKPKGVVHTHGGY--LVHAATTAKYVlDLKPGdvFWCTADIGWatghsYIVY- 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  660 eifSALLKGGTLHIVPEAIKRDVPQ-LFAFINKHQTNIVFL-PTAFIKMIFSERELANSFP-DGVKHLIAAGEQLMiSDL 736
Cdd:COG0365    247 ---GPLLNGATVVLYEGRPDFPDPGrLWELIEKYGVTVFFTaPTAIRALMKAGDEPLKKYDlSSLRLLGSAGEPLN-PEV 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  737 FQDVLRKRGIHLHNHYGPSET--HVVStytihpgdPIPELPP----IGKPI-GCtDLYILNHQKQLQPCGVPGELYISGA 809
Cdd:COG0365    323 WEWWYEAVGVPIVDGWGQTETggIFIS--------NLPGLPVkpgsMGKPVpGY-DVAVVDEDGNPVPPGEEGELVIKGP 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  810 --SVARGYVNHDKLTSDKFSSDPfkPDVimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEA 887
Cdd:COG0365    394 wpGMFRGYWNDPERYRETYFGRF--PGW--YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997  888 AILIWQDQNGEHELCAYycsVqKLN---------TIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:COG0365    470 AVVGVPDEIRGQVVKAF---V-VLKpgvepsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 2558-3014 7.03e-52

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: 191.05  E-value: 7.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2558 TLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTI 2637
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2638 NEadlgvladFEGeiltiesveeddKSPLPQMSSahhLAYIIYTSGTTGRPKGVMVEHKGI-ANTLQWRRNaYAFNETDT 2716
Cdd:cd05903     81 ER--------FRQ------------FDPAAMPDA---VALLLFTSGTTGEPKGVMHSHNTLsASIRQYAER-LGLGPGDV 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2717 ILQLFSFS-FDGFITSMFTPLLSGAKAVLLHEEEAKDILAIkhqLSRQRITHMIIVPVLYRALLDVV--QPEDVKTLRVV 2793
Cdd:cd05903    137 FLVASPMAhQTGFVYGFTLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVeeAGEPLSRLRTF 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2794 TLAGEAADRELIARsLAICPHTELANEYGPTENSVATTVMR-HMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELC 2872
Cdd:cd05903    214 VCGGATVPRSLARR-AAELLGAKVCSAYGSTECPGAVTSITpAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELL 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2873 IAGTGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDqVKIR-GYRVETKEIESVIRCIKGV 2951
Cdd:cd05903    293 SRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGHPGV 364

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 2952 KDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNK-LPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:cd05903    365 IEAAVVALPDERLGERACAVVVTKSGalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1491-1983 6.22e-51

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 190.50  E-value: 6.22e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1491 SMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:PRK07656     2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYPEERISFLLEDSGTNILL--------LQSAGLHVPEFtgEIVYLNQTNSGLAHR---------LSNPNVD-- 1631
Cdd:PRK07656    82 VVPLNTRYTADEAAYILARGDAKALFvlglflgvDYSATTRLPAL--EHVVICETEEDDPHTekmktftdfLAAGDPAer 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1632 ---VLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HKTSY--SFDASIwelfwwpYA 1700
Cdd:PRK07656   160 apeVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLaanpffHVFGYkaGVNAPL-------MR 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1701 GASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLkrVFSGGEQLGTHLVSRFYELLPN 1780
Cdd:PRK07656   233 GATILPLPV---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRL--AVTGAASMPVALLERFESELGV 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1781 VSITNSYGPTEATVEAAFfdCPPHEKLERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTE 1858
Cdd:PRK07656   308 DIVLTGYGLSEASGVTTF--NRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATA 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1859 ERFLEDPFypgerMYkTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEPE---- 1934
Cdd:PRK07656   386 AAIDADGW-----LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI-----GVPDerlg 454

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1935 --LCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK07656   455 evGKAYVvlkpgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 2556-3019 7.00e-51

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: 188.45  E-value: 7.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2556 DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLM 2635
Cdd:cd17654     14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2636 TiNEADlgvlaDFEGEILTIESVEEDdksplpqMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAyaFNET- 2714
Cdd:cd17654     94 Q-NKEL-----DNAPLSFTPEHRHFN-------IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL--FNITs 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2715 DTILQLFSF-SFDGFITSMFTPLLSGAkaVLLHEEEAKDILAIKHQ---LSRQRITHMIIVPVLYRALLDVVQPEDV--- 2787
Cdd:cd17654    159 EDILFLTSPlTFDPSVVEIFLSLSSGA--TLLIVPTSVKVLPSKLAdilFKRHRITVLQATPTLFRRFGSQSIKSTVlsa 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2788 -KTLRVVTLAGEAADRELIARSLA-ICPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQpi 2865
Cdd:cd17654    237 tSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEG-- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2866 gvAGELCIAGtgLARGYVNLPELTeraftqnpfKPEARMYRTGDAARwMADGTLEYLGRIDDQVKIRGYRVETKEIESVI 2945
Cdd:cd17654    315 --TGQVFLGG--LNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVI 380

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2946 RCIKGVkdaaVVAHVTASGQTELSAYVVTKPglSTNAVRSELQ-NKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd17654    381 ESCLGV----ESCAVTLSDQQRLIAFIVGES--SSSRIHKELQlTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1533-1983 9.66e-51

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: 188.42  E-value: 9.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1533 AWELIGrGVKPETTVAIIGKRSPEMLLgIYGILKAGGA----YLPIDPDYPEERISFLLEDSGTNILLLQSAGlhVPEFT 1608
Cdd:cd05922      9 ALLEAG-GVRGERVVLILPNRFTYIEL-SFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGA--ADRLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1609 -GEIVYLNQTNS----GLAHRLSN-PNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHK 1682
Cdd:cd05922     85 dALPASPDPGTVldadGIRAARASaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1683 TSYSFDASIWELFWWPYAGASVYLLPQGgeKEPEVIAKAIEEQKITAMHFVPSmLHAFLEHIKYRsvPIKTNRLKRVFSG 1762
Cdd:cd05922    165 LPLSYDYGLSVLNTHLLRGATLVLTNDG--VLDDAFWEDLREHGATGLAGVPS-TYAMLTRLGFD--PAKLPSLRYLTQA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1763 GEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFdcPPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYI 1841
Cdd:cd05922    240 GGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYL--PPERILEKPgSIGLAIPGGEFEILDDDGTPTPPGEPGEIVH 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1842 AGAGVARGYLNRPAlteerFLEDPFYPGERMYkTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE 1921
Cdd:cd05922    318 RGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIE 391

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1922 AAVTVRTDSGEPELCAYVEGLQRNEVRAQLERL---LPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05922    392 AAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLaerLPPYKVPATVRVVDELPLTASGKVDYAAL 456
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 11-328 2.17e-50

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: 186.41  E-value: 2.17e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   11 YPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVIVLE 90
Cdd:cd19531      2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVD-GEPVQVILPPLPLPLPV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   91 EDITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNA 170
Cdd:cd19531     81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  171 SPITLE--PVQpYGKYIKW---LMEQDK-EQAVSYWDHYLSGHeqQTVL--------PKQKKTKGKSrqehVTFSFSKEE 236
Cdd:cd19531    161 RPSPLPplPIQ-YADYAVWqreWLQGEVlERQLAYWREQLAGA--PPVLelptdrprPAVQSFRGAR----VRFTLPAEL 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  237 SSRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRP-AEIEGiehMVGLFINTMPVRVQ--GAKTpFLQL 313
Cdd:cd19531    234 TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNrAELEG---LIGFFVNTLVLRTDlsGDPT-FREL 309

                          330
                   ....*....|....*
gi 1678550997  314 IKDMQKDrlAAEAYS 328
Cdd:cd19531    310 LARVRET--ALEAYA 322
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 462-952 2.21e-50

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: 188.73  E-value: 2.21e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIV 541
Cdd:cd05959      3 YNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  542 PVDPHYPADRIRYILHDCGCS-HVVSQAHLP---SSLEDNY------IITHPEDIESKVD----------GSNIKSVNNA 601
Cdd:cd05959     83 PVNTLLTPDDYAYYLEDSRARvVVVSGELAPvlaAALTKSEhtlvvlIVSGGAGPEAGALllaelvaaeaEQLKPAATHA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDLLYMIYTSGTTGKPKGVQFEHRNMA--------NLLKFEythsgidfEADVLqFATPSFDVCY---QEIFSALLKGGT 670
Cdd:cd05959    163 DDPAFWLYSSGSTGRPKGVVHLHADIYwtaelyarNVLGIR--------EDDVC-FSAAKLFFAYglgNSLTFPLSVGAT 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  671 LHIVPEaikRDVPQL-FAFINKHQTNIVF-LPTAFIKMIFSERELANSFpDGVKHLIAAGEQLMiSDLFQDVLRKRGIHL 748
Cdd:cd05959    234 TVLMPE---RPTPAAvFKRIRRYRPTVFFgVPTLYAAMLAAPNLPSRDL-SSLRLCVSAGEALP-AEVGERWKARFGLDI 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  749 HNHYGPSET-HVVSTYT---IHPGDPipelppiGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSD 824
Cdd:cd05959    309 LDGIGSTEMlHIFLSNRpgrVRYGTT-------GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRD 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  825 KFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAY 904
Cdd:cd05959    382 TFQGE-------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAF 454

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997  905 Y-----CSVQKLNTIDLRSYMASELPEYMIPaKWI-WVDSIPLTPNGKVDRAAL 952
Cdd:cd05959    455 VvlrpgYEDSEALEEELKEFVKDRLAPYKYP-RWIvFVDELPKTATGKIQRFKL 507
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 13-251 1.61e-49

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 177.54  E-value: 1.61e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   13 LSYMQEGMLFhslLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVIVLEED 92
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   93 ITHLNEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNASP 172
Cdd:COG4908     77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  173 ITLEPVQ-PYGKYIKWLMEQ----DKEQAVSYWDHYLSGHEQQTVLPKQKK--TKGKSRQEHVTFSFSKEESSRLSELAA 245
Cdd:COG4908    157 PPLPELPiQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPrpAVQTFRGATLSFTLPAELTEALKALAK 236


                   ....*.
gi 1678550997  246 REEVTL 251
Cdd:COG4908    237 AHGATV 242
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 3123-3570 2.28e-49

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: 183.38  E-value: 2.28e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQK--WFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQnEQGKWDQYNRPLSHSDDalygL 3200
Cdd:cd19066      5 SPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCE-EAGRYEQVVLDKTVRFR----I 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3201 QMIDLSapDGTDGNRPYEPLIKRhvlDIQQKMDLKNGPLLQAGLFHT-IDGDFLFLSAHHLVVDGISWRVLLEDLALGYR 3279
Cdd:cd19066     80 EIIDLR--NLADPEARLLELIDQ---IQQTIYDLERGPLVRVALFRLaDERDVLVVAIHHIIVDGGSFQILFEDISSVYD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3280 QAAGGEDIkLPPKTSSFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPF--DQIDGTRAHEGQRsTISFTLNDKET 3357
Cdd:cd19066    155 AAERQKPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLpkAKRPSQVASYEVL-TLEFFLRSEET 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3358 AAlLKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREDVlkgiDVSRTIGWFTAIYPLLIKLNADlpdseE 3437
Cdd:cd19066    233 KR-LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE----AVEDTIGLFLNLLPLRIDTSPD-----A 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3438 SMVHVLKTTKDTLRRVPDKGFGYGVIKYLTPPGKKDINFTGAPEISFNYLGQFESGRTAEVPEEDafsfsplgaGGDIST 3517
Cdd:cd19066    303 TFPELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFT---------TPVYTS 373

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 3518 TWNREQSLDISAIA-AEGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHC 3570
Cdd:cd19066    374 SEGTVFDLDLEASEdPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 2088-2489 7.66e-49

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: 181.49  E-value: 7.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2088 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIH--------- 2158
Cdd:cd19536      2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHrqaqvpvte 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2159 -DEVPFTLQTTVLGARTEQEaaaaFIKPFDLSQAPLFRAQIVKVSDERHLLLV-DMHHIISDGVSVNILIQEFGELYN-- 2234
Cdd:cd19536     82 lDLTPLEEQLDPLRAYKEET----KIRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNql 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2235 ---NRKLPALRIQYKDYAVWQEGFKTGDAYkmqEAYWLKQLEGelpvLDLPADHARPPVRSFAGDKVSFTLEPEVASGL- 2310
Cdd:cd19536    158 leyKPLSLPPAQPYRDFVAHERASIQQAAS---ERYWREYLAG----ATLATLPALSEAVGGGPEQDSELLVSVPLPVRs 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2311 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGkPFVQYLQEVRE 2388
Cdd:cd19536    231 RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQE 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2389 TALEAFEHQNYPFEelvdklELTRDMSRNPVFDAMLVVQNNDY---------EPLHLHDLQMkpaqvSHLVSKFDLTLQA 2459
Cdd:cd19536    310 QELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHFDLdfglpewgsDEGMRRGLLF-----SEFKSNYDVNLSV 378

                          410       420       430
                   ....*....|....*....|....*....|
gi 1678550997 2460 SEGDGNIHFLFEYSTALFEKTTIERWASHL 2489
Cdd:cd19536    379 LPKQDRLELKLAYNSQVLDEEQAQRLAAYY 408
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 1508-1983 2.82e-48

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


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 180.75  E-value: 2.82e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFE----DGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:cd17654      1 PDRPALIIDqttsDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLQSAGLHVPE-FTGEIVYLNQTnsglahrlsnpnvdvLPQSLAYVIYTSGSTGMPKGVEIEHRSAVN 1662
Cdd:cd17654     81 LTVMKKCHVSYLLQNKELDNAPLsFTPEHRHFNIR---------------TDECLAYVIHTSGTTGTPKIVAVPHKCILP 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1663 FLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAI-EEQKITAMHFVPSMLHAFL 1741
Cdd:cd17654    146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFG 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1742 EHIKYRSVPIKTNRLKRVFSGGEQL--GTHLVSRFYElLPNVSITNSYGPTEATVEAAFFDCPphEKLERIPIGKPVHHV 1819
Cdd:cd17654    226 SQSIKSTVLSATSSLRVLALGGEPFpsLVILSSWRGK-GNRTRIFNIYGITEVSCWALAYKVP--EEDSPVQLGSPLLGT 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1820 RLYLLNQNQRMLPvgciGELY---IAGAGVARGYLNRPALTeerfledpfypgerMYKTGDVARwLPDGNVEFLGRTDDQ 1896
Cdd:cd17654    303 VIEVRDQNGSEGT----GQVFlggLNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQ 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1897 VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDsgEPELCAYVEGLQRNEVRAQLER-LLPGYMVPAYMIEMEQWPVTPS 1975
Cdd:cd17654    364 IKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ--QRLIAFIVGESSSSRIHKELQLtLLSSHAIPDTFVQIDKLPLTSH 441


                   ....*...
gi 1678550997 1976 GKLDRNAL 1983
Cdd:cd17654    442 GKVDKSEL 449
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 2557-3022 4.01e-48

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: 182.33  E-value: 4.01e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:cd17647     19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 INEADLGVLADfegeiltiesveeddksPLPQMSsahhlayiiYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDT 2716
Cdd:cd17647     99 IRAAGVVVGPD-----------------SNPTLS---------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2717 ILQLFSFSFDGFITSMFTPLLSGAKavlLHEEEAKDI-----LAIKHQLSRQRITHMII-------------VPVLYRAL 2778
Cdd:cd17647    153 FTMLSGIAHDPIQRDMFTPLFLGAQ---LLVPTQDDIgtpgrLAEWMAKYGATVTHLTPamgqlltaqattpFPKLHHAF 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2779 L--DVVQPEDVktLRVVTLAgeaadreliarslaicPHTELANEYGPTENSVATT---VMRHMEKQAY-------VSIGQ 2846
Cdd:cd17647    230 FvgDILTKRDC--LRLQTLA----------------ENVRIVNMYGTTETQRAVSyfeVPSRSSDPTFlknlkdvMPAGR 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2847 PIDGTQVLILNSN--HQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF----------------------KPEA 2902
Cdd:cd17647    292 GMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlGPRD 371

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2903 RMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKP------ 2976
Cdd:cd17647    372 RLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFdkpdde 451

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2977 ------------------GLS-----TNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKP 3022
Cdd:cd17647    452 sfaqedvpkevstdpivkGLIgyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
 3441-3596 5.67e-48

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 169.38  E-value: 5.67e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3441 HVLKTTKDTLRRVPDKGFGYGVIKYLTPPGKKdINFTGAPEISFNYLGQFESGRtaevpEEDAFSFSPLGAGGDISTTWN 3520
Cdd:TIGR01720    4 RLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK-LAASPQPEISFNYLGQFDADS-----NDELFQPSSYSPGEAISPESP 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 3521 REQSLDISAIAAEGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTEDALQEI 3596
Cdd:TIGR01720   78 RPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 488-955 8.09e-48

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: 181.56  E-value: 8.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHdcgcshvVSQ 567
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLG-------VAK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 AHLPSSLEDNYIITHPEDIESkvdgsniksvnnaddllyMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVL 647
Cdd:cd17647     93 PRGLIVIRAAGVVVGPDSNPT------------------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  648 QFATPSFDVCYQEIFSALLKGGTLhIVPEAIKRDVP-QLFAFINKHQTNIVFLPTAFIKMIFSERelANSFPdGVKHLIA 726
Cdd:cd17647    155 MLSGIAHDPIQRDMFTPLFLGAQL-LVPTQDDIGTPgRLAEWMAKYGATVTHLTPAMGQLLTAQA--TTPFP-KLHHAFF 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  727 AGEQLMISDLFQDVLRKRGIHLHNHYGPSETH------VVSTYTIHPG--DPIPELPPIGKPIGCTDLYILNHQKQLQPC 798
Cdd:cd17647    231 VGDILTKRDCLRLQTLAENVRIVNMYGTTETQravsyfEVPSRSSDPTflKNLKDVMPAGRGMLNVQLLVVNRNDRTQIC 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  799 GVP--GELYISGASVARGYVNHDKLTSDKF-----------------SSDP-----FKPDVIMYRTGDLARRLEDGNIEY 854
Cdd:cd17647    311 GIGevGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvepdhwnyldkdNNEPwrqfwLGPRDRLYRTGDLGRYLPNGDCEC 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  855 IGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYY---------------------------CS 907
Cdd:cd17647    391 CGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIvprfdkpddesfaqedvpkevstdpivKG 470

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997  908 VQKLNTI--DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEP 955
Cdd:cd17647    471 LIGYRKLikDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 2088-2500 1.25e-47

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: 177.50  E-value: 1.25e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2088 YPVSSAQKRIyVLQQLEDGGTGYNmPAVLELEGKLNPERMDRAFQELIKRHESLRTSF-EQDEGGDPVQRIHDEVPFTLQ 2166
Cdd:cd19542      2 YPCTPMQEGM-LLSQLRSPGLYFN-HFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLDPPIE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2167 TTvlgaRTEQEAAAAFIKPFD----LSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRKLPAlR 2242
Cdd:cd19542     80 EV----ETDEDSLDALTRDLLddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-A 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2243 IQYKDYAVWQEGFKTGDAYkmqeAYWLKQLEGELPVLDLPADHARPPVRSfaGDKVSFTLEPevasgLHKLARENGSTLY 2322
Cdd:cd19542    155 PPFSDYISYLQSQSQEESL----QYWRKYLQGASPCAFPSLSPKRPAERS--LSSTRRSLAK-----LEAFCASLGVTLA 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2323 MVLLAAYTAFLSRLSGQEDIIVGSPIAGR--PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYP 2400
Cdd:cd19542    224 SLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLS 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2401 FEELVDKLELTRdmsRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVS-HLVSKFDLTLQASEGDGNIHFLFEYSTALFEK 2479
Cdd:cd19542    304 LREIQRALGLWP---SGTLFNTLVSYQNFEASPESELSGSSVFELSAaEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSE 380

                          410       420
                   ....*....|....*....|.
gi 1678550997 2480 TTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19542    381 EQAEELLEQFDDILEALLANP 401
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1057-1460 2.19e-47

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: 176.73  E-value: 2.19e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1057 YPVSSAQKRIyVLQQLDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEP-VQ----RIHTEVPF 1131
Cdd:cd19542      2 YPCTPMQEGM-LLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQvvlkSLDPPIEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1132 TLSKETTIEGFVRPFD----LSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKPlRIQYKD 1207
Cdd:cd19542     81 VETDEDSLDALTRDLLddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFSD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1208 YAVWQQkfkkGDSYQKQETYWQQQFSGDLPIlELPTdkrrpaerQFIGGKVTFQLDKEITARIKrlAHKNRSTLYMTLLA 1287
Cdd:cd19542    160 YISYLQ----SQSQEESLQYWRKYLQGASPC-AFPS--------LSPKRPAERSLSSTRRSLAK--LEAFCASLGVTLAS 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1288 LYSA----FLSRLSGQDDIVIGSPIAGR--PHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPF 1361
Cdd:cd19542    225 LFQAawalVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSL 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1362 EELVDKLGVqreMSRNPLFDTTLVLQNME-QQKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQFEYSTALFEKE 1440
Cdd:cd19542    305 REIQRALGL---WPSGTLFNTLVSYQNFEaSPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEE 381

                          410       420
                   ....*....|....*....|
gi 1678550997 1441 TIQRWASLFTTLVEHTAASP 1460
Cdd:cd19542    382 QAEELLEQFDDILEALLANP 401
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 2534-3019 4.36e-47

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 179.41  E-value: 4.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIM-MHRS---FSMIASILgvwkAGGC 2609
Cdd:PRK06188    13 TYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLsLNRPevlMAIGAAQL----AGLR 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2610 YVPIDPEYPKERKRYILSDSGTKLLMTIN----EADLGVLADFEG--EILTIESVEED----------DKSPLPQMSSAH 2673
Cdd:PRK06188    89 RTALHPLGSLDDHAYVLEDAGISTLIVDPapfvERALALLARVPSlkHVLTLGPVPDGvdllaaaakfGPAPLVAAALPP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 HLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGfiTSMFTP-LLSGAKAVLLHEEEAKD 2752
Cdd:PRK06188   169 DIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAG--GAFFLPtLLRGGTVIVLAKFDPAE 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2753 ILAIkhqLSRQRITHMIIVPVLYRALLDVVQPE--DVKTLRVVTLAGEAAD----RELIARSLAIcphteLANEYGPTEN 2826
Cdd:PRK06188   247 VLRA---IEEQRITATFLVPTMIYALLDHPDLRtrDLSSLETVYYGASPMSpvrlAEAIERFGPI-----FAQYYGQTEA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2827 SVATTVMR---HMEKQAYV--SIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNpfkpe 2901
Cdd:PRK06188   319 PMVITYLRkrdHDPDDPKRltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG----- 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2902 arMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTE-LSAYVVTKPGLST 2980
Cdd:PRK06188   394 --WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIG-VPDEKWGEaVTAVVVLRPGAAV 470

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 2981 NAvrSELQN-----KLPVFMhPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06188   471 DA--AELQAhvkerKGSVHA-PKQVDFVDSLPLTALGKPDKKAL 511
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 1509-1983 4.55e-47

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: 177.10  E-value: 4.55e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1509 DQAAVIFEDGVMTYKELNEQANRIAWELIGRG-VKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLlqsaglhvpeftgeivylnqtnsglahrlsnpnvdvlpqSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSL 1667
Cdd:cd05941     81 TDSEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMH-----KTSYSFDASIWELFwwpyAGASVYLLPqggEKEPEVIAKAIEEQKITAMHFVPSML----- 1737
Cdd:cd05941    122 VDAWRWTEDDVLLHvlplhHVHGLVNALLCPLF----AGASVEFLP---KFDPKEVAISRLMPSITVFMGVPTIYtrllq 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1738 ---HAFLEHIKYRSVPIKTNRLkrVFSGGEQLGTHLVSRFYELLPNVsITNSYGPTEATVEAAffdCPPHEklERIP--I 1812
Cdd:cd05941    195 yyeAHFTDPQFARAAAAERLRL--MVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMALS---NPLDG--ERRPgtV 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1813 GKPVHHVRLYLLNQN-QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLG 1891
Cdd:cd05941    267 GMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILG 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1892 RT-DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEPE------LCAYV------EGLQRNEVRAQLERLLPGY 1958
Cdd:cd05941    341 RSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVI-----GVPDpdwgerVVAVVvlragaAALSLEELKEWAKQRLAPY 415

                          490       500
                   ....*....|....*....|....*
gi 1678550997 1959 MVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05941    416 KRPRRLILVDELPRNAMGKVNKKEL 440
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 460-955 4.94e-47

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 178.84  E-value: 4.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  460 PVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGA 539
Cdd:PRK06187     3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  540 IVPVDPHYPADRIRYILHDCGCSHV-VSQAHLP--SSLEDN------YIITHPEDIESKV-------DGSNIKSVN---- 599
Cdd:PRK06187    83 LHPINIRLKPEEIAYILNDAEDRVVlVDSEFVPllAAILPQlptvrtVIVEGDGPAAPLApevgeyeELLAAASDTfdfp 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 --NADDLLYMIYTSGTTGKPKGVQFEHRNManLLKFEYTHSGIDF-EADVLQFATPSFDV-----CYQeifsALLKGGTL 671
Cdd:PRK06187   163 diDENDAAAMLYTSGTTGHPKGVVLSHRNL--FLHSLAVCAWLKLsRDDVYLVIVPMFHVhawglPYL----ALMAGAKQ 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  672 hIVPEAIkrDVPQLFAFINKHQTNIVFL-PTAFiKMIFseRELANSFPD--GVKHLIAAG----EQLMisdlfQDVLRKR 744
Cdd:PRK06187   237 -VIPRRF--DPENLLDLIETERVTFFFAvPTIW-QMLL--KAPRAYFVDfsSLRLVIYGGaalpPALL-----REFKEKF 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 GIHLHNHYGPSETHVVSTYTiHPGDPIPELPPI----GKPIGCTDLYILNHQKQLQPC--GVPGELYISGASVARGYVNH 818
Cdd:PRK06187   306 GIDLVQGYGMTETSPVVSVL-PPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNR 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  819 DKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-G 897
Cdd:PRK06187   385 PEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwG 457

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997  898 EhELCAYYcsVQK----LNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEP 955
Cdd:PRK06187   458 E-RPVAVV--VLKpgatLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 3123-3370 1.29e-46

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 169.06  E-value: 1.29e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQKWFLSQDiKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQnEQGKWDQYNRPlshsdDALYGLQM 3202
Cdd:COG4908      2 SPAQKRFLFLE-PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVE-EDGEPVQRIDP-----DADLPLEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3203 IDLSAPDGTDGNRPYEPLIKRhvlDIQQKMDLKNGPLLQAGLFHT-IDGDFLFLSAHHLVVDGISWRVLLEDLALGYRQA 3281
Cdd:COG4908     75 VDLSALPEPEREAELEELVAE---EASRPFDLARGPLLRAALIRLgEDEHVLLLTIHHIISDGWSLGILLRELAALYAAL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3282 AGGEDIKLPPKTSSFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEA--LPFDQIDG-TRAHEGqrSTISFTLNDKETA 3358
Cdd:COG4908    152 LEGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVleLPTDRPRPaVQTFRG--ATLSFTLPAELTE 229

                          250
                   ....*....|..
gi 1678550997 3359 ALLKDAnSAYNT 3370
Cdd:COG4908    230 ALKALA-KAHGA 240
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 477-952 1.56e-46

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: 175.74  E-value: 1.56e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQAC----SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:cd17654      1 PDRPALIIDQTtsdtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQAHLPSSLEdnYIITHPEDIESKVDGSniksvnnaddLLYMIYTSGTTGKPKGVQFEHRNMANLLk 632
Cdd:cd17654     81 LTVMKKCHVSYLLQNKELDNAPL--SFTPEHRHFNIRTDEC----------LAYVIHTSGTTGTPKIVAVPHKCILPNI- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  633 feyTHSGIDFE---ADVLQFATP-SFDVCYQEIFSALLKGGTLHIVPEAIKRdVPQLFAFI--NKHQTNIVFLPTAFIKM 706
Cdd:cd17654    148 ---QHFRSLFNitsEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKV-LPSKLADIlfKRHRITVLQATPTLFRR 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IFSE--RELANSFPDGVKHLIAAGEQLmISDLFQDVLRKRG--IHLHNHYGPSETHVVSTYTIHPGDPIPElpPIGKPIG 782
Cdd:cd17654    224 FGSQsiKSTVLSATSSLRVLALGGEPF-PSLVILSSWRGKGnrTRIFNIYGITEVSCWALAYKVPEEDSPV--QLGSPLL 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  783 CTDLYIlnhqKQLQPCGVPGELYISGasVARGYVNHDKLTsdkfssdpfKPDVIMYRTGDLARRlEDGNIEYIGRADNQV 862
Cdd:cd17654    301 GTVIEV----RDQNGSEGTGQVFLGG--LNRVCILDDEVT---------VPKGTMRATGDFVTV-KDGELFFLGRKDSQI 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNgeheLCAYYCSVQKLNTIDLRSYMaSELPEYMIPAKWIWVDSIPLT 942
Cdd:cd17654    365 KRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGESSSSRIHKELQL-TLLSSHAIPDTFVQIDKLPLT 439

                          490
                   ....*....|
gi 1678550997  943 PNGKVDRAAL 952
Cdd:cd17654    440 SHGKVDKSEL 449
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 459-954 2.91e-46

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 176.63  E-value: 2.91e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  459 TPVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGG 538
Cdd:PRK07656     1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  539 AIVPVDPHYPADRIRYILHDCGCSHVVSQAHL----------PSSLEDNYIITHPEDIESKVDGSNIKSVN--------- 599
Cdd:PRK07656    81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFlgvdysattrLPALEHVVICETEEDDPHTEKMKTFTDFLaagdpaera 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 ---NADDLLYMIYTSGTTGKPKGVQFEHRNM-------ANLLKFEythsgidfEADVLQFATPSFDV-CYQE-IFSALLK 667
Cdd:PRK07656   161 pevDPDDVADILFTSGTTGRPKGAMLTHRQLlsnaadwAEYLGLT--------EGDRYLAANPFFHVfGYKAgVNAPLMR 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  668 GGTLHIVPeaiKRDVPQLFAFINKHQTNiVF--LPTAFIKMIfserelanSFPDGVKH------LIAAGEQLMISDLFQD 739
Cdd:PRK07656   233 GATILPLP---VFDPDEVFRLIETERIT-VLpgPPTMYNSLL--------QHPDRSAEdlsslrLAVTGAASMPVALLER 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  740 VLRKRGI-HLHNHYGPSETHVVSTYTiHPGDPIPELP-PIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVN 817
Cdd:PRK07656   301 FESELGVdIVLTGYGLSEASGVTTFN-RLDDDRKTVAgTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYD 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  818 hdkltsdkfssDP------FKPDVIMYrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILI 891
Cdd:PRK07656   380 -----------DPeataaaIDADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997  892 WQDQN-GEhELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK07656   448 VPDERlGE-VGKAYVVlkPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 2547-3019 3.14e-46

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: 175.96  E-value: 3.14e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVS--GDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRY 2624
Cdd:cd05926      1 PDAPALVVpgSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2625 ILSDSGTKLLMTINEADLGVL-ADFEGEILTIESVEED-------DKSPLPQMSSAHH------------LAYIIYTSGT 2684
Cdd:cd05926     81 YLADLGSKLVLTPKGELGPASrAASKLGLAILELALDVgvlirapSAESLSNLLADKKnaksegvplpddLALILHTSGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2685 TGRPKGVMVEHKGIANTLQWRRNAYAFNETD-TILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILaikhQLSRQ 2763
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDrTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFW----PDVRD 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2764 -RITHMIIVPVLYRALLDVVQPEDVK---TLRVVTLAGEAADrELIARSLAICPHTELANEYGPTENS--VATTVMRHmE 2837
Cdd:cd05926    237 yNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLP-PAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPP-G 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2838 KQAYVSIGQPiDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADG 2917
Cdd:cd05926    315 PRKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLDADG 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2918 TLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVA--HVTAsGQtELSAYVVTKPG--LSTNAVRSELQNKLPV 2993
Cdd:cd05926    388 YLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGvpDEKY-GE-EVAAAVVLREGasVTEEELRAFCRKHLAA 465

                          490       500
                   ....*....|....*....|....*.
gi 1678550997 2994 FMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05926    466 FKVPKKVYFVDELPKTATGKIQRRKV 491
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 497-952 3.85e-46

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: 174.55  E-value: 3.85e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  497 AANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI----VPVDPHYPADRIRYILHDCGCSHVVSQAHLPS 572
Cdd:cd05922      2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLglvfVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  573 SLEDNYIITHPEDIESKVD-----GSNIKSVNNA-DDLLYMIYTSGTTGKPKGVQFEHRNM---ANLLKfEYThsGIDfE 643
Cdd:cd05922     82 RLRDALPASPDPGTVLDADgiraaRASAPAHEVShEDLALLLYTSGSTGSPKLVRLSHQNLlanARSIA-EYL--GIT-A 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  644 ADVLQFATP-SFDVCYQEIFSALLKGGTLHI-----VPEAIKRDvpqlfafINKHQ-TNIVFLPTAF---IKMIFSEREL 713
Cdd:cd05922    158 DDRALTVLPlSYDYGLSVLNTHLLRGATLVLtndgvLDDAFWED-------LREHGaTGLAGVPSTYamlTRLGFDPAKL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  714 ANsfpdgVKHLIAAGEQLmiSDLFQDVLRK--RGIHLHNHYGPSETHVVSTYTihPGDPIPELP-PIGKPIGCTDLYILN 790
Cdd:cd05922    231 PS-----LRYLTQAGGRL--PQETIARLREllPGAQVYVMYGQTEATRRMTYL--PPERILEKPgSIGLAIPGGEFEILD 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  791 HQKQLQPCGVPGELYISGASVARGYVNhdkltSDKFSSDPFKPDVIMYrTGDLARRLEDGNIEYIGRADNQVKIRGYRIE 870
Cdd:cd05922    302 DDGTPTPPGEPGEIVHRGPNVMKGYWN-----DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRIS 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  871 PQEIEVTLMNHPDISEAAILIWQDQNGEhELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRA 950
Cdd:cd05922    376 PTEIEAAARSIGLIIEAAAVGLPDPLGE-KLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454


                   ..
gi 1678550997  951 AL 952
Cdd:cd05922    455 AL 456
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 490-953 7.38e-46

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: 172.86  E-value: 7.38e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSqah 569
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  570 lpsslednyiithpedieskvdgsniksvnnadDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDfEADVLQF 649
Cdd:cd05934     82 ---------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG-EDDVYLT 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  650 ATPSFD---VCYQeIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELansfPDGVKHLI- 725
Cdd:cd05934    128 VLPLFHinaQAVS-VLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPS----PDDRAHRLr 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  726 AAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVstyTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELY 805
Cdd:cd05934    200 AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVG---VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELV 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  806 ISGA---SVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHP 882
Cdd:cd05934    277 IRGLrgwGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHP 349

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  883 DISEAAILIWQDQNGEHELCAYYCSV--QKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:cd05934    350 AVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1071-1448 1.09e-45

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: 171.60  E-value: 1.09e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1071 QLDEGV-AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGaDDEPVQRIHTEVP-------FTLSKEttiegF 1142
Cdd:cd19537     16 QLSTGTsSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPR-DGGLRRSYSSSPPrvqrvdtLDVWKE-----I 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1143 VRPFDLSQAPLFRaglIEVSNEkHVLLVdMHHIISDGVSVQLLIREFTDLYANRQLKPLRIQYKDYAVWQQkfkkgDSYQ 1222
Cdd:cd19537     90 NRPFDLEREDPIR---VFISPD-TLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSR-----PASP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1223 KQETYWQQQFSGdLPILELPtdkRRPAERQFIGGKVTFQLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDI 1302
Cdd:cd19537    160 EDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDI 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1303 VIGSPIAGRPHADLEAVLGMFVNTLALRTR--PAGNKTFEEFLKEVRQTALEAYEHQdYPFEELVDKLGVQREMSRNPLF 1380
Cdd:cd19537    236 VLGAPYLNRTSEEDMETVGLFLEPLPIRIRfpSSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLF 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1381 DT--TLVLQNMEQQKLKMNDVQLQwndlehPI----SKFDISLYVTE-HDSELFCQFEYSTALFEKETIQRWASL 1448
Cdd:cd19537    315 DVmvTFHDDRGVSLALPIPGVEPL------YTwaegAKFPLMFEFTAlSDDSLLLRLEYDTDCFSEEEIDRIESL 383
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 489-952 1.70e-45

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: 172.14  E-value: 1.70e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSqa 568
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslednyiithpedieskvdgsniksvnNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKfeYTHSGIDFEADVLQ 648
Cdd:cd05972     79 -------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIP--TAAYWLGLRPDDIH 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  649 FAT--PSFDVC-YQEIFSALLKGGTLhIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPdGVKHLI 725
Cdd:cd05972    126 WNIadPGWAKGaWSSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFS-HLRLVV 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  726 AAGEQLM--ISDLFQDVLrkrGIHLHNHYGPSETHVV----STYTIHPGDpipelppIGKPIGCTDLYILNHQKQLQPCG 799
Cdd:cd05972    204 SAGEPLNpeVIEWWRAAT---GLPIRDGYGQTETGLTvgnfPDMPVKPGS-------MGRPTPGYDVAIIDDDGRELPPG 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  800 VPGELYI--SGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVT 877
Cdd:cd05972    274 EEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESA 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  878 LMNHPDISEAAI------LIWQDQNGEHELCAYYCSVQKLnTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAA 951
Cdd:cd05972    347 LLEHPAVAEAAVvgspdpVRGEVVKAFVVLTSGYEPSEEL-AEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVE 425


                   .
gi 1678550997  952 L 952
Cdd:cd05972    426 L 426
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 478-952 2.82e-45

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: 171.70  E-value: 2.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  478 DAHAVIDQACSLTYRELNKAANRLARHLRMKGVV-RQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYIL 556
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  557 HDCGCSHVVsqahlpsslednyiithpedieskvdgsniksvnnadDLLYMIYTSGTTGKPKGVQFEHRNMANLLK---- 632
Cdd:cd05941     81 TDSEPSLVL-------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRalvd 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  633 -FEYThsgidfEADVLQFATPSFDV--CYQEIFSALLKGGTLHIVPeaiKRDVPQlfAFINKHQTNIVFL---PTAFIKM 706
Cdd:cd05941    124 aWRWT------EDDVLLHVLPLHHVhgLVNALLCPLFAGASVEFLP---KFDPKE--VAISRLMPSITVFmgvPTIYTRL 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IfSERELANSFPDGVKHLIAAGEQLMIS-------DLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHpGDPIPElpPIGK 779
Cdd:cd05941    193 L-QYYEAHFTDPQFARAAAAERLRLMVSgsaalpvPTLEEWEAITGHTLLERYGMTEIGMALSNPLD-GERRPG--TVGM 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  780 PIGCTDLYIL-NHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGR- 857
Cdd:cd05941    269 PLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRs 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  858 ADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-----IWqdqnGEhELCAYYC---SVQKLNTIDLRSYMASELPEYMI 929
Cdd:cd05941    343 SVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgvpdpDW----GE-RVVAVVVlraGAAALSLEELKEWAKQRLAPYKR 417

                          490       500
                   ....*....|....*....|...
gi 1678550997  930 PAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05941    418 PRRLILVDELPRNAMGKVNKKEL 440
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1057-1460 2.91e-45

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: 171.09  E-value: 2.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1057 YPVSSAQKRIYVLQQLD-EGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPFTLSK 1135
Cdd:cd19536      2 YPLSSLQEGMLFHSLLNpGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1136 ETTIEG--------------FVRPFDLSQAPLFRAGLIEVSNEKHVLLV-DMHHIISDGVSVQLLIREFTDLYANR---- 1196
Cdd:cd19536     82 LDLTPLeeqldplraykeetKIRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQLleyk 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1197 --QLKPlRIQYKDYAVWQQKfkkgdSYQKQET--YWQQQFSG-DLPILELPTDKRRPAERQfigGKVTFqLDKEITARIK 1271
Cdd:cd19536    162 plSLPP-AQPYRDFVAHERA-----SIQQAASerYWREYLAGaTLATLPALSEAVGGGPEQ---DSELL-VSVPLPVRSR 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1272 RLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPH--ADLEAVLGMFVNTLALRTRPAGNkTFEEFLKEVRQT 1349
Cdd:cd19536    232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQ 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1350 ALEAYEHQDYPFEELvdklgvQREMSRNPLFDTTLVLQNMEQqklkmnDVQLQWNDLEHPI----------SKFDISLYV 1419
Cdd:cd19536    311 ELESLSHEQVPLADI------QRCSEGEPLFDSIVNFRHFDL------DFGLPEWGSDEGMrrgllfsefkSNYDVNLSV 378

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1678550997 1420 TEHDSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19536    379 LPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1499-1983 5.19e-45

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: 172.55  E-value: 5.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:cd05959      9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSA-------GLHVPEFTGEIVYLNQTNSGLAHRL-----------SNPNVDVLPQSLAYV 1640
Cdd:cd05959     89 TPDDYAYYLEDSRARVVVVSGElapvlaaALTKSEHTLVVLIVSGGAGPEAGALllaelvaaeaeQLKPAATHADDPAFW 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1641 IYTSGSTGMPKGVEIEHRS----AVNFL-NSLQSRyqlkHSDMIMHKT----SYSFDASIWELFWwpyAGASVYLLPqgG 1711
Cdd:cd05959    169 LYSSGSTGRPKGVVHLHADiywtAELYArNVLGIR----EDDVCFSAAklffAYGLGNSLTFPLS---VGATTVLMP--E 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1712 EKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHikyrSVPIKTN--RLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGP 1789
Cdd:cd05959    240 RPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAA----PNLPSRDlsSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGS 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1790 TEATveAAFFDCPPHEKlERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLedpfypG 1869
Cdd:cd05959    315 TEML--HIFLSNRPGRV-RYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------G 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1870 ErMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV--------E 1940
Cdd:cd05959    386 E-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgVEDEDGLTKPKAFVvlrpgyedS 464

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 1941 GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05959    465 EALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 2102-2499 9.60e-45

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: 168.90  E-value: 9.60e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2102 QLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEVPFTLQTTVLGARTEqeaaaa 2181
Cdd:cd19537     16 QLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGG-LRRSYSSSPPRVQRVDTLDVWKE------ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2182 FIKPFDLSQAPLFRaqiVKVSDeRHLLLVdMHHIISDGVSVNILIQEFGELYNNRKLPALRIQYKDYAVWQegfKTGDAY 2261
Cdd:cd19537     89 INRPFDLEREDPIR---VFISP-DTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS---RPASPE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2262 KMQeaYWLKQLEGeLPVLDLPAdhaRPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQED 2341
Cdd:cd19537    161 DLD--FWSEYLSG-LPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTD 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2342 IIVGSPIAGRPHKDLEPILGMFVNTLALRTR--PEGGKPFVQYLQEVRETALEAFEHQnYPFEELVDKLELTRDMSRNPV 2419
Cdd:cd19537    235 IVLGAPYLNRTSEEDMETVGLFLEPLPIRIRfpSSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPL 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2420 FDAMlvVQNNDYEPLHLHdLQMKPAQVSHLV---SKFDLTLQASE-GDGNIHFLFEYSTALFEKTTIERWASHLTNVLSI 2495
Cdd:cd19537    314 FDVM--VTFHDDRGVSLA-LPIPGVEPLYTWaegAKFPLMFEFTAlSDDSLLLRLEYDTDCFSEEEIDRIESLILAALEL 390


                   ....
gi 1678550997 2496 IGKN 2499
Cdd:cd19537    391 LVEG 394
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 490-952 1.46e-44

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: 169.54  E-value: 1.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSqah 569
Cdd:cd05971      8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  570 lpsslednyiithpedieskvDGSniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRN-MANLLKFEYTHSGIDFEADVlq 648
Cdd:cd05971     85 ---------------------DGS--------DDPALIIYTSGTTGPPKGALHAHRVlLGHLPGVQFPFNLFPRDGDL-- 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  649 FATPS--------FDVcyqeIFSALLKGGTLhIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDG 720
Cdd:cd05971    134 YWTPAdwawigglLDV----LLPSLYFGVPV-LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  721 VKHLIAAGEQLMiSDLFQDVLRKRGIHLHNHYGPSETHVVST-----YTIHPGDpipelppIGKPIGCTDLYILNHQKQL 795
Cdd:cd05971    209 LRAIATGGESLG-EELLGWAREQFGVEVNEFYGQTECNLVIGncsalFPIKPGS-------MGKPIPGHRVAIVDDNGTP 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  796 QPCGVPGELYIS-GASVAR-GYVNHDKLTSDKFSSDPFkpdvimyRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQE 873
Cdd:cd05971    281 LPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAE 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  874 IEVTLMNHPDISEAAILIWQDQNGEHELCAYYC---SVQKLNTI--DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd05971    354 IEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpGETPSDALarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIR 433


                   ....
gi 1678550997  949 RAAL 952
Cdd:cd05971    434 RREL 437
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 2559-3019 1.55e-44

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: 169.05  E-value: 1.55e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTin 2638
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 eadlgvladfegeiltiesvEEDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHK-------GIANTLQWRRNAYAF 2711
Cdd:cd05972     79 --------------------DAED------------PALIYFTSGTTGLPKGVLHTHSyplghipTAAYWLGLRPDDIHW 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2712 NETDTILQLFSFSfdgfitSMFTPLLSGAkAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQPE-DVKTL 2790
Cdd:cd05972    127 NIADPGWAKGAWS------SFFGPWLLGA-TVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSyKFSHL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2791 RVVTLAGEAADRELIARSLAiCPHTELANEYGPTENSVATTVMRHME-KQAyvSIGQPIDGTQVLILNSNHQLQPIGVAG 2869
Cdd:cd05972    200 RLVVSAGEPLNPEVIEWWRA-ATGLPIRDGYGQTETGLTVGNFPDMPvKPG--SMGRPTPGYDVAIIDDDGRELPPGEEG 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2870 ELCI--AGTGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRC 2947
Cdd:cd05972    277 DIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2948 IKGVKDAAVVAHV-TASGQTeLSAYVVTKPG-LSTNAVRSELQNK----LPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05972    350 HPAVAEAAVVGSPdPVRGEV-VKAFVVLTSGyEPSEELAEELQGHvkkvLAPYKYPREIEFVEELPKTISGKIRRVEL 426
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 488-947 2.35e-44

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: 170.09  E-value: 2.35e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQ 567
Cdd:cd05911     10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 AH--------------------LPSSLEDnyiITHPEDIESKVDGSNIKSV-----NNADDLLYMIYTSGTTGKPKGVQF 622
Cdd:cd05911     90 PDglekvkeaakelgpkdkiivLDDKPDG---VLSIEDLLSPTLGEEDEDLppplkDGKDDTAAILYSSGTTGLPKGVCL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  623 EHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCY--QEIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFL- 699
Cdd:cd05911    167 SHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYglFTTLASLLNGATVIIMP---KFDSELFLDLIEKYKITFLYLv 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  700 PTAFIKMIFSERELANSFPDgVKHLIAAGEQLmiSDLFQDVLRKRGI--HLHNHYGPSETHVVSTYTIhPGDPIPElpPI 777
Cdd:cd05911    244 PPIAAALAKSPLLDKYDLSS-LRVILSGGAPL--SKELQELLAKRFPnaTIKQGYGMTETGGILTVNP-DGDDKPG--SV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  778 GKPIGCTDLYILNHQ-KQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIG 856
Cdd:cd05911    318 GRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVD 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  857 RADNQVKIRGYRIEPQEIEVTLMNHPDISEAA-ILIWQDQNGEhelcAYYCSV-----QKLNTIDLRSYMASELPEYmip 930
Cdd:cd05911    392 RKKELIKYKGFQVAPAELEAVLLEHPGVADAAvIGIPDEVSGE----LPRAYVvrkpgEKLTEKEVKDYVAKKVASY--- 464

                          490       500
                   ....*....|....*....|..
gi 1678550997  931 aKW-----IWVDSIPLTPNGKV 947
Cdd:cd05911    465 -KQlrggvVFVDEIPKSASGKI 485
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2557-3019 1.61e-43

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: 166.45  E-value: 1.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 ineadlgvlaDfegeiltiesvEEDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHK---GIANTLQ-----WRRNA 2708
Cdd:cd05971     85 ----------D-----------GSDD------------PALIIYTSGTTGPPKGALHAHRvllGHLPGVQfpfnlFPRDG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2709 YAFNETDtilqlfSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPV---LYRALLDVVQPE 2785
Cdd:cd05971    132 DLYWTPA------DWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkMMRQQGEQLKHA 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2786 DVKtLRVVTLAGEAADRELIA---RSLAIcphtELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQL 2862
Cdd:cd05971    206 QVK-LRAIATGGESLGEELLGwarEQFGV----EVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTP 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2863 QPIGVAGELCI----AGTGLarGYVNLPELTERaftqnpfKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVET 2938
Cdd:cd05971    281 LPPGEVGEIAVelpdPVAFL--GYWNNPSATEK-------KMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2939 KEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTN-AVRSELQN----KLPVFMHPAFIEKLDSLPLSPNGK 3013
Cdd:cd05971    352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdALAREIQElvktRLAAHEYPREIEFVNELPRTATGK 431


                   ....*.
gi 1678550997 3014 LDRGAL 3019
Cdd:cd05971    432 IRRREL 437
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1494-1983 5.23e-43

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 166.57  E-value: 5.23e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYL 1572
Cdd:PRK06839     2 QGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1573 PIDPDYPEERISFLLEDSGTNILLLQsaglhvPEFTGEIVYLnQTNSGLAH--RLSNP---------NVDVLPQSLAYVI 1641
Cdd:PRK06839    82 PLNIRLTENELIFQLKDSGTTVLFVE------KTFQNMALSM-QKVSYVQRviSITSLkeiedrkidNFVEKNESASFII 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1642 -YTSGSTGMPKGVEIehrSAVN-FLNSLQSRYQLkhsDMIMHKTSYS----FDASIWELFWWP--YAGASVyLLPqgGEK 1713
Cdd:PRK06839   155 cYTSGTTGKPKGAVL---TQENmFWNALNNTFAI---DLTMHDRSIVllplFHIGGIGLFAFPtlFAGGVI-IVP--RKF 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1714 EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLkrVFSGGEQLGTHLVSRFYEllPNVSITNSYGPTEaT 1793
Cdd:PRK06839   226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRW--FYNGGAPCPEELMREFID--RGFLFGQGFGMTE-T 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1794 VEAAFFdcPPHEKLERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpger 1871
Cdd:PRK06839   301 SPTVFM--LSEEDARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC---- 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 mykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYV----EGLQRN 1945
Cdd:PRK06839   375 ---TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVkwGEIPIAFIVkkssSVLIEK 451

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1678550997 1946 EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK06839   452 DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1521-1984 7.98e-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: 7.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLlqsa 1600
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeivylnqtnsglahrlsnpnVDvlpqsLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMI- 1679
Cdd:cd05934     81 -----------------------------VD-----PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYl 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1680 -------MHKTSYSFDASIWelfwwpyAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEhiKYRSVPIK 1752
Cdd:cd05934    127 tvlplfhINAQAVSVLAALS-------VGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSYLLA--QPPSPDDR 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1753 TNRLKRVFSGG--EQLGTHLVSRFyellpNVSITNSYGPTEATVEAAffdCPPHEKLERIPIGKPVHHVRLYLLNQNQRM 1830
Cdd:cd05934    195 AHRLRAAYGAPnpPELHEEFEERF-----GVRLLEGYGMTETIVGVI---GPRDEPRRPGSIGRPAPGYEVRIVDDDGQE 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1831 LPVGCIGELYIAGA---GVARGYLNRPALTEERFledpfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 1907
Cdd:cd05934    267 LPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1908 EIEAALRSIEGVREAAV-TVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 1981
Cdd:cd05934    340 EVERAILRHPAVREAAVvAVPDEVGEDEVKAVVvlrpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419


                   ...
gi 1678550997 1982 ALP 1984
Cdd:cd05934    420 QLR 422
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 1500-1983 9.09e-43

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: 165.55  E-value: 9.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:cd12118     10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSaglhvpEFTGEIVylnqTNSGlahrlsNPNVDVLP-----QSLAyVIYTSGSTGMPKGVE 1654
Cdd:cd12118     90 AEEIAFILRHSEAKVLFVDR------EFEYEDL----LAEG------DPDFEWIPpadewDPIA-LNYTSGTTGRPKGVV 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 IEHRSAvnFLNSLQS--RYQLKHSDMIMHkTSYSFDASIWELFWWPYA-GASVYLLPQggeKEPEVIAKAIEEQKITAMH 1731
Cdd:cd12118    153 YHHRGA--YLNALANilEWEMKQHPVYLW-TLPMFHCNGWCFPWTVAAvGGTNVCLRK---VDAKAIYDLIEKHKVTHFC 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1732 FVPSMLHAFLEHIKYRSVPIktNRLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTEATVEAAFfdCPPHEKLERIP 1811
Cdd:cd12118    227 GAPTVLNMLANAPPSDARPL--PHRVHVMTAGAPPPAAVLAKMEEL--GFDVTHVYGLTETYGPATV--CAWKPEWDELP 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1812 IG-----KPVHHVRLYLLNQ-----NQRMLPV----GCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGD 1877
Cdd:cd12118    301 TEerarlKARQGVRYVGLEEvdvldPETMKPVprdgKTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFH-------SGD 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1878 VARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVE-----GLQRNEVRAQ 1950
Cdd:cd12118    374 LAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEkwGE-VPCAFVElkegaKVTEEEIIAF 452

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1678550997 1951 LERLLPGYMVPAYMIEMEqWPVTPSGKLDRNAL 1983
Cdd:cd12118    453 CREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 2560-3019 1.91e-42

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: 163.39  E-value: 1.91e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2560 TYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTine 2639
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2640 ADLgvladFEGEILTIESVEEDDKSPLPQMS-----SAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNET 2714
Cdd:TIGR01923   78 DSL-----LEEKDFQADSLDRIEAAGRYETSlsasfNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTED 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2715 DT---ILQLFSFSFDGFItsmFTPLLSGAkAVLLHEEEAkdilAIKHQLSRQRITHMIIVPVLYRALLDVVQPEDvkTLR 2791
Cdd:TIGR01923  153 DNwllSLPLYHISGLSIL---FRWLIEGA-TLRIVDKFN----QLLEMIANERVTHISLVPTQLNRLLDEGGHNE--NLR 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2792 VVTLAGEAADRELIARslAICPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQpigvaGEL 2871
Cdd:TIGR01923  223 KILLGGSAIPAPLIEE--AQQYGLPIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEI 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2872 CIAGTGLARGYVNLPELTERAFTQNPFKpearmyrTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGV 2951
Cdd:TIGR01923  296 MVKGANLMKGYLYQGELTPAFEQQGWFN-------TGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGI 368

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2952 KDAAVVAHVTAS-GQTELsAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:TIGR01923  369 QEAVVVPKPDAEwGQVPV-AYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 481-952 2.02e-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: 2.02e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  481 AVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCG 560
Cdd:cd05919      3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  561 CSHVVSqahlpsslednyiithpedieskvdgsniksvnNADDLLYMIYTSGTTGKPKGVQFEHRN---MANLLKFEYTh 637
Cdd:cd05919     83 ARLVVT---------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDpllFADAMAREAL- 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  638 sGIDfEADVLqFATPSFDVCY---QEIFSALLKGGTLHIVPEAikRDVPQLFAFINKHQTNIVF-LPTAFIKMIFSEREL 713
Cdd:cd05919    129 -GLT-PGDRV-FSSAKMFFGYglgNSLWFPLAVGASAVLNPGW--PTAERVLATLARFRPTVLYgVPTFYANLLDSCAGS 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  714 ANSFPDgVKHLIAAGEQLMiSDLFQDVLRKRGIHLHNHYGPSET-HV-VSTytiHPGDpiPELPPIGKPIGCTDLYILNH 791
Cdd:cd05919    204 PDALRS-LRLCVSAGEALP-RGLGERWMEHFGGPILDGIGATEVgHIfLSN---RPGA--WRLGSTGRPVPGYEIRLVDE 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  792 QKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEP 871
Cdd:cd05919    277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  872 QEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYC-----SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGK 946
Cdd:cd05919    350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlkspaAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429


                   ....*.
gi 1678550997  947 VDRAAL 952
Cdd:cd05919    430 LQRFKL 435
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1521-1983 4.04e-42

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: 164.34  E-value: 4.04e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIG---KRSPEMLLGIYGIlkagGAYL-PIDPDYPEERISFLLEDSGTNILL 1596
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM----GAVLhTINPRLFPEQIAYIINHAEDRVVF 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1597 LQSAGL--------------HVPEFTGEIVYLNQTNSGLAH--RL--SNPNVDVLPQS---LAYVI-YTSGSTGMPKGVE 1654
Cdd:cd12119    103 VDRDFLplleaiaprlptveHVVVMTDDAAMPEPAGVGVLAyeELlaAESPEYDWPDFdenTAAAIcYTSGTTGNPKGVV 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 IEHRSavNFLNSLQSRYQ----LKHSDMIMHKTSYsFDASIWELfwwPYAGASV---YLLPqGGEKEPEVIAKAIEEQKI 1727
Cdd:cd12119    183 YSHRS--LVLHAMAALLTdglgLSESDVVLPVVPM-FHVNAWGL---PYAAAMVgakLVLP-GPYLDPASLAELIEREGV 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1728 TAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLpnVSITNSYGPTE-------ATVEAAFFD 1800
Cdd:cd12119    256 TFAAGVPTVWQGLLDHLEANGRDLSS--LRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTEtsplgtvARPPSEHSN 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1801 CPPHEKLE-RIPIGKPVHHVRLYLLNQNQRMLPV--GCIGELYIAGAGVARGYLNRPALTEErFLEDPFYpgermyKTGD 1877
Cdd:cd12119    332 LSEDEQLAlRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWL------RTGD 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1878 VARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE-PELCAYV---EGLQRNEVRAQL 1951
Cdd:cd12119    405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPkwGErPLAVVVLkegATVTAEELLEFL 484

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1678550997 1952 ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd12119    485 ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 1521-1983 7.22e-42

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: 161.46  E-value: 7.22e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNiLLLQSA 1600
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQ-LLLTDS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 GLHVPEFTgeIVYLNQTnSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHR----SAVNFLNSL----QSRYQ 1672
Cdd:TIGR01923   80 LLEEKDFQ--ADSLDRI-EAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRnhyaSAVGSKENLgfteDDNWL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1673 LkhSDMIMHKTSYSFdasiweLFWWPYAGASVYLlPQGGEKepevIAKAIEEQKITAMHFVPSMLHAFLEhikyrsvpiK 1752
Cdd:TIGR01923  157 L--SLPLYHISGLSI------LFRWLIEGATLRI-VDKFNQ----LLEMIANERVTHISLVPTQLNRLLD---------E 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1753 TN---RLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTEA--TVEAAffdcPPHEKLERIPIGKPVHHVRLYLLNQN 1827
Cdd:TIGR01923  215 GGhneNLRKILLGGSAIPAPLIEEAQQY--GLPIYLSYGMTETcsQVTTA----TPEMLHARPDVGRPLAGREIKIKVDN 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1828 QRMlpvgcIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 1907
Cdd:TIGR01923  289 KEG-----HGEIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPE 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1908 EIEAALRSIEGVREAAVTVRTDS--GE-PElcAYVEGlqRNEV-RAQLERLLPG----YMVPAYMIEMEQWPVTPSGKLD 1979
Cdd:TIGR01923  357 EIETVLYQHPGIQEAVVVPKPDAewGQvPV--AYIVS--ESDIsQAKLIAYLTEklakYKVPIAFEKLDELPYNASGKIL 432


                   ....
gi 1678550997 1980 RNAL 1983
Cdd:TIGR01923  433 RNQL 436
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 2538-3016 1.02e-41

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: 162.79  E-value: 1.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2538 LFEQQAARTPkasALV--SGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDP 2615
Cdd:cd05904     13 LFASAHPSRP---ALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2616 EY-PKERKRYIlSDSGTKLLMTINE-----ADLGVL------ADFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSG 2683
Cdd:cd05904     90 LStPAEIAKQV-KDSGAKLAFTTAElaeklASLALPvvlldsAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSG 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2684 TTGRPKGVMVEHKG-IANTLQ--WRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIkhqL 2760
Cdd:cd05904    169 TTGRSKGVMLTHRNlIAMVAQfvAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAA---I 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2761 SRQRITHMIIVPVLYRALL--DVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENS--VATTVMRHM 2836
Cdd:cd05904    246 ERYKVTHLPVVPPIVLALVksPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTgvVAMCFAPEK 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2837 EKQAYVSIGQPIDGTQVLILNSNH-QLQPIGVAGELCIAGTGLARGYVNLPELTERAFTqnpfkpEARMYRTGDAARWMA 2915
Cdd:cd05904    326 DRAKYGSVGRLVPNVEAKIVDPETgESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLCYIDE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2916 DGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVV-AHVTASGQTELsAYVVTKPGLSTNAvrSELQNklpvf 2994
Cdd:cd05904    400 DGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIpYPDEEAGEVPM-AFVVRKPGSSLTE--DEIMD----- 471

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997 2995 mhpaFIEK-------------LDSLPLSPNGKLDR 3016
Cdd:cd05904    472 ----FVAKqvapykkvrkvafVDAIPKSPSGKILR 502
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 10-341 1.16e-41

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: 160.30  E-value: 1.16e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   10 IYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVLRERNVIVl 89
Cdd:cd19544      1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPV- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 eediTHLNEAEQSQFIEQWKEKDRDRGFHLqkDV----LMRIALIQTGESQ-YSCIWTFHHIMMDGWCLSIVLKEFlhiy 164
Cdd:cd19544     80 ----EELTLDPGDDALAQLRARFDPRRYRL--DLrqapLLRAHVAEDPANGrWLLLLLFHHLISDHTSLELLLEEI---- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  165 ASYVNASPITLEPVQPYGKYI-KWLMEQDKEQAVSYWDHYLSGHEQQT----VLPKQkkTKGKSRQEHvTFSFSKEESSR 239
Cdd:cd19544    150 QAILAGRAAALPPPVPYRNFVaQARLGASQAEHEAFFREMLGDVDEPTapfgLLDVQ--GDGSDITEA-RLALDAELAQR 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  240 LSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMPVRVQGAKTPFLQLIKDMQk 319
Cdd:cd19544    227 LRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVREAVRQTH- 305

                          330       340
                   ....*....|....*....|...
gi 1678550997  320 DRLAA-EAYSYHPLYEIQSRSAV 341
Cdd:cd19544    306 ARLAElLRHEHASLALAQRCSGV 328
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2559-3021 2.50e-41

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: 159.99  E-value: 2.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTiN 2638
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-D 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 EADLGVLadfegeiltiesveedDKSPLPQMSsahhlayiiyTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTIL 2718
Cdd:cd05973     80 AANRHKL----------------DSDPFVMMF----------TSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFW 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2719 QLFSFSFD-GFITSMFTPLLSGAKAVLLH----EEEAKDIlaikhqLSRQRITHMIIVPVLYRALL--DVVQPEDVK-TL 2790
Cdd:cd05973    134 NAADPGWAyGLYYAITGPLALGHPTILLEggfsVESTWRV------IERLGVTNLAGSPTAYRLLMaaGAEVPARPKgRL 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2791 RVVTLAGEAADRELIaRSLAICPHTELANEYGPTENSVATTVMRHMEKQAYV-SIGQPIDGTQVLILNSNHQLQPIGVAG 2869
Cdd:cd05973    208 RRVSSAGEPLTPEVI-RWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAgSAGRAMPGWRVAVLDDDGDELGPGEPG 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2870 ELCIagtglarGYVNLPELTERAFTQNPFK-PEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCI 2948
Cdd:cd05973    287 RLAI-------DIANSPLMWFRGYQLPDTPaIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEH 359

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2949 KGVKDAAVVAhVTASGQTE-LSAYVVTKPGL-STNAVRSELQ----NKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPK 3021
Cdd:cd05973    360 PAVAEAAVIG-VPDPERTEvVKAFVVLRGGHeGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 477-954 3.61e-41

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: 160.94  E-value: 3.61e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVI--DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRY 554
Cdd:cd05926      1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  555 ILHDCGCSHVVSQ----------------AHLPSSLEDNYIITHPEDIE---SKVDGSNIKSVNNA--DDLLYMIYTSGT 613
Cdd:cd05926     81 YLADLGSKLVLTPkgelgpasraasklglAILELALDVGVLIRAPSAESlsnLLADKKNAKSEGVPlpDDLALILHTSGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  614 TGKPKGVQFEHRNMANLLK-----FEYThsgidfEADVLQFATPSFDVCYQ--EIFSALLKGGTLhIVPEaikRDVPQLF 686
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATnitntYKLT------PDDRTLVVMPLFHVHGLvaSLLSTLAAGGSV-VLPP---RFSASTF 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  687 --AFINKHQTNIVFLPTafIKMIFSERELANsfPDGVKHL---IAAGEQLMISDLFQDVLRKRGIHLHNHYGPSET-HVV 760
Cdd:cd05926    231 wpDVRDYNATWYTAVPT--IHQILLNRPEPN--PESPPPKlrfIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAaHQM 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  761 STytihpgDPIPELPP----IGKPIGcTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvi 836
Cdd:cd05926    307 TS------NPLPPGPRkpgsVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW----- 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  837 mYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEHELCAYYCSVQKLNTI- 914
Cdd:cd05926    375 -FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFgVPDEKYGEEVAAAVVLREGASVTEe 453

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997  915 DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:cd05926    454 ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1508-1983 4.20e-41

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: 160.94  E-value: 4.20e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVM--TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISF 1585
Cdd:cd05926      1 PDAPALVVPGSTPalTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1586 LLEDSGTNILLLQSAGLH-----VPEFTGEIVYL-----NQTNSGLAHRLSNPNVD---------VLPQSLAYVIYTSGS 1646
Cdd:cd05926     81 YLADLGSKLVLTPKGELGpasraASKLGLAILELaldvgVLIRAPSAESLSNLLADkknaksegvPLPDDLALILHTSGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1647 TGMPKGVEIEHRsavNFLNS---LQSRYQLKHSD---MIM-----HKTSYSFDASIwelfwwpYAGASVyLLPqggekeP 1715
Cdd:cd05926    161 TGRPKGVPLTHR---NLAASatnITNTYKLTPDDrtlVVMplfhvHGLVASLLSTL-------AAGGSV-VLP------P 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1716 EVIAKA----IEEQKITAMHFVPSMLHAFL--EHIKYRSVPIKtnrLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGP 1789
Cdd:cd05926    224 RFSASTfwpdVRDYNATWYTAVPTIHQILLnrPEPNPESPPPK---LRFIRSCSASLPPAVLEALEATF-GAPVLEAYGM 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1790 TEATVEAAffdCPPHEKLERIP--IGKPVHhVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFy 1867
Cdd:cd05926    300 TEAAHQMT---SNPLPPGPRKPgsVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW- 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 pgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG- 1941
Cdd:cd05926    375 -----FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEkyGE-EVAAAVvlrEGa 448

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 1942 -LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05926    449 sVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1521-1983 6.33e-41

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: 158.75  E-value: 6.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILllqsa 1600
Cdd:cd05971      8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL----- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeivylnqtnsglahrlsnpnVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM 1680
Cdd:cd05971     83 -----------------------------VTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDL 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1681 HKTSYSFdASIWELF-----WWpYAGasVYLLPQGGEK-EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIktN 1754
Cdd:cd05971    134 YWTPADW-AWIGGLLdvllpSL-YFG--VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ--V 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1755 RLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATV----EAAFFDCPPHEkleripIGKPVHHVRLYLLNQNQRM 1830
Cdd:cd05971    208 KLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLvignCSALFPIKPGS------MGKPIPGHRVAIVDDNGTP 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1831 LPVGCIGELYI--AGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGE 1908
Cdd:cd05971    281 LPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAE 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1909 IEAALRSIEGVREAAVTVRTD--SGEpELCAYV---------EGLQRnEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 1977
Cdd:cd05971    354 IEECLLKHPAVLMAAVVGIPDpiRGE-IVKAFVvlnpgetpsDALAR-EIQELVKTRLAAHEYPREIEFVNELPRTATGK 431


                   ....*.
gi 1678550997 1978 LDRNAL 1983
Cdd:cd05971    432 IRRREL 437
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1500-1983 7.35e-41

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 159.74  E-value: 7.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PRK03640     8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTnILLLQSAGLHVPEFTGEIVYLNQTNSGlahrlsnPNVDVLPQS------LAYVIYTSGSTGMPKGV 1653
Cdd:PRK03640    88 REELLWQLDDAEV-KCLITDDDFEAKLIPGISVKFAELMNG-------PKEEAEIQEefdldeVATIMYTSGTTGKPKGV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1654 EIEHR----SAV-NFLNslqsrYQLKHSDM------IMHKTSYS--FDASIWelfwwpyaGASVYLLPQGGEKEpevIAK 1720
Cdd:PRK03640   160 IQTYGnhwwSAVgSALN-----LGLTEDDCwlaavpIFHISGLSilMRSVIY--------GMRVVLVEKFDAEK---INK 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1721 AIEEQKITAMHFVPSMLHAFLEHIKYRSVPiktNRLKRVFSGG--------EQLGTHlvsrfyellpNVSITNSYGPTEA 1792
Cdd:PRK03640   224 LLQTGGVTIISVVSTMLQRLLERLGEGTYP---SSFRCMLLGGgpapkpllEQCKEK----------GIPVYQSYGMTET 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1793 TVEAAFFdcPPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPvGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypger 1871
Cdd:PRK03640   291 ASQIVTL--SPEDALTKLgSAGKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF----- 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 myKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEPEL------CAYV---EGL 1942
Cdd:PRK03640   363 --KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV-----GVPDDkwgqvpVAFVvksGEV 435

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1678550997 1943 QRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK03640   436 TEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 2559-3019 1.34e-40

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: 157.64  E-value: 1.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTIN 2638
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 EADlgvladfegeiltiesveeddksplpqmssahHLAYIIYTSGTTGRPKGVMVEHKGI-ANTLQWRRnAYAFNETDTI 2717
Cdd:cd05935     82 ELD--------------------------------DLALIPYTSGTTGLPKGCMHTHFSAaANALQSAV-WTGLTPSDVI 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2718 LQ-LFSFSFDGFITSMFTPLLSGAKAVLL---HEEEAKDIlaikhqLSRQRITHMIIVPVLYRALLDVV--QPEDVKTLR 2791
Cdd:cd05935    129 LAcLPLFHVTGFVGSLNTAVYVGGTYVLMarwDRETALEL------IEKYKVTFWTNIPTMLVDLLATPefKTRDLSSLK 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2792 VVTlAGEAADRELIARSLAICPHTELANEYGPTEnSVATTVMRHMEKQAYVSIGQPIDGTQVLILN-SNHQLQPIGVAGE 2870
Cdd:cd05935    203 VLT-GGGAPMPPAVAEKLLKLTGLRFVEGYGLTE-TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGE 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2871 LCIAGTGLARGYVNLPELTERAFTQNPFKpeaRMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKG 2950
Cdd:cd05935    281 IVVRGPQIFKGYWNRPEETEESFIEIKGR---RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 2951 VKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05935    358 I*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIiewaREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1486-1924 3.08e-40

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 160.27  E-value: 3.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1486 EETGYSMNQTLHYALEQQAEKTPDQAAVIF-EDGV---MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGI 1561
Cdd:COG1022      3 EFSDVPPADTLPDLLRRRAARFPDRVALREkEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIAD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1562 YGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGL---------HVPEFTgEIVYLNQTNSGLAHRL------- 1625
Cdd:COG1022     83 LAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQldkllevrdELPSLR-HIVVLDPRGLRDDPRLlsldell 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1626 ------SNPN------VDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMhktSY-----SFd 1688
Cdd:COG1022    162 algrevADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL---SFlplahVF- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1689 ASIWELFWWpYAGASVYLLPqggekEPEVIAKAIEEQKITAMHFVP---------------------------------- 1734
Cdd:COG1022    238 ERTVSYYAL-AAGATVAFAE-----SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalavgrr 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 ---------------SMLHAFLEHIKYRsvPIKT---NRLKRVFSGGEQLGTHLVsRFYELLpNVSITNSYGPTEATVeA 1796
Cdd:COG1022    312 yararlagkspslllRLKHALADKLVFS--KLREalgGRLRFAVSGGAALGPELA-RFFRAL-GIPVLEGYGLTETSP-V 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1797 AFFDCPPHEKLERipIGKPVHHVRLYLLNQnqrmlpvgciGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTG 1876
Cdd:COG1022    387 ITVNRPGDNRIGT--VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTG 448

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997 1877 DVARWLPDGNVEFLGRTDDQVKIR-GYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:COG1022    449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 2529-3021 1.57e-39

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 157.40  E-value: 1.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2529 QYGvqTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMM--HRSFsmIASILGVWKA 2606
Cdd:PRK07788    47 RYG--PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLArnHRGF--VLALYAAGKV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDPEYPKERKRYILSDSGTKLLMtINEADLGVLADFE---GEILTI------------------ESVEEDDKSP 2665
Cdd:PRK07788   123 GARIILLNTGFSGPQLAEVAAREGVKALV-YDDEFTDLLSALPpdlGRLRAWggnpdddepsgstdetldDLIAGSSTAP 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2666 LPQMSSAHHLayIIYTSGTTGRPKGVMVEH-------KGIANTLQWRRNayafnetDTILQ---LF-SFSFDGFITSMFT 2734
Cdd:PRK07788   202 LPKPPKPGGI--VILTSGTTGTPKGAPRPEpsplaplAGLLSRVPFRAG-------ETTLLpapMFhATGWAHLTLAMAL 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2735 pllsGAKAVLLHEEEAKDILAikhQLSRQRITHMIIVPVLYRALLD----VVQPEDVKTLRVVTLAGEAADRELIARSL- 2809
Cdd:PRK07788   273 ----GSTVVLRRRFDPEATLE---DIAKHKATALVVVPVMLSRILDlgpeVLAKYDTSSLKIIFVSGSALSPELATRALe 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2810 AICPhtELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNlpelt 2889
Cdd:PRK07788   346 AFGP--VLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----- 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2890 eraftqNPFKPEAR-MYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhV--TASGQt 2966
Cdd:PRK07788   419 ------GRDKQIIDgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG-VddEEFGQ- 490

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2967 ELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPK 3021
Cdd:PRK07788   491 RLRAFVVKAPGaaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 2534-3015 3.43e-39

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 155.81  E-value: 3.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI 2613
Cdd:PRK07798     4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 DPEYPKERKRYILSDSGTKLLmtINEADLG-----VLADFEGEILTIEsVEEDDKSPLP-----------QMSSAHHLA- 2676
Cdd:PRK07798    84 NYRYVEDELRYLLDDSDAVAL--VYEREFAprvaeVLPRLPKLRTLVV-VEDGSGNDLLpgavdyedalaAGSPERDFGe 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 ------YIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSM---------------FTP 2735
Cdd:PRK07798   161 rspddlYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEELAKRAAAGPGMRRfpapplmhgagqwaaFAA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2736 LLSGAKAVLLHEEE--AKDILAIKHqlsRQRITHMIIV-PVLYRALLDVVQPE---DVKTLRVVTLAGEAADRELIARSL 2809
Cdd:PRK07798   241 LFSGQTVVLLPDVRfdADEVWRTIE---REKVNVITIVgDAMARPLLDALEARgpyDLSSLFAIASGGALFSPSVKEALL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2810 AICPHTELANEYGPTEnsvATTVMRHMEKQAYVSIGQP---IDGTQVLILNSNHQLQP-IGVAGElcIAGTG-LARGYVN 2884
Cdd:PRK07798   318 ELLPNVVLTDSIGSSE---TGFGGSGTVAKGAVHTGGPrftIGPRTVVLDEDGNPVEPgSGEIGW--IARRGhIPLGYYK 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2885 LPELTERAFtqnpfkPEARMYR---TGDAARWMADGTLEYLGRidDQVKIR--GYRVETKEIESVIRCIKGVKDAAVVAh 2959
Cdd:PRK07798   393 DPEKTAETF------PTIDGVRyaiPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVG- 463

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2960 vTAS---GQtELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:PRK07798   464 -VPDerwGQ-EVVAVVQLREGarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 1520-1983 4.10e-39

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: 153.40  E-value: 4.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQS 1599
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 AglhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVnfLNSLQSR--YQLKHSD 1677
Cdd:cd05935     82 E---------------------------------LDDLALIPYTSGTTGLPKGCMHTHFSAA--ANALQSAvwTGLTPSD 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1678 MIM------HKTSY--SFDASIwelfwwpYAGASVYLLpqgGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSV 1749
Cdd:cd05935    127 VILaclplfHVTGFvgSLNTAV-------YVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTR 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1750 PIKTnrLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEAtveaaffdCP-----PHEKLERIPIGKPVHHVRLYLL 1824
Cdd:cd05935    197 DLSS--LKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTET--------MSqthtnPPLRPKLQCLGIP*FGVDARVI 265

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1825 N-QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYR 1903
Cdd:cd05935    266 DiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK---GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1904 IEPGEIEAALRSIEGVREAAVTVRTD--SGEpELCAYVegLQRNEVRAQL---------ERLLPGYMVPAYMIEMEQWPV 1972
Cdd:cd05935    343 VWPAEVEAKLYKHPAI*EVCVISVPDerVGE-EVKAFI--VLRPEYRGKVteediiewaREQMAAYKYPREVEFVDELPR 419

                          490
                   ....*....|.
gi 1678550997 1973 TPSGKLDRNAL 1983
Cdd:cd05935    420 SASGKILWRLL 430
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1521-1983 5.20e-39

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: 152.88  E-value: 5.20e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSa 1600
Cdd:cd05972      2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeivylnqtnsglahrlsnpnvdvlpQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIm 1680
Cdd:cd05972     81 ----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH- 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1681 hktsYSFDASIWELFWWpYAGASVYLLP------QGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPiktN 1754
Cdd:cd05972    126 ----WNIADPGWAKGAW-SSFFGPWLLGatvfvyEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF---S 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1755 RLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAFFDC-PPHekleriP--IGKPVHHVRLYLLNQNQRML 1831
Cdd:cd05972    198 HLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFPDmPVK------PgsMGRPTPGYDVAIIDDDGREL 270

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1832 PVGCIGELYI--AGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEI 1909
Cdd:cd05972    271 PPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1910 EAALRSIEGVREAAVTVRTD--------------SGEPELCAYVEGLQrNEVRAQLERllpgYMVPaYMIEM-EQWPVTP 1974
Cdd:cd05972    344 ESALLEHPAVAEAAVVGSPDpvrgevvkafvvltSGYEPSEELAEELQ-GHVKKVLAP----YKYP-REIEFvEELPKTI 417


                   ....*....
gi 1678550997 1975 SGKLDRNAL 1983
Cdd:cd05972    418 SGKIRRVEL 426
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1494-1983 7.25e-39

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: 154.20  E-value: 7.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAVIFEDG--VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAY 1571
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1572 LPIDPDYPEERISFLLEDSGTNILLLQSAGLHVPEF---TGEIVYLNQ-TNSGLAHRLSNPNVD--VLPQSLAYVIYTSG 1645
Cdd:cd05923     81 ALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIfqsGVRVLALSDlVGLGEPESAGPLIEDppREPEQPAFVFYTSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1646 STGMPKGVEIEHRSAVNFLNSLQSRYQLKHSD-------MIMHKTSYSFdasiwELFWWPYAGASVYLLPQggEKEPEVI 1718
Cdd:cd05923    161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhnvvlglMPLYHVIGFF-----AVLVAALALDGTYVVVE--EFDPADA 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1719 AKAIEEQKITAMHFVPSMLHAFLEHIKYrsVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNvSITNSYGPTEATveAAF 1798
Cdd:cd05923    234 LKLIEQERVTSLFATPTHLDALAAAAEF--AGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAM--NSL 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1799 FDCPPHEKLEripiGKP--VHHVRLY-LLNQNQRMLPVGCIGELYIAGAGVA--RGYLNRPALTEERFLEdpfypgeRMY 1873
Cdd:cd05923    309 YMRDARTGTE----MRPgfFSEVRIVrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWY 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1874 KTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYVeglqRNEVRAQL 1951
Cdd:cd05923    378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADErwGQSVTACVV----PREGTLSA 453

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997 1952 ERL--------LPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05923    454 DELdqfcraseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 2533-3014 8.48e-39

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 154.71  E-value: 8.48e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVP 2612
Cdd:PRK08316    11 QTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2613 IDPEYPKERKRYILSDSGTKLLMTinEADLGVLADFEGEILTIESVEEDDKSPLPQMSSAHH------------------ 2674
Cdd:PRK08316    91 VNFMLTGEELAYILDHSGARAFLV--DPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLdfadwaeagsvaepdvel 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 ----LAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQ---LF-SFSFDGFitsMFTPLLSGAKAVLLH 2746
Cdd:PRK08316   169 adddLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHalpLYhCAQLDVF---LGPYLYVGATNVILD 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2747 EEEAKDILAIkhqLSRQRITHMIIVPVLYRALL--DVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPT 2824
Cdd:PRK08316   246 APDPELILRT---IEAERITSFFAPPTVWISLLrhPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQT 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2825 ENSVATTVMR---HMEKQAyvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpe 2901
Cdd:PRK08316   323 EIAPLATVLGpeeHLRRPG--SAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--- 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2902 armyRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVA--H------VTasgqtelsAYVV 2973
Cdd:PRK08316   398 ----HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGlpDpkwieaVT--------AVVV 465

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 2974 TKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:PRK08316   466 PKAGatVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 490-952 1.38e-38

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: 151.83  E-value: 1.38e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQAH 569
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  570 LpsSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN-----MANLLKFEYThsgidfEA 644
Cdd:TIGR01923   81 L--EEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNhyasaVGSKENLGFT------ED 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  645 DVLQFATPSFDVCYQEI-FSALLKGGTLHIV-PEAikrdvpQLFAFINKHQ-TNIVFLPTAFIKMIfseRELanSFPDGV 721
Cdd:TIGR01923  153 DNWLLSLPLYHISGLSIlFRWLIEGATLRIVdKFN------QLLEMIANERvTHISLVPTQLNRLL---DEG--GHNENL 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  722 KHLIAAGEQLMISdLFQDVlRKRGIHLHNHYGPSEThvVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQpcgvp 801
Cdd:TIGR01923  222 RKILLGGSAIPAP-LIEEA-QQYGLPIYLSYGMTET--CSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH----- 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  802 GELYISGASVARGYVNHDKLTSDKFSSDPFKpdvimyrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNH 881
Cdd:TIGR01923  293 GEIMVKGANLMKGYLYQGELTPAFEQQGWFN-------TGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH 365

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  882 PDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:TIGR01923  366 PGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 1521-1985 1.40e-38

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: 151.89  E-value: 1.40e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLlqsa 1600
Cdd:cd05969      2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeivylnqTNSGLAHRLSnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM 1680
Cdd:cd05969     78 ----------------TTEELYERTD-------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1681 HKTSYSFDASIWELFWWPYA-GASVYLlpQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRV 1759
Cdd:cd05969    135 CTADPGWVTGTVYGIWAPWLnGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFI 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1760 FSGGEQLGTHLVSRFYELLpNVSITNSYGPTE-ATVEAAFFDCPPhekLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGE 1838
Cdd:cd05969    213 HSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTEtGSIMIANYPCMP---IKPGSMGKPLPGVKAAVVDENGNELPPGTKGI 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1839 LYIAGA--GVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSI 1916
Cdd:cd05969    289 LALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH 361

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 1917 EGVREAAVTVRTDSGEPELC-AYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:cd05969    362 PAVAEAGVIGKPDPLRGEIIkAFIslkEGFEpsdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1501-1985 2.06e-38

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 153.93  E-value: 2.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1501 EQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPE 1580
Cdd:PRK07788    56 AHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1581 ERISFLLEDSGTNILLlqsaglHVPEFTGEIVYLNQTNSGL--------AHRLSNPNVDVLPQSLA-------------- 1638
Cdd:PRK07788   136 PQLAEVAAREGVKALV------YDDEFTDLLSALPPDLGRLrawggnpdDDEPSGSTDETLDDLIAgsstaplpkppkpg 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1639 -YVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HKTSYSFDASIWELfwwpyaGASVYLLpqgg 1711
Cdd:PRK07788   210 gIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLlpapmfHATGWAHLTLAMAL------GSTVVLR---- 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1712 EK-EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPT 1790
Cdd:PRK07788   280 RRfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGST 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1791 EATVeAAFFDcpPHEkLERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLN-RPALTEERFLEdpfy 1867
Cdd:PRK07788   359 EVAF-ATIAT--PED-LAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQIIDGLLS---- 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 pgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---EGLQ 1943
Cdd:PRK07788   431 -------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQRLRAFVvkaPGAA 503

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1678550997 1944 RNE------VRAQLERllpgYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:PRK07788   504 LDEdaikdyVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKRELRE 547
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 460-954 2.68e-38

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 153.38  E-value: 2.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  460 PVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGA 539
Cdd:PRK06155    18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  540 IVPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLEdnYIITHPEDIES--KVDGSNIKSVNNA---------------- 601
Cdd:PRK06155    98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALE--AADPGDLPLPAvwLLDAPASVSVPAGwstaplppldapapaa 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 ----DDLLYMIYTSGTTGKPKGVQFEH-------RNMANLLKFEythsgidfEADVLQFATPSFDVCYQEIF-SALLKGG 669
Cdd:PRK06155   176 avqpGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLEIG--------ADDVLYTTLPLFHTNALNAFfQALLAGA 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  670 TLHIVPeaiKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDGVKHLIAAGeqlmISDLFQDVLRKR-GIHL 748
Cdd:PRK06155   248 TYVLEP---RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG----VPAALHAAFRERfGVDL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  749 HNHYGPSETHVVStytihpGDPIPELPP--IGKPIGCTDLYILNHQKQLQPCGVPGELYISGA---SVARGYVNHDKLTS 823
Cdd:PRK06155   321 LDGYGSTETNFVI------AVTHGSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTV 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  824 DKFSSdpfkpdvIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCA 903
Cdd:PRK06155   395 EAWRN-------LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMA 467

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997  904 yycSV-----QKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK06155   468 ---AVvlrdgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 2533-3019 2.74e-38

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: 152.28  E-value: 2.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALV--SGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCY 2610
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2611 VPIDPEY-PKERKRYILSDSGTKLLMTINEADLGVLADFEGEILTIE------SVEEDDKSPLPQMSSAHHLAYIIYTSG 2683
Cdd:cd05923     81 ALINPRLkAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSdlvglgEPESAGPLIEDPPREPEQPAFVFYTSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2684 TTGRPKGVMVEHKGIANTLQW--RRNAYAFNETDTILQLFS-FSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIkhqL 2760
Cdd:cd05923    161 TTGLPKGAVIPQRAAESRVLFmsTQAGLRHGRHNVVLGLMPlYHVIGFFAVLVAALALDGTYVVVEEFDPADALKL---I 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2761 SRQRITHMIIVPVLYRALLDVVQ--PEDVKTLRVVTLAGEAADRELIARsLAICPHTELANEYGPTEnSVATTVMRHMEK 2838
Cdd:cd05923    238 EQERVTSLFATPTHLDALAAAAEfaGLKLSSLRHVTFAGATMPDAVLER-VNQHLPGEKVNIYGTTE-AMNSLYMRDART 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2839 QAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLA--RGYVNLPELTERaftqnpfKPEARMYRTGDAARWMAD 2916
Cdd:cd05923    316 GTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAK-------KLQDGWYRTGDVGYVDPS 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2917 GTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG-LSTNAVR-----SELQNk 2990
Cdd:cd05923    389 GDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGtLSADELDqfcraSELAD- 467

                          490       500
                   ....*....|....*....|....*....
gi 1678550997 2991 lpvFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05923    468 ---FKRPRRYFFLDELPKNAMNKVLRRQL 493
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 463-952 5.43e-38

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: 152.22  E-value: 5.43e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGgaIVP 542
Cdd:COG1021     25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIP 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  543 VDPhYPADRIRYILHDCGCS----HVVSQAHLP--------------SSLEDNYIITHPEDIES-----KVDGSNIKSVN 599
Cdd:COG1021    103 VFA-LPAHRRAEISHFAEQSeavaYIIPDRHRGfdyralarelqaevPSLRHVLVVGDAGEFTSldallAAPADLSEPRP 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 NADDLLYMIYTSGTTGKPKGVQFEHRnmanllkfEYTHS--------GIDfEADVLQFATP---SFDVCYQEIFSALLKG 668
Cdd:COG1021    182 DPDDVAFFQLSGGTTGLPKLIPRTHD--------DYLYSvrasaeicGLD-ADTVYLAALPaahNFPLSSPGVLGVLYAG 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  669 GT--LHIVPEAikrdvPQLFAFINKHQTNIVFL-PTAFIKMI-FSERELANsfPDGVKHLIAAGEQLmisdlfQDVLRKR 744
Cdd:COG1021    253 GTvvLAPDPSP-----DTAFPLIERERVTVTALvPPLALLWLdAAERSRYD--LSSLRVLQVGGAKL------SPELARR 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 -----GIHLHNHYGPSETHVvsTYTiHPGDPiPELppI----GKPIgCTD--LYILNHQKQLQPCGVPGELYISGASVAR 813
Cdd:COG1021    320 vrpalGCTLQQVFGMAEGLV--NYT-RLDDP-EEV--IlttqGRPI-SPDdeVRIVDEDGNPVPPGEVGELLTRGPYTIR 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVkIR-GYRIEPQEIEVTLMNHPDISEAAILIW 892
Cdd:COG1021    393 GYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAM 465

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  893 QDQN-GEhELCAYY-CSVQKLNTIDLRSYMAS-ELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:COG1021    466 PDEYlGE-RSCAFVvPRGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 12-356 6.31e-38

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: 149.72  E-value: 6.31e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNV-IVLE 90
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED-GVPYQLILEEDEAtPKLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   91 edITHLNEAEQSQFIEQWKEkdrdRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNA 170
Cdd:cd19538     82 --IKEVDEEELESEINEAVR----YPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  171 SPITLE--PVQpYGKYIKW---LMEQDKEQA------VSYWDHYLSGHEQQTVL------PKQKKTKGksrqEHVTFSFS 233
Cdd:cd19538    156 EAPELAplPVQ-YADYALWqqeLLGDESDPDsliarqLAYWKKQLAGLPDEIELptdyprPAESSYEG----GTLTFEID 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  234 KEESSRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRpaEIEGIEHMVGLFINTMPVRVQGAKTP-FLQ 312
Cdd:cd19538    231 SELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLVLRTDTSGNPsFRE 308

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997  313 LIKDMQKDRLAAEAYSYHPLYEI-----QSRSAVKQGLIDHILVFENYP 356
Cdd:cd19538    309 LLERVKETNLEAYEHQDIPFERLvealnPTRSRSRHPLFQIMLALQNTP 357
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1510-1983 1.02e-37

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: 149.53  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1510 QAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLED 1589
Cdd:cd05919      1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1590 SGTNILLLQSAglhvpeftgeivylnqtnsglahrlsnpnvdvlpqSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQS 1669
Cdd:cd05919     81 CEARLVVTSAD-----------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1670 RY-QLKHSDMIMHKTSYSFDASIWELFWWP-YAGASVYLLPqgGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYR 1747
Cdd:cd05919    126 EAlGLTPGDRVFSSAKMFFGYGLGNSLWFPlAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1748 SVPIKTNRLkrVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEAtveAAFFDCPPHEKLERIPIGKPVHHVRLYLLNQN 1827
Cdd:cd05919    204 PDALRSLRL--CVSAGEALPRGLGERWMEHF-GGPILDGIGATEV---GHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1828 QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 1907
Cdd:cd05919    278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPV 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1908 EIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---------EGLQRNEVRAQLERlLPGYMVPAYMIEMEQWPVTPSGK 1977
Cdd:cd05919    351 EVESLIIQHPAVAEAAVVaVPESTGLSRLTAFVvlkspaapqESLARDIHRHLLER-LSAHKVPRRIAFVDELPRTATGK 429


                   ....*.
gi 1678550997 1978 LDRNAL 1983
Cdd:cd05919    430 LQRFKL 435
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 2543-3014 2.00e-37

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 150.04  E-value: 2.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERK 2622
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 RYILSDSGTKLLMTINEADlgVLADFEGEILTIESVEEDDKSPL--------PQMSSA-HHLAYIIYTSGTTGRPKGVMV 2693
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFD--AIVALETPKIVIDAAAQADSRRLaqggleipPQAAVApTDLVRLMYTSGTTDRPKGVMH 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2694 EHkgiaNTLQWRRN----AYAFNETDTIL------QLFSFSFDGFITsmftpLLSGAKAVLLHEEEAKDILAikhQLSRQ 2763
Cdd:PRK06145   170 SY----GNLHWKSIdhviALGLTASERLLvvgplyHVGAFDLPGIAV-----LWVGGTLRIHREFDPEAVLA---AIERH 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2764 RITHMIIVPVLYRALLDVVQPE--DVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVM---RHMEK 2838
Cdd:PRK06145   238 RLTCAWMAPVMLSRVLTVPDRDrfDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMeagREIEK 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2839 QAyvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmyRTGDAARWMADGT 2918
Cdd:PRK06145   318 IG--STGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGF 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2919 LEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMH 2996
Cdd:PRK06145   389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGatLTLEALDRHCRQRLASFKV 468

                          490
                   ....*....|....*...
gi 1678550997 2997 PAFIEKLDSLPLSPNGKL 3014
Cdd:PRK06145   469 PRQLKVRDELPRNPSGKV 486
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 2533-3019 2.03e-37

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: 150.68  E-value: 2.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGcyVP 2612
Cdd:COG1021     25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IP 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2613 IDPeYPKERK---RYILSDSGTKLLMTINEADL--------GVLADFE-----------GEILTIESVEEDDKSPLPQMS 2670
Cdd:COG1021    103 VFA-LPAHRRaeiSHFAEQSEAVAYIIPDRHRGfdyralarELQAEVPslrhvlvvgdaGEFTSLDALLAAPADLSEPRP 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2671 SAHHLAYIIYTSGTTGRPKGvmvehkgIANT-----LQWRRNAYA--FNETDTILQL------FSFSFDGFitsmFTPLL 2737
Cdd:COG1021    182 DPDDVAFFQLSGGTTGLPKL-------IPRThddylYSVRASAEIcgLDADTVYLAAlpaahnFPLSSPGV----LGVLY 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2738 SGAKAVLLHEEEAKDILAIkhqLSRQRITHMIIVPVLYRALLDVVQ--PEDVKTLRVV-----TLAGEAADR---ELIAR 2807
Cdd:COG1021    251 AGGTVVLAPDPSPDTAFPL---IERERVTVTALVPPLALLWLDAAErsRYDLSSLRVLqvggaKLSPELARRvrpALGCT 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2808 slaicphteLANEYGPTENSVATTVMRHMEKQAYVSIGQPI-DGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLP 2886
Cdd:COG1021    328 ---------LQQVFGMAEGLVNYTRLDDPEEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAP 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2887 ELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVkIR-GYRVETKEIESVIRCIKGVKDAAVVAHVTAS-G 2964
Cdd:COG1021    399 EHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYlG 471

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2965 qtELS-AYVVTK-PGLSTNAVRSELQNK-LPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:COG1021    472 --ERScAFVVPRgEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 2527-3019 2.59e-37

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 150.94  E-value: 2.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2527 ANQYgvQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKA 2606
Cdd:PRK07059    19 ASQY--PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDPEY-PKERKrYILSDSGTKLLMTINE-------------------ADLGVLADFEGEI--LTIESVeeddKS 2664
Cdd:PRK07059    97 GYVVVNVNPLYtPRELE-HQLKDSGAEAIVVLENfattvqqvlaktavkhvvvASMGDLLGFKGHIvnFVVRRV----KK 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2665 PLPQMSSAHH------------------------LAYIIYTSGTTGRPKGVMVEHKGI-ANTLQ---WRRNAYA----FN 2712
Cdd:PRK07059   172 MVPAWSLPGHvrfndalaegarqtfkpvklgpddVAFLQYTGGTTGVSKGATLLHRNIvANVLQmeaWLQPAFEkkprPD 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2713 ETDTILQL-----FSFSFDGFITsmftpLLSGAKAVLLheEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDvvQPE-- 2785
Cdd:PRK07059   252 QLNFVCALplyhiFALTVCGLLG-----MRTGGRNILI--PNPRDIPGFIKELKKYQVHIFPAVNTLYNALLN--NPDfd 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2786 --DVKTLRVVTLAGEAADRELIARSLAI--CPHTElanEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQ 2861
Cdd:PRK07059   323 klDFSKLIVANGGGMAVQRPVAERWLEMtgCPITE---GYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGN 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2862 LQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEI 2941
Cdd:PRK07059   400 DLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEI 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2942 ESVIRCIKGVKDAAVVA-HVTASGQTeLSAYVVTK-PGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK07059   474 EEVVASHPGVLEVAAVGvPDEHSGEA-VKLFVVKKdPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
2531-2962 7.50e-37

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 150.25  E-value: 7.50e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2531 GVQTISQLFEQQAARTPKASAL---VSGD-KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKA 2606
Cdd:COG1022      9 PADTLPDLLRRRAARFPDRVALrekEDGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDPEYPKERKRYILSDSGTKLLMTINEADLGVLADFEGE------ILTIESVEEDDKSPLPQMS---------- 2670
Cdd:COG1022     89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElpslrhIVVLDPRGLRDDPRLLSLDellalgreva 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2671 ------------SAHHLAYIIYTSGTTGRPKGVMVEHKGI-ANTLQWRRnAYAFNETDTILqlfSF-----SFDGFITSM 2732
Cdd:COG1022    169 dpaelearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLlSNARALLE-RLPLGPGDRTL---SFlplahVFERTVSYY 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2733 FtpLLSGAKAVLlheeeAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQ------PEDVKTL-----RVVTLAGEA-- 2799
Cdd:COG1022    245 A--LAAGATVAF-----AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQakaeeaGGLKRKLfrwalAVGRRYARArl 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2800 ---------------ADReLIARSL----------AIC------PHT------------ELaneYGPTENSVATTVMRhM 2836
Cdd:COG1022    318 agkspslllrlkhalADK-LVFSKLrealggrlrfAVSggaalgPELarffralgipvlEG---YGLTETSPVITVNR-P 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2837 EKQAYVSIGQPIDGTQVlilnsnhqlqPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMAD 2916
Cdd:COG1022    393 GDNRIGTVGPPLPGVEV----------KIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDED 456

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2917 GTLEYLGRIDDQVKIR-GYRVETKEIESVIRCIKGVKDAAVVAH----VTA 2962
Cdd:COG1022    457 GFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGDgrpfLAA 507
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 473-952 1.26e-36

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: 147.09  E-value: 1.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGgaIVPVDPhYPADRI 552
Cdd:cd05920     25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPVLA-LPSHRR 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSqahlpsslednYIIthpEDIESKVDGSN--IKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANL 630
Cdd:cd05920    102 SELSAFCAHAEAVA-----------YIV---PDRHAGFDHRAlaRELAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  631 LKFEYTHSGIDfEADVLQFATP---SFDVCYQEIFSALLKGGTLHIVPEAIKRDVpqlFAFINKHQTNIVFLPTAFIKMI 707
Cdd:cd05920    168 VRASAEVCGLD-QDTVYLAVLPaahNFPLACPGVLGTLLAGGRVVLAPDPSPDAA---FPLIEREGVTVTALVPALVSLW 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  708 FSERElANSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVvsTYTiHPGDPiPELppI----GKPIGC 783
Cdd:cd05920    244 LDAAA-SRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL--NYT-RLDDP-DEV--IihtqGRPMSP 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TD-LYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:cd05920    317 DDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRIKDQI 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEhELCAY-YCSVQKLNTIDLRSYM-ASELPEYMIPAKWIWVDSI 939
Cdd:cd05920    391 NRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGE-RSCAFvVLRDPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSL 469

                          490
                   ....*....|...
gi 1678550997  940 PLTPNGKVDRAAL 952
Cdd:cd05920    470 PLTAVGKIDKKAL 482
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 2533-3019 3.10e-36

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 147.21  E-value: 3.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVP 2612
Cdd:PRK06155    21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2613 IDPEYPKERKRYILSDSGTKLLMT-------INEADLGVLAdfEGEILTIESVEED------DKSPLPQMSSA------- 2672
Cdd:PRK06155   101 INTALRGPQLEHILRNSGARLLVVeaallaaLEAADPGDLP--LPAVWLLDAPASVsvpagwSTAPLPPLDAPapaaavq 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2673 -HHLAYIIYTSGTTGRPKGVMVEHkgiANTLQWRRN---AYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEE 2748
Cdd:PRK06155   179 pGDTAAILYTSGTTGPSKGVCCPH---AQFYWWGRNsaeDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRF 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2749 EAKDILA--IKHQLSrqrITHMI--IVPVLyralldVVQP----EDVKTLRVVTLAGEAAD--RELIARSlaicpHTELA 2818
Cdd:PRK06155   256 SASGFWPavRRHGAT---VTYLLgaMVSIL------LSQParesDRAHRVRVALGPGVPAAlhAAFRERF-----GVDLL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 NEYGPTENSVATTVMRHMEKQAYvsIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGT---GLARGYVNLPELTERAFtQ 2895
Cdd:PRK06155   322 DGYGSTETNFVIAVTHGSQRPGS--MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW-R 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2896 NPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTK 2975
Cdd:PRK06155   399 NLW------FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLR 472

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1678550997 2976 PGLSTN--AVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06155   473 DGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2114-2399 3.69e-36

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: 144.55  E-value: 3.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2114 AVLELEGK-LNPERMDRAFQELIKRHESLRTSFeqDEGGDpvQRIHDEVP-FTLQTTVLGARTEQEAAAAFIK------- 2184
Cdd:cd19535     28 AYLEFDGEdLDPDRLERAWNKLIARHPMLRAVF--LDDGT--QQILPEVPwYGITVHDLRGLSEEEAEAALEElrerlsh 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2185 -PFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRK--LPALRIQYKDYAVWQEGFKtGDAY 2261
Cdd:cd19535    104 rVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGepLPPLELSFRDYLLAEQALR-ETAY 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2262 KMQEAYWLKQLEG-----ELPVLDLPADHARPPVRSFagdkvSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRL 2336
Cdd:cd19535    183 ERARAYWQERLPTlppapQLPLAKDPEEIKEPRFTRR-----EHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2337 SGQEDIIVGSPIAGRP--HKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNY 2399
Cdd:cd19535    258 SGQPRFLLNLTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSY 322
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 2549-3019 4.14e-36

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: 144.54  E-value: 4.14e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2549 ASALVSGDKTLTYQELDEWSNGIARALRSRGV-KPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILS 2627
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2628 DSgtkllmtinEADLGVLADfegeiltiesveeddksplpQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQ-WRR 2706
Cdd:cd05958     81 KA---------RITVALCAH--------------------ALTASDDICILAFTSGTTGAPKATMHFHRDPLASADrYAV 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2707 NAYAFNETDTILQL----FSFSFDGFitsMFTPLLSGAKAVLLHEEEAKDILAIkhqLSRQRITHMIIVPVLYRALL--- 2779
Cdd:cd05958    132 NVLRLREDDRFVGSpplaFTFGLGGV---LLFPFGVGASGVLLEEATPDLLLSA---IARYKPTVLFTAPTAYRAMLahp 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2780 DVVQPeDVKTLRVVTLAGEAADRELIARSLAICpHTELANEYGPTEnsvattvMRHM-----EKQAYV-SIGQPIDGTQV 2853
Cdd:cd05958    206 DAAGP-DLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTE-------MFHIfisarPGDARPgATGKPVPGYEA 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2854 LILNSNHQLQPIGVAGELCIAGtglARGYVNLPELTERAFTQNPFKPearmyrTGDAARWMADGTLEYLGRIDDQVKIRG 2933
Cdd:cd05958    277 KVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGG 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2934 YRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTN-AVRSELQN----KLPVFMHPAFIEKLDSLPL 3008
Cdd:cd05958    348 YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpVLARELQDhakaHIAPYKYPRAIEFVTELPR 427

                          490
                   ....*....|.
gi 1678550997 3009 SPNGKLDRGAL 3019
Cdd:cd05958    428 TATGKLQRFAL 438
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 2559-3019 4.30e-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: 144.57  E-value: 4.30e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTIN 2638
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 EadlgvLADfegeiltiesvEEDDKSPlpqmssahhlAYIIYTSGTTGRPKGVMVEHKgiANTLQWRRNAYAFNETDTil 2718
Cdd:cd05969     81 E-----LYE-----------RTDPEDP----------TLLHYTSGTTGTPKGVLHVHD--AMIFYYFTGKYVLDLHPD-- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2719 QLFSFSFD-GFIT----SMFTPLLSGAKAVLlhEEEAKDILAIKHQLSRQRITHMIIVPVLYRALL----DVVQPEDVKT 2789
Cdd:cd05969    131 DIYWCTADpGWVTgtvyGIWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMkegdELARKYDLSS 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2790 LRVVTLAGEAADRELIARSLAICpHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAG 2869
Cdd:cd05969    209 LRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKG 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2870 ELCI-AG-TGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRC 2947
Cdd:cd05969    288 ILALkPGwPSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALME 360

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2948 IKGVKDAAVVAHVTASGQTELSAYVVTKPGLS-TNAVRSELQN----KLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05969    361 HPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEpSDELKEEIINfvrqKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 1508-1986 5.74e-36

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 145.90  E-value: 5.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1508 PDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLL 1587
Cdd:PRK06188    26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLL--------------QSAGL-HVpeFT-GEIVYLNQTNSGLAHRLSNPNVDV-LPQSLAYVIYTSGSTGMP 1650
Cdd:PRK06188   106 EDAGISTLIVdpapfveralallaRVPSLkHV--LTlGPVPDGVDLLAAAAKFGPAPLVAAaLPPDIAGLAYTGGTTGKP 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1651 KGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASiweLFWWP--YAGASVYLLPQggeKEPEVIAKAIEEQKIT 1728
Cdd:PRK06188   184 KGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG---AFFLPtlLRGGTVIVLAK---FDPAEVLRAIEEQRIT 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1729 AMHFVPSMLHAFLEH-------------IKYRSVPIKTNRLKRvfsGGEQLGTHLVsrfyellpnvsitNSYGPTEATVE 1795
Cdd:PRK06188   258 ATFLVPTMIYALLDHpdlrtrdlssletVYYGASPMSPVRLAE---AIERFGPIFA-------------QYYGQTEAPMV 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1796 AAFFD----CPPHEKLeRIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpger 1871
Cdd:PRK06188   322 ITYLRkrdhDPDDPKR-LTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLH---- 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 mykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EGLQRN- 1945
Cdd:PRK06188   397 ---TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEkwGE-AVTAVVvlrPGAAVDa 472

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 1946 -EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAP 1986
Cdd:PRK06188   473 aELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 488-952 5.94e-36

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: 144.16  E-value: 5.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQ 567
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 AHLpsslednyiithpedieskvdgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEaDVL 647
Cdd:cd05935     81 SEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS-DVI 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  648 QFATPSFDVC--YQEIFSALLKGGTLHIVPEAIKRDVPQLF-AFINKHQTNIvflPTAFIKMI----FSERELANsfpdg 720
Cdd:cd05935    129 LACLPLFHVTgfVGSLNTAVYVGGTYVLMARWDRETALELIeKYKVTFWTNI---PTMLVDLLatpeFKTRDLSS----- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  721 vKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSEThVVSTYTIHPGDpiPELPPIGKPIGCTDLYILNHQ--KQLQPc 798
Cdd:cd05935    201 -LKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET-MSQTHTNPPLR--PKLQCLGIP*FGVDARVIDIEtgRELPP- 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  799 GVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTL 878
Cdd:cd05935    276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRR---FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997  879 MNHPDISEAAILIWQDQNGEHELCAYYC----SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05935    353 YKHPAI*EVCVISVPDERVGEEVKAFIVlrpeYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 1500-1979 8.93e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 145.80  E-value: 8.93e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PRK07798     9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSaglhvpEFTGEIVYLNQTNSGLAHRL-----------------------SNPNVDVLPQS 1636
Cdd:PRK07798    89 EDELRYLLDDSDAVALVYER------EFAPRVAEVLPRLPKLRTLVvvedgsgndllpgavdyedalaaGSPERDFGERS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1637 L--AYVIYTSGSTGMPKGV----EIEHRSA---VNFLNSLQSRYQLKHSDMI--------------MHKTSYSfdASIWE 1693
Cdd:PRK07798   163 PddLYLLYTGGTTGMPKGVmwrqEDIFRVLlggRDFATGEPIEDEEELAKRAaagpgmrrfpapplMHGAGQW--AAFAA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1694 LFwwpyAGASVYLLPqGGEKEPEVIAKAIEEQKITAMHFV------PsMLHAFLEHIKYRsvpikTNRLKRVFSGGEQLG 1767
Cdd:PRK07798   241 LF----SGQTVVLLP-DVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGPYD-----LSSLFAIASGGALFS 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1768 THLVSRFYELLPNVSITNSYGPTEA----TVEAAffDCPPHEKLERIPIGKPVHhvrlyLLNQNQRMLPVGCIGELYIAG 1843
Cdd:PRK07798   310 PSVKEALLELLPNVVLTDSIGSSETgfggSGTVA--KGAVHTGGPRFTIGPRTV-----VLDEDGNPVEPGSGEIGWIAR 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1844 AG-VARGYLNRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRtdDQVKIR--GYRIEPGEIEAALRSIEGVR 1920
Cdd:PRK07798   383 RGhIPLGYYKDPEKTAETFPT---IDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVA 457

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1921 EAAVTVRTDS--GEpELCAYVE-----GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 1979
Cdd:PRK07798   458 DALVVGVPDErwGQ-EVVAVVQlregaRPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 1494-1983 9.11e-36

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: 145.89  E-value: 9.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAV-IFEDG---VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGG 1569
Cdd:cd05906     10 RTLLELLLRAAERGPTKGITyIDADGseeFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1570 --AYLPIDPDYPE--------ERISFLLEDSgtniLLLQSAGLhVPEF---TGEIVYLNQTNSGLAHRLSNPNVDVLPQS 1636
Cdd:cd05906     90 vpAPLTVPPTYDEpnarlrklRHIWQLLGSP----VVLTDAEL-VAEFaglETLSGLPGIRVLSIEELLDTAADHDLPQS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1637 ----LAYVIYTSGSTGMPKGVEIEHRsavNFLNSLQSRYQLKHSDmimhktsySFDASiweLFWWP--YAGASVYL---- 1706
Cdd:cd05906    165 rpddLALLMLTSGSTGFPKAVPLTHR---NILARSAGKIQHNGLT--------PQDVF---LNWVPldHVGGLVELhlra 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1707 LPQGGE----KEPEVIAKA------IEEQKIT---AMHFVPSMLHAFLEHIKYRSVPIktNRLKRVFSGGEQLGTHLVSR 1773
Cdd:cd05906    231 VYLGCQqvhvPTEEILADPlrwldlIDRYRVTitwAPNFAFALLNDLLEEIEDGTWDL--SSLRYLVNAGEAVVAKTIRR 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1774 FYELL------PNVsITNSYGPTEaTVEAAFFD----CPPH-EKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIA 1842
Cdd:cd05906    309 LLRLLepyglpPDA-IRPAFGMTE-TCSGVIYSrsfpTYDHsQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1843 GAGVARGYLNRPALTEERFLEDPFypgermYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE- 1921
Cdd:cd05906    387 GPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPs 459

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1922 --AAVTVRTDSGEPELCA--YVEGLQRNEVRAQLER-----------LLPGYMVPaymIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05906    460 ftAAFAVRDPGAETEELAifFVPEYDLQDALSETLRairsvvsrevgVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 2558-3019 1.03e-35

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: 142.87  E-value: 1.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2558 TLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDpeypkerkryilsdsgTKLlmTI 2637
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN----------------TRL--TP 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2638 NEadlgvLADfegEILTIESVEEDdksplpqmssahhLAYIIYTSGTTGRPKGVmvehkgiantLQWRRNAYA------- 2710
Cdd:cd05912     63 NE-----LAF---QLKDSDVKLDD-------------IATIMYTSGTTGKPKGV----------QQTFGNHWWsaigsal 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2711 ---FNETD---TILQLFSFSfdGfITSMFTPLLSGAKAVLLHEEEAKDILaikHQLSRQRITHMIIVPVLYRALLDVVQP 2784
Cdd:cd05912    112 nlgLTEDDnwlCALPLFHIS--G-LSILMRSVIYGMTVYLVDKFDAEQVL---HLINSGKVTIISVVPTMLQRLLEILGE 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2785 EDVKTLRVVTLAGEAADRELiarsLAICPHTELA--NEYGPTENS---VATTVMRHMEKQAyvSIGQPIDGTQVLIlnsN 2859
Cdd:cd05912    186 GYPNNLRCILLGGGPAPKPL----LEQCKEKGIPvyQSYGMTETCsqiVTLSPEDALNKIG--SAGKPLFPVELKI---E 256

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2860 HQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKpearmyrTGDAARWMADGTLEYLGRIDDQVKIRGYRVETK 2939
Cdd:cd05912    257 DDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2940 EIESVIRCIKGVKDAAVVAHVTAS-GQTELsAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGA 3018
Cdd:cd05912    330 EIEEVLLSHPAIKEAGVVGIPDDKwGQVPV-AFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408


                   .
gi 1678550997 3019 L 3019
Cdd:cd05912    409 L 409
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 2550-3014 1.34e-35

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: 146.18  E-value: 1.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2550 SALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDS 2629
Cdd:cd17634     76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2630 GTKLLMTINEA-------DLGVLADfEGEILTIESVEE-------------------------DDKSP--LPQMSSAHHL 2675
Cdd:cd17634    156 SSRLLITADGGvragrsvPLKKNVD-DALNPNVTSVEHvivlkrtgsdidwqegrdlwwrdliAKASPehQPEAMNAEDP 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 AYIIYTSGTTGRPKGVMVEHKGIANTLQWR-RNAYAFNETDTIlqlFSFSFDGFITS----MFTPLLSGAKAVLLH-EEE 2749
Cdd:cd17634    235 LFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIY---WCTADVGWVTGhsylLYGPLACGATTLLYEgVPN 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2750 AKDILAIKHQLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAADRELIARSLAI-----CPhteLANE 2820
Cdd:cd17634    312 WPTPARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKigkekCP---VVDT 388

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2821 YGPTENSVA-TTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGT--GLARGYVNLPElterAFTQNP 2897
Cdd:cd17634    389 WWQTETGGFmITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTY 464

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2898 FKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG 2977
Cdd:cd17634    465 FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHG 544

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 2978 LS-----TNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:cd17634    545 VEpspelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1521-1983 1.58e-35

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: 142.10  E-value: 1.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSgtnilllqsa 1600
Cdd:cd05912      3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS---------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeivylnqtnsglahrlsnpnvDVLPQSLAYVIYTSGSTGMPKGVEIEHR----SAVNFLNSLQsryqLKHS 1676
Cdd:cd05912     73 ------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGnhwwSAIGSALNLG----LTED 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1677 DM------IMHKTSYSFdasiweLFWWPYAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEhIKYRSVP 1750
Cdd:cd05912    119 DNwlcalpLFHISGLSI------LMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLE-ILGEGYP 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1751 iktNRLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTEATVEAAFFdcPPHEKLERI-PIGKPVHHVRLYLLNQNQr 1829
Cdd:cd05912    189 ---NNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETCSQIVTL--SPEDALNKIgSAGKPLFPVELKIEDDGQ- 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1830 mlPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEI 1909
Cdd:cd05912    261 --PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEI 331

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1910 EAALRSIEGVREAAVTVRTDS--GE-PelCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05912    332 EEVLLSHPAIKEAGVVGIPDDkwGQvP--VAFVvseRPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 2541-2958 1.73e-35

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: 145.07  E-value: 1.73e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2541 QQAARTPKASALV------SGDKTLTYQELDEWSNGIARALRSRGvKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI- 2613
Cdd:cd05931      1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 DPEYPKERKRY--ILSDSGTKLLMTINEADLGVLADFEG-------EILTIESVEEDDKSPLPQMSSAHH-LAYIIYTSG 2683
Cdd:cd05931     80 PPTPGRHAERLaaILADAGPRVVLTTAAALAAVRAFAASrpaagtpRLLVVDLLPDTSAADWPPPSPDPDdIAYLQYTSG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2684 TTGRPKGVMVEHKGI-ANTLQWRRnAYAFNETDTI---LQLFSfsfD-GFITSMFTPLLSGAKAVLLHEEE--AKDILAI 2756
Cdd:cd05931    160 STGTPKGVVVTHRNLlANVRQIRR-AYGLDPGDVVvswLPLYH---DmGLIGGLLTPLYSGGPSVLMSPAAflRRPLRWL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2757 KHqLSRQRITHMIIVPVLYRALLDVVQPE-----DVKTLRVVTLAGEAADRELIARSL-----------AICPHtelane 2820
Cdd:cd05931    236 RL-ISRYRATISAAPNFAYDLCVRRVRDEdleglDLSSWRVALNGAEPVRPATLRRFAeafapfgfrpeAFRPS------ 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2821 YGPTENSVATT--------VMRHMEKQAY-----------------VSIGQPIDGTQVLILNSN-HQLQPIGVAGELCIA 2874
Cdd:cd05931    309 YGLAEATLFVSggppgtgpVVLRVDRDALagravavaaddpaarelVSCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVR 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2875 GTGLARGYVNLPELTERAFTQNPFKPEARMYRTGDAARwMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDA 2954
Cdd:cd05931    389 GPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRP 467


                   ....
gi 1678550997 2955 AVVA 2958
Cdd:cd05931    468 GCVA 471
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1519-1978 3.24e-35

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: 142.13  E-value: 3.24e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1519 VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLlq 1598
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1599 saglhVPEFTGEIVYLNQtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDM 1678
Cdd:cd05903     79 -----VPERFRQFDPAAM-----------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDV 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1679 IM------HKTSYSFDASIWELfwwpyAGASVYLLPQGgekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIK 1752
Cdd:cd05903    137 FLvaspmaHQTGFVYGFTLPLL-----LGAPVVLQDIW---DPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLS 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1753 tnRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPTEatVEAAFFDCPPHEKLERIPI-GKPVHHVRLYLLNQNQRML 1831
Cdd:cd05903    209 --RLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTE--CPGAVTSITPAPEDRRLYTdGRPLPGVEIKVVDDTGATL 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1832 PVGCIGELYIAGAGVARGYLNRPALTEErfledpFYPgERMYKTGDVARWLPDGNVEFLGRTDDqVKIR-GYRIEPGEIE 1910
Cdd:cd05903    284 APGVEGELLSRGPSVFLGYLDRPDLTAD------AAP-EGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVE 355

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1911 AALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRAQLERL-LPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:cd05903    356 DLLLGHPGVIEAAVVALPDErlGE-RACAVVvtkSGalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 2557-2958 4.40e-35

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


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 141.96  E-value: 4.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:cd05907      4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 INEADLgvladfegeiltiesveeddksplpqmssahhlAYIIYTSGTTGRPKGVMVEHKGIAntlqwrRNAYAFNETDT 2716
Cdd:cd05907     84 EDPDDL---------------------------------ATIIYTSGTTGRPKGVMLSHRNIL------SNALALAERLP 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2717 ILQ---LFSF-----SFdGFITSMFTPLLSGakAVLLHEEEAKDILAikhQLSRQRITHMIIVPVLYRALLDVVQPEDVK 2788
Cdd:cd05907    125 ATEgdrHLSFlplahVF-ERRAGLYVPLLAG--ARIYFASSAETLLD---DLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2789 T-------------LRVVTLAGEAADRELIARSLAI-CPHTELaneYGPTENSVATTVMrHMEKQAYVSIGQPIDGTQVl 2854
Cdd:cd05907    199 GlkrklfdlavggrLRFAASGGAPLPAELLHFFRALgIPVYEG---YGLTETSAVVTLN-PPGDNRIGTVGKPLPGVEV- 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2855 ilnsnhqlqPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDD-QVKIRG 2933
Cdd:cd05907    274 ---------RIADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDlIITSGG 338

                          410       420
                   ....*....|....*....|....*
gi 1678550997 2934 YRVETKEIESVIRCIKGVKDAAVVA 2958
Cdd:cd05907    339 KNISPEPIENALKASPLISQAVVIG 363
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 488-952 5.66e-35

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


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 141.58  E-value: 5.66e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVsq 567
Cdd:cd05907      5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF-- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 ahlpsslednyiithpedieskvdgsniksVNNADDLLYMIYTSGTTGKPKGVQFEHRNMA----NLLKFeythsgIDFE 643
Cdd:cd05907     83 ------------------------------VEDPDDLATIIYTSGTTGRPKGVMLSHRNILsnalALAER------LPAT 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  644 AD-----VLQFATpsfdvCYQEI---FSALLKGGTLHIVP------EAIKRDVPQLFA----FINKHQTNIVF-LPTAFI 704
Cdd:cd05907    127 EGdrhlsFLPLAH-----VFERRaglYVPLLAGARIYFASsaetllDDLSEVRPTVFLavprVWEKVYAAIKVkAVPGLK 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  705 KMIFSERELANsfpdgVKHLIAAGeqlmiSDLFQDVL---RKRGIHLHNHYGPSETHVVSTYTiHPGDPIPELppIGKPI 781
Cdd:cd05907    202 RKLFDLAVGGR-----LRFAASGG-----APLPAELLhffRALGIPVYEGYGLTETSAVVTLN-PPGDNRIGT--VGKPL 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  782 GCTDLYIlnhqkqlqpcGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADN- 860
Cdd:cd05907    269 PGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDl 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  861 QVKIRGYRIEPQEIEVTLMNHPDISEAAI----------LI---------WQDQNGEH-----ELCAYYCSVQklntiDL 916
Cdd:cd05907    333 IITSGGKNISPEPIENALKASPLISQAVVigdgrpflvaLIvpdpealeaWAEEHGIAytdvaELAANPAVRA-----EI 407

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1678550997  917 RSYMAS---ELPEYMIPAKWI-----W-VDSIPLTPNGKVDRAAL 952
Cdd:cd05907    408 EAAVEAanaRLSRYEQIKKFLllpepFtIENGELTPTLKLKRPVI 452
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1485-1983 6.34e-35

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: 142.08  E-value: 6.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1485 FEETGYSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGI 1564
Cdd:cd05920      6 YRAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFAL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1565 LKAGGAYLPIDPDYPEERISFLLEDSgtnilllQSAGLHVPEFTGEIVYLNqtnsgLAHRLSNPNVDVlpqslAYVIYTS 1644
Cdd:cd05920     86 LRLGAVPVLALPSHRRSELSAFCAHA-------EAVAYIVPDRHAGFDHRA-----LARELAESIPEV-----ALFLLSG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1645 GSTGMPKGVEIEHRSAVnflnslqsrYQLKHSDMIMHktsysFDASIWELFWWP----------------YAGASVYLLP 1708
Cdd:cd05920    149 GTTGTPKLIPRTHNDYA---------YNVRASAEVCG-----LDQDTVYLAVLPaahnfplacpgvlgtlLAGGRVVLAP 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1709 QGgekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVfsGGEQLGTHLVSRFYELLpNVSITNSYG 1788
Cdd:cd05920    215 DP---SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV--GGARLSPALARRVPPVL-GCTLQQVFG 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1789 PTEATVEAAFFDcPPHEKLERIPiGKPVH-HVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFY 1867
Cdd:cd05920    289 MAEGLLNYTRLD-DPDEVIIHTQ-GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFY 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 pgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV----EG 1941
Cdd:cd05920    367 ------RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEllGE-RSCAFVvlrdPP 439

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 1942 LQRNEVRAQL-ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05920    440 PSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
2541-3016 6.41e-35

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 142.02  E-value: 6.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2541 QQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKE 2620
Cdd:PRK03640    10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2621 RKRYILSDSGTKLLMTineADLGVLADFEGEILTIESVEEDDKSPlPQMSSAHHL---AYIIYTSGTTGRPKGVMVEHKg 2697
Cdd:PRK03640    90 ELLWQLDDAEVKCLIT---DDDFEAKLIPGISVKFAELMNGPKEE-AEIQEEFDLdevATIMYTSGTTGKPKGVIQTYG- 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2698 iaNTLqWRRNAYAFN----ETDTIL---QLFSFSfdGFiTSMFTPLLSGAKAVLLHEEEAKDILAIkhqLSRQRITHMII 2770
Cdd:PRK03640   165 --NHW-WSAVGSALNlgltEDDCWLaavPIFHIS--GL-SILMRSVIYGMRVVLVEKFDAEKINKL---LQTGGVTIISV 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2771 VPVLYRALLDVVQPEDV-KTLRVVTLAGEAADRELiarsLAICPHTELA--NEYGPTENS---VATTVMRHMEKQAyvSI 2844
Cdd:PRK03640   236 VSTMLQRLLERLGEGTYpSSFRCMLLGGGPAPKPL----LEQCKEKGIPvyQSYGMTETAsqiVTLSPEDALTKLG--SA 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2845 GQPIDGTQVLILNSNHQLQPiGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKpearmyrTGDAARWMADGTLEYLGR 2924
Cdd:PRK03640   310 GKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDR 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2925 IDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVahvtasGQTELS------AYVVTKPGLSTNAVRSELQNKLPVFMHPA 2998
Cdd:PRK03640   382 RSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV------GVPDDKwgqvpvAFVVKSGEVTEEELRHFCEEKLAKYKVPK 455

                          490
                   ....*....|....*...
gi 1678550997 2999 FIEKLDSLPLSPNGKLDR 3016
Cdd:PRK03640   456 RFYFVEELPRNASGKLLR 473
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 463-952 7.12e-35

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: 142.26  E-value: 7.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVIDQACS--LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI 540
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  541 VPVDPHYPADRIRY-ILHDCGCSHVVSQAHLP------SSLEDNYIITHPEDIESKVDGSNIKS-VNNADDLLYMIYTSG 612
Cdd:cd05923     81 ALINPRLKAAELAElIERGEMTAAVIAVDAQVmdaifqSGVRVLALSDLVGLGEPESAGPLIEDpPREPEQPAFVFYTSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  613 TTGKPKGVQFEHRNMANLLKFEYTHSGIDFEA-DVLQFATPSFDVC-YQEIFSALLKGGTLHIVPEAIKRdvPQLFAFIN 690
Cdd:cd05923    161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhNVVLGLMPLYHVIgFFAVLVAALALDGTYVVVEEFDP--ADALKLIE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  691 KHQ-TNIVFLPTAFIKMIFSErELANSFPDGVKHLIAAGeqlmiSDLFQDVLRKRGIHLH----NHYGPSEThVVSTYti 765
Cdd:cd05923    239 QERvTSLFATPTHLDALAAAA-EFAGLKLSSLRHVTFAG-----ATMPDAVLERVNQHLPgekvNIYGTTEA-MNSLY-- 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  766 hpgDPIPELPPIGKPigctDLY-------ILNHQKQLQPCGVPGELYISGASVA--RGYVNHDKLTSDKFSSDpfkpdvi 836
Cdd:cd05923    310 ---MRDARTGTEMRP----GFFsevrivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQDG------- 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  837 MYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAyyCSVQKLNTI-- 914
Cdd:cd05923    376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA--CVVPREGTLsa 453

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997  915 -DLRSY-MASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05923    454 dELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 1520-1983 7.84e-35

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


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 141.19  E-value: 7.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILllqs 1599
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 aglhvpeFTGEivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRsavNFLNSLQSRYQLKHSDMI 1679
Cdd:cd05907     82 -------FVED-----------------------PDDLATIIYTSGTTGRPKGVMLSHR---NILSNALALAERLPATEG 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1680 MHKTSY-----SFDASIWELFWWpYAGASVYLLPqggekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVP---- 1750
Cdd:cd05907    129 DRHLSFlplahVFERRAGLYVPL-LAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPglkr 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1751 -----IKTNRLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTE--ATVEAAFFDCPPHEKleripIGKPVH--HVRl 1821
Cdd:cd05907    203 klfdlAVGGRLRFAASGGAPLPAELLHFFRAL--GIPVYEGYGLTEtsAVVTLNPPGDNRIGT-----VGKPLPgvEVR- 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1822 yllnqnqrmlpVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDD-QVKIR 1900
Cdd:cd05907    275 -----------IADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDlIITSG 337

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1901 GYRIEPGEIEAALRSIEGVREAAV------------TVRTDSGE-------PELCAYVEGLQRNEVRAQLER-------L 1954
Cdd:cd05907    338 GKNISPEPIENALKASPLISQAVVigdgrpflvaliVPDPEALEawaeehgIAYTDVAELAANPAVRAEIEAaveaanaR 417

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997 1955 LPGY-MVPAYMIEMEQWPV-----TPSGKLDRNAL 1983
Cdd:cd05907    418 LSRYeQIKKFLLLPEPFTIengelTPTLKLKRPVI 452
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1504-1983 7.99e-35

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 141.84  E-value: 7.99e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETtVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:PRK07638    11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLQSAGLH-VPEFTGEIVYLNQTNSGLAHRLSNP-NVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAV 1661
Cdd:PRK07638    90 KERLAISNADMIVTERYKLNdLPDEEGRVIEIDEWKRMIEKYLPTYaPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1662 NFLNSLQSRYQLKHSDMI------MHktSYSFDASIWELfwwpYAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPS 1735
Cdd:PRK07638   170 HSFDCNVHDFHMKREDSVliagtlVH--SLFLYGAISTL----YVGQTVHLMRK---FIPNQVLDKLETENISVMYTVPT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1736 MLHAFLEHIKYRSVPIKtnrlkrVFSGGEQLGTHLVSRFYELLPNVSITNSYGpteaTVEAAFFDCPPHEKLERIP--IG 1813
Cdd:PRK07638   241 MLESLYKENRVIENKMK------IISSGAKWEAEAKEKIKNIFPYAKLYEFYG----ASELSFVTALVDEESERRPnsVG 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1814 KPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEErfledpfyPGERMYKT-GDVARWLPDGNVEFLGR 1892
Cdd:PRK07638   311 RPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTvRDVGYEDEEGFIYIVGR 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE-PElcAYVEGLQ-RNEVRAQLERLLPGYMVPAYMIEME 1968
Cdd:PRK07638   383 EKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSywGEkPV--AIIKGSAtKQQLKSFCLQRLSSFKIPKEWHFVD 460

                          490
                   ....*....|....*
gi 1678550997 1969 QWPVTPSGKLDRNAL 1983
Cdd:PRK07638   461 EIPYTNSGKIARMEA 475
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
470-954 8.55e-35

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 141.92  E-value: 8.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMK-GVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:PRK06839     9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRIRYILHDCGCSHVVSQ---AHLPSSLEDNYIITHPEDIESKVDGSNIKSVN----NADDLLYMIYTSGTTGKPKGVQ 621
Cdd:PRK06839    89 ENELIFQLKDSGTTVLFVEktfQNMALSMQKVSYVQRVISITSLKEIEDRKIDNfvekNESASFIICYTSGTTGKPKGAV 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  622 FEHRNM-----ANLLKFEYTHSgidfeaDVLQFATPSFDVCYQEIFS--ALLKGGTLhIVPEaiKRDVPQLFAFINKHQT 694
Cdd:PRK06839   169 LTQENMfwnalNNTFAIDLTMH------DRSIVLLPLFHIGGIGLFAfpTLFAGGVI-IVPR--KFEPTKALSMIEKHKV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  695 NIVF-LPTAFIKMIFSERELANSFpDGVKHLIAAG----EQLMISdlFQDvlrkRGIHLHNHYGPSEThVVSTYTIHPGD 769
Cdd:PRK06839   240 TVVMgVPTIHQALINCSKFETTNL-QSVRWFYNGGapcpEELMRE--FID----RGFLFGQGFGMTET-SPTVFMLSEED 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  770 PIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimyRTGDLARRLED 849
Cdd:PRK06839   312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  850 GNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEHELCAYYC-SVQKLNTIDLRSYMASELPEY 927
Cdd:PRK06839   385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKkSSSVLIEKDVIEHCRLFLAKY 464

                          490       500
                   ....*....|....*....|....*..
gi 1678550997  928 MIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK06839   465 KIPKEIVFLKELPKNATGKIQKAQLVN 491
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
440-952 9.80e-35

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 142.96  E-value: 9.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  440 IDITTDTEKRQL---IGEITDqtpvyETIHAMFEKQAEKTPDAHAVID-QACSLTYRELNKAANRLARHLRMKGVVRQEP 515
Cdd:PRK06087     2 VTLTFNEQRRAAyrqQGYWGD-----ASLADYWQQTARAMPDKIAVVDnHGASYTYSALDHAASRLANWLLAKGIEPGDR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  516 VAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCG-----CSHVVSQ-----------AHLPS----SLE 575
Cdd:PRK06087    77 VAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQakmffAPTLFKQtrpvdlilplqNQLPQlqqiVGV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  576 DNYIITHPEDIESKV--DGSNIK-SVN-NADDLLYMIYTSGTTGKPKGVQFEHRNM-----ANLLKFEYTHSGIDFEADV 646
Cdd:PRK06087   157 DKLAPATSSLSLSQIiaDYEPLTtAITtHGDELAAVLFTSGTEGLPKGVMLTHNNIlaserAYCARLNLTWQDVFMMPAP 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  647 LQFATPSFdvcyQEIFSALLKGGTlhIVPEAIKRDVpQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDGVKHLIA 726
Cdd:PRK06087   237 LGHATGFL----HGVTAPFLIGAR--SVLLDIFTPD-ACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLC 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  727 AGEQLMiSDLFQDVLRkRGIHLHNHYGPSET--HVVstytIHPGDPIPELPPI-GKPIGCTDLYILNHQKQLQPCGVPGE 803
Cdd:PRK06087   310 GGTTIP-KKVARECQQ-RGIKLLSVYGSTESspHAV----VNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGE 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  804 LYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRaDNQVKIRG-YRIEPQEIEVTLMNHP 882
Cdd:PRK06087   384 EASRGPNVFMGYLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGR-KKDIIVRGgENISSREVEDILLQHP 456

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997  883 DISEAAILIWQDQNGEHELCAYYC---SVQKLNTIDLRSYMASE-LPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK06087   457 KIHDACVVAMPDERLGERSCAYVVlkaPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 2543-3019 1.74e-34

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 142.49  E-value: 1.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERK 2622
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 RYILSDSGTKLLMTINE---------ADLGV-------LADFEGEILTIE-------------------SVEEDDKSPLP 2667
Cdd:PRK06178   123 SYELNDAGAEVLLALDQlapvveqvrAETSLrhvivtsLADVLPAEPTLPlpdslraprlaaagaidllPALRACTAPVP 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2668 QMSSA-HHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLF--SFSFDGFITSMFTPLLSGAKAVL 2744
Cdd:PRK06178   203 LPPPAlDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFlpEFWIAGENFGLLFPLFSGATLVL 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2745 LHEEEAKDILAIKHqlsRQRITHMIIVPVLYRALLDvvQPE----DVKTLRVVTLAG--EAADRELIARSLAICPHTELA 2818
Cdd:PRK06178   283 LARWDAVAFMAAVE---RYRVTRTVMLVDNAVELMD--HPRfaeyDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAE 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 NEYGPTENSVATTVMRHMEKQAY------VSIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARGYVNLPELTER 2891
Cdd:PRK06178   358 AAWGMTETHTCDTFTAGFQDDDFdllsqpVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAE 437

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2892 AFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTA-SGQTELsA 2970
Cdd:PRK06178   438 ALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPdKGQVPV-A 509

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2971 YVVTKPG--LSTNAVRSELQNKLPVFMHPAfIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06178   510 FVQLKPGadLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 1504-1983 3.66e-34

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 140.02  E-value: 3.66e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSGLAHRLSNPNVDVLPQS------LAYVIYTSGSTGMPKGVeieH 1657
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAavaptdLVRLMYTSGTTDRPKGV---M 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1658 RSAVNFlnslqsryqlkHSDMIMHKTSYSFDASIWELFWWP--YAGA----SVYLLPQGG------EKEPEVIAKAIEEQ 1725
Cdd:PRK06145   169 HSYGNL-----------HWKSIDHVIALGLTASERLLVVGPlyHVGAfdlpGIAVLWVGGtlrihrEFDPEAVLAAIERH 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1726 KITAMHFVPSMLHAFLehikyrSVPIK----TNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDc 1801
Cdd:PRK06145   238 RLTCAWMAPVMLSRVL------TVPDRdrfdLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLME- 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1802 pPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVAR 1880
Cdd:PRK06145   311 -AGREIEKIgSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGY 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1881 WLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---EG--LQRNEVRAQLERL 1954
Cdd:PRK06145   383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVvlnPGatLTLEALDRHCRQR 462

                          490       500
                   ....*....|....*....|....*....
gi 1678550997 1955 LPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK06145   463 LASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 464-948 5.68e-34

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 140.02  E-value: 5.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPV 543
Cdd:PRK07798     4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 DPHYPADRIRYILHDCGCSHVVSQAH--------LPS--------SLEDNYIITHP------EDIESKVDGSNIKSVNNA 601
Cdd:PRK07798    84 NYRYVEDELRYLLDDSDAVALVYEREfaprvaevLPRlpklrtlvVVEDGSGNDLLpgavdyEDALAAGSPERDFGERSP 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDlLYMIYTSGTTGKPKGVQFEHRNM-------ANLLKFEYTHSGIDFEADVLQ-FATPSFDVC-------YQEIFSALL 666
Cdd:PRK07798   164 DD-LYLLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGEPIEDEEELAKRAAAgPGMRRFPAPplmhgagQWAAFAALF 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  667 KGGTLhIVPEAIKRDVPQLFAFINKHQTNIVFLP-TAFIK-MIfseRELANSFPDGVKHL--IAAGEQLM---ISDLFQD 739
Cdd:PRK07798   243 SGQTV-VLLPDVRFDADEVWRTIEREKVNVITIVgDAMARpLL---DALEARGPYDLSSLfaIASGGALFspsVKEALLE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  740 VLrkRGIHLHNHYGPSET-----HVVSTYTIHPGDPIPELPPIGKPIGcTDLYIlnhqkqLQP-CGVPGELYISGAsVAR 813
Cdd:PRK07798   319 LL--PNVVLTDSIGSSETgfggsGTVAKGAVHTGGPRFTIGPRTVVLD-EDGNP------VEPgSGEIGWIARRGH-IPL 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GYVNHDKLTSDKFssdpfkPDVIMYR---TGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL 890
Cdd:PRK07798   389 GYYKDPEKTAETF------PTIDGVRyaiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV 462

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997  891 IWQDQNGEHELCAyycsVQKLNT------IDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:PRK07798   463 GVPDERWGQEVVA----VVQLREgarpdlAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 1495-1924 6.01e-34

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 140.48  E-value: 6.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLP 1573
Cdd:PRK08314    11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1574 IDPDYPEERISFLLEDSGTNIL------------LLQSAGLH------------------VPEF-----------TGEIV 1612
Cdd:PRK08314    91 VNPMNREEELAHYVTDSGARVAivgselapkvapAVGNLRLRhvivaqysdylpaepeiaVPAWlraepplqalaPGGVV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1613 YLNQTnsgLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSaVNFLNSLQSRYQLKHSDMIM-------HKTS- 1684
Cdd:PRK08314   171 AWKEA---LAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRT-VMANAVGSVLWSNSTPESVVlavlplfHVTGm 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1685 -YSFDASIwelfwwpYAGASVYLLPQGgekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGG 1763
Cdd:PRK08314   247 vHSMNAPI-------YAGATVVLMPRW---DREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSS--LRYIGGGG 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1764 EQLGTHLVSRFYELLpNVSITNSYGPTEaTVEAAFFDCPPHEKLEriPIGKPVHHVRLYLLN-QNQRMLPVGCIGELYIA 1842
Cdd:PRK08314   315 AAMPEAVAERLKELT-GLDYVEGYGLTE-TMAQTHSNPPDRPKLQ--CLGIPTFGVDARVIDpETLEELPPGEVGEIVVH 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1843 GAGVARGYLNRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA 1922
Cdd:PRK08314   391 GPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467


                   ..
gi 1678550997 1923 AV 1924
Cdd:PRK08314   468 CV 469
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 473-952 7.36e-34

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: 140.11  E-value: 7.36e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAV-IDQACS---LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGG--AIVPVDPH 546
Cdd:cd05906     20 AERGPTKGITyIDADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFvpAPLTVPPT 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  547 YPADR--------IRYILHDCGCshVVSQAHLPSSLEDNYIITHPED----IESKVDGSNIKSVNNA--DDLLYMIYTSG 612
Cdd:cd05906    100 YDEPNarlrklrhIWQLLGSPVV--LTDAELVAEFAGLETLSGLPGIrvlsIEELLDTAADHDLPQSrpDDLALLMLTSG 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  613 TTGKPKGVQFEHRNMANLLKFEYTHSGIdFEADVlQFATPSFD----VCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAF 688
Cdd:cd05906    178 STGFPKAVPLTHRNILARSAGKIQHNGL-TPQDV-FLNWVPLDhvggLVELHLRAVYLGCQQVHVPTEEILADPLRWLDL 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  689 INKHQTNIVFLPTAFIKMIfseRELANSFPDG------VKHLIAAGEQLMIS--DLFQDVLRKRGIH---LHNHYGPSET 757
Cdd:cd05906    256 IDRYRVTITWAPNFAFALL---NDLLEEIEDGtwdlssLRYLVNAGEAVVAKtiRRLLRLLEPYGLPpdaIRPAFGMTET 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  758 HVVSTYTIHPG-DPIPELPP---IGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkp 833
Cdd:cd05906    333 CSGVIYSRSFPtYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-- 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  834 dvimYRTGDLArRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDI---SEAAILIWQDQNGEHELCAYYCSVQK 910
Cdd:cd05906    411 ----FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEELAIFFVPEYD 485

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  911 LNtiDLRSYMASEL-----------PEYMIPakwIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05906    486 LQ--DALSETLRAIrsvvsrevgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 2524-3019 1.05e-33

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 139.53  E-value: 1.05e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2524 TGQANQYGVQTISQLFEQQAAR----TPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIAS 2599
Cdd:PRK07786     4 LTLAQEQPYLARRQNWVNQLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVES 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2600 ILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTinEADLGVLA------------------DFEGEILTIES-VEE 2660
Cdd:PRK07786    84 VLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALAPVAtavrdivpllstvvvaggSSDDSVLGYEDlLAE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2661 DDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGI-ANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSG 2739
Cdd:PRK07786   162 AGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLtGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLG 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2740 AKAVlLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDV--VQPEDVKtLRVVTLAGEAADRELIARSLAICPHTEL 2817
Cdd:PRK07786   242 APTV-IYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEqqARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQI 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2818 ANEYGPTENSVATTVMRHMEKQAYV-SIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFtqn 2896
Cdd:PRK07786   320 LAAFGQTEMSPVTCMLLGEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF--- 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2897 pfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS-GQTELSAYVVTK 2975
Cdd:PRK07786   397 ----AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRN 472

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1678550997 2976 PG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK07786   473 DDaaLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 1502-1982 1.77e-33

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: 138.91  E-value: 1.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1502 QQAEKTPDQAAVIF------EDGVMTYKELNEQANRIAWELIGRGvKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPID 1575
Cdd:cd05931      1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPE---ERISFLLEDSGTNILLLQSAGL-HVPEF--------TGEIVYLNQTNSGLAHRLSNPNVDvlPQSLAYVIYT 1643
Cdd:cd05931     80 PPTPGrhaERLAAILADAGPRVVLTTAAALaAVRAFaasrpaagTPRLLVVDLLPDTSAADWPPPSPD--PDDIAYLQYT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1644 SGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMImhktsysfdasiweLFWWP---------------YAGASVYLL- 1707
Cdd:cd05931    158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV--------------VSWLPlyhdmgligglltplYSGGPSVLMs 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1708 PQGGEKEPEVIAKAIEEQKITAMhFVPSMlhAFlEHIKYRSVPIKT-----NRLKRVFSGGEQLGTHLVSRFYEL----- 1777
Cdd:cd05931    224 PAAFLRRPLRWLRLISRYRATIS-AAPNF--AY-DLCVRRVRDEDLegldlSSWRVALNGAEPVRPATLRRFAEAfapfg 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1778 LPNVSITNSYGPTEATV-----------------------EAAFFDCPPHEKLERIPIGKPVHHVRLYLLN-QNQRMLPV 1833
Cdd:cd05931    300 FRPEAFRPSYGLAEATLfvsggppgtgpvvlrvdrdalagRAVAVAADDPAARELVSCGRPLPDQEVRIVDpETGRELPD 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1834 GCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAAL 1913
Cdd:cd05931    380 GEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1914 RSIEGV----REAAVTVRTDSGEP-----ELCAYVEGLQ----RNEVRAQLER---------LLpgymVPAYMIemeqwP 1971
Cdd:cd05931    459 EEAHPAlrpgCVAAFSVPDDGEERlvvvaEVERGADPADlaaiAAAIRAAVARehgvapadvVL----VRPGSI-----P 529

                          570
                   ....*....|.
gi 1678550997 1972 VTPSGKLDRNA 1982
Cdd:cd05931    530 RTSSGKIQRRA 540
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1485-1983 1.99e-33

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: 138.35  E-value: 1.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1485 FEETGYSMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGI 1564
Cdd:COG1021     16 YREAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFAL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1565 LKAGGayLPIDPdYPEER---ISFLLEdsgtnilLLQSAGLHVPEFTGEIVY------LNQTNSGLAHRL---------- 1625
Cdd:COG1021     96 FRAGA--IPVFA-LPAHRraeISHFAE-------QSEAVAYIIPDRHRGFDYralareLQAEVPSLRHVLvvgdagefts 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1626 -----------SNPNVDvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVnflnslqsrYQLKHSDMIMHKTSYS-------- 1686
Cdd:COG1021    166 ldallaapadlSEPRPD--PDDVAFFQLSGGTTGLPKLIPRTHDDYL---------YSVRASAEICGLDADTvylaalpa 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1687 ---FDASIWELFWWPYAGASVYLLPQGgekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGG 1763
Cdd:COG1021    235 ahnFPLSSPGVLGVLYAGGTVVLAPDP---SPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSS--LRVLQVGG 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1764 EQLGTHLVSRFYELLPnVSITNSYGPTEATVEAAFFDCPPheklERI--PIGKPVHH---VRLylLNQNQRMLPVGCIGE 1838
Cdd:COG1021    310 AKLSPELARRVRPALG-CTLQQVFGMAEGLVNYTRLDDPE----EVIltTQGRPISPddeVRI--VDEDGNPVPPGEVGE 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1839 LYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVkIR-GYRIEPGEIEAALRSIE 1917
Cdd:COG1021    383 LLTRGPYTIRGYYRAPEHNARAFTPDGFY------RTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHP 455

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1918 GVREAAVTVRTDS--GEpELCAYV----EGLQRNEVRAQL-ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:COG1021    456 AVHDAAVVAMPDEylGE-RSCAFVvprgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 2538-3013 4.82e-33

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 136.93  E-value: 4.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2538 LFEQQAARTPKASAL---VSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:PRK07514     5 LFDALRAAFADRDAPfieTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYPKERKRYILSDSGTKLLMT--INEADLGVLADFEGEIlTIESVEEDDKSPLPQ----MSSAHH--------LAYIIY 2680
Cdd:PRK07514    85 TAYTLAELDYFIGDAEPALVVCdpANFAWLSKIAAAAGAP-HVETLDADGTGSLLEaaaaAPDDFEtvprgaddLAAILY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2681 TSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQ-LFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIkhq 2759
Cdd:PRK07514   164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHaLPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLAL--- 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2760 lsRQRITHMIIVPVLYRALLD--VVQPEDVKTLRVVTlAGEA---AD--RELIARSlaicPHTELaNEYGPTENSVATTV 2832
Cdd:PRK07514   241 --MPRATVMMGVPTFYTRLLQepRLTREAAAHMRLFI-SGSApllAEthREFQERT----GHAIL-ERYGMTETNMNTSN 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2833 MRHMEKQAyVSIGQPIDGTQVLILN--SNHQLqPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDA 2910
Cdd:PRK07514   313 PYDGERRA-GTVGFPLPGVSLRVTDpeTGAEL-PPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDL 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV--VAH------VTasgqtelsAYVVTKPG--LST 2980
Cdd:PRK07514   385 GKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVigVPHpdfgegVT--------AVVVPKPGaaLDE 456

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1678550997 2981 NAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGK 3013
Cdd:PRK07514   457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 2560-3019 4.86e-33

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: 136.99  E-value: 4.86e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2560 TYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMtINE 2639
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVF-VDR 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2640 ADLGVLADFEGEILTIESV---EEDDKSPLPQMSSAHHL---------------------AYIIYTSGTTGRPKGVMVEH 2695
Cdd:cd12119    106 DFLPLLEAIAPRLPTVEHVvvmTDDAAMPEPAGVGVLAYeellaaespeydwpdfdentaAAICYTSGTTGNPKGVVYSH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2696 K-------GIANTlqwrrNAYAFNETDTILQlfsfsfdgfITSMF------TP---LLSGAKAVL----LHeeeAKDILA 2755
Cdd:cd12119    186 RslvlhamAALLT-----DGLGLSESDVVLP---------VVPMFhvnawgLPyaaAMVGAKLVLpgpyLD---PASLAE 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2756 IkhqLSRQRITHMIIVPVLYRALLDVV--QPEDVKTLRVVTLAGEAADRELIARSLAIcpHTELANEYGPTENSVATTVM 2833
Cdd:cd12119    249 L---IEREGVTFAAGVPTVWQGLLDHLeaNGRDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWGMTETSPLGTVA 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 R---------HMEKQAY-VSIGQPIDGTQVLILNSNHQLQPI-GVA-GELCIAGTGLARGYVNLPELTErAFTQNPFkpe 2901
Cdd:cd12119    324 RppsehsnlsEDEQLALrAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESE-ALTEDGW--- 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2902 armYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTN 2981
Cdd:cd12119    400 ---LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVT 476

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997 2982 A--VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd12119    477 AeeLLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 489-895 5.20e-33

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: 135.95  E-value: 5.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQa 568
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslednyiithpedieskvdgsniksvNNADDLLYMIYTSGTTGKPKGVQFEHRN----MANLLKFEYTHSGidfea 644
Cdd:cd17640     85 ------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANllhqIRSLSDIVPPQPG----- 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  645 DVLQFATPSFDVcYQEIFS--ALLKGGTLHIV-PEAIKRD-----------VPQLF-AFINKHQTNIVflptafiKMIFS 709
Cdd:cd17640    130 DRFLSILPIWHS-YERSAEyfIFACGCSQAYTsIRTLKDDlkrvkphyivsVPRLWeSLYSGIQKQVS-------KSSPI 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  710 ERELANSFPDG--VKHLIAAGEQLMIS-DLFQDVLrkrGIHLHNHYGPSETHVVSTYTIHPGdpiPELPPIGKPIGCTDL 786
Cdd:cd17640    202 KQFLFLFFLSGgiFKFGISGGGALPPHvDTFFEAI---GIEVLNGYGLTETSPVVSARRLKC---NVRGSVGRPLPGTEI 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  787 YILNHQ-KQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRA-DNQVKI 864
Cdd:cd17640    276 KIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTIVLS 349

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1678550997  865 RGYRIEPQEIEVTLMNHPDIsEAAILIWQDQ 895
Cdd:cd17640    350 NGENVEPQPIEEALMRSPFI-EQIMVVGQDQ 379
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 2675-3019 5.99e-33

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: 132.45  E-value: 5.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 LAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDT-ILQLFSFSFDGFITsMFTPLLSGAKAVLLheeEAKDI 2753
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSwLLSLPLYHVGGLAI-LVRSLLAGAELVLL---ERNQA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2754 LAIKHQlsRQRITHMIIVPV-LYRALLDVVQPEDVKTLRVVTLAGEAADRELIARslAICPHTELANEYGPTENS--VAT 2830
Cdd:cd17630     78 LAEDLA--PPGVTHVSLVPTqLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETAsqVAT 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2831 TVMRHMEKQayvSIGQPIDGTQVLILNsnhqlqpigvAGELCIAGTGLARGYVNLPElteraftQNPFkPEARMYRTGDA 2910
Cdd:cd17630    154 KRPDGFGRG---GVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL-------VPEF-NEDGWFTTKDL 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS-GQTeLSAYVVTKPGLSTNAVRSELQN 2989
Cdd:cd17630    213 GELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQR-PVAVIVGRGPADPAELRAWLKD 291

                          330       340       350
                   ....*....|....*....|....*....|
gi 1678550997 2990 KLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd17630    292 KLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 1494-1978 9.46e-33

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 136.22  E-value: 9.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLP 1573
Cdd:PRK08316    11 QTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1574 IDPDYPEERISFLLEDSGTNILLLQSA---------GLHVPEFTGEIVYLNQTNSG--------LAHRLSNPNVDVLPQS 1636
Cdd:PRK08316    91 VNFMLTGEELAYILDHSGARAFLVDPAlaptaeaalALLPVDTLILSLVLGGREAPggwldfadWAEAGSVAEPDVELAD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1637 --LAYVIYTSGSTGMPKGVEIEHRSAV----------------NFLNSLqsryQLKHSDMiMHktsysfdasiweLFWWP 1698
Cdd:PRK08316   171 ddLAQILYTSGTESLPKGAMLTHRALIaeyvscivagdmsaddIPLHAL----PLYHCAQ-LD------------VFLGP 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 --YAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYE 1776
Cdd:PRK08316   234 ylYVGATNVILDA---PDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSS--LRKGYYGASIMPVEVLKELRE 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1777 LLPNVSITNSYGPTE----ATVeaaffdCPPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYL 1851
Cdd:PRK08316   309 RLPGLRFYNCYGQTEiaplATV------LGPEEHLRRPgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYW 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1852 NRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV------- 1924
Cdd:PRK08316   383 DDPEKTAEAFRGGWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAViglpdpk 455

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1925 -------TVRTDSG----EPELCAYveglqrneVRAQlerlLPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:PRK08316   456 wieavtaVVVPKAGatvtEDELIAH--------CRAR----LAGFKVPKRVIFVDELPRNPSGKI 508
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 2517-3020 1.13e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 135.89  E-value: 1.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2517 QLLNEFNTGQANQYGVQTISqlfeqqAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSM 2596
Cdd:PRK13383    25 RLLREASRGGTNPYTLLAVT------AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGF 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2597 IASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINE-ADLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHL 2675
Cdd:PRK13383    99 VTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEfAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 ayIIYTSGTTGRPKGVMVEHK-----GIANTLQWRRNAyafnETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEE-E 2749
Cdd:PRK13383   179 --VLLTSGTTGKPKGVPRAPQlrsavGVWVTILDRTRL----RTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHfD 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2750 AKDILAikhQLSRQRITHMIIVPVLYRALLDVvqPEDVKT------LRVVTLAGEAADRELIARSLAICPHTeLANEYGP 2823
Cdd:PRK13383   253 AEAALA---QASLHRADAFTAVPVVLARILEL--PPRVRArnplpqLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGS 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2824 TENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHqlQPIG--VAGELCIAGtglargyvnlpELTERAFTQNPFKPE 2901
Cdd:PRK13383   327 TEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNN--RPVGprVTGRIFVGG-----------ELAGTRYTDGGGKAV 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2902 AR-MYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--L 2978
Cdd:PRK13383   394 VDgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGsgV 473

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 2979 STNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALP 3020
Cdd:PRK13383   474 DAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1082-1376 1.15e-32

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: 134.15  E-value: 1.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1082 AVLELEGA-LDVAKLSAVCKELISRHEPLRTSFvsgaDDEPVQRIHTEVPF---------TLSKETTIEGFV-------- 1143
Cdd:cd19535     28 AYLEFDGEdLDPDRLERAWNKLIARHPMLRAVF----LDDGTQQILPEVPWygitvhdlrGLSEEEAEAALEelrerlsh 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1144 RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR--QLKPLRIQYKDYAVWQQKFKKgDSY 1221
Cdd:cd19535    104 RVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPgePLPPLELSFRDYLLAEQALRE-TAY 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1222 QKQETYWQQQFSgDLPI-LELPTdKRRPAERQfiggKVTF-----QLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSR 1295
Cdd:cd19535    183 ERARAYWQERLP-TLPPaPQLPL-AKDPEEIK----EPRFtrrehRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLAR 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1296 LSGQDDIVIGSPIAGRP--HADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPfeelvdklG--VQ 1371
Cdd:cd19535    257 WSGQPRFLLNLTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYS--------GvvVV 328


                   ....*
gi 1678550997 1372 REMSR 1376
Cdd:cd19535    329 RRLLR 333
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 2549-3028 1.59e-32

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 135.60  E-value: 1.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2549 ASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSD 2628
Cdd:PRK12406     2 YATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2629 SGTKLLmtINEADLgvLADFEG---------------EILTIESVEEDDKSP----------LPQMSSAHHL-----AYI 2678
Cdd:PRK12406    82 SGARVL--IAHADL--LHGLASalpagvtvlsvptppEIAAAYRISPALLTPpagaidwegwLAQQEPYDGPpvpqpQSM 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2679 IYTSGTTGRPKGV-----MVEHKgiANTLQWRRNAYAFNETDTIL---QLFSFSFDGFitSMFTPLLsGAKAVLLHEEEA 2750
Cdd:PRK12406   158 IYTSGTTGHPKGVrraapTPEQA--AAAEQMRALIYGLKPGIRALltgPLYHSAPNAY--GLRAGRL-GGVLVLQPRFDP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2751 KDILAIkhqLSRQRITHMIIVPVLYRALLDVvqPE------DVKTLRVVTLAGeaadreliarslAICP-HTELA----- 2818
Cdd:PRK12406   233 EELLQL---IERHRITHMHMVPTMFIRLLKL--PEevrakyDVSSLRHVIHAA------------APCPaDVKRAmieww 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 ----NE-YGPTENSVATTvmrHMEKQAYV---SIGQPIDGTQVLILNSNHQLQPIGVAGELciagtglargYVNLPELTE 2890
Cdd:PRK12406   296 gpviYEyYGSTESGAVTF---ATSEDALShpgTVGKAAPGAELRFVDEDGRPLPQGEIGEI----------YSRIAGNPD 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2891 raFTQNPfKPEAR-------MYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS 2963
Cdd:PRK12406   363 --FTYHN-KPEKRaeidrggFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAE 439

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2964 GQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNHEG 3028
Cdd:PRK12406   440 FGEALMAVVEPQPGatLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAG 506
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
2533-3019 1.80e-32

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 136.16  E-value: 1.80e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKAGGCYV 2611
Cdd:PRK08751    25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPEYPKERKRYILSDSGTKLLMTINE---------AD----------LGVLADF----------------------EG 2650
Cdd:PRK08751   105 NVNPLYTPRELKHQLIDSGASVLVVIDNfgttvqqviADtpvkqvittgLGDMLGFpkaalvnfvvkyvkklvpeyriNG 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2651 EILTIESVEEDDKSPLPQMSSAHH-LAYIIYTSGTTGRPKGVMVEHKG-IANTLQ---WRRNAYAFNETDTIL------- 2718
Cdd:PRK08751   185 AIRFREALALGRKHSMPTLQIEPDdIAFLQYTGGTTGVAKGAMLTHRNlVANMQQahqWLAGTGKLEEGCEVVitalply 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2719 QLFSFSFDGFITSMFtpllSGAKAVLlheEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDV--VQPEDVKTLRVvTLA 2796
Cdd:PRK08751   265 HIFALTANGLVFMKI----GGCNHLI---SNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTpgFDQIDFSSLKM-TLG 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2797 GEAADRELIARSLAICPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGT 2876
Cdd:PRK08751   337 GGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2877 GLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV 2956
Cdd:PRK08751   417 QVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAA 490

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2957 VAhVTASGQTELSAYVVTK--PGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK08751   491 VG-VPDEKSGEIVKVVIVKkdPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 464-952 1.92e-32

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 134.91  E-value: 1.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVvRQEPVAIMMERSAAFITGVLGILKAGGAIVPV 543
Cdd:PRK07638     2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKES-KNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 DPHYPADRIRYILHDCGCSHVVSQAHLPSSL--EDNYIITHPE---DIESKVD-GSNIKSVNNADdlLYMIYTSGTTGKP 617
Cdd:PRK07638    81 DIKWKQDELKERLAISNADMIVTERYKLNDLpdEEGRVIEIDEwkrMIEKYLPtYAPIENVQNAP--FYMGFTSGSTGKP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  618 KGVQFEHRNmanllkfeYTHSgidFEADVLQFATPSFD------------VCYQEIfSALLKGGTLHIVPEAIKRDVPQl 685
Cdd:PRK07638   159 KAFLRAQQS--------WLHS---FDCNVHDFHMKREDsvliagtlvhslFLYGAI-STLYVGQTVHLMRKFIPNQVLD- 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  686 faFINKHQTNIVF-LPT---AFIKmifserelANSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVS 761
Cdd:PRK07638   226 --KLETENISVMYtVPTmleSLYK--------ENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVT 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  762 TytIHPGDPipELPP--IGKPIGCTDLYILNH-QKQLQPcGVPGELYISGASVARGYVNHdkltsdkfSSDPFKPDVIMY 838
Cdd:PRK07638   296 A--LVDEES--ERRPnsVGRPFHNVQVRICNEaGEEVQK-GEIGTVYVKSPQFFMGYIIG--------GVLARELNADGW 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  839 RT-GDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQKLNTIDLR 917
Cdd:PRK07638   363 MTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLK 440

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997  918 SYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK07638   441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 1511-1986 1.98e-32

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 135.21  E-value: 1.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1511 AAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDS 1590
Cdd:PRK12406     3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1591 GTNIL-----LLQSAGLHVPEftGEIVYLNQT------NSGL--AHRLSNPN-VDV---LPQSLAY----------VIYT 1643
Cdd:PRK12406    83 GARVLiahadLLHGLASALPA--GVTVLSVPTppeiaaAYRIspALLTPPAGaIDWegwLAQQEPYdgppvpqpqsMIYT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1644 SGSTGMPKGVEIEHRSAVNFLNSLQSR---YQLKHSDMIM------HKTSYSFDASIWELfwwpyaGASVYLLPQggeKE 1714
Cdd:PRK12406   161 SGTTGHPKGVRRAAPTPEQAAAAEQMRaliYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQPR---FD 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1715 PEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPTEATV 1794
Cdd:PRK12406   232 PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1795 eAAFfdCPPHEKLERiP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVAR-GYLNRPaltEERFLEDPfypgER 1871
Cdd:PRK12406   311 -VTF--ATSEDALSH-PgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKP---EKRAEIDR----GG 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 MYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVE-----GLQR 1944
Cdd:PRK12406   380 FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAefGE-ALMAVVEpqpgaTLDE 458

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 1945 NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAP 1986
Cdd:PRK12406   459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 2531-3019 2.10e-32

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 135.20  E-value: 2.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2531 GVQTISQLFEQQAARTPKASALV----SGD-KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWK 2605
Cdd:PRK08008     5 GGQHLRQMWDDLADVYGHKTALIfessGGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2606 AGGCYVPIDPEYPKERKRYILSDSGTKLLMT---------------------------INEADLGVLaDFEgEILTIESV 2658
Cdd:PRK08008    85 IGAIMVPINARLLREESAWILQNSQASLLVTsaqfypmyrqiqqedatplrhicltrvALPADDGVS-SFT-QLKAQQPA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2659 EEDDKSPLpqmsSAHHLAYIIYTSGTTGRPKGVMVEHkgiANTL------QWRrnaYAFNETDTILQLF-SFSFDGFITS 2731
Cdd:PRK08008   163 TLCYAPPL----STDDTAEILFTSGTTSRPKGVVITH---YNLRfagyysAWQ---CALRDDDVYLTVMpAFHIDCQCTA 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2732 MFTPLLSGAKAVLLHEEEAKdilAIKHQLSRQR--ITHMIivPVLYRALLdvVQP----EDVKTLRVVTLAGEAADREli 2805
Cdd:PRK08008   233 AMAAFSAGATFVLLEKYSAR---AFWGQVCKYRatITECI--PMMIRTLM--VQPpsanDRQHCLREVMFYLNLSDQE-- 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2806 arSLAICPH--TELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCI---AGTGLAR 2880
Cdd:PRK08008   304 --KDAFEERfgVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFK 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2881 GYVNLPELTERAFTqnpfkPEARMYrTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhV 2960
Cdd:PRK08008   382 EYYLDPKATAKVLE-----ADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVG-I 454

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 2961 TASGQTE-LSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK08008   455 KDSIRDEaIKAFVVLNEGetLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2678-3016 2.12e-32

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: 131.25  E-value: 2.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHKGIANtlqwrrNAY------AFNETDTI-LQLFSFSFDGFITSMFTPLLSGAKAVLLheEEA 2750
Cdd:cd05917      7 IQFTSGTTGSPKGATLTHHNIVN------NGYfigerlGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFP--SPS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2751 KDILAIKHQLSRQRITHMIIVPVLYRALLDvvQPE----DVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTEN 2826
Cdd:cd05917     79 FDPLAVLEAIEKEKCTALHGVPTMFIAELE--HPDfdkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTET 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2827 SVATTVMR---HMEKQaYVSIGQPIDGTQVLILNS-NHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNpfkpea 2902
Cdd:cd05917    157 SPVSTQTRtddSIEKR-VNTVGRIMPHTEAKIVDPeGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD------ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2903 RMYRTGDAARWMADGTLEYLGRIDDQVkIRG-YRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTN 2981
Cdd:cd05917    230 GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELT 308

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1678550997 2982 A--VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd05917    309 EedIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 489-952 2.23e-32

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: 133.78  E-value: 2.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDcgcshvvSQA 568
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLEN-------SEA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLpsslednyIITHPEDIESKvdgsniksvnNADDLLYMIYTSGTTGKPKGVQFEHRNMAnllkFEY--THSGIDFEADV 646
Cdd:cd05969     74 KV--------LITTEELYERT----------DPEDPTLLHYTSGTTGTPKGVLHVHDAMI----FYYftGKYVLDLHPDD 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  647 LQFAT--PSF--DVCYQeIFSALLKGGTLHIVPEaiKRDVPQLFAFINKHQTNIVFL-PTAFIKMIFSERELANSFP-DG 720
Cdd:cd05969    132 IYWCTadPGWvtGTVYG-IWAPWLNGVTNVVYEG--RFDAESWYGIIERVKVTVWYTaPTAIRMLMKEGDELARKYDlSS 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  721 VKHLIAAGEQLMisdlfQDVLR----KRGIHLHNHYGPSEThvvSTYTI--HPGDPIpELPPIGKPIGCTDLYILNHQKQ 794
Cdd:cd05969    209 LRFIHSVGEPLN-----PEAIRwgmeVFGVPIHDTWWQTET---GSIMIanYPCMPI-KPGSMGKPLPGVKAAVVDENGN 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  795 LQPCGVPGELYISGA--SVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQ 872
Cdd:cd05969    280 ELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  873 EIEVTLMNHPDISEAAILIWQDQNGEHELCAY------YCSVQKLNTiDLRSYMASELPEYMIPAKWIWVDSIPLTPNGK 946
Cdd:cd05969    353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFislkegFEPSDELKE-EIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431


                   ....*.
gi 1678550997  947 VDRAAL 952
Cdd:cd05969    432 IMRRVL 437
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1504-1983 2.91e-32

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 135.55  E-value: 2.91e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLQSAGLHVPEFTgeivyLNQTnsGLAHRLSNPNVDVLP----------------------------- 1634
Cdd:PRK06178   123 SYELNDAGAEVLLALDQLAPVVEQV-----RAET--SLRHVIVTSLADVLPaeptlplpdslraprlaaagaidllpalr 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 -------------QSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMhktsysfdASIWELFW----- 1696
Cdd:PRK06178   196 actapvplpppalDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVF--------LSFLPEFWiagen 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1697 ----WP-YAGASVYLLPQGgekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLV 1771
Cdd:PRK06178   268 fgllFPlFSGATLVLLARW---DAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNPDYR 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1772 SRFYELLPNVSITNSYGPTEA----TVEAAF----FDcpphekLERIPI--GKPVHHVRLYLLN-QNQRMLPVGCIGELY 1840
Cdd:PRK06178   345 QRWRALTGSVLAEAAWGMTEThtcdTFTAGFqdddFD------LLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIV 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1841 IAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 1920
Cdd:PRK06178   419 VRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVL 491

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 1921 EAAVTVRTDSGEPEL-CAYVE-----GLQRNEVRAQLERLLPGYMVPAYMIeMEQWPVTPSGKLDRNAL 1983
Cdd:PRK06178   492 GSAVVGRPDPDKGQVpVAFVQlkpgaDLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
456-890 3.02e-32

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 136.00  E-value: 3.02e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  456 TDQTPVYETIHAMFEKQAEKTPDAHAVI----DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVL 531
Cdd:COG1022      4 FSDVPPADTLPDLLRRRAARFPDRVALRekedGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  532 GILKAGGAIVPVDPHYPADRIRYILHDCGCSHVV------------SQAHLPS-----------SLEDNYIIT------- 581
Cdd:COG1022     84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvedqeqldklleVRDELPSlrhivvldprgLRDDPRLLSldellal 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  582 -----HPEDIESKVDGSniksvnNADDLLYMIYTSGTTGKPKGVQFEHRNMA----NLLKFEythsGIDFEADVLQFATP 652
Cdd:COG1022    164 grevaDPAELEARRAAV------KPDDLATIIYTSGTTGRPKGVMLTHRNLLsnarALLERL----PLGPGDRTLSFLPL 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  653 S--FDVCYQeiFSALLKGGTLHIV--PEAIKRD-----------VPQLF-AFINKHQTNIVFLPtAFIKMIF-------- 708
Cdd:COG1022    234 AhvFERTVS--YYALAAGATVAFAesPDTLAEDlrevkptfmlaVPRVWeKVYAGIQAKAEEAG-GLKRKLFrwalavgr 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  709 --SERELAN---SFPDGVKHLIAagEQLMISDLfQDVL--RKR--------------------GIHLHNHYGPSETHVVS 761
Cdd:COG1022    311 ryARARLAGkspSLLLRLKHALA--DKLVFSKL-REALggRLRfavsggaalgpelarffralGIPVLEGYGLTETSPVI 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  762 TYTiHPGDPIPElpPIGKPIGCTDLYIlnhqkqlqpcGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTG 841
Cdd:COG1022    388 TVN-RPGDNRIG--TVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTG 448

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997  842 DLARRLEDGNIEYIGRADNQVKIR-GYRIEPQEIEVTLMNHPDISEAAIL 890
Cdd:COG1022    449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 2533-3016 3.17e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 135.29  E-value: 3.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSG--DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCY 2610
Cdd:PRK12583    18 QTIGDAFDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2611 VPIDPEYPKERKRYILSDSGTKLLMTIN-----------EADLGVLADFEGEILTIESVEE------DDKSPLPQMSSAH 2673
Cdd:PRK12583    98 VNINPAYRASELEYALGQSGVRWVICADafktsdyhamlQELLPGLAEGQPGALACERLPElrgvvsLAPAPPPGFLAWH 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 HLAY------------------------IIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFsFDGFI 2729
Cdd:PRK12583   178 ELQArgetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL-YHCFG 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2730 TSMFTPLLSGAKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDvvQPE----DVKTLRVVTLAGEAADRELI 2805
Cdd:PRK12583   257 MVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELD--HPQrgnfDLSSLRTGIMAGAPCPIEVM 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2806 ARSLAICPHTELANEYGPTENS---VATTVMRHMEKQAyVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGY 2882
Cdd:PRK12583   335 RRVMDEMHMAEVQIAYGMTETSpvsLQTTAADDLERRV-ETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2883 VNLPELTERAFTQNPFkpearMYrTGDAARWMADGTLEYLGRIDDQVkIR-GYRVETKEIESVIRCIKGVKDAAVVAHVT 2961
Cdd:PRK12583   414 WNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEEFLFTHPAVADVQVFGVPD 486

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2962 ASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:PRK12583   487 EKYGEEIVAWVRLHPGhaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1077-1460 4.09e-32

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: 131.65  E-value: 4.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1077 AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPFTLSKETTIEGFV-----RPFDLSQa 1151
Cdd:cd19545     21 AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWTESTSLDEYLeedraAPMGLGG- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1152 PLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKPlRIQYKDYavwQQKFKKGDSYQKQEtYWQQQ 1231
Cdd:cd19545    100 PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPFSRF---VKYLRQLDDEAAAE-FWRSY 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1232 FSGDLPIL--ELPTDKRRPaerqfiggkvtfQLDKEITARIKRLAHKNRS-TLYMTLLALYSAFLSRLSGQDDIVIGSPI 1308
Cdd:cd19545    175 LAGLDPAVfpPLPSSRYQP------------RPDATLEHSISLPSSASSGvTLATVLRAAWALVLSRYTGSDDVVFGVTL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1309 AGR--PHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQTALEA--YEHqdypfeelvdkLGVQ--REMSRN----P 1378
Cdd:cd19545    243 SGRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMipFEH-----------TGLQniRRLGPDaraaC 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1379 LFDTTLVLQNMEQQklkmNDVQLQWNDLEHPISKFD------ISLYVTEHDSELFCQFEYSTALFEKETIQRWASLFTTL 1452
Cdd:cd19545    312 NFQTLLVVQPALPS----STSESLELGIEEESEDLEdfssygLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHV 387


                   ....*...
gi 1678550997 1453 VEHTAASP 1460
Cdd:cd19545    388 LQQLASAP 395
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 2533-3019 4.15e-32

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


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 133.61  E-value: 4.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVP 2612
Cdd:cd05920     15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2613 IDPEYPKERKRYILSDSGTKLLmtineADLGVLADFEGEILTIESVEEddkspLPQmssahhLAYIIYTSGTTGRPKGVM 2692
Cdd:cd05920     95 ALPSHRRSELSAFCAHAEAVAY-----IVPDRHAGFDHRALARELAES-----IPE------VALFLLSGGTTGTPKLIP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2693 VEHKGIANTLqwRRNAYA--FNETDTILQLFSFSFdGFITS---MFTPLLSGAKAVLLHEEEAKDILAIkhqLSRQRITH 2767
Cdd:cd05920    159 RTHNDYAYNV--RASAEVcgLDQDTVYLAVLPAAH-NFPLAcpgVLGTLLAGGRVVLAPDPSPDAAFPL---IEREGVTV 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2768 MIIVPVLYRALLDVV--QPEDVKTLRVVTLAGEAADRELIARSLAI--CphtELANEYGPTENSVATTVMRHMEKQAYVS 2843
Cdd:cd05920    233 TALVPALVSLWLDAAasRRADLSSLRLLQVGGARLSPALARRVPPVlgC---TLQQVFGMAEGLLNYTRLDDPDEVIIHT 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2844 IGQPID-GTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYL 2922
Cdd:cd05920    310 QGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVE 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2923 GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHV-TASGQTELSAYVVTKPGLSTNAVRSELQNK-LPVFMHPAFI 3000
Cdd:cd05920    384 GRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdELLGERSCAFVVLRDPPPSAAQLRRFLRERgLAAYKLPDRI 463

                          490
                   ....*....|....*....
gi 1678550997 3001 EKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05920    464 EFVDSLPLTAVGKIDKKAL 482
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 12-433 4.40e-32

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: 132.50  E-value: 4.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVVL--RERNVIVL 89
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILppGPAPLEVR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 EEDIThlnEAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVN 169
Cdd:cd19539     83 DLSDP---DSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 ASPITL-EPVQPYGKYIKWLMEQDKEQAVS----YWDHYLSGHEQQTVLPKQKKTKGKSRQEHVT-FSFSKEESSRLSEL 243
Cdd:cd19539    160 GPAAPLpELRQQYKEYAAWQREALAAPRAAelldFWRRRLRGAEPTALPTDRPRPAGFPYPGADLrFELDAELVAALREL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  244 AAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDMQKDRL 322
Cdd:cd19539    240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDvSDCATFRDLIARVRKALV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  323 AAEAYSYHPLYEI-----QSRSAVKQGLIDHILVFENYP-VQQEIQMLNKQEHASDlfqihnftVADETNYSFYLMVAP- 395
Cdd:cd19539    318 DAQRHQELPFQQLvaelpVDRDAGRHPLVQIVFQVTNAPaGELELAGGLSYTEGSD--------IPDGAKFDLNLTVTEe 389

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1678550997  396 GEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19539    390 GTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 488-947 4.68e-32

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: 132.50  E-value: 4.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVsq 567
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 ahLPSSLEDNYIITHPedieskvdgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDfEADVL 647
Cdd:cd05903     79 --VPERFRQFDPAAMP------------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG-PGDVF 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  648 QFATPsfdVCYQE-----IFSALLKGGTLHIVPEAIKRDVPQLfafINKHQTNIVFLPTAFIKMIFSERELANSFPDGVK 722
Cdd:cd05903    138 LVASP---MAHQTgfvygFTLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLR 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  723 HLIAAG--------EQLmisdlfQDVLrkrGIHLHNHYGPSET-HVVSTytIHPGDPIPELPPIGKPIGCTDLYILNHQK 793
Cdd:cd05903    212 TFVCGGatvprslaRRA------AELL---GAKVCSAYGSTECpGAVTS--ITPAPEDRRLYTDGRPLPGVEIKVVDDTG 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  794 QLQPCGVPGELYISGASVARGYVNHDKLTSDKFssdpfkpDVIMYRTGDLARRLEDGNIEYIGRADNqVKIR-GYRIEPQ 872
Cdd:cd05903    281 ATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVL 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  873 EIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQK----LNTIDLRSYM-ASELPEYMIPAKWIWVDSIPLTPNGKV 947
Cdd:cd05903    353 EVEDLLLGHPGVIEAAVVALPDERLGERACAVV--VTKsgalLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 2543-3019 7.66e-32

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: 133.77  E-value: 7.66e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGD-----KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEY 2617
Cdd:cd05970     27 AKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2618 PKERKRYILSDSGTKLLMTINEADlgVLADFEGEILTIESVEE-------------------DDKSPL------PQMSSA 2672
Cdd:cd05970    107 TAKDIVYRIESADIKMIVAIAEDN--IPEEIEKAAPECPSKPKlvwvgdpvpegwidfrkliKNASPDferptaNSYPCG 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2673 HHLAYIIYTSGTTGRPKgvMVEHKG------IANTLQW---RRNAYAFNETDTilqlfsfsfdGFITSMFTPL----LSG 2739
Cdd:cd05970    185 EDILLVYFSSGTTGMPK--MVEHDFtyplghIVTAKYWqnvREGGLHLTVADT----------GWGKAVWGKIygqwIAG 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2740 AkAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALL-DVVQPEDVKTLRVVTLAGEAADRELIARSLAicpHT--E 2816
Cdd:cd05970    253 A-AVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIrEDLSRYDLSSLRYCTTAGEALNPEVFNTFKE---KTgiK 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2817 LANEYGPTENSVATTVMRHMEKQAYvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGT-----GLARGYVNLPELTER 2891
Cdd:cd05970    329 LMEGFGQTETTLTIATFPWMEPKPG-SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAE 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2892 AFTQNpfkpearMYRTGDAArWM-ADGTLEYLGRIDDQVKIRGYRVETKEIES-------VIRC-IKGVKDAavvahvtA 2962
Cdd:cd05970    408 VWHDG-------YYHTGDAA-WMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESaliqhpaVLECaVTGVPDP-------I 472

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2963 SGQTELSAYVVTKPGLSTNAVRSELQNKL----PVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05970    473 RGQVVKATIVLAKGYEPSEELKKELQDHVkkvtAPYKYPRIVEFVDELPKTISGKIRRVEI 533
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 1493-1925 8.03e-32

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: 133.13  E-value: 8.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1493 NQTLHYALEQQAEKTPDQAAVIfeDGV----MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAG 1568
Cdd:cd05904      4 DLPLDSVSFLFASAHPSRPALI--DAAtgraLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1569 GAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLH-VPEFTGEIVYLNQTNSGLAHRLSN---------PNVDVLPQSLA 1638
Cdd:cd05904     82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEkLASLALPVVLLDSAEFDSLSFSDLlfeadeaepPVVVIKQDDVA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1639 YVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRY--QLKHSDMIM------HktSYSFDASIWELFwwpYAGASVYLLPQg 1710
Cdd:cd05904    162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgsNSDSEDVFLcvlpmfH--IYGLSSFALGLL---RLGATVVVMPR- 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1711 geKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPT 1790
Cdd:cd05904    236 --FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSS--LRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMT 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1791 EATVEAAFfdCPPHEKlERIPIGK-----PVHHVRLYLLNQNQrMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDP 1865
Cdd:cd05904    312 ESTGVVAM--CFAPEK-DRAKYGSvgrlvPNVEAKIVDPETGE-SLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEG 387

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1866 FYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT 1925
Cdd:cd05904    388 WL------HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1642-1983 1.27e-31

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: 128.93  E-value: 1.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1642 YTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMI------MHktsySFDASIWELFWWPYAGASVYllPQGGEKeP 1715
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFH----CFGSVLGVLACLTHGATMVF--PSPSFD-P 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1716 EVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEAT-- 1793
Cdd:cd05917     82 LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSS--LRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpv 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1794 VEAAFFDCPPHEKLEriPIGKPVHHVRLYLLNQNQR-MLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDpfypgeRM 1872
Cdd:cd05917    160 STQTRTDDSIEKRVN--TVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD------GW 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1873 YKTGDVARWLPDGNVEFLGRTDDQVkIRG-YRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQR 1944
Cdd:cd05917    232 LHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDEryGE-EVCAWIrlkEGaeLTE 309

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1678550997 1945 NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05917    310 EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1484-1983 1.32e-31

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 133.33  E-value: 1.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1484 LFEETGYSMNQTLHYALEQQAEKTPDQAAVIFEDGV-MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIY 1562
Cdd:PRK06087    13 AYRQQGYWGDASLADYWQQTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1563 GILKAGGAYLPIDPDYPEERISFLLEDSGTNILL---LQSAGLHVPEFT---------GEIVYLNQ----TNS-GLAHRL 1625
Cdd:PRK06087    93 ACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptLFKQTRPVDLILplqnqlpqlQQIVGVDKlapaTSSlSLSQII 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1626 SN-------PNVDvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HKTSYsFDASIW 1692
Cdd:PRK06087   173 ADyeplttaITTH--GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMmpaplgHATGF-LHGVTA 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1693 ELFwwpyAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIkyRSVPIKTNRLKRVFSGGEQLGTHLVS 1772
Cdd:PRK06087   250 PFL----IGARSVLLDI---FTPDACLALLEQQRCTCMLGATPFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVAR 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1773 RFYEllPNVSITNSYGPTEATVEAAffdCPPHEKLERI--PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGY 1850
Cdd:PRK06087   321 ECQQ--RGIKLLSVYGSTESSPHAV---VNLDDPLSRFmhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGY 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1851 LNRPALTeERFLEDpfypgERMYKTGDVARWLPDGNVEFLGRTDDqVKIR-GYRIEPGEIEAALRSIEGVREAAVTVRTD 1929
Cdd:PRK06087   396 LDEPELT-ARALDE-----EGWYYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAMPD 468

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1930 S--GEpELCAYVEgLQRNEVRAQLERLL--------PGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK06087   469 ErlGE-RSCAYVV-LKAPHHSLTLEEVVaffsrkrvAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
 1504-1980 2.91e-31

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 131.50  E-value: 2.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:TIGR02262   15 VEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDY 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLQSAGLHV-PEFTGEIVYLNQTNsgLAHRLSNPNVDVL----------------PQSLAYVIYTSGS 1646
Cdd:TIGR02262   95 AYMLEDSRARVVFVSGALLPViKAALGKSPHLEHRV--VVGRPEAGEVQLAellateseqfkpaatqADDPAFWLYSSGS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1647 TGMPKGVEIEHRSA-VNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYA-GASVYLLPQggEKEPEVIAKAIEE 1724
Cdd:TIGR02262  173 TGMPKGVVHTHSNPyWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSvGATTVLMGE--RPTPDAVFDRLRR 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1725 QKITAMHFVPSMLHAFLEHIKYRSVpiKTNRLKRVFSGGE----QLGTHLVSRFyellpNVSITNSYGPTEatVEAAFFD 1800
Cdd:TIGR02262  251 HQPTIFYGVPTLYAAMLADPNLPSE--DQVRLRLCTSAGEalpaEVGQRWQARF-----GVDIVDGIGSTE--MLHIFLS 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1801 CPPHEkLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLedpfypGErMYKTGDVAR 1880
Cdd:TIGR02262  322 NLPGD-VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ------GE-WTRSGDKYV 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1881 WLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV-----EGLQRNEVRAQLERL 1954
Cdd:TIGR02262  394 RNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdGLIKPKAFVvlrpgQTALETELKEHVKDR 473

                          490       500
                   ....*....|....*....|....*.
gi 1678550997 1955 LPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:TIGR02262  474 LAPYKYPRWIVFVDDLPKTATGKIQR 499
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 488-952 2.97e-31

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: 129.39  E-value: 2.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILhdcgcshvvsq 567
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQL----------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 ahlpsslednyiithpEDIESKVDgsniksvnnadDLLYMIYTSGTTGKPKGVQFEHRN--------MANLlkfeythsG 639
Cdd:cd05912     70 ----------------KDSDVKLD-----------DIATIMYTSGTTGKPKGVQQTFGNhwwsaigsALNL--------G 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  640 IDfEADVLQFATPSFDVCYQEI-FSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFL-PTAFIKMIfseRELANSF 717
Cdd:cd05912    115 LT-EDDNWLCALPLFHISGLSIlMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVvPTMLQRLL---EILGEGY 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  718 PDGVKHLIAAGEQLMISDLFQdvLRKRGIHLHNHYGPSET--HVVstyTIHPGDPIPELPPIGKPIGCTDLYIlnhQKQL 795
Cdd:cd05912    188 PNNLRCILLGGGPAPKPLLEQ--CKEKGIPVYQSYGMTETcsQIV---TLSPEDALNKIGSAGKPLFPVELKI---EDDG 259

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  796 QPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKpdvimyrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:cd05912    260 QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 332

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  876 VTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05912    333 EVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 2534-3012 3.78e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 131.79  E-value: 3.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI 2613
Cdd:PRK06164    11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 DPEYPKERKRYILSDSGTKLLMT------------INEADLGVLADFEGeILTIESVEEDDKSPLP--------QMSSAH 2673
Cdd:PRK06164    91 NTRYRSHEVAHILGRGRARWLVVwpgfkgidfaaiLAAVPPDALPPLRA-IAVVDDAADATPAPAPgarvqlfaLPDPAP 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 H------------LAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFS--FdGFITsmftpLLSG 2739
Cdd:PRK06164   170 PaaageraadpdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvF-GFST-----LLGA 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2740 -AKAVLLHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVV-QPEDVKTLRVVTLAGEA-ADRELIARSLAicPHTE 2816
Cdd:PRK06164   244 lAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAgERADFPSARLFGFASFApALGELAALARA--RGVP 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2817 LANEYGPTE-------NSVATTV-MRH------MEKQAYVSIGQPIDGTqvlilnsnhqLQPIGVAGELCIAGTGLARGY 2882
Cdd:PRK06164   322 LTGLYGSSEvqalvalQPATDPVsVRIegggrpASPEARVRARDPQDGA----------LLPDGESGEIEIRAPSLMRGY 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2883 VNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTA 2962
Cdd:PRK06164   392 LDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-ATR 464

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2963 SGQTELSAYVVTKPGLSTNA--VRSELQNKLPVFMHPAFIEKLDSLP--LSPNG 3012
Cdd:PRK06164   465 DGKTVPVAFVIPTDGASPDEagLMAACREALAGFKVPARVQVVEAFPvtESANG 518
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 489-952 3.84e-31

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: 129.95  E-value: 3.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA 568
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslednyiithpeDIESKVDgsniksvnnaDDLLYMIYTSGTTGKPKGVQFEHRNmanLLKFE-YTHSGIDFEAD-- 645
Cdd:cd05973     81 ----------------ANRHKLD----------SDPFVMMFTSGTTGLPKGVPVPLRA---LAAFGaYLRDAVDLRPEds 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  646 VLQFATPSFDV-CYQEIFSALLKGgTLHIVPEAiKRDVPQLFAFINKHQ-TNIVFLPTAFIKMIFSERELANSFPDGVKH 723
Cdd:cd05973    132 FWNAADPGWAYgLYYAITGPLALG-HPTILLEG-GFSVESTWRVIERLGvTNLAGSPTAYRLLMAAGAEVPARPKGRLRR 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  724 LIAAGEQLM--ISDLFQDVLrkrGIHLHNHYGPSETHVVSTYTIHPGDPIPElPPIGKPIGCTDLYILNHQKQLQPCGVP 801
Cdd:cd05973    210 VSSAGEPLTpeVIRWFDAAL---GVPIHDHYGQTELGMVLANHHALEHPVHA-GSAGRAMPGWRVAVLDDDGDELGPGEP 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  802 GELYISGASVA----RGYVNHDklTSDkfssdpfkPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVT 877
Cdd:cd05973    286 GRLAIDIANSPlmwfRGYQLPD--TPA--------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  878 LMNHPDISEAAILIWQD-QNGEH-----ELCAYYCSVQKLNTiDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAA 951
Cdd:cd05973    356 LIEHPAVAEAAVIGVPDpERTEVvkafvVLRGGHEGTPALAD-ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFL 434


                   .
gi 1678550997  952 L 952
Cdd:cd05973    435 L 435
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 1521-1913 3.85e-31

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: 130.56  E-value: 3.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSA 1600
Cdd:cd17640      7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEND 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM 1680
Cdd:cd17640     87 ---------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFL 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1681 hktsysfdaSIWELfWWPYAGASVY-LLPQGGEK---EPEVIAKAIEEQKITAMHFVPSMLHAFLEHI---KYRSVPIKT 1753
Cdd:cd17640    134 ---------SILPI-WHSYERSAEYfIFACGCSQaytSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIqkqVSKSSPIKQ 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1754 ---------NRLKRVFSGGEQLGTHlVSRFYELLpNVSITNSYGPTEATVEAAffdCPPHEKLERIPIGKPVHHVRLYLL 1824
Cdd:cd17640    204 flflfflsgGIFKFGISGGGALPPH-VDTFFEAI-GIEVLNGYGLTETSPVVS---ARRLKCNVRGSVGRPLPGTEIKIV 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1825 NQNQR-MLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIR-GY 1902
Cdd:cd17640    279 DPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWF------NTGDLGWLTCGGELVLTGRAKDTIVLSnGE 352

                          410
                   ....*....|.
gi 1678550997 1903 RIEPGEIEAAL 1913
Cdd:cd17640    353 NVEPQPIEEAL 363
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 1491-1983 5.68e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 131.40  E-value: 5.68e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1491 SMNQTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:PRK06164     7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYPEERISFLLEDSGTNILLLQSA--GLHVPEFTGEIVY-----------LNQTNSGLAHRLSNPNVDVLPQ-- 1635
Cdd:PRK06164    87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGfkGIDFAAILAAVPPdalpplraiavVDDAADATPAPAPGARVQLFALpd 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1636 ---------------SLAYVIYTSGSTGMPKGVEieHRSAVnflnslqsryQLKHSDMIMHKTSYSFDASIweLFWWPY- 1699
Cdd:PRK06164   167 pappaaageraadpdAGALLFTTSGTTSGPKLVL--HRQAT----------LLRHARAIARAYGYDPGAVL--LAALPFc 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1700 -------------AGASVYLLPQggeKEPEVIAKAIEEQKITamhfvpsmlHAFLEHIKYRSVpIKTNRLKRVFSGGEQL 1766
Cdd:PRK06164   233 gvfgfstllgalaGGAPLVCEPV---FDAARTARALRRHRVT---------HTFGNDEMLRRI-LDTAGERADFPSARLF 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1767 G-THLVSRFYELLP-----NVSITNSYGPTEATVEAAFFDCPPHEKLERIPIGKPVH---HVRLyLLNQNQRMLPVGCIG 1837
Cdd:PRK06164   300 GfASFAPALGELAAlararGVPLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPASpeaRVRA-RDPQDGALLPDGESG 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1838 ELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 1917
Cdd:PRK06164   379 EIEIRAPSLMRGYLDNPDATARALTDDGYF------RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALP 452

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1918 GVREAAVTVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSG---KLDRNAL 1983
Cdd:PRK06164   453 GVAAAQVVGATRDGKTVPVAFViptdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 11-433 6.08e-31

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: 128.97  E-value: 6.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   11 YPLSYMQEGMLfhsLLQK---DSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERNVI 87
Cdd:cd20484      2 SPLSEGQKGLW---MLQKmspEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEED-GVPFQKIEPSKPLS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   88 VLEEDITHLNEAEQSQFIeqwKEKDRDrGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASY 167
Cdd:cd20484     78 FQEEDISSLKESEIIAYL---REKAKE-PFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQAL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  168 VNASPITLEPVQP-YGKYIKW----LMEQDKEQAVSYWDHYLSGHEQQTVLPKQK-KTKGKSRQEHV-TFSFSKEESSRL 240
Cdd:cd20484    154 LQGKQPTLASSPAsYYDFVAWeqdmLAGAEGEEHRAYWKQQLSGTLPILELPADRpRSSAPSFEGQTyTRRLPSELSNQI 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  241 SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQ-GAKTPFLQLIKDMQ- 318
Cdd:cd20484    234 KSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPE--ERFDSLIGYFINMLPIRSRiLGEETFSDFIRKLQl 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  319 --KDRLAAEAYSYHPLYE------IQSRSAVKQglidhiLVFENYPVQQEIQMLNKQEHASDLFQIhNFT--VADETNYS 388
Cdd:cd20484    312 tvLDGLDHAAYPFPAMVRdlniprSQANSPVFQ------VAFFYQNFLQSTSLQQFLAEYQDVLSI-EFVegIHQEGEYE 384

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1678550997  389 FYLMVAPGEE---IHIKmnYDAEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd20484    385 LVLEVYEQEDrftLNIK--YNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 472-954 6.56e-31

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 130.31  E-value: 6.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  472 QAEKTPDAHAVIDQACSL--TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA 549
Cdd:PRK09088     4 HARLQPQRLAAVDLALGRrwTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  550 DRIRYILHDCGCSHVVSQAHLPSSLEDnyiithPEDIE---SKVDGSNIKSVNNAD-DLLYMI-YTSGTTGKPKGVQFEH 624
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVAAGRTD------VEDLAafiASADALEPADTPSIPpERVSLIlFTSGTSGQPKGVMLSE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  625 RNManllkfeyTHSGIDF-------EADVLQFATPSFDVC--YQEIFSALLKGGTLHIVP-----EAIKR---------- 680
Cdd:PRK09088   158 RNL--------QQTAHNFgvlgrvdAHSSFLCDAPMFHIIglITSVRPVLAVGGSILVSNgfepkRTLGRlgdpalgith 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  681 --DVPQLFAFINKHQTnivFLPTAFikmifseRELANSFPDGVKHliaAGEQLM--ISDlfqdvlrkrGIHLHNHYGPSE 756
Cdd:PRK09088   230 yfCVPQMAQAFRAQPG---FDAAAL-------RHLTALFTGGAPH---AAEDILgwLDD---------GIPMVDGFGMSE 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  757 THVVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvi 836
Cdd:PRK09088   288 AGTVFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW----- 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  837 mYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEHELCAYYCSVQ-KLNTI 914
Cdd:PRK09088   363 -FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGaPLDLE 441

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997  915 DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK09088   442 RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 1496-1933 1.01e-30

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 129.34  E-value: 1.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LHYALEQQAEKTPDqaAVIFEDGVMTYKELNEQANRIAWELIGRGvkpetTVAIIGKRSPEMLLGIYGILKAGGAYLPID 1575
Cdd:PRK07787     4 LNPAAVAAAADIAD--AVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPEERISFLLEDSGTNILL----LQSAGL-HVPeftgeiVYLNQTNsglAHRLSNPNvdvlPQSLAYVIYTSGSTGMP 1650
Cdd:PRK07787    77 PDSGVAERRHILADSGAQAWLgpapDDPAGLpHVP------VRLHARS---WHRYPEPD----PDAPALIVYTSGTTGPP 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1651 KGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSysfdasiweLFwwpyagaSVYLLPQG--------------GEKEPE 1716
Cdd:PRK07787   144 KGVVLSRRAIAADLDALAEAWQWTADDVLVHGLP---------LF-------HVHGLVLGvlgplrignrfvhtGRPTPE 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1717 VIAKAIEEQkiTAMHF-VPSMLH---AFLEHIKyrsvPIKTNRLkrVFSGGEQLGTHLVSRFYELlPNVSITNSYGPTEA 1792
Cdd:PRK07787   208 AYAQALSEG--GTLYFgVPTVWSriaADPEAAR----ALRGARL--LVSGSAALPVPVFDRLAAL-TGHRPVERYGMTET 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1793 --TVeAAFFDCppheklERIP--IGKPVHHVRLYLLNQNQRMLPVG--CIGELYIAGAGVARGYLNRPALTEERFLEDPF 1866
Cdd:PRK07787   279 liTL-STRADG------ERRPgwVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGW 351

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 1867 YpgermyKTGDVARWLPDGNVEFLGR-TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEP 1933
Cdd:PRK07787   352 F------RTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVV-----GVP 408
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1066-1460 1.40e-30

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


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 127.81  E-value: 1.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1066 IYVLQQLDEGV-----------AYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEV--PFT 1132
Cdd:cd19547      1 VYPLAPMQEGMlfrglfwpdsdAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLapPWA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1133 L------SKETTIEGFVR--------PFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLL----IREFTDLYA 1194
Cdd:cd19547     81 LldwsgeDPDRRAELLERlladdraaGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIwgdvFRVYEELAH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1195 NR--QLKPLRiQYKDYAVW-QQKFKKGDsyqKQETYWqQQFSGDLPilelPTD-KRRPAERQFIGGKVTFQLDKEITARI 1270
Cdd:cd19547    161 GRepQLSPCR-PYRDYVRWiRARTAQSE---ESERFW-REYLRDLT----PSPfSTAPADREGEFDTVVHEFPEQLTRLV 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1271 KRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPH--ADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQ 1348
Cdd:cd19547    232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1349 TALEAYEHQDYPFEELVDKLGVQReMSRNPLFDTTLVLQNMEQQKLKMNDVQLQWNDL------EHPISKFDISLyvteh 1422
Cdd:cd19547    312 DLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLhaqektEYPIGLIVLPL----- 385

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1678550997 1423 dSELFCQFEYSTALFEKETIQRWASLFTTLVEHTAASP 1460
Cdd:cd19547    386 -QKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1494-1980 1.47e-30

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 130.28  E-value: 1.47e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAVIF-EDGV-MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAY 1571
Cdd:PRK12583    18 QTIGDAFDATVARFPDREALVVrHQALrYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1572 LPIDPDYPEERISFLLEDSGTNILLLQSA---------------GLH-----------VPEFTGEIVYLNQTNSGLA--H 1623
Cdd:PRK12583    98 VNINPAYRASELEYALGQSGVRWVICADAfktsdyhamlqellpGLAegqpgalacerLPELRGVVSLAPAPPPGFLawH 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1624 RLSNPNVDVLPQSLAY------------VIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTS--YSFDA 1689
Cdd:PRK12583   178 ELQARGETVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPlyHCFGM 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1690 SIWELFWWPYAGASVYllPQGgEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTH 1769
Cdd:PRK12583   258 VLANLGCMTVGACLVY--PNE-AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSS--LRTGIMAGAPCPIE 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1770 LVSRFYELLPNVSITNSYGPTEATveAAFFDCPPHEKLER--IPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVA 1847
Cdd:PRK12583   333 VMRRVMDEMHMAEVQIAYGMTETS--PVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1848 RGYLNRPALTEERFLEDPFypgerMYkTGDVARWLPDGNVEFLGRTDDQVkIR-GYRIEPGEIEAALRSIEGVREAAVTV 1926
Cdd:PRK12583   411 KGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEEFLFTHPAVADVQVFG 483

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 1927 RTDS--GEpELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:PRK12583   484 VPDEkyGE-EIVAWVrlhpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2530-3021 1.80e-30

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 129.87  E-value: 1.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2530 YGVQTISQLFEQQAARTPKASALVSGDKT-LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHR--SFSMIAsiLGVWKA 2606
Cdd:PRK06087    20 WGDASLADYWQQTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGwcEFTIIY--LACLKV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDPEYPKERKRYILSDSGTKLLMT------INEADL-------------GVLADFEGEILTIESVEE--DDKSP 2665
Cdd:PRK06087    98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqTRPVDLilplqnqlpqlqqIVGVDKLAPATSSLSLSQiiADYEP 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2666 L--PQMSSAHHLAYIIYTSGTTGRPKGVMVEHkgiaNTLQWRRNAYA----FNETDTILQLFSFSF-DGFITSMFTPLLS 2738
Cdd:PRK06087   178 LttAITTHGDELAAVLFTSGTEGLPKGVMLTH----NNILASERAYCarlnLTWQDVFMMPAPLGHaTGFLHGVTAPFLI 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2739 GAKAVLLHEEEAKDILAIkhqLSRQRITHMI-IVPVLYRALLDV-VQPEDVKTLRVVTLAGEAADRELIARSLAicPHTE 2816
Cdd:PRK06087   254 GARSVLLDIFTPDACLAL---LEQQRCTCMLgATPFIYDLLNLLeKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIK 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2817 LANEYGPTENSVATTVM--RHMEKQAYVSiGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFT 2894
Cdd:PRK06087   329 LLSVYGSTESSPHAVVNldDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALD 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2895 QNPFkpearmYRTGDAARWMADGTLEYLGRIDDqVKIR-GYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVV 2973
Cdd:PRK06087   408 EEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVV 480

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 2974 TKPGLSTNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPK 3021
Cdd:PRK06087   481 LKAPHHSLTLEEVVaffsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 2528-3019 2.16e-30

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 129.88  E-value: 2.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2528 NQYgvQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKA 2606
Cdd:PRK05677    21 DEY--PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRA 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDPEYPKERKRYILSDSGTKLLMTI-NEADL--------GV-------LADFEGEI--LTIESVEEDDKSPLPQ 2668
Cdd:PRK05677    99 GLIVVNTNPLYTAREMEHQFNDSGAKALVCLaNMAHLaekvlpktGVkhvivteVADMLPPLkrLLINAVVKHVKKMVPA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2669 MS------------------------SAHHLAYIIYTSGTTGRPKGVMVEHKG-IANTLQWRR-NAYAFNETDTIL---- 2718
Cdd:PRK05677   179 YHlpqavkfndalakgagqpvteanpQADDVAVLQYTGGTTGVAKGAMLTHRNlVANMLQCRAlMGSNLNEGCEILiapl 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2719 ---QLFSFSFDgfitSMFTpLLSGAKAVLLheEEAKDILAIKHQLSRQRITHMIIVPVLYRALldvVQPEDVKTLRV--- 2792
Cdd:PRK05677   259 plyHIYAFTFH----CMAM-MLIGNHNILI--SNPRDLPAMVKELGKWKFSGFVGLNTLFVAL---CNNEAFRKLDFsal 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2793 -VTLAGEAADRELIA---RSLAICPHTElanEYGPTENSVATTVmRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVA 2868
Cdd:PRK05677   329 kLTLSGGMALQLATAerwKEVTGCAICE---GYGMTETSPVVSV-NPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEV 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2869 GELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCI 2948
Cdd:PRK05677   405 GELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2949 KGVKD-AAVVAHVTASGQTeLSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK05677   479 PGVLQcAAIGVPDEKSGEA-IKVFVVVKPGetLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
471-949 2.69e-30

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 128.16  E-value: 2.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  471 KQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPAD 550
Cdd:PRK03640    10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  551 RIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN---- 626
Cdd:PRK03640    90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNhwws 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 -MANLLKFEYThsgidfEADVLQFATPSFDVcyqEIFSALLK----GGTLHIVPeaiKRDVPQLFAFINKHQTNIVFLPT 701
Cdd:PRK03640   170 aVGSALNLGLT------EDDCWLAAVPIFHI---SGLSILMRsviyGMRVVLVE---KFDAEKINKLLQTGGVTIISVVS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  702 AFIKMIFSERELANsFPDGVKHLIAAGEQLMISDLfqDVLRKRGIHLHNHYGPSET--HVVstyTIHPGDPIPELPPIGK 779
Cdd:PRK03640   238 TMLQRLLERLGEGT-YPSSFRCMLLGGGPAPKPLL--EQCKEKGIPVYQSYGMTETasQIV---TLSPEDALTKLGSAGK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  780 PIGCTDLYILNHQKQLQPcGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKpdvimyrTGDLARRLEDGNIEYIGRAD 859
Cdd:PRK03640   312 PLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRS 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  860 NQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSI 939
Cdd:PRK03640   384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEEL 463

                          490
                   ....*....|
gi 1678550997  940 PLTPNGKVDR 949
Cdd:PRK03640   464 PRNASGKLLR 473
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 2558-3015 3.91e-30

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: 127.83  E-value: 3.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2558 TLTYQELDEWSNGIARALRsRGVKPDTPVGIMMHRSFSMIASILGVWKAGgcYVPIDPEYP--KERKRYILSDSGTKLLM 2635
Cdd:cd05909      7 SLTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2636 T----INEADL--GVLADFEGEILTIESVEED----DK---------SPLPQMS-------SAHHLAYIIYTSGTTGRPK 2689
Cdd:cd05909     84 TskqfIEKLKLhhLFDVEYDARIVYLEDLRAKiskaDKckaflagkfPPKWLLRifgvapvQPDDPAVILFTSGSEGLPK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2690 GVMVEHKGIANTLQWRRNAYAFNETDTILQLFSF--SFdGFITSMFTPLLSGAKAVLL-HEEEAKDILAIKHQlsrQRIT 2766
Cdd:cd05909    164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSF-GLTGCLWLPLLSGIKVVFHpNPLDYKKIPELIYD---KKAT 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2767 HMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEA---ADRELIARSLAICPhtelaNE-YGPTENS-VATTVMRHMEKQAY 2841
Cdd:cd05909    240 ILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKlkdTLRQEFQEKFGIRI-----LEgYGTTECSpVISVNTPQSPNKEG 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2842 vSIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARGYVNLPELTEraftqnpFKPEARMYRTGDAARWMADGTLE 2920
Cdd:cd05909    315 -TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLT 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2921 YLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQN-KLPVFMHPAF 2999
Cdd:cd05909    387 ITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNaGISNLAKPSY 466

                          490
                   ....*....|....*.
gi 1678550997 3000 IEKLDSLPLSPNGKLD 3015
Cdd:cd05909    467 IHQVEEIPLLGTGKPD 482
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 463-952 4.13e-30

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 128.26  E-value: 4.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVIDQAC-----SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAG 537
Cdd:PRK08008     7 QHLRQMWDDLADVYGHKTALIFESSggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  538 GAIVPVDPHYPADRIRYILHDCGCSHVVSQAHL-----------PSSLEDNYII-THPEDIESKVDGSNIKSVN------ 599
Cdd:PRK08008    87 AIMVPINARLLREESAWILQNSQASLLVTSAQFypmyrqiqqedATPLRHICLTrVALPADDGVSSFTQLKAQQpatlcy 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 ----NADDLLYMIYTSGTTGKPKGVQFEHRNmanlLKFE--YTHSGIDFEA-DVLQFATPSFDVCYQ--EIFSALLKGGT 670
Cdd:PRK08008   167 applSTDDTAEILFTSGTTSRPKGVVITHYN----LRFAgyYSAWQCALRDdDVYLTVMPAFHIDCQctAAMAAFSAGAT 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  671 LHIVPEAIKRdvpqlfAF---INKHQTNIvflpTAFIKMIFSERELANSFPDGVKHLIaagEQLM----ISDLFQDVLRK 743
Cdd:PRK08008   243 FVLLEKYSAR------AFwgqVCKYRATI----TECIPMMIRTLMVQPPSANDRQHCL---REVMfylnLSDQEKDAFEE 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  744 R-GIHLHNHYGPSEThVVSTYTIHPGDPiPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGA---SVARGYVNHD 819
Cdd:PRK08008   310 RfGVRLLTSYGMTET-IVGIIGDRPGDK-RRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDP 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  820 KLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEH 899
Cdd:PRK08008   388 KATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  900 ELCAYYCSVQ--KLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK08008   462 AIKAFVVLNEgeTLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 463-954 8.31e-30

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 127.97  E-value: 8.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVI--DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI 540
Cdd:PRK12583    18 QTIGDAFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  541 VPVDPHYPADRIRYILHDCGCS-------------HVVSQAHLPSSLEDNYIITHPE----------------------- 584
Cdd:PRK12583    98 VNINPAYRASELEYALGQSGVRwvicadafktsdyHAMLQELLPGLAEGQPGALACErlpelrgvvslapapppgflawh 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  585 DIESKVDGSNIKSVN------NADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDfEADVLQFATPSFDvCY 658
Cdd:PRK12583   178 ELQARGETVSREALAerqaslDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLT-EHDRLCVPVPLYH-CF 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  659 QEIFSALL---KGGTLHIVPEAIKRDVpQLFAFINKHQTNIVFLPTAFIKMI----FSERELAnSFPDGvkhlIAAGEQL 731
Cdd:PRK12583   256 GMVLANLGcmtVGACLVYPNEAFDPLA-TLQAVEEERCTALYGVPTMFIAELdhpqRGNFDLS-SLRTG----IMAGAPC 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  732 MIsdlfqDVLRKRGIHLHNH-----YGPSETHVVSTYTIhPGDPIP-ELPPIGKPIGCTDLYILNHQKQLQPCGVPGELY 805
Cdd:PRK12583   330 PI-----EVMRRVMDEMHMAevqiaYGMTETSPVSLQTT-AADDLErRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  806 ISGASVARGYVNHDKLTSDKFSSDPFkpdviMYrTGDLARRLEDGNIEYIGRADNQVkIR-GYRIEPQEIEVTLMNHPDI 884
Cdd:PRK12583   404 TRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEEFLFTHPAV 476

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  885 SEAAILIWQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMIPaKWIW-VDSIPLTPNGKVDRAALPE 954
Cdd:PRK12583   477 ADVQVFGVPDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFKVP-RYFRfVDEFPMTVTGKVQKFRMRE 548
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 464-947 8.88e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 127.36  E-value: 8.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPV 543
Cdd:PRK08316    12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 DPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIE-------SKVDGSNIKSVN--------------NAD 602
Cdd:PRK08316    92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIlslvlggREAPGGWLDFADwaeagsvaepdvelADD 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  603 DLLYMIYTSGTTGKPKGVQFEHRNmanlLKFEYTHSGIDFE---ADVLQFATPSFDvCYQ-EIF--SALLKGGTLHIVPE 676
Cdd:PRK08316   172 DLAQILYTSGTESLPKGAMLTHRA----LIAEYVSCIVAGDmsaDDIPLHALPLYH-CAQlDVFlgPYLYVGATNVILDA 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  677 AikrDVPQLFAFINKHQTNIVFL-PTAFIKMI----FSERELANsfpdgvkhLIAA--GEQLMISDLFQDvLRKR--GIH 747
Cdd:PRK08316   247 P---DPELILRTIEAERITSFFApPTVWISLLrhpdFDTRDLSS--------LRKGyyGASIMPVEVLKE-LRERlpGLR 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  748 LHNHYGPSETHVVSTyTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFS 827
Cdd:PRK08316   315 FYNCYGQTEIAPLAT-VLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  828 SDPFkpdvimyRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAyyCS 907
Cdd:PRK08316   394 GGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTA--VV 464

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1678550997  908 VQK----LNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKV 947
Cdd:PRK08316   465 VPKagatVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 2542-3019 9.36e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 126.85  E-value: 9.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2542 QAARTPKASA---LVSGDKtLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYP 2618
Cdd:PRK09088     4 HARLQPQRLAavdLALGRR-WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2619 KERKRYILSDSGTKLLMtineADLGVLA------DFEGEILTIESVEEDDKSPLPqmssAHHLAYIIYTSGTTGRPKGVM 2692
Cdd:PRK09088    83 ASELDALLQDAEPRLLL----GDDAVAAgrtdveDLAAFIASADALEPADTPSIP----PERVSLILFTSGTSGQPKGVM 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2693 VEHKGIANTlqwrrnAYAFNETDTILQLFSFSFD-------GFITSMFTPLLSGAKAVLLHEEEAKDILAikhQLSRQR- 2764
Cdd:PRK09088   155 LSERNLQQT------AHNFGVLGRVDAHSSFLCDapmfhiiGLITSVRPVLAVGGSILVSNGFEPKRTLG---RLGDPAl 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2765 -ITHMIIVPVLYRALLDvvQPE-DVKTLRVVT--LAGEA--ADRELIARSLAICPhteLANEYGPTEnsvATTVMrHMEK 2838
Cdd:PRK09088   226 gITHYFCVPQMAQAFRA--QPGfDAAALRHLTalFTGGAphAAEDILGWLDDGIP---MVDGFGMSE---AGTVF-GMSV 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2839 QAYV------SIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTqnpfkpEARMYRTGDAAR 2912
Cdd:PRK09088   297 DCDVirakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIAR 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2913 WMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNA--VRSELQNK 2990
Cdd:PRK09088   371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLerIRSHLSTR 450

                          490       500
                   ....*....|....*....|....*....
gi 1678550997 2991 LPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK09088   451 LAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK07529 PRK07529
AMP-binding domain protein; Validated
 1485-1983 9.43e-30

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 128.53  E-value: 9.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1485 FEETGYS---MNQTLHYALEQQAEKTPDQAAVIF--------EDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKR 1553
Cdd:PRK07529    13 IEAVPLAardLPASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPN 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1554 SPEMLLGIYGILKAGGAYlPIDPDYPEERISFLLEDSGTNIL---------------------------LLQSAGL-HVP 1605
Cdd:PRK07529    93 LPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLvtlgpfpgtdiwqkvaevlaalpelrtVVEVDLArYLP 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1606 EFTGEIVYLNQTNSGL-------------AHRLSNPNVdVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQ 1672
Cdd:PRK07529   172 GPKRLAVPLIRRKAHArildfdaelarqpGDRLFSGRP-IGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLG 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1673 LKHSDMIMHKTS-YSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIA---KAIEEQKITAMHFVPSMLHAFLEhikyrs 1748
Cdd:PRK07529   251 LGPGDTVFCGLPlFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVIAnfwKIVERYRINFLSGVPTVYAALLQ------ 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1749 VPIK---TNRLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAffdCPPHEKLERI-PIGKPV--HHVRLY 1822
Cdd:PRK07529   325 VPVDghdISSLRYALCGAAPLPVEVFRRFEAAT-GVRIVEGYGLTEATCVSS---VNPPDGERRIgSVGLRLpyQRVRVV 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1823 LLNQN---QRMLPVGCIGELYIAGAGVARGYL----NRPALTEERFLedpfypgermyKTGDVARWLPDGNVEFLGRTDD 1895
Cdd:PRK07529   401 ILDDAgryLRDCAVDEVGVLCIAGPNVFSGYLeaahNKGLWLEDGWL-----------NTGDLGRIDADGYFWLTGRAKD 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1896 QVkIR-GYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL-CAYVE---GLQRNE------VRAQL-ERLlpgyMVPAY 1963
Cdd:PRK07529   470 LI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQlkpGASATEaellafARDHIaERA----AVPKH 544

                          570       580
                   ....*....|....*....|
gi 1678550997 1964 MIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK07529   545 VRILDALPKTAVGKIFKPAL 564
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 1503-1983 1.03e-29

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 126.46  E-value: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1503 QAEKTPDQ-AAVIFEDGV-MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPE 1580
Cdd:PRK09088     4 HARLQPQRlAAVDLALGRrWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1581 ERISFLLEDSGTNILL----LQSAGLHVPEFTGEIVYLNQtnSGLAHRLSNPnvdvlPQSLAYVIYTSGSTGMPKGVEIE 1656
Cdd:PRK09088    84 SELDALLQDAEPRLLLgddaVAAGRTDVEDLAAFIASADA--LEPADTPSIP-----PERVSLILFTSGTSGQPKGVMLS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1657 HR----SAVNFlnSLQSRyqlkhsdmIMHKTSYSFDASIWELFwwpyaGASVYLLP---QGGEK------EPEVIAKAIE 1723
Cdd:PRK09088   157 ERnlqqTAHNF--GVLGR--------VDAHSSFLCDAPMFHII-----GLITSVRPvlaVGGSIlvsngfEPKRTLGRLG 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1724 EQKITAMHF--VPSMLHAFLEHIKYRsvPIKTNRLKRVFSGGeqlGTHLVSRFYELLPN-VSITNSYGPTEA-TVEAAFF 1799
Cdd:PRK09088   222 DPALGITHYfcVPQMAQAFRAQPGFD--AAALRHLTALFTGG---APHAAEDILGWLDDgIPMVDGFGMSEAgTVFGMSV 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1800 DCppheklERI-----PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyK 1874
Cdd:PRK09088   297 DC------DVIrakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWF------R 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1875 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYV--EG--LQRNEVR 1948
Cdd:PRK09088   365 TGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAqwGEVGYLAIVpaDGapLDLERIR 444

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997 1949 AQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK09088   445 SHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 477-952 1.30e-29

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 126.64  E-value: 1.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  477 PDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIM-MERSAAFITGVLGILkAGGAIVPVDPHYPADRIRYI 555
Cdd:PRK06188    26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLsLNRPEVLMAIGAAQL-AGLRRTALHPLGSLDDHAYV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 LHDCGCSHVVS------------QAHLPSSLEdnyIITH-----PEDIESKVDGSNIKSVNNAD---DLLYMIYTSGTTG 615
Cdd:PRK06188   105 LEDAGISTLIVdpapfveralalLARVPSLKH---VLTLgpvpdGVDLLAAAAKFGPAPLVAAAlppDIAGLAYTGGTTG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  616 KPKGVQFEHRNMANLLKFEYTHSGIDFEADVLqFATPSFDVCYQEIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTN 695
Cdd:PRK06188   182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFL-MCTPLSHAGGAFFLPTLLRGGTVIVLA---KFDPAEVLRAIEEQRIT 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  696 IVFL-PTafikMIFSERELansfPDGVKH------LIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTI--- 765
Cdd:PRK06188   258 ATFLvPT----MIYALLDH----PDLRTRdlssleTVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRkrd 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  766 HPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLAR 845
Cdd:PRK06188   330 HDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTGDVAR 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  846 RLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEH-ELCAYYCSVQKLNTIDLRSYMASE 923
Cdd:PRK06188   403 EDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgVPDEKWGEAvTAVVVLRPGAAVDAAELQAHVKER 482

                          490       500
                   ....*....|....*....|....*....
gi 1678550997  924 LPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK06188   483 KGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 2555-3016 1.42e-29

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: 125.63  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2555 GDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLL 2634
Cdd:cd05914      4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2635 MTINEADLgvladfegeiltiesveeddksplpqmssahhlAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNET 2714
Cdd:cd05914     84 FVSDEDDV---------------------------------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2715 DTILQLFSFSFD-GFITSMFTPLLSGAKAVLLHEEEAKDILAikhqLSRQRITHMIIVPVLY----RALLDVVQPED--- 2786
Cdd:cd05914    131 DKILSILPLHHIyPLTFTLLLPLLNGAHVVFLDKIPSAKIIA----LAFAQVTPTLGVPVPLviekIFKMDIIPKLTlkk 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2787 --------VKTLRVVTLAGEAAD-------RELIARSLAICPHTE---------LANEYGPTENS--VATTVmrhMEKQA 2840
Cdd:cd05914    207 fkfklakkINNRKIRKLAFKKVHeafggniKEFVIGGAKINPDVEeflrtigfpYTIGYGMTETApiISYSP---PNRIR 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2841 YVSIGQPIDGTQVLILNSNhqlqPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLE 2920
Cdd:cd05914    284 LGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAEGYLY 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2921 YLGRIDDQ-VKIRGYRVETKEIESVIRCIKGV---------KDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNK 2990
Cdd:cd05914    354 IRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVleslvvvqeKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVNQK 433

                          490       500
                   ....*....|....*....|....*..
gi 1678550997 2991 LPVFMHPA-FIEKLDSLPLSPNGKLDR 3016
Cdd:cd05914    434 VPNYKKISkVKIVKEEFEKTPKGKIKR 460
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 1636-1980 1.71e-29

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: 122.13  E-value: 1.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1636 SLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLlpQGGEKEP 1715
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG--QRKFNPK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1716 EVIAKaIEEQKITAMHFVPSMLHAFLEHikyrSVPIktNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVE 1795
Cdd:cd17633     79 SWIRK-INQYNATVIYLVPTMLQALART----LEPE--SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1796 AAFFD---CPPHEkleripIGKPVHHVRLYLLNQNQrmlpvGCIGELYIAGAGVARGYLNRPALTEERFledpfypgerm 1872
Cdd:cd17633    152 TYNFNqesRPPNS------VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW----------- 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1873 YKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV---EGLQRNEVRA 1949
Cdd:cd17633    210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALysgDKLTYKQLKR 289

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1678550997 1950 QLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd17633    290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 602-949 1.86e-29

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 122.77  E-value: 1.86e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDLLYMIYTSGTTGKPKGVQFEHRNMAN-------LLKFEythsgidfEADVLQFATPSFDV--CYQEIFSALLKGGTlh 672
Cdd:cd05917      2 DDVINIQFTSGTTGSPKGATLTHHNIVNngyfigeRLGLT--------EQDRLCIPVPLFHCfgSVLGVLACLTHGAT-- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  673 IVPEAIKRDVPQLFAFINKHQTNIVF-LPTAFIKMIFSERELANSFpDGVKHLIAAG----EQLMisdlfQDVLRKRGI- 746
Cdd:cd05917     72 MVFPSPSFDPLAVLEAIEKEKCTALHgVPTMFIAELEHPDFDKFDL-SSLRTGIMAGapcpPELM-----KRVIEVMNMk 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  747 HLHNHYGPSETHVVSTYTIhPGDPIPE-LPPIGKPIGCTDLYILNHQ-KQLQPCGVPGELYISGASVARGYVNHDKLTSD 824
Cdd:cd05917    146 DVTIAYGMTETSPVSTQTR-TDDSIEKrVNTVGRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  825 KFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVkIRG-YRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEhELC 902
Cdd:cd05917    225 AIDGDGW------LHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVgVPDERYGE-EVC 296

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997  903 AYycsVQ-----KLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd05917    297 AW---IRlkegaELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 2557-3016 2.15e-29

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: 127.22  E-value: 2.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:cd05968     90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 ----------IN---EADLGVLADFEGEILTIE---------------SVEEDDKSPLPQMSSAHHL--AYIIYTSGTTG 2686
Cdd:cd05968    170 adgftrrgreVNlkeEADKACAQCPTVEKVVVVrhlgndftpakgrdlSYDEEKETAGDGAERTESEdpLMIIYTSGTTG 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2687 RPKGVMVEHKGIAntLQWRRNAY-AFN--ETDTilqLFSFSFDGFITS---MFTPLLSGAKAVLLheEEAKDILA---IK 2757
Cdd:cd05968    250 KPKGTVHVHAGFP--LKAAQDMYfQFDlkPGDL---LTWFTDLGWMMGpwlIFGGLILGATMVLY--DGAPDHPKadrLW 322

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2758 HQLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAADRE---------LIARslaiCPhteLANEYGPT 2824
Cdd:cd05968    323 RMVEDHEITHLGLSPTLIRALKprgdAPVNAHDLSSLRVLGSTGEPWNPEpwnwlfetvGKGR----NP---IINYSGGT 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2825 ENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSnhQLQPI-GVAGELCIAG--TGLARGYvnlpelteraftqnpFKPE 2901
Cdd:cd05968    396 EISGGILGNVLIKPIKPSSFNGPVPGMKADVLDE--SGKPArPEVGELVLLApwPGMTRGF---------------WRDE 458

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2902 ARMYRT-----------GDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSA 2970
Cdd:cd05968    459 DRYLETywsrfdnvwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVC 538

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2971 YVVTKPGLS-TNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd05968    539 FVVLKPGVTpTEALAEELmervADELGKPLSPERILFVKDLPKTRNAKVMR 589
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 481-952 2.61e-29

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: 124.51  E-value: 2.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  481 AVIDQACSLTYRELNKAANRLARHLRMKGVVRQ-EPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDC 559
Cdd:cd05958      3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  560 GCSHVVsqahlpsslednyiITHpedieskvdgsnikSVNNADDLLYMIYTSGTTGKPKGVQFEHRNManLLKFE-YTHS 638
Cdd:cd05958     83 RITVAL--------------CAH--------------ALTASDDICILAFTSGTTGAPKATMHFHRDP--LASADrYAVN 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  639 GIDFEADVLQFATPsfdvcyqEIFSALLKGGTL---HIVPEAI----KRDVPQLFAFINKHQTNIVF-LPTAFIKMI--- 707
Cdd:cd05958    133 VLRLREDDRFVGSP-------PLAFTFGLGGVLlfpFGVGASGvlleEATPDLLLSAIARYKPTVLFtAPTAYRAMLahp 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  708 -FSERELAnsfpdGVKHLIAAGEQL--MISDLFQDVLrkrGIHLHNHYGPSET-HVVSTYTihPGDPIPElpPIGKPIGC 783
Cdd:cd05958    206 dAAGPDLS-----SLRKCVSAGEALpaALHRAWKEAT---GIPIIDGIGSTEMfHIFISAR--PGDARPG--ATGKPVPG 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 TDLYILNHQKQLQPCGVPGELYISGASVARGyvNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVK 863
Cdd:cd05958    274 YEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY--LADKRQRTYVQGG-------WNITGDTYSRDPDGYFRHQGRSDDMIV 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  864 IRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQKLNTI-------DLRSYMASELPEYMIPAKWIWV 936
Cdd:cd05958    345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFV--VLRPGVIpgpvlarELQDHAKAHIAPYKYPRAIEFV 422

                          490
                   ....*....|....*.
gi 1678550997  937 DSIPLTPNGKVDRAAL 952
Cdd:cd05958    423 TELPRTATGKLQRFAL 438
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 2533-3019 2.76e-29

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 126.32  E-value: 2.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVS------GDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKA 2606
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2607 GGCYVPIDPEYPKERKRYILSDSGTKLLMTINE-----------------ADLG--VLADFEG----EILTIESVEEDDK 2663
Cdd:PRK13295   104 GAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaamarrlrpelPALRhvVVVGGDGadsfEALLITPAWEQEP 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2664 SpLPQMSSAHH-----LAYIIYTSGTTGRPKGVMveHKgiANTLQWRRNAYA----FNETDTILQLFSFSF-DGFITSMF 2733
Cdd:PRK13295   184 D-APAILARLRpgpddVTQLIYTSGTTGEPKGVM--HT--ANTLMANIVPYAerlgLGADDVILMASPMAHqTGFMYGLM 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2734 TPLLSGAKAVLLHEEEAKDILAIkhqLSRQRITH-MIIVPVLYRaLLDVVQ--PEDVKTLRVVTLAGEAADRELIARSLA 2810
Cdd:PRK13295   259 MPVMLGATAVLQDIWDPARAAEL---IRTEGVTFtMASTPFLTD-LTRAVKesGRPVSSLRTFLCAGAPIPGALVERARA 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2811 ICpHTELANEYGPTEN-SVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELT 2889
Cdd:PRK13295   335 AL-GAKIVSAWGMTENgAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN 413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2890 ERAFTQnpfkpearMYRTGDAARWMADGTLEYLGRIDDqVKIRG-YRVETKEIESVIRCIKGVKDAAVVAHVTASGQTEL 2968
Cdd:PRK13295   414 GTDADG--------WFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERA 484

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2969 SAYVVTKPGLS---TNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK13295   485 CAFVVPRPGQSldfEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1495-1980 3.22e-29

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 126.27  E-value: 3.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI 1574
Cdd:PRK05605    33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1575 DPDYPEERISFLLEDSGTNIL--------------------------------LLQSAGLHVP---------EFTGEI-- 1611
Cdd:PRK05605   113 NPLYTAHELEHPFEDHGARVAivwdkvaptverlrrttpletivsvnmiaampLLQRLALRLPipalrkaraALTGPApg 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1612 -----VYLNQTNSGLAHRLSNPNVDvlPQSLAYVIYTSGSTGMPKGVEIEHRSAvnFLNSLQSRY---QLKHSDMIMHKT 1683
Cdd:PRK05605   193 tvpweTLVDAAIGGDGSDVSHPRPT--PDDVALILYTSGTTGKPKGAQLTHRNL--FANAAQGKAwvpGLGDGPERVLAA 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1684 SYSFDA---SIWELFWwPYAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRlkRVF 1760
Cdd:PRK05605   269 LPMFHAyglTLCLTLA-VSIGGELVLLPA---PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVR--NAF 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1761 SGGEQLGTHLVSRfYELLPNVSITNSYGPTEATVEAAFFDCPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELY 1840
Cdd:PRK05605   343 SGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEGELL 421

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1841 IAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 1920
Cdd:PRK05605   422 VRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVE 494

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1921 EAAVT--VRTDSGEPELCAYV--EG--LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:PRK05605   495 DAAVVglPREDGSEEVVAAVVlePGaaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1520-1983 3.94e-29

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


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 123.78  E-value: 3.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQS 1599
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 AGLHVpeftgeivylnqtnsglahrlsnpnvdvLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMI 1679
Cdd:cd05973     81 ANRHK----------------------------LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1680 MHKTSYSFDASIWELFWWPYAGASVYLLPQGGeKEPEVIAKAIEEQKITAMHFVPSMlhaflehikYR-------SVPIK 1752
Cdd:cd05973    133 WNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTA---------YRllmaagaEVPAR 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1753 -TNRLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAFFDCPPHEkLERIPIGKPVHHVRLYLLNQNQRML 1831
Cdd:cd05973    203 pKGRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHP-VHAGSAGRAMPGWRVAVLDDDGDEL 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1832 PVGCIGELYIAGAGVA----RGYLNrpalteerfLEDPFYPGeRMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 1907
Cdd:cd05973    281 GPGEPGRLAIDIANSPlmwfRGYQL---------PDTPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1908 EIEAALRSIEGVREAAVTVRTDSGEPELC-AYV---EGLQRN-EVRAQLERL----LPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:cd05973    351 DVESALIEHPAVAEAAVIGVPDPERTEVVkAFVvlrGGHEGTpALADELQLHvkkrLSAHAYPRTIHFVDELPKTPSGKI 430


                   ....*
gi 1678550997 1979 DRNAL 1983
Cdd:cd05973    431 QRFLL 435
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 458-947 6.39e-29

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 125.07  E-value: 6.39e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  458 QTPVYETIhamfEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMK-GVVRQEPVAIMMERSAAFITGVLGILKA 536
Cdd:PRK08314     9 ETSLFHNL----EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  537 GGAIVPVDPHYPADRIRYILHDCGCS----------------------HVVSqAHLPSSLEDNYIITHPEDIESKVDGSN 594
Cdd:PRK08314    85 NAVVVPVNPMNREEELAHYVTDSGARvaivgselapkvapavgnlrlrHVIV-AQYSDYLPAEPEIAVPAWLRAEPPLQA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  595 IKSVN-------------------NADDLLYMIYTSGTTGKPKGVQFEHRN-MANLLKFeYTHSGIDFEADVLQFAtPSF 654
Cdd:PRK08314   164 LAPGGvvawkealaaglappphtaGPDDLAVLPYTSGTTGVPKGCMHTHRTvMANAVGS-VLWSNSTPESVVLAVL-PLF 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  655 DVCYQE--IFSALLKGGTLHIVPEAIKRDVPQLfafINKHQ----TNIvflPTAFIKMI----FSERELAN--------- 715
Cdd:PRK08314   242 HVTGMVhsMNAPIYAGATVVLMPRWDREAAARL---IERYRvthwTNI---PTMVVDFLaspgLAERDLSSlryigggga 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 SFPDGVkhliaaGEQLMisDLFqdvlrkrGIHLHNHYGPSEThvVSTYTIHPGDPiPELPPIGKPIGCTDLYILNHQ--K 793
Cdd:PRK08314   316 AMPEAV------AERLK--ELT-------GLDYVEGYGLTET--MAQTHSNPPDR-PKLQCLGIPTFGVDARVIDPEtlE 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  794 QLqPCGVPGELYISGASVARGYVNHDKLTSDKF---SSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIE 870
Cdd:PRK08314   378 EL-PPGEVGEIVVHGPQVFKGYWNRPEATAEAFieiDGKRF------FRTGDLGRMDEEGYFFITDRLKRMINASGFKVW 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  871 PQEIEVTLMNHPDISEAAILIWQDQ-NGEhELCAYYC-------SVQKLNTID-LRSYMASelpeYMIPAKWIWVDSIPL 941
Cdd:PRK08314   451 PAEVENLLYKHPAIQEACVIATPDPrRGE-TVKAVVVlrpeargKTTEEEIIAwAREHMAA----YKYPRIVEFVDSLPK 525


                   ....*.
gi 1678550997  942 TPNGKV 947
Cdd:PRK08314   526 SGSGKI 531
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 2540-3013 8.74e-29

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: 123.56  E-value: 8.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2540 EQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPK 2619
Cdd:cd12118     11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2620 ERKRYILSDSGTKLLMTINEadlgvladFEGEILtiesVEEDDKSPLPQMSSAHHLAYII-YTSGTTGRPKGVMVEHKG- 2697
Cdd:cd12118     91 EEIAFILRHSEAKVLFVDRE--------FEYEDL----LAEGDPDFEWIPPADEWDPIALnYTSGTTGRPKGVVYHHRGa 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2698 ----IANTLQWR---RNAYAfnetdTILQLFSFSFDGFITSMFTpllSGAKAVLLHEEEAKDILAIkhqLSRQRITHMII 2770
Cdd:cd12118    159 ylnaLANILEWEmkqHPVYL-----WTLPMFHCNGWCFPWTVAA---VGGTNVCLRKVDAKAIYDL---IEKHKVTHFCG 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2771 VPVLYRALLDvVQPEDVKTL--RV-VTLAGEAADRELIAR--SLAICP-HTelaneYGPTENSVATTVMR--------HM 2836
Cdd:cd12118    228 APTVLNMLAN-APPSDARPLphRVhVMTAGAPPPAAVLAKmeELGFDVtHV-----YGLTETYGPATVCAwkpewdelPT 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2837 EKQAYVSIGQPI-----DGTQVLilnSNHQLQPI---GV-AGELCIAGTGLARGYVNLPELTERAFtqnpfkpEARMYRT 2907
Cdd:cd12118    302 EERARLKARQGVryvglEEVDVL---DPETMKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAF-------RGGWFHS 371

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2908 GDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAvrSEL 2987
Cdd:cd12118    372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE--EEI 449

                          490       500       510
                   ....*....|....*....|....*....|
gi 1678550997 2988 Q----NKLPVFMHPAFIEKLDsLPLSPNGK 3013
Cdd:cd12118    450 IafcrEHLAGFMVPKTVVFGE-LPKTSTGK 478
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2532-3019 9.04e-29

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 123.82  E-value: 9.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2532 VQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKAGGCY 2610
Cdd:PRK06839     1 MQGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2611 VPIDPEYPKERKRYILSDSGTKLLMTINE-----ADLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHLAYII-YTSGT 2684
Cdd:PRK06839    81 VPLNIRLTENELIFQLKDSGTTVLFVEKTfqnmaLSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIIcYTSGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2685 TGRPKG-VMVEHKGIANTLQwrrNAYAFNETD-----TILQLFSFSFDGFITsmFTPLLSGAKAVLLHEEEAKDILAIkh 2758
Cdd:PRK06839   161 TGKPKGaVLTQENMFWNALN---NTFAIDLTMhdrsiVLLPLFHIGGIGLFA--FPTLFAGGVIIVPRKFEPTKALSM-- 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2759 qLSRQRITHMIIVPVLYRALLDVVQPE--DVKTLRVVTLAGEAADRELI----ARSLaicphtELANEYGPTENSvaTTV 2832
Cdd:PRK06839   234 -IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMrefiDRGF------LFGQGFGMTETS--PTV 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2833 MRHMEKQAYV---SIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmyRTGD 2909
Cdd:PRK06839   305 FMLSEEDARRkvgSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGD 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2910 AARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSEL 2987
Cdd:PRK06839   378 LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHC 457

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1678550997 2988 QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06839   458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1639-1979 1.52e-28

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 120.56  E-value: 1.52e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1639 YVIYTSGSTGMPKGV-------------------------EIEHRSAVNflNSLQSRYQLKHsdmIMHKTSysfdasIWE 1693
Cdd:cd05924      7 YILYTGGTTGMPKGVmwrqedifrmlmggadfgtgeftpsEDAHKAAAA--AAGTVMFPAPP---LMHGTG------SWT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1694 LFWWPYAGASVyLLPqGGEKEPEVIAKAIEEQKITAMHFV-PSMLHAFLEHIK-YRSVPIKTnrLKRVFSGGEQLGTHLV 1771
Cdd:cd05924     76 AFGGLLGGQTV-VLP-DDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRdAGPYDLSS--LFAISSGGALLSPEVK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1772 SRFYELLPNVSITNSYGPTEA-TVEAAFFDCPPHEKLERIPIGKpvhhvRLYLLNQNQRMLPVGCIGELYIAGAG-VARG 1849
Cdd:cd05924    152 QGLLELVPNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP-----DTVVLDDDGRVVPPGSGGVGWIARRGhIPLG 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1850 YLNRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD 1929
Cdd:cd05924    227 YYGDEAKTAETFPE---VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPD 303

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1930 S--GEpELCAYVE-----GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 1979
Cdd:cd05924    304 ErwGQ-EVVAVVQlregaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 2540-3014 1.56e-28

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 123.92  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2540 EQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYP 2618
Cdd:PRK08314    17 EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2619 KERKRYILSDSGTKLLMTINE---------ADLG----VLADF--------------------------EGEILTIESVE 2659
Cdd:PRK08314    97 EEELAHYVTDSGARVAIVGSElapkvapavGNLRlrhvIVAQYsdylpaepeiavpawlraepplqalaPGGVVAWKEAL 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2660 EDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGI-ANTL---QWrRNAYAFNETDTILQLFSFSfdGFITSMFTP 2735
Cdd:PRK08314   177 AAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmANAVgsvLW-SNSTPESVVLAVLPLFHVT--GMVHSMNAP 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2736 LLSGAKAVLL---HEEEAKDIlaikhqLSRQRITHMIIVPVLyraLLDV-----VQPEDVKTLRVVTlAGEAADRELIAR 2807
Cdd:PRK08314   254 IYAGATVVLMprwDREAAARL------IERYRVTHWTNIPTM---VVDFlaspgLAERDLSSLRYIG-GGGAAMPEAVAE 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2808 SLaicphTELAN----E-YGPTEnSVATTVMRHMEKQAYVSIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARG 2881
Cdd:PRK08314   324 RL-----KELTGldyvEgYGLTE-TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKG 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2882 YVNLPELTERAFTQNPFKpeaRMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESV------IR--CIKGVKD 2953
Cdd:PRK08314   398 YWNRPEATAEAFIEIDGK---RFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLlykhpaIQeaCVIATPD 474

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2954 AAVvahvtasGQTeLSAYVVTKPGLSTNAVRSELQN----KLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:PRK08314   475 PRR-------GET-VKAVVVLRPEARGKTTEEEIIAwareHMAAYKYPRIVEFVDSLPKSGSGKI 531
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 2530-3019 1.84e-28

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 123.99  E-value: 1.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2530 YGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGC 2609
Cdd:PRK06710    21 YDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGI 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2610 YVPIDPEYPKERKRYILSDSGTKLLM----------------TINEADLGVLADF------------------------E 2649
Cdd:PRK06710   101 VVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsatKIEHVIVTRIADFlpfpknllypfvqkkqsnlvvkvsE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2650 GEILTI-ESVEEDDKSPLPQMSSAHH-LAYIIYTSGTTGRPKGVMVEHKG-IANTL---QWRRNAYAFNETDTILQLFsF 2723
Cdd:PRK06710   181 SETIHLwNSVEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNlVSNTLmgvQWLYNCKEGEEVVLGVLPF-F 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2724 SFDGFITSMFTPLLSGAKAVLLHEEEAKDIL-AIKhqlsRQRITHMIIVPVLYRALLD--VVQPEDVKTLRVVtLAGEAA 2800
Cdd:PRK06710   260 HVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFeAIK----KHKVTLFPGAPTIYIALLNspLLKEYDISSIRAC-ISGSAP 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2801 DRELIARSLAICPHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLI--LNSNHQLQPiGVAGELCIAGTGL 2878
Cdd:PRK06710   335 LPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMImsLETGEALPP-GEIGEIVVKGPQI 413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2879 ARGYVNLPELTErAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVA 2958
Cdd:PRK06710   414 MKGYWNKPEETA-AVLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 2959 HVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06710   487 VPDPYRGETVKAFVVLKEGteCSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 1520-1983 1.99e-28

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: 121.82  E-value: 1.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGV-KPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPdypeerisflledsgtnilLLQ 1598
Cdd:cd05958     11 WTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------------LLR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1599 SaglhvPEFTGEIVYLNQTNSGLAHRLSNPNvDVlpqslAYVIYTSGSTGMPKGVEIEHRS--------AVNFLnslqsr 1670
Cdd:cd05958     72 P-----KELAYILDKARITVALCAHALTASD-DI-----CILAFTSGTTGAPKATMHFHRDplasadryAVNVL------ 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1671 yQLKHSDMIMH--KTSYSFDASIWELFWWpYAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRS 1748
Cdd:cd05958    135 -RLREDDRFVGspPLAFTFGLGGVLLFPF-GVGASGVLLEE---ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1749 VPIKTnrLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEAT---VEAAFFDCPPHEkleripIGKPVHHVRLYLLN 1825
Cdd:cd05958    210 PDLSS--LRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEMFhifISARPGDARPGA------TGKPVPGYEAKVVD 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1826 QNQRMLPVGCIGELYIAGAGVARGylnrpaLTEERflEDPFYPGERMYkTGDVARWLPDGNVEFLGRTDDQVKIRGYRIE 1905
Cdd:cd05958    281 DEGNPVPDGTIGRLAVRGPTGCRY------LADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1906 PGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---------EGLQRnEVRAQLERLLPGYMVPAYMIEMEQWPVTPS 1975
Cdd:cd05958    352 PPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVvlrpgvipgPVLAR-ELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430


                   ....*...
gi 1678550997 1976 GKLDRNAL 1983
Cdd:cd05958    431 GKLQRFAL 438
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 2088-2396 5.44e-28

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: 119.85  E-value: 5.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2088 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEgklNPERMDR---AFQELIKRHESLRTSF-----EQdeggdPVQRIHD 2159
Cdd:cd19544      2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAIlweglSE-----PVQVVWR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2160 EVPFTLQTTVL-GARTEQEAAAAFIKP----FDLSQAPLFRAQIVKVSD-ERHLLLVDMHHIISDGVSVNILIQEFGELY 2233
Cdd:cd19544     74 QAELPVEELTLdPGDDALAQLRARFDPrryrLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAIL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2234 NNR--KLPALrIQYKDY-AVWQEGFKTGDAykmqEAYWLKQL----EGELP--VLDLPADHARPpvrsfagDKVSFTLEP 2304
Cdd:cd19544    154 AGRaaALPPP-VPYRNFvAQARLGASQAEH----EAFFREMLgdvdEPTAPfgLLDVQGDGSDI-------TEARLALDA 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2305 EVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPeGGKPFVQY 2382
Cdd:cd19544    222 ELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRL-GGRSVREA 300

                          330
                   ....*....|....*.
gi 1678550997 2383 LQEVRE--TALEAFEH 2396
Cdd:cd19544    301 VRQTHArlAELLRHEH 316
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 1494-1983 9.04e-28

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 121.68  E-value: 9.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLP 1573
Cdd:PRK06710    24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1574 IDPDYPEERISFLLEDSGTNILL-----------LQSAGL--HVP--------EFTGEIVY--LNQTNSGLAHRLS---- 1626
Cdd:PRK06710   104 TNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKieHVIvtriadflPFPKNLLYpfVQKKQSNLVVKVSeset 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1627 -----------NPNVDVL--PQS-LAYVIYTSGSTGMPKGVEIEHRSAV-NFLNSLQSRYQLKHSDMI---------MHK 1682
Cdd:PRK06710   184 ihlwnsvekevNTGVEVPcdPENdLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVvlgvlpffhVYG 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1683 TSYSFDASIWElfwwpyaGASVYLLPQGGEKepeVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSG 1762
Cdd:PRK06710   264 MTAVMNLSIMQ-------GYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISS--IRACISG 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1763 GEQLGTHLVSRFyELLPNVSITNSYGPTEAT--VEAAFFdcppHEKleRIP--IGKPVHHVRLYLLN-QNQRMLPVGCIG 1837
Cdd:PRK06710   332 SAPLPVEVQEKF-ETVTGGKLVEGYGLTESSpvTHSNFL----WEK--RVPgsIGVPWPDTEAMIMSlETGEALPPGEIG 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1838 ELYIAGAGVARGYLNRPALTEErFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 1917
Cdd:PRK06710   405 EIVVKGPQIMKGYWNKPEETAA-VLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1918 GVREAAVTVRTDSGEPELCAYVEGLQRNEVRAQLE------RLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK06710   478 KVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEElnqfarKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 473-949 1.20e-27

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


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 120.42  E-value: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQA--CSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPAD 550
Cdd:cd05904     15 ASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  551 RIRYILHDCGCSHVVSQA---------HLPSSLEDNYII--THPEDIESKVDGSNIKSVN-NADDLLYMIYTSGTTGKPK 618
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAelaeklaslALPVVLLDSAEFdsLSFSDLLFEADEAEPPVVViKQDDVAALLYSSGTTGRSK 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  619 GVQFEHRNM-ANLLKFE-YTHSGIDFEaDVLQFATPSFDVcY--QEIFSALLK-GGTLHIVPeaiKRDVPQLFAFINKHQ 693
Cdd:cd05904    175 GVMLTHRNLiAMVAQFVaGEGSNSDSE-DVFLCVLPMFHI-YglSSFALGLLRlGATVVVMP---RFDLEELLAAIERYK 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  694 -TNIVFLPTAFIKMifserelansfpdgVKHLIAAGEQL----MIS--------DLFQDVLRK-RGIHLHNHYGPSETHV 759
Cdd:cd05904    250 vTHLPVVPPIVLAL--------------VKSPIVDKYDLsslrQIMsgaaplgkELIEAFRAKfPNVDLGQGYGMTESTG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  760 VSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQK-QLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimY 838
Cdd:cd05904    316 VVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETgESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW------L 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  839 RTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsVQK----LNTI 914
Cdd:cd05904    390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV--VRKpgssLTED 467

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1678550997  915 DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd05904    468 EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILR 502
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 2532-3020 1.32e-27

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 120.53  E-value: 1.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2532 VQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYV 2611
Cdd:PRK07470     6 VMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPEYPKERKRYILSDSGTKLLM-----------------------TINEADLG-----VLADFEGEILTIESVEEDDk 2663
Cdd:PRK07470    86 PTNFRQTPDEVAYLAEASGARAMIchadfpehaaavraaspdlthvvAIGGARAGldyeaLVARHLGARVANAAVDHDD- 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2664 sPLpqmssahhlaYIIYTSGTTGRPKGVMVEHKGIANTLQwrrNAYA-----FNETDTILQLFSFSfDGFITSMFTPLLS 2738
Cdd:PRK07470   165 -PC----------WFFFTSGTTGRPKAAVLTHGQMAFVIT---NHLAdlmpgTTEQDASLVVAPLS-HGAGIHQLCQVAR 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2739 GAKAVLLHEEEAkDILAIKHQLSRQRITHMIIVPVLYRALLD--VVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTe 2816
Cdd:PRK07470   230 GAATVLLPSERF-DPAEVWALVERHRVTNLFTVPTILKMLVEhpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2817 LANEYGPTENSVATTV----MRHMEKQAYVSIGQ---PIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELT 2889
Cdd:PRK07470   308 LVQYFGLGEVTGNITVlppaLHDAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEAN 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2890 ERAFTQNPFkpearmyRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELS 2969
Cdd:PRK07470   388 AKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLG-VPDPVWGEVG 459

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2970 -AYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGK----------LDRGALP 3020
Cdd:PRK07470   460 vAVCVARDGapVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKitkkmvreelEERGLLD 523
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 2530-3016 1.33e-27

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 121.26  E-value: 1.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2530 YGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGC 2609
Cdd:PRK05605    29 YGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2610 YVPIDPEYPKERKRYILSDSGTKLLMTINE-ADL--GVLADFEGEilTIESVEEDDKSPLPQ------------------ 2668
Cdd:PRK05605   109 VVEHNPLYTAHELEHPFEDHGARVAIVWDKvAPTveRLRRTTPLE--TIVSVNMIAAMPLLQrlalrlpipalrkaraal 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2669 -------------MSSA---------------HHLAYIIYTSGTTGRPKGVMVEHKGI-ANTLQ---W-------RRNAY 2709
Cdd:PRK05605   187 tgpapgtvpwetlVDAAiggdgsdvshprptpDDVALILYTSGTTGKPKGAQLTHRNLfANAAQgkaWvpglgdgPERVL 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2710 AfnetdtILQLFSfSFDGFITSMFTPLLsGAKAVLLHEEEAKDILAIkhqLSRQRITHMIIVPVLYRALLDVVQPEDVkt 2789
Cdd:PRK05605   267 A------ALPMFH-AYGLTLCLTLAVSI-GGELVLLPAPDIDLILDA---MKKHPPTWLPGVPPLYEKIAEAAEERGV-- 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2790 lrvvTLAGEaadRELIARSLAICPHT----------ELANEYGPTENS--VATTVMRHMEKQAYVSIgqPIDGTQVLILN 2857
Cdd:PRK05605   334 ----DLSGV---RNAFSGAMALPVSTvelwekltggLLVEGYGLTETSpiIVGNPMSDDRRPGYVGV--PFPDTEVRIVD 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2858 SNH--QLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYR 2935
Cdd:PRK05605   405 PEDpdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFN 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2936 VETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGK 3013
Cdd:PRK05605   478 VYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGaaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGK 557


                   ...
gi 1678550997 3014 LDR 3016
Cdd:PRK05605   558 VRR 560
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 2533-3019 1.39e-27

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 121.08  E-value: 1.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKAGGCYV 2611
Cdd:PRK12492    24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPEYPKERKRYILSDSGTKLLMTINEadLG-----VLADFEGEILtIESVEEDDKSPL------------PQMSSAHH 2674
Cdd:PRK12492   104 NTNPLYTAREMRHQFKDSGARALVYLNM--FGklvqeVLPDTGIEYL-IEAKMGDLLPAAkgwlvntvvdkvKKMVPAYH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 L----------------------------AYIIYTSGTTGRPKGVMVEHKG-IANTLQWRRNAYAFNETD---------- 2715
Cdd:PRK12492   181 LpqavpfkqalrqgrglslkpvpvglddiAVLQYTGGTTGLAKGAMLTHGNlVANMLQVRACLSQLGPDGqplmkegqev 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2716 TILQLFSFSFDGFITSMFTPLLSGAKAVLLheEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDvvQPE----DVKTLR 2791
Cdd:PRK12492   261 MIAPLPLYHIYAFTANCMCMMVSGNHNVLI--TNPRDIPGFIKELGKWRFSALLGLNTLFVALMD--HPGfkdlDFSALK 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2792 VVTLAGEAADRELIAR--SLAICPHTElanEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAG 2869
Cdd:PRK12492   337 LTNSGGTALVKATAERweQLTGCTIVE---GYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERG 413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2870 ELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIK 2949
Cdd:PRK12492   414 ELCIKGPQVMKGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2950 GVKDAAVVAHVTASGQTELSAYVVTK-PGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK12492   488 KVANCAAIGVPDERSGEAVKLFVVARdPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 1513-1980 1.56e-27

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: 119.47  E-value: 1.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1513 VIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGT 1592
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1593 NILllqsaglhvpeFTGEivylnqtnsglahrlsnpnvdvlPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQ 1672
Cdd:cd05914     81 KAI-----------FVSD-----------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1673 LKHSDMIMHKTSYSfdaSIWEL---FWWP-YAGASVYLLpqggEKEPEVIAKAIEEQKITAMHFVPSMLHafLEHI---- 1744
Cdd:cd05914    127 LGKGDKILSILPLH---HIYPLtftLLLPlLNGAHVVFL----DKIPSAKIIALAFAQVTPTLGVPVPLV--IEKIfkmd 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1745 ----------KYR-SVPIKTN----------------RLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTEaTVEAA 1797
Cdd:cd05914    198 iipkltlkkfKFKlAKKINNRkirklafkkvheafggNIKEFVIGGAKINPDVEEFLRTI--GFPYTIGYGMTE-TAPII 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1798 FFDCPPHEKLERipIGKPVHHVRLYLLNQNqrmlPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGD 1877
Cdd:cd05914    275 SYSPPNRIRLGS--AGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGD 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1878 VARWLPDGNVEFLGRTDDQ-VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSG------EPELCAYVEGLQRN----- 1945
Cdd:cd05914    343 LGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLvalayiDPDFLDVKALKQRNiidai 422

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1678550997 1946 --EVRAQLERLLPGY-MVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd05914    423 kwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 488-946 2.18e-27

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 119.62  E-value: 2.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQ 567
Cdd:PRK08276    11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 A-----------HLPSSLEDNYIITHP----EDIESKVDG---SNIKSVNNADDllyMIYTSGTTGKPKGV--QFEHRN- 626
Cdd:PRK08276    91 AaladtaaelaaELPAGVPLLLVVAGPvpgfRSYEEALAAqpdTPIADETAGAD---MLYSSGTTGRPKGIkrPLPGLDp 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 ----MANLLKFEYTHSGID----------FEADVLQFATpsfdvcyqeifSALLKGGTLHIVPeaiKRDVPQLFAFINKH 692
Cdd:PRK08276   168 deapGMMLALLGFGMYGGPdsvylspaplYHTAPLRFGM-----------SALALGGTVVVME---KFDAEEALALIERY 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  693 Q-TNIVFLPTAFIKMIFSERELANSFpD--GVKHLIAAG-------EQLMIsDLFQDVlrkrgihLHNHYGPSETHVVST 762
Cdd:PRK08276   234 RvTHSQLVPTMFVRMLKLPEEVRARY-DvsSLRVAIHAAapcpvevKRAMI-DWWGPI-------IHEYYASSEGGGVTV 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  763 YT-----IHPGDpipelppIGKPIGCTdLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSsdpfkpDVIM 837
Cdd:PRK08276   305 ITsedwlAHPGS-------VGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGW 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  838 YRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEhELCAYycsVQKLNTIDL 916
Cdd:PRK08276   371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGE-RVKAV---VQPADGADA 446

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1678550997  917 RSYMASELPE--------YMIPAKWIWVDSIPLTPNGK 946
Cdd:PRK08276   447 GDALAAELIAwlrgrlahYKCPRSIDFEDELPRTPTGK 484
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 2678-3014 2.52e-27

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: 116.06  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHK-GIANTLQWRRNAyAFNETDT--ILQLFSFSFdGFITSMFTPLLSGAKAVllhEEEAKDIL 2754
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRqTLRAAAAWADCA-DLTEDDRylIINPFFHTF-GYKAGIVACLLTGATVV---PVAVFDVD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2755 AIKHQLSRQRITHMIIVPVLYRALLDVVQPE--DVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVAtTV 2832
Cdd:cd17638     80 AILEAIERERITVLPGPPTLFQSLLDHPGRKkfDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA-TM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2833 MRHMEKQAYVS--IGQPIDGTQVlilnsnhqlqPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDA 2910
Cdd:cd17638    159 CRPGDDAETVAttCGRACPGFEV----------RIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGW------LHTGDV 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2911 ARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELS-AYVVTKPG--LSTNAVRSEL 2987
Cdd:cd17638    223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG-VPDERMGEVGkAFVVARPGvtLTEEDVIAWC 301

                          330       340
                   ....*....|....*....|....*..
gi 1678550997 2988 QNKLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:cd17638    302 RERLANYKVPRFVRFLDELPRNASGKV 328
PRK13382 PRK13382
bile acid CoA ligase;
2534-3022 3.18e-27

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 119.86  E-value: 3.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMM--HRSFsmIASILGVWKAGGCYV 2611
Cdd:PRK13382    44 GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCrnHRGF--VEALLAANRIGADIL 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPEYPKERKRYILSDSGTKLLMTINEADLGVLADFEGEILTIESV---EEDDKSPLPQMSSAH----------HLAYI 2678
Cdd:PRK13382   122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIVawtDEDHDLTVEVLIAAHagqrpeptgrKGRVI 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2679 IYTSGTTGRPKGVMVEHKGIANTLQ-------WRrnayafNETDTILQLFSFSFDGFITSMFTPLLSgAKAVLLHEEEAK 2751
Cdd:PRK13382   202 LLTSGTTGTPKGARRSGPGGIGTLKaildrtpWR------AEEPTVIVAPMFHAWGFSQLVLAASLA-CTIVTRRRFDPE 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2752 DILAIkhqLSRQRITHMIIVPVLYRALLDVVQ----PEDVKTLRVVTLAGEAAdRELIARSLAICPHTELANEYGPTENS 2827
Cdd:PRK13382   275 ATLDL---IDRHRATGLAVVPVMFDRIMDLPAevrnRYSGRSLRFAAASGSRM-RPDVVIAFMDQFGDVIYNNYNATEAG 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2828 VATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNlpeLTERAFTQNpfkpearMYRT 2907
Cdd:PRK13382   351 MIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTS---GSTKDFHDG-------FMAS 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2908 GDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTAS--GQtELSAYVVTKPGLST--NAV 2983
Cdd:PRK13382   421 GDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIG-VDDEqyGQ-RLAAFVVLKPGASAtpETL 498

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1678550997 2984 RSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKP 3022
Cdd:PRK13382   499 KQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 2535-3019 4.28e-27

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 119.56  E-value: 4.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAarTPKASALV--SGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWKAGGCYV 2611
Cdd:PLN02574    43 VSFIFSHHN--HNGDTALIdsSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPEYPKERKRYILSDSGTKLLMTINE-----ADLGVLAdfegeILTIESVEEDDKSP---------------LPQ-MS 2670
Cdd:PLN02574   121 TMNPSSSLGEIKKRVVDCSVGLAFTSPEnveklSPLGVPV-----IGVPENYDFDSKRIefpkfyelikedfdfVPKpVI 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2671 SAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQ----WRRNAYAFNETDTILQLFSFSFDGFITSMF-TPLLS-GAKAVL 2744
Cdd:PLN02574   196 KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrFEASQYEYPGSDNVYLAALPMFHIYGLSLFvVGLLSlGSTIVV 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2745 LHEEEAKDILAIKHqlsRQRITHMIIVPVLYRALLDVVQP---EDVKTLRVVTLAGEAADRELIARSLAICPHTELANEY 2821
Cdd:PLN02574   276 MRRFDASDMVKVID---RFKVTHFPVVPPILMALTKKAKGvcgEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGY 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2822 GPTENSVATTVMRHMEK-QAYVSIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFk 2899
Cdd:PLN02574   353 GMTESTAVGTRGFNTEKlSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW- 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2900 pearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG-- 2977
Cdd:PLN02574   432 -----LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGst 506

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 2978 LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PLN02574   507 LSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 603-949 4.71e-27

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: 114.81  E-value: 4.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  603 DLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHI----VPEAI 678
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGqrkfNPKSW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  679 KRDVPQLFAfinkhqTNIVFLPTafikMIfseRELANS-FPDGVKHLIAAGEQLMISDLFQDVlrKRG---IHLHNHYGP 754
Cdd:cd17633     81 IRKINQYNA------TVIYLVPT----ML---QALARTlEPESKIKSIFSSGQKLFESTKKKL--KNIfpkANLIEFYGT 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  755 SETHVVsTYTIhPGDPIPELPpIGKPIGCTDLYILNHQKqlqpcGVPGELYISGASVARGYVNHDKLTSDKFSSdpfkpd 834
Cdd:cd17633    146 SELSFI-TYNF-NQESRPPNS-VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGWMS------ 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  835 vimyrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcSVQKLNTI 914
Cdd:cd17633    212 -----VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY-SGDKLTYK 285

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1678550997  915 DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd17633    286 QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK13382 PRK13382
bile acid CoA ligase;
464-955 5.21e-27

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 119.09  E-value: 5.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPV 543
Cdd:PRK13382    44 GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLL 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 DPHYPADRIRYILHDCGCSHVVsqahlpssLEDNYIITHPEDIESKVDGSNIKSVNNADDLL------------------ 605
Cdd:PRK13382   124 NTSFAGPALAEVVTREGVDTVI--------YDEEFSATVDRALADCPQATRIVAWTDEDHDLtvevliaahagqrpeptg 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  606 ----YMIYTSGTTGKPKGVQfeHRNMANLLKFEYTHSGIDFEAD-VLQFATPSFdvcYQEIFSALLKGGTLH--IV---- 674
Cdd:PRK13382   196 rkgrVILLTSGTTGTPKGAR--RSGPGGIGTLKAILDRTPWRAEePTVIVAPMF---HAWGFSQLVLAASLActIVtrrr 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  675 --PEAIkrdvpqlFAFINKHQ-TNIVFLPTAFIKMIFSERELANSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNH 751
Cdd:PRK13382   271 fdPEAT-------LDLIDRHRaTGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNN 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  752 YGPSETHVVSTYTihPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVN-HDKLTSDKFSSdp 830
Cdd:PRK13382   344 YNATEAGMIATAT--PADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSgSTKDFHDGFMA-- 419

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  831 fkpdvimyrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQK 910
Cdd:PRK13382   420 ---------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG 490

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997  911 LNTI--DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEP 955
Cdd:PRK13382   491 ASATpeTLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 452-952 5.97e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 119.38  E-value: 5.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  452 IGEItdqtPVYETIHAMfekqAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVL 531
Cdd:PRK06178    30 HGER----PLTEYLRAW----ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFF 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  532 GILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQ---------------------------------AHLPSSLEDNY 578
Cdd:PRK06178   102 GILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALdqlapvveqvraetslrhvivtsladvlpaeptLPLPDSLRAPR 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  579 II-THPEDIESKVDGSNIKSVNNA---DDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSF 654
Cdd:PRK06178   182 LAaAGAIDLLPALRACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEF 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  655 -----DVCyqeIFSALLKGGTLHIvpeaIKRDVPQLF-AFINKHQTNIVFLPT-AFIKMI----FSEREL-------ANS 716
Cdd:PRK06178   262 wiageNFG---LLFPLFSGATLVL----LARWDAVAFmAAVERYRVTRTVMLVdNAVELMdhprFAEYDLsslrqvrVVS 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  717 FpdgVKHLIAAgeqlmisdlfqdvLRKRGIHLHNH------YGPSETHVVSTYT--IHPGDPIPELPPI--GKPIGCTDL 786
Cdd:PRK06178   335 F---VKKLNPD-------------YRQRWRALTGSvlaeaaWGMTETHTCDTFTagFQDDDFDLLSQPVfvGLPVPGTEF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  787 YILNHQK-QLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIR 865
Cdd:PRK06178   399 KICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  866 GYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYycsVQ-----KLNTIDLRSYMASELPEYMIPAKWIwVDSIP 940
Cdd:PRK06178   472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAF---VQlkpgaDLTAAALQAWCRENMAVYKVPEIRI-VDALP 547

                          570
                   ....*....|..
gi 1678550997  941 LTPNGKVDRAAL 952
Cdd:PRK06178   548 MTATGKVRKQDL 559
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 473-954 6.12e-27

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 118.61  E-value: 6.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:PRK07470    17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQA----HLPSSLEDNYIITH---------PEDIESKVDGSNIKSVNNA----DDLLYMIYTSGTTG 615
Cdd:PRK07470    97 AYLAEASGARAMICHAdfpeHAAAVRAASPDLTHvvaiggaraGLDYEALVARHLGARVANAavdhDDPCWFFFTSGTTG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  616 KPKGVQFEHRNMA----NLLkfeythsgidfeADVLQfATPSFDVCYqeIFSALLKGGTLH-----------IVPEAIKR 680
Cdd:PRK07470   177 RPKAAVLTHGQMAfvitNHL------------ADLMP-GTTEQDASL--VVAPLSHGAGIHqlcqvargaatVLLPSERF 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  681 DVPQLFAFINKHQ-TNIVFLPTaFIKMIFSERELANSFPDGVKHLIAAGEQLMISDLfQDVLRKRGIHLHNHYGPSEthV 759
Cdd:PRK07470   242 DPAEVWALVERHRvTNLFTVPT-ILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQ-KRALAKLGKVLVQYFGLGE--V 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  760 VSTYTI-----HPGDPIPE--LPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFk 832
Cdd:PRK07470   318 TGNITVlppalHDAEDGPDarIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF- 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  833 pdvimyRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-----IWqdqnGEHELCAYYCS 907
Cdd:PRK07470   397 ------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLgvpdpVW----GEVGVAVCVAR 466

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1678550997  908 V-QKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK07470   467 DgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 12-330 7.17e-27

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: 116.98  E-value: 7.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLF-HSLLQkDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSSPQQVV-LRERNVIVL 89
Cdd:cd20483      3 PMSTFQRRLWFlHNFLE-DKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLdDPSFHLIVI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 EEDITHLNEAEQSQFIEQWKEKDrdrgFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVN 169
Cdd:cd20483     82 DLSEAADPEAALDQLVRNLRRQE----LDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 ASP-ITLEPVqPYGkYI-------KWLMEQDKEQAVSYWDHYLSGHEQQ-TVLPKQKKTKGKSRQEH---VTFSFSKEES 237
Cdd:cd20483    158 GRDlATVPPP-PVQ-YIdftlwhnALLQSPLVQPLLDFWKEKLEGIPDAsKLLPFAKAERPPVKDYErstVEATLDKELL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  238 SRLSELAAREEVtlsTIFHTI---WGILLQKYNNNDDAVFGSVISGRP-AEiegIEHMVGLFINTMPVRVQGA-KTPFLQ 312
Cdd:cd20483    236 ARMKRICAQHAV---TPFMFLlaaFRAFLYRYTEDEDLTIGMVDGDRPhPD---FDDLVGFFVNMLPIRCRMDcDMSFDD 309

                          330
                   ....*....|....*...
gi 1678550997  313 LIKDMQKdrLAAEAYSYH 330
Cdd:cd20483    310 LLESTKT--TCLEAYEHS 325
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 1489-1978 8.69e-27

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: 118.83  E-value: 8.69e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1489 GYSMNqTLHYALEQQAEKTPDQAAVIFEdGVM-------TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGI 1561
Cdd:cd17634     49 DATLN-LAANALDRHLRENGDRTAIIYE-GDDtsqsrtiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1562 YGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLHvpefTGEIV-YLNQTNSGLAHRLSNP-NVDVL------ 1633
Cdd:cd17634    127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVR----AGRSVpLKKNVDDALNPNVTSVeHVIVLkrtgsd 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 ----------------------------PQSLAYVIYTSGSTGMPKGVEIEHRSavnflnslqsrYQLKHS-DMimhktS 1684
Cdd:cd17634    203 idwqegrdlwwrdliakaspehqpeamnAEDPLFILYTSGTTGKPKGVLHTTGG-----------YLVYAAtTM-----K 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1685 YSFDASIWELFWW----------PY-------AGASVYLL---PQGgeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHI 1744
Cdd:cd17634    267 YVFDYGPGDIYWCtadvgwvtghSYllygplaCGATTLLYegvPNW--PTPARMWQVVDKHGVNILYTAPTAIRALMAAG 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1745 KYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVS--ITNSYGPTEAtveaAFFDCPPHEKLERIPIG---KPVHHV 1819
Cdd:cd17634    345 DDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTET----GGFMITPLPGAIELKAGsatRPVFGV 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1820 RLYLLNQNQRMLPVGCIGELYIAGA--GVARGYLNRPalteERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQV 1897
Cdd:cd17634    421 QPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVI 496

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1898 KIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---------EGLqRNEVRAQLERLLPGYMVPAYMIEM 1967
Cdd:cd17634    497 NVAGHRLGTAEIESVLVAHPKVAEAAVVgIPHAIKGQAPYAYVvlnhgvepsPEL-YAELRNWVRKEIGPLATPDVVHWV 575

                          570
                   ....*....|.
gi 1678550997 1968 EQWPVTPSGKL 1978
Cdd:cd17634    576 DSLPKTRSGKI 586
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 1636-1983 9.07e-27

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: 114.35  E-value: 9.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1636 SLAYVIYTSGSTGMPKGVeiehrsavnflnsLQSRYQLKHSDMIMHKtSYSFDASI-W-------------ELFWWPYAG 1701
Cdd:cd17630      1 RLATVILTSGSTGTPKAV-------------VHTAANLLASAAGLHS-RLGFGGGDsWllslplyhvgglaILVRSLLAG 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1702 ASVYLLpqggEKEPEViAKAIEEQKITAMHFVPSMLHAFLEhikYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELlpNV 1781
Cdd:cd17630     67 AELVLL----ERNQAL-AEDLAPPGVTHVSLVPTQLQRLLD---SGQGPAALKSLRAVLLGGAPIPPELLERAADR--GI 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1782 SITNSYGPTEATVEAAFFDCPPHEKLEripIGKPVHHVRLYLLNQnqrmlpvgciGELYIAGAGVARGYLNRPalTEERF 1861
Cdd:cd17630    137 PLYTTYGMTETASQVATKRPDGFGRGG---VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ--LVPEF 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1862 LEDPFYPgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV 1939
Cdd:cd17630    202 NEDGWFT------TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelGQ-RPVAVI 274

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997 1940 EGLQRN---EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd17630    275 VGRGPAdpaELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 490-952 9.15e-27

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: 118.12  E-value: 9.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHV----- 564
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVfvdrd 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  565 ---VSQAHLPSSLEDNYIITHPEDIESKVDGsnIKSVNNADDLL------------------YMIYTSGTTGKPKGVQFE 623
Cdd:cd12119    107 flpLLEAIAPRLPTVEHVVVMTDDAAMPEPA--GVGVLAYEELLaaespeydwpdfdentaaAICYTSGTTGNPKGVVYS 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  624 HRN-----MANLLKfeythSGIDFEA-DVLQFATPSFDVCYQEI-FSALLKGGTLhIVPEaiKRDVPQ-LFAFINKHQ-T 694
Cdd:cd12119    185 HRSlvlhaMAALLT-----DGLGLSEsDVVLPVVPMFHVNAWGLpYAAAMVGAKL-VLPG--PYLDPAsLAELIEREGvT 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  695 NIVFLPTaFIKMIFSERELANS-FPDGVKHLI---AAGEQLMISdlfqdvLRKRGIHLHNHYGPSETHVVSTyTIHPGDP 770
Cdd:cd12119    257 FAAGVPT-VWQGLLDHLEANGRdLSSLRRVVIggsAVPRSLIEA------FEERGVRVIHAWGMTETSPLGT-VARPPSE 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  771 IPELPP---------IGKPIGCTDLYILNHQKQLQPC-GVP-GELYISGASVARGYVNHDKlTSDKFSSDPFkpdvimYR 839
Cdd:cd12119    329 HSNLSEdeqlalrakQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW------LR 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  840 TGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEHELCayyCSV----QKLNTI 914
Cdd:cd12119    402 TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPLA---VVVlkegATVTAE 478

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1678550997  915 DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd12119    479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1073-1356 9.43e-27

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: 116.00  E-value: 9.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1073 DEGVAYNMPAVLEL--EGALD--VAKLSAVckelISRHEPLRTSFVSGADDEPVQRIHTEVP-----FTLSKETTIEGFV 1143
Cdd:cd19544     19 EEGDPYLLRSLLAFdsRARLDafLAALQQV----IDRHDILRTAILWEGLSEPVQVVWRQAElpveeLTLDPGDDALAQL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1144 R--------PFDLSQAPLFRAGLIE-VSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANR--QLKPLrIQYKDYaVWQ 1212
Cdd:cd19544     95 RarfdprryRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRaaALPPP-VPYRNF-VAQ 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1213 QkfKKGDSYQKQETYWQQQFsGD-----LP--ILELPTDKRRPAErqfiggkVTFQLDKEITARIKRLAhknrSTLYMTL 1285
Cdd:cd19544    173 A--RLGASQAEHEAFFREML-GDvdeptAPfgLLDVQGDGSDITE-------ARLALDAELAQRLRAQA----RRLGVSP 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 1286 LALY-SAF---LSRLSGQDDIVIGSPIAGRPHADLEA--VLGMFVNTLALRTRpAGNKTFEEFLKEVRQ--TALEAYEH 1356
Cdd:cd19544    239 ASLFhLAWalvLARCSGRDDVVFGTVLSGRMQGGAGAdrALGMFINTLPLRVR-LGGRSVREAVRQTHArlAELLRHEH 316
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 468-946 9.51e-27

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 117.87  E-value: 9.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  468 MF-EKQAEKTPDAHAVIDQAC--SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVD 544
Cdd:PRK13391     1 MYpGIHAQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  545 PHYPADRIRYILHDCGCSHVV-SQAHL---PSSLEDNYIITHPEDIESKVDGSNIKSVNNA----------DDLL--YMI 608
Cdd:PRK13391    81 SHLTPAEAAYIVDDSGARALItSAAKLdvaRALLKQCPGVRHRLVLDGDGELEGFVGYAEAvaglpatpiaDESLgtDML 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  609 YTSGTTGKPKGV--QFEHRNMANLLK-FEYTHSGIDFEADV-------LQFATPSFDVcyqeiFSALLKGGTlHIVPEAI 678
Cdd:PRK13391   161 YSSGTTGRPKGIkrPLPEQPPDTPLPlTAFLQRLWGFRSDMvylspapLYHSAPQRAV-----MLVIRLGGT-VIVMEHF 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  679 krDVPQLFAFINKHQ-TNIVFLPTAFIKMIFSERELANSFP----DGVKHLIAAGEQlmisDLFQDVLRKRGIHLHNHYG 753
Cdd:PRK13391   235 --DAEQYLALIEEYGvTHTQLVPTMFSRMLKLPEEVRDKYDlsslEVAIHAAAPCPP----QVKEQMIDWWGPIIHEYYA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  754 PSE---THVVST--YTIHPGDpipelppIGKPIgCTDLYILNHQKQLQPCGVPGELYISGASVARgYVNHDKLTSDKFSS 828
Cdd:PRK13391   309 ATEglgFTACDSeeWLAHPGT-------VGRAM-FGDLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHP 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  829 DPfkpdvIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEhELCAYycs 907
Cdd:PRK13391   380 DG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFgVPNEDLGE-EVKAV--- 450

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997  908 VQKLNTID--------LRSYMASELPEYMIPAKWIWVDSIPLTPNGK 946
Cdd:PRK13391   451 VQPVDGVDpgpalaaeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGK 497
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 2549-3023 1.14e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 117.01  E-value: 1.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2549 ASALVSGDKTLTYQELdewsNGIARALRSRgVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEY-PKERkRYILS 2627
Cdd:PRK07787    16 ADAVRIGGRVLSRSDL----AGAATAVAER-VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSgVAER-RHILA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2628 DSGTKLLmtineadLGVLADfEGEILTIESVEEDDKS----PLPQMSSAhhlAYIIYTSGTTGRPKGVMVEHKGIANTLQ 2703
Cdd:PRK07787    90 DSGAQAW-------LGPAPD-DPAGLPHVPVRLHARSwhryPEPDPDAP---ALIVYTSGTTGPPKGVVLSRRAIAADLD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2704 WRRNAYAFNETDTILQ-LFSFSFDGFITSMFTPLLSGAKAVLLheeeAKDILAIKHQLSRQRITHMIIVPVLYRALLDvv 2782
Cdd:PRK07787   159 ALAEAWQWTADDVLVHgLPLFHVHGLVLGVLGPLRIGNRFVHT----GRPTPEAYAQALSEGGTLYFGVPTVWSRIAA-- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2783 QPEDVKTLRVVTL--AGEAA----DRELIArslAICPHtELANEYGPTENSVATTVMRHMEKQAYvSIGQPIDGTQVLIL 2856
Cdd:PRK07787   233 DPEAARALRGARLlvSGSAAlpvpVFDRLA---ALTGH-RPVERYGMTETLITLSTRADGERRPG-WVGLPLAGVETRLV 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVA--GELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRID-DQVKIRG 2933
Cdd:PRK07787   308 DEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGREStDLIKSGG 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2934 YRVETKEIESVIRCIKGVKDAAVVAHVTAS-GQtELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNG 3012
Cdd:PRK07787   382 YRIGAGEIETALLGHPGVREAAVVGVPDDDlGQ-RIVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMG 460

                          490
                   ....*....|.
gi 1678550997 3013 KLDRGALPKPV 3023
Cdd:PRK07787   461 KVLKKQLLSEG 471
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 2091-2500 1.25e-26

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: 115.47  E-value: 1.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2091 SSAQKRIYVLQQledggtgynmpaVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPFTLQTtvl 2170
Cdd:cd19545     15 TARQPGAYVGQR------------VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWTE--- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2171 gARTEQEA-AAAFIKPFDLSQaPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNNRKLPAlRIQYKDYA 2249
Cdd:cd19545     80 -STSLDEYlEEDRAAPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPFSRFV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2250 vwqeGF-KTGDAYKMQEaYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLePEVASGLHKLArengstlyMVLLAA 2328
Cdd:cd19545    157 ----KYlRQLDDEAAAE-FWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISL-PSSASSGVTLA--------TVLRAA 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2329 YTAFLSRLSGQEDIIVGSPIAGR--PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEA--FEH---QNypf 2401
Cdd:cd19545    223 WALVLSRYTGSDDVVFGVTLSGRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMipFEHtglQN--- 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2402 eelvdKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFD--LTLQASEGDGNIHFLFEYSTALFEK 2479
Cdd:cd19545    300 -----IRRLGPDARAACNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFSSygLTLECQLSGSGLRVRARYDSSVISE 374

                          410       420
                   ....*....|....*....|.
gi 1678550997 2480 TTIERWASHLTNVLSIIGKNP 2500
Cdd:cd19545    375 EQVERLLDQFEHVLQQLASAP 395
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 1499-2075 1.39e-26

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: 119.81  E-value: 1.39e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:COG3319      6 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSGLAHRLSNPNVDVLPQSL---AYVIYTSGSTGMPKGVEI 1655
Cdd:COG3319     86 LALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAaaaLAAAAGLGGGGGGAGVLV 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1656 EHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPS 1735
Cdd:COG3319    166 LVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLA 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1736 MLHAFLEHIKYRSVPiktnRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFDCPPHEKLERIPIGKP 1815
Cdd:COG3319    246 ALLLLLALALLLLLA----LLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGG 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1816 VHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPF--YPGERMYKTGDVARWLPDGNVEFLGRT 1893
Cdd:COG3319    322 PGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAgaGARGRLRRGGDRGRRLGGGLLLGLGRL 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1894 DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV- 1972
Cdd:COG3319    402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLl 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1973 ---TPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQ 2049
Cdd:COG3319    482 lllLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561

                          570       580
                   ....*....|....*....|....*.
gi 1678550997 2050 VPLKDVFAHPTVEGLATVIREGTDSP 2075
Cdd:COG3319    562 LLLLALLLAPTLAALAAALAAAAAAA 587
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
2535-3019 1.49e-26

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 117.68  E-value: 1.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDK--TLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVP 2612
Cdd:PRK05852    18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2613 IDPEYPKERKRYILSDSGTKLLMTINEA--------------DLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHL--- 2675
Cdd:PRK05852    98 LDPALPIAEQRVRSQAAGARVVLIDADGphdraepttrwwplTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLrpd 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 -AYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETD-TILQLFSFSFDGFITSMFTPLLSGAkAVLLHEEEAKDI 2753
Cdd:PRK05852   178 dAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDaTVAVMPLYHGHGLIAALLATLASGG-AVLLPARGRFSA 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2754 LAIKHQLSRQRITHMIIVPVLYRALLDVVQPEDVKTLRvvtlageAADRELIARSLAICPHTELANE----------YGP 2823
Cdd:PRK05852   257 HTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKP-------AALRFIRSCSAPLTAETAQALQtefaapvvcaFGM 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2824 TE--NSVATTVMR---HMEKQAyVSIG--QPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQN 2896
Cdd:PRK05852   330 TEatHQVTTTQIEgigQTENPV-VSTGlvGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2897 PFkpearmyRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVtkP 2976
Cdd:PRK05852   409 WL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--P 479

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997 2977 GLSTNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK05852   480 RESAPPTAEELvqfcRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK09274 PRK09274
peptide synthase; Provisional
 1500-1956 1.90e-26

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 117.31  E-value: 1.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGV----------MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGG 1569
Cdd:PRK09274    12 LPRAAQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1570 AYLPIDP--DY-----------PEERI--------SFLLEDSGTNILLLQSAGlhVPEFTGEIVyLNQTNSGLAHrLSNP 1628
Cdd:PRK09274    92 VPVLVDPgmGIknlkqclaeaqPDAFIgipkahlaRRLFGWGKPSVRRLVTVG--GRLLWGGTT-LATLLRDGAA-APFP 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1629 NVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDmimhktsysFDASIWELF--WWPYAG-ASVy 1705
Cdd:PRK09274   168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGE---------IDLPTFPLFalFGPALGmTSV- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1706 lLP-----QGGEKEPEVIAKAIEEQKITAMhFV-PSMLHAFLEHIKYRsvPIKTNRLKRVFSGGEQLGTHLVSRFYELLP 1779
Cdd:PRK09274   238 -IPdmdptRPATVDPAKLFAAIERYGVTNL-FGsPALLERLGRYGEAN--GIKLPSLRRVISAGAPVPIAVIERFRAMLP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1780 N-VSITNSYGPTEA----TVE--AAFFDCPPH-EKLERIPIGKPVHHVRLYLLN---------QNQRMLPVGCIGELYIA 1842
Cdd:PRK09274   314 PdAEILTPYGATEAlpisSIEsrEILFATRAAtDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1843 GAGVARGYLNRPALTEERFLEDPfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV-RE 1921
Cdd:PRK09274   394 GPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRS 471

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1678550997 1922 AAVTVRTD-SGEPELCayVEGLQRNEV-RAQLERLLP 1956
Cdd:PRK09274   472 ALVGVGVPgAQRPVLC--VELEPGVACsKSALYQELR 506
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 462-952 3.03e-26

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 117.04  E-value: 3.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIV 541
Cdd:PRK07059    22 YPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  542 PVDPHYPADRIRYILHDCGC---------SHVVSQA-------H-LPSSLED---------NYIITH-----PE------ 584
Cdd:PRK07059   102 NVNPLYTPRELEHQLKDSGAeaivvlenfATTVQQVlaktavkHvVVASMGDllgfkghivNFVVRRvkkmvPAwslpgh 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  585 ----DIESKVDGSNIKSVNNA-DDLLYMIYTSGTTGKPKGVQFEHRNM-ANLLKFE-YTHSGIDFEADVLQF----ATP- 652
Cdd:PRK07059   182 vrfnDALAEGARQTFKPVKLGpDDVAFLQYTGGTTGVSKGATLLHRNIvANVLQMEaWLQPAFEKKPRPDQLnfvcALPl 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  653 ----SFDVCYqeiFSALLKGGTLHIVPEAikRDVPQLFAFINKHQTNIvfLPT------------AFIKMIFSERELANS 716
Cdd:PRK07059   262 yhifALTVCG---LLGMRTGGRNILIPNP--RDIPGFIKELKKYQVHI--FPAvntlynallnnpDFDKLDFSKLIVANG 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  717 FPDGVKHLIAagEQLmisdlfqdvLRKRGIHLHNHYGPSETHVVSTytIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQ 796
Cdd:PRK07059   335 GGMAVQRPVA--ERW---------LEMTGCPITEGYGLSETSPVAT--CNPVDATEFSGTIGLPLPSTEVSIRDDDGNDL 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  797 PCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEV 876
Cdd:PRK07059   402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  877 TLMNHPDISEAAILIWQDQNGEHELCAYYcsVQK---LNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK07059   476 VVASHPGVLEVAAVGVPDEHSGEAVKLFV--VKKdpaLTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 2534-3028 3.87e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 115.65  E-value: 3.87e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTpVGIMMHRSFSMIASILGVWKAGGCYVPI 2613
Cdd:PRK07638     2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 DPEYPKERKRYILSDSGTKLLMTiNEADLGVLADFEGEILTI----ESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPK 2689
Cdd:PRK07638    81 DIKWKQDELKERLAISNADMIVT-ERYKLNDLPDEEGRVIEIdewkRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2690 GVMVEHKGIANTLQWRRNAYAFNETDTIL---QLFSfsfdgfitSMFtplLSGAKAVL-----LHEEEAKDILAIKHQLS 2761
Cdd:PRK07638   160 AFLRAQQSWLHSFDCNVHDFHMKREDSVLiagTLVH--------SLF---LYGAISTLyvgqtVHLMRKFIPNQVLDKLE 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2762 RQRITHMIIVPVLYRALLDVVQ-PEDvktlrVVTLAGEAADRELIA--RSLAICPHTELANEYGPTENSVATTVMRHMEK 2838
Cdd:PRK07638   229 TENISVMYTVPTMLESLYKENRvIEN-----KMKIISSGAKWEAEAkeKIKNIFPYAKLYEFYGASELSFVTALVDEESE 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2839 QAYVSIGQPIDGTQVLILNSnhqlqpigvAGELCIAG-TGlaRGYVNLPELteraFTQnpFKPEARMYRTGDAARWMA-- 2915
Cdd:PRK07638   304 RRPNSVGRPFHNVQVRICNE---------AGEEVQKGeIG--TVYVKSPQF----FMG--YIIGGVLARELNADGWMTvr 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2916 -------DGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELSAYVVtKPGLSTNAVRSELQ 2988
Cdd:PRK07638   367 dvgyedeEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG-VPDSYWGEKPVAII-KGSATKQQLKSFCL 444

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997 2989 NKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNHEG 3028
Cdd:PRK07638   445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 603-952 4.17e-26

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: 112.42  E-value: 4.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  603 DLLYMIYTSGTTGKPKGVQFEHRNManLLKFEYTHSGIDFEA-DVLQFATPSFDVC-YQEIFSALLKGGTLHIvpeaikR 680
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANL--LASAAGLHSRLGFGGgDSWLLSLPLYHVGgLAILVRSLLAGAELVL------L 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  681 DVPQLFAfINKHQTNIVFL---PTAFIKMIfsERELANSFPDGVKHLIAAGEQLMISDLfqDVLRKRGIHLHNHYGPSET 757
Cdd:cd17630     73 ERNQALA-EDLAPPGVTHVslvPTQLQRLL--DSGQGPAALKSLRAVLLGGAPIPPELL--ERAADRGIPLYTTYGMTET 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  758 hvVSTYTIHPGDpIPELPPIGKPIGCTDLYILNhqkqlqpcgvPGELYISGASVARGYVNHDklTSDKFSSDPFkpdvim 837
Cdd:cd17630    148 --ASQVATKRPD-GFGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQ--LVPEFNEDGW------ 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  838 YRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLR 917
Cdd:cd17630    207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELR 286

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1678550997  918 SYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd17630    287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 463-956 5.25e-26

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 116.29  E-value: 5.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVP 542
Cdd:PRK06710    24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  543 VDPHYPADRIRYILHDCGC----------------------SHVV---------------------SQAHLPSSLEDNYI 579
Cdd:PRK06710   104 TNPLYTERELEYQLHDSGAkvilcldlvfprvtnvqsatkiEHVIvtriadflpfpknllypfvqkKQSNLVVKVSESET 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  580 ITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMAN--LLKFEYTHSGIDFEADVLQfATPSFDVC 657
Cdd:PRK06710   184 IHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSntLMGVQWLYNCKEGEEVVLG-VLPFFHVY 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  658 YQEIFS--ALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIV-FLPTAFIKMIFSerELANSFPDGVKHLIAAGEQLMIS 734
Cdd:PRK06710   263 GMTAVMnlSIMQGYKMVLIP---KFDMKMVFEAIKKHKVTLFpGAPTIYIALLNS--PLLKEYDISSIRACISGSAPLPV 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  735 DLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPElpPIGKPIGCTDLYILNHQK-QLQPCGVPGELYISGASVAR 813
Cdd:PRK06710   338 EVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPG--SIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMK 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQ 893
Cdd:PRK06710   416 GYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVP 488

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  894 DQNGEHELCAYY-------CSVQKLNTIdLRSYMASelpeYMIPAKWIWVDSIPLTPNGKVDRAALPEPD 956
Cdd:PRK06710   489 DPYRGETVKAFVvlkegteCSEEELNQF-ARKYLAA----YKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 470-967 6.34e-26

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 115.64  E-value: 6.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA 549
Cdd:PRK07786    24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  550 DRIRYILHDCGCSHVVSQAHLPSslednyIITHPEDIESKVD------GSNIKSVNNADDLL------------------ 605
Cdd:PRK07786   104 PEIAFLVSDCGAHVVVTEAALAP------VATAVRDIVPLLStvvvagGSSDDSVLGYEDLLaeagpahapvdipndspa 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  606 YMIYTSGTTGKPKGVQFEHRNM-ANLLKFEYThSGIDFEADVLQFATPSFDVC-YQEIFSALLKGGTLHIVPEAiKRDVP 683
Cdd:PRK07786   178 LIMYTSGTTGRPKGAVLTHANLtGQAMTCLRT-NGADINSDVGFVGVPLFHIAgIGSMLPGLLLGAPTVIYPLG-AFDPG 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  684 QLFAFINKHQTNIVFLPTAFIKMIFSE-------------------------RELANSFPDGvkHLIAAGEQLMISD--- 735
Cdd:PRK07786   256 QLLDVLEAEKVTGIFLVPAQWQAVCAEqqarprdlalrvlswgaapasdtllRQMAATFPEA--QILAAFGQTEMSPvtc 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  736 --LFQDVLRKRGihlhnhygpsethvvstytihpgdpipelpPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVAR 813
Cdd:PRK07786   334 mlLGEDAIRKLG------------------------------SVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMS 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GYVNHDKLTSDKFSSDPFkpdvimyRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQ 893
Cdd:PRK07786   384 GYWNNPEATAEAFAGGWF-------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRA 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  894 DQN-GEH--ELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE----PDASISGNPYTA 966
Cdd:PRK07786   457 DEKwGEVpvAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRErygaCVNVERRSASAG 536


                   .
gi 1678550997  967 P 967
Cdd:PRK07786   537 F 537
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 462-956 7.72e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 115.41  E-value: 7.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIV 541
Cdd:PRK07788    48 YGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARII 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  542 PVDPHYPA---------DRIRYILHDCGCSHVVSQahLPSSLED-NYIITHPEDIESKVDGsniksVNNADDLL------ 605
Cdd:PRK07788   128 LLNTGFSGpqlaevaarEGVKALVYDDEFTDLLSA--LPPDLGRlRAWGGNPDDDEPSGST-----DETLDDLIagssta 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  606 ----------YMIYTSGTTGKPKGVQFEHRN----MANLLkfeythSGIDFEAD-VLQFATPSFD----VCYQEIFsALl 666
Cdd:PRK07788   201 plpkppkpggIVILTSGTTGTPKGAPRPEPSplapLAGLL------SRVPFRAGeTTLLPAPMFHatgwAHLTLAM-AL- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  667 kGGTL----HIVPEAIKRDvpqlfafINKHQ-TNIVFLPTaFIKMIFSERELANSFPD--GVKHLIAAGEQLMiSDLFQD 739
Cdd:PRK07788   273 -GSTVvlrrRFDPEATLED-------IAKHKaTALVVVPV-MLSRILDLGPEVLAKYDtsSLKIIFVSGSALS-PELATR 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  740 VLRKRGIHLHNHYGPSEthvVSTYTI-HPGDpIPELPPI-GK-PIGCTdLYILNHQKQLQPCGVPGELYISGASVARGYV 816
Cdd:PRK07788   343 ALEAFGPVLYNLYGSTE---VAFATIaTPED-LAEAPGTvGRpPKGVT-VKILDENGNEVPRGVVGRIFVGNGFPFEGYT 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  817 N-HDKLTSDKFSSdpfkpdvimyrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQ 895
Cdd:PRK07788   418 DgRDKQIIDGLLS-----------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  896 NGEHELCAYYcsVQK----LNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPD 956
Cdd:PRK07788   487 EFGQRLRAFV--VKApgaaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 2550-3046 8.17e-26

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: 116.26  E-value: 8.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2550 SALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMM----HRSFSMIAS---------ILGVWKAGGCYVPIDPE 2616
Cdd:cd05967     74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMpmipEAAIAMLACarigaihsvVFGGFAAKELASRIDDA 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2617 YPK---------ERKRYI---------LSDSGTK---------LLMTINEADLGVLADFEGEILTIESVEeddksPLPqm 2669
Cdd:cd05967    154 KPKlivtascgiEPGKVVpykplldkaLELSGHKphhvlvlnrPQVPADLTKPGRDLDWSELLAKAEPVD-----CVP-- 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2670 SSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWR-RNAYAFNETDTilqLFSFSFDGFIT----SMFTPLLSGAKAVL 2744
Cdd:cd05967    227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSmRNIYGIKPGDV---WWAASDVGWVVghsyIVYGPLLHGATTVL 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2745 LheeEAK-----DILAIKHQLSRQRITHMIIVPVLYRAL------LDVVQPEDVKTLRVVTLAGEAAD---RELIARSLa 2810
Cdd:cd05967    304 Y---EGKpvgtpDPGAFWRVIEKYQVNALFTAPTAIRAIrkedpdGKYIKKYDLSSLRTLFLAGERLDpptLEWAENTL- 379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2811 icpHTELANEYGPTEN--SVATTVM--RHMEKQAYvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGT---GLARGYV 2883
Cdd:cd05967    380 ---GVPVIDHWWQTETgwPITANPVglEPLPIKAG-SPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLW 455

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2884 NLPELTERAFTQNpFKPearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTA- 2962
Cdd:cd05967    456 KNDERFKKLYLSK-FPG---YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEl 531

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2963 SGQTELsAYVVTKPGLSTNAvrSELQNKL---------PV--FMHPAFIEKldsLPLSPNGKLDRGALPKPVynhEGERP 3031
Cdd:cd05967    532 KGQVPL-GLVVLKEGVKITA--EELEKELvalvreqigPVaaFRLVIFVKR---LPKTRSGKILRRTLRKIA---DGEDY 602

                          570
                   ....*....|....*
gi 1678550997 3032 FLPPSSKMEQILADI 3046
Cdd:cd05967    603 TIPSTIEDPSVLDEI 617
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 2678-3016 8.97e-26

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: 111.59  E-value: 8.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHKG-IANTLQWRrNAYAFNETDT---ILQLFSFSfdGFITSmFTPLLSGAKAVLLH----EEE 2749
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNlIAANLQLI-HAMGLTEADVylnMLPLFHIA--GLNLA-LATFHAGGANVVMEkfdpAEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2750 AKDILAikhqlsrQRITHMIIVPVLYRALLDVVQ--PEDVKTLRVVTlaGEAADrELIARSLAICPHTELANeYGPTENS 2827
Cdd:cd17637     81 LELIEE-------EKVTLMGSFPPILSNLLDAAEksGVDLSSLRHVL--GLDAP-ETIQRFEETTGATFWSL-YGQTETS 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2828 VATTVMRHMEKQAyvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFtQNPFkpearmYRT 2907
Cdd:cd17637    150 GLVTLSPYRERPG--SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGW------HHT 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2908 GDAARWMADGTLEYLGRI--DDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTE-LSAYVVTKPG--LSTNA 2982
Cdd:cd17637    221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIG-VPDPKWGEgIKAVCVLKPGatLTADE 299

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1678550997 2983 VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd17637    300 LIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 462-956 9.49e-26

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: 115.29  E-value: 9.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMfekqAEKTPDAHAVI---DQACS--LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKA 536
Cdd:cd05970     20 YDVVDAM----AKEYPDKLALVwcdDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  537 GGAIVPVDPHYPADRIRYILHDCGCSHVVS------QAHLPSSLEDNYIIT-----HPEDIESKVDGSniKSVNNA---- 601
Cdd:cd05970     96 GAIAIPATHQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPECPSKPklvwvGDPVPEGWIDFR--KLIKNAspdf 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 -----------DDLLYMIYTSGTTGKPKGVqfEHRN---MANLLKFEYTHsgiDFEADVLQFA---TPSFDVCYQEIFSA 664
Cdd:cd05970    174 erptansypcgEDILLVYFSSGTTGMPKMV--EHDFtypLGHIVTAKYWQ---NVREGGLHLTvadTGWGKAVWGKIYGQ 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  665 LLKGGTLhIVPEAIKRDVPQLFAFINKHQ-TNIVFLPTAF---IKMIFSERELAnsfpdGVKHLIAAGEQLMiSDLFQDV 740
Cdd:cd05970    249 WIAGAAV-FVYDYDKFDPKALLEKLSKYGvTTFCAPPTIYrflIREDLSRYDLS-----SLRYCTTAGEALN-PEVFNTF 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  741 LRKRGIHLHNHYGPSEThVVSTYTIHPGDPIPElpPIGKPIGCTDLYILNHQKQLQPCGVPGELYI---SGASVA--RGY 815
Cdd:cd05970    322 KEKTGIKLMEGFGQTET-TLTIATFPWMEPKPG--SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGlfGGY 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  816 VNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQ 895
Cdd:cd05970    399 YKDAEKTAEVWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDP 471

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  896 -NGEhelcayycsVQKLNTIDLRSYMASELPE-------------YMIPAKWIWVDSIPLTPNGKVDRAALPEPD 956
Cdd:cd05970    472 iRGQ---------VVKATIVLAKGYEPSEELKkelqdhvkkvtapYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1489-1983 9.76e-26

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 115.15  E-value: 9.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1489 GYSMNQTLHYALEQQAEKTPDQAAVI-FEDGV-----MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIY 1562
Cdd:PRK13295    19 GHWHDRTINDDLDACVASCPDKTAVTaVRLGTgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1563 GILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQS-----------AGLH--VPEFTGEIVYLNQTNSGLAHRLSNPN 1629
Cdd:PRK13295    99 ACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKtfrgfdhaamaRRLRpeLPALRHVVVVGGDGADSFEALLITPA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1630 VD-------VL------PQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HKTSYSFDAS 1690
Cdd:PRK13295   179 WEqepdapaILarlrpgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILmaspmaHQTGFMYGLM 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1691 IwelfwwP-YAGASVYLLPQGgekEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTH 1769
Cdd:PRK13295   259 M------PvMLGATAVLQDIW---DPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSS--LRTFLCAGAPIPGA 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1770 LVSRFYELLpNVSITNSYGPTE-ATVEAAFFDCPPheklERIPI--GKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGV 1846
Cdd:PRK13295   328 LVERARAAL-GAKIVSAWGMTEnGAVTLTKLDDPD----ERASTtdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSN 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1847 ARGYLNRPALTEERFledpfypgERMYKTGDVARWLPDGNVEFLGRTDDqVKIRG-YRIEPGEIEAALRSIEGVREAAVT 1925
Cdd:PRK13295   403 FGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIV 473

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1926 VRTDS--GEpELCAYV-----EGLQRNEVRAQLE--RLLPGYMvPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK13295   474 AYPDErlGE-RACAFVvprpgQSLDFEEMVEFLKaqKVAKQYI-PERLVVRDALPRTPSGKIQKFRL 538
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 2557-2945 1.04e-25

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: 113.99  E-value: 1.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSgtkllmt 2636
Cdd:cd17640      4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHS------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 ineadlgvladfEGEILTIESVEEDdksplpqmssahhLAYIIYTSGTTGRPKGVMVEHkgiANTLQWRRNAYAFNETD- 2715
Cdd:cd17640     77 ------------ESVALVVENDSDD-------------LATIIYTSGTTGNPKGVMLTH---ANLLHQIRSLSDIVPPQp 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2716 -----TILQL---FSFSFDGFItsmftpLLSGAkavllhEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQPEdv 2787
Cdd:cd17640    129 gdrflSILPIwhsYERSAEYFI------FACGC------SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQ-- 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2788 ktlrvvtLAGEAADRELIARSL--------------AICPHT---------ELANEYGPTENSVATTVMRHMEKQAYvSI 2844
Cdd:cd17640    195 -------VSKSSPIKQFLFLFFlsggifkfgisgggALPPHVdtffeaigiEVLNGYGLTETSPVVSARRLKCNVRG-SV 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2845 GQPIDGTQVLI--LNSNHQLQPiGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYL 2922
Cdd:cd17640    267 GRPLPGTEIKIvdPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLT 339

                          410       420
                   ....*....|....*....|....
gi 1678550997 2923 GRIDDQVKIR-GYRVETKEIESVI 2945
Cdd:cd17640    340 GRAKDTIVLSnGENVEPQPIEEAL 363
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 489-949 1.28e-25

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: 113.69  E-value: 1.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCgcshvvsqa 568
Cdd:cd05914      8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS--------- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslEDNYIIthpedieskvdgsniksVNNADDLLYMIYTSGTTGKPKGVQFEHRNMAnllkfeythSGIDF------ 642
Cdd:cd05914     79 ------EAKAIF-----------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIV---------SNVDGvkevvl 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  643 --EADVLQFATP---SFDVCYQEIFsALLKGGTLH----------------------IVP-------EAIKRDVPQLFAF 688
Cdd:cd05914    127 lgKGDKILSILPlhhIYPLTFTLLL-PLLNGAHVVfldkipsakiialafaqvtptlGVPvplviekIFKMDIIPKLTLK 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  689 INKHQTNIVFLPTAFIKMIFseRELANSFPDGVKHLIAAGEQlMISDLFQDvLRKRGIHLHNHYGPSETHVVSTYTIhPG 768
Cdd:cd05914    206 KFKFKLAKKINNRKIRKLAF--KKVHEAFGGNIKEFVIGGAK-INPDVEEF-LRTIGFPYTIGYGMTETAPIISYSP-PN 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  769 DPIpeLPPIGKPIGCTDLYIlnhqKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLE 848
Cdd:cd05914    281 RIR--LGSAGKVIDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDA 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  849 DGNIEYIGRADNQ-VKIRGYRIEPQEIEVTLMNHPDISEAAILIwQDQNGEHELCAYYCSVQKL-----NTID-----LR 917
Cdd:cd05914    349 EGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVV-QEKKLVALAYIDPDFLDVKalkqrNIIDaikweVR 427

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1678550997  918 SYMASELPEYMIPAKWIWV-DSIPLTPNGKVDR 949
Cdd:cd05914    428 DKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
PRK08315 PRK08315
AMP-binding domain protein; Validated
 2533-3013 1.92e-25

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 114.52  E-value: 1.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTL--TYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCY 2610
Cdd:PRK08315    16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2611 VPIDPEYPKERKRYILSDSGTKLLMTIN---EAD-LGVLADFEGEILTIESVE---------------EDDKSP------ 2665
Cdd:PRK08315    96 VTINPAYRLSELEYALNQSGCKALIAADgfkDSDyVAMLYELAPELATCEPGQlqsarlpelrrviflGDEKHPgmlnfd 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2666 ----LPQMSSAHHLAY------------IIYTSGTTGRPKGVMVEHKGIANtlqwrrNAY------AFNETDTI---LQL 2720
Cdd:PRK08315   176 ellaLGRAVDDAELAArqatldpddpinIQYTSGTTGFPKGATLTHRNILN------NGYfigeamKLTEEDRLcipVPL 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2721 FS-FsfdGFITSMFTPLLSGAKAVLLHEeeAKDILAIKHQLSRQRITHMIIVPVLYRALLDvvQPE----DVKTLRVVTL 2795
Cdd:PRK08315   250 YHcF---GMVLGNLACVTHGATMVYPGE--GFDPLATLAAVEEERCTALYGVPTMFIAELD--HPDfarfDLSSLRTGIM 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2796 AGeaadreliarslAICP-----------H-TELANEYGPTENS---------------VAT--TVMRHMEkqayVSIGQ 2846
Cdd:PRK08315   323 AG------------SPCPievmkrvidkmHmSEVTIAYGMTETSpvstqtrtddplekrVTTvgRALPHLE----VKIVD 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2847 PIDGTQVlilnsnhqlqPIGVAGELCIAGTGLARGYVNLPELTERAFtqnpfkpearmyrtgDAARWM---------ADG 2917
Cdd:PRK08315   387 PETGETV----------PRGEQGELCTRGYSVMKGYWNDPEKTAEAI---------------DADGWMhtgdlavmdEEG 441

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2918 TLEYLGRIDDQVkIRG----YrveTKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG--LSTNAVRSELQNKL 2991
Cdd:PRK08315   442 YVNIVGRIKDMI-IRGgeniY---PREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGatLTEEDVRDFCRGKI 517

                          570       580
                   ....*....|....*....|..
gi 1678550997 2992 PVFMHPAFIEKLDSLPLSPNGK 3013
Cdd:PRK08315   518 AHYKIPRYIRFVDEFPMTVTGK 539
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1520-1983 1.93e-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.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 112.94  E-value: 1.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGtnilllqs 1599
Cdd:cd05910      3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE-------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 aglhvPE-FTGEivylnqtnsglahrlsnPNVDvlpqSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDM 1678
Cdd:cd05910     75 -----PDaFIGI-----------------PKAD----EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1679 imhktsysfDASIWELF--WWPYAG-ASV-----YLLPqgGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVP 1750
Cdd:cd05910    129 ---------DLATFPLFalFGPALGlTSVipdmdPTRP--ARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1751 IKTnrLKRVFSGGEQLGTHLVSRFYELL-PNVSITNSYGPTEATVEAAFFD-------CPPHEKLERIPIGKPVHHVRLY 1822
Cdd:cd05910    198 LPS--LRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEALPVSSIGSrellattTAATSGGAGTCVGRPIPGVRVR 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1823 LLN---------QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDpfyPGERM-YKTGDVARWLPDGNVEFLGR 1892
Cdd:cd05910    276 IIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFwHRMGDLGYLDDEGRLWFCGR 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAA-VTVRTDSG-------EPELCAYVEGLQ-RNEVRAQLERLLPGYMVPAY 1963
Cdd:cd05910    353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSAlVGVGKPGCqlpvlcvEPLPGTITPRARlEQELRALAKDYPHTQRIGRF 432

                          490       500
                   ....*....|....*....|..
gi 1678550997 1964 MIEmEQWPVTP--SGKLDRNAL 1983
Cdd:cd05910    433 LIH-PSFPVDIrhNAKIFREKL 453
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 2547-2975 1.98e-25

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: 113.74  E-value: 1.98e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2547 PKASALVSGDKT---LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGgcYVPIdPEYPKERKR 2623
Cdd:cd05908      1 PEGIIFILGDKKekfVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGG--MIAV-PVSIGSNEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2624 YILsdsgtKLLMTINEADLGVLadfegeiLTIESVEEDDKSplpqmssahHLAYIIYTSGTTGRPKGVMVEHKGIANTLQ 2703
Cdd:cd05908     78 HKL-----KLNKVWNTLKNPYL-------ITEEEVLCELAD---------ELAFIQFSSGSTGDPKGVMLTHENLVHNMF 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2704 WRRNAYAFNETDTILQLFSFSFD-GFITSMFTPLLSGAKAVLLHEEE--AKDILAIKhQLSRQRITHMIIVPVLYRALLD 2780
Cdd:cd05908    137 AILNSTEWKTKDRILSWMPLTHDmGLIAFHLAPLIAGMNQYLMPTRLfiRRPILWLK-KASEHKATIVSSPNFGYKYFLK 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2781 VVQPE-----DVKTLRVVTLAGEAADRELIARSLAIC-PH----TELANEYGPTENSVATTV-------------MRHM- 2836
Cdd:cd05908    216 TLKPEkandwDLSSIRMILNGAEPIDYELCHEFLDHMsKYglkrNAILPVYGLAEASVGASLpkaqspfktitlgRRHVt 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2837 -----------EKQAY--VSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpear 2903
Cdd:cd05908    296 hgepepevdkkDSECLtfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW----- 370

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2904 mYRTGDAArWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVA---HVTASGQTELSAYVVTK 2975
Cdd:cd05908    371 -LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHR 443
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 473-947 2.28e-25

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 113.44  E-value: 2.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQAHL--PSSLEDNYIIThpeDIESKVDGSNI---------KSVNNADDLLYMIYTSGTTGKPKGVQ 621
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFdaIVALETPKIVI---DAAAQADSRRLaqggleippQAAVAPTDLVRLMYTSGTTDRPKGVM 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  622 FEHRNMAnLLKFEYTHS-GIDFEaDVLQFATPSFDV--CYQEIFSALLKGGTLHIV----PEAIkrdvpqlFAFINKHQT 694
Cdd:PRK06145   169 HSYGNLH-WKSIDHVIAlGLTAS-ERLLVVGPLYHVgaFDLPGIAVLWVGGTLRIHrefdPEAV-------LAAIERHRL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  695 NIVFLPTAFIKMIFSERELANSFPDGVKHLIAAGE---QLMISDLFQDVLRKRGIhlhNHYGPSETHVVSTYtIHPGDPI 771
Cdd:PRK06145   240 TCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEktpESRIRDFTRVFTRARYI---DAYGLTETCSGDTL-MEAGREI 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  772 PELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimyRTGDLARRLEDGN 851
Cdd:PRK06145   316 EKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGF 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  852 IEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMI 929
Cdd:PRK06145   389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQRLASFKV 468

                          490
                   ....*....|....*...
gi 1678550997  930 PAKWIWVDSIPLTPNGKV 947
Cdd:PRK06145   469 PRQLKVRDELPRNPSGKV 486
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 1500-1925 2.38e-25

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: 113.74  E-value: 2.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIF-----EDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLP- 1573
Cdd:cd05970     23 VDAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPa 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1574 -----------------------IDPDYPEERISFLLEDSGTNILLLQSAGlhvPEFTGEIVYlNQTNSGLAHRLSNPNV 1630
Cdd:cd05970    103 thqltakdivyriesadikmivaIAEDNIPEEIEKAAPECPSKPKLVWVGD---PVPEGWIDF-RKLIKNASPDFERPTA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1631 DVLP--QSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFW--WpYAGASVYL 1706
Cdd:cd05970    179 NSYPcgEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYgqW-IAGAAVFV 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1707 LPQGgEKEPEVIAKAIEEQKITAMhFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELlPNVSITNS 1786
Cdd:cd05970    258 YDYD-KFDPKALLEKLSKYGVTTF-CAPPTIYRFLIREDLSRYDLSS--LRYCTTAGEALNPEVFNTFKEK-TGIKLMEG 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATVEAAFFDCpphekLERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGA-----GVARGYLNRPALTEE 1859
Cdd:cd05970    333 FGQTETTLTIATFPW-----MEPKPgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAE 407

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1860 RFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT 1925
Cdd:cd05970    408 VWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 464-947 2.41e-25

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: 114.21  E-value: 2.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPDAHAVI------DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAG 537
Cdd:cd17634     54 LAANALDRHLRENGDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  538 GAIVPVDPHYPADRIRYILHDCGCSHVVS-------------QAHLPSSLEDNyiITHPEDI------ESKVDGSNIKSV 598
Cdd:cd17634    134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsvplKKNVDDALNPN--VTSVEHVivlkrtGSDIDWQEGRDL 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  599 N-----------------NADDLLYMIYTSGTTGKPKGVQfeHRNMANLLKFEYTHSGI-DFEA-DVLQFATpsfDVCYQ 659
Cdd:cd17634    212 WwrdliakaspehqpeamNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKYVfDYGPgDIYWCTA---DVGWV 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  660 EIFSALLKGGTLHIVPEAIKRDVP------QLFAFINKHQTNIVFL-PTAFikmifseRELANSFPDGV--------KHL 724
Cdd:cd17634    287 TGHSYLLYGPLACGATTLLYEGVPnwptpaRMWQVVDKHGVNILYTaPTAI-------RALMAAGDDAIegtdrsslRIL 359

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  725 IAAGEQLMIS--DLFQDVLRKRGIHLHNHYGPSEThvvsTYTIHPGDPIPELPPIG---KPIGCTDLYILNHQKQLQPCG 799
Cdd:cd17634    360 GSVGEPINPEayEWYWKKIGKEKCPVVDTWWQTET----GGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGG 435

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  800 VPGELYISGA--SVARGYV-NHDKLTSDKFSSdpFKPdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEV 876
Cdd:cd17634    436 TEGNLVITDPwpGQTRTLFgDHERFEQTYFST--FKG---MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIES 510

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  877 TLMNHPDISEAAIL-IWQDQNGEhelcAYYCSVQ-KLNTID-------LRSYMASELPEYMIPAKWIWVDSIPLTPNGKV 947
Cdd:cd17634    511 VLVAHPKVAEAAVVgIPHAIKGQ----APYAYVVlNHGVEPspelyaeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 462-952 2.95e-25

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 113.70  E-value: 2.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQ-EPVAIMMERSAAFITGVLGILKAGGAI 540
Cdd:PRK05677    23 YPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPgDRIAVQLPNVLQYPVAVFGAMRAGLIV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  541 VPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLED---------------------------NYIITH----------P 583
Cdd:PRK05677   103 VNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKvlpktgvkhvivtevadmlpplkrlliNAVVKHvkkmvpayhlP 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  584 E-----DIESKVDGSNIKSVN-NADDLLYMIYTSGTTGKPKGVQFEHRNM-ANLLKFEYTHSGIDFEA-DVLQFATPSFD 655
Cdd:PRK05677   183 QavkfnDALAKGAGQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCRALMGSNLNEGcEILIAPLPLYH 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  656 VcYQEIF---SALLKGGTLHIVPEAikRDVPQLFAFINKHQ-TNIVFLPTAFIKMIFSE--RELANSfpdGVKHLIAAGE 729
Cdd:PRK05677   263 I-YAFTFhcmAMMLIGNHNILISNP--RDLPAMVKELGKWKfSGFVGLNTLFVALCNNEafRKLDFS---ALKLTLSGGM 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  730 --QLMISDLFQDVlrkRGIHLHNHYGPSETHVVSTytIHPGDPIpELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYIS 807
Cdd:PRK05677   337 alQLATAERWKEV---TGCAICEGYGMTETSPVVS--VNPSQAI-QVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  808 GASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISE- 886
Cdd:PRK05677   411 GPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQc 484

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  887 AAILIWQDQNGEH-ELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK05677   485 AAIGVPDEKSGEAiKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 1640-1980 4.12e-25

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: 109.66  E-value: 4.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 VIYTSGSTGMPKGVEIEHRSAVNFLNSLQSrYQLKHSD-----MIMHkTSYSFdASIWELFWWPYAGASVYllpqGGE-K 1713
Cdd:cd17635      6 VIFTSGTTGEPKAVLLANKTFFAVPDILQK-EGLNWVVgdvtyLPLP-ATHIG-GLWWILTCLIHGGLCVT----GGEnT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1714 EPEVIAKAIEEQKITAMHFVPSMLHAFLehIKYRSVPIKTNRLKRVFSGGEQLgTHLVSRFYELLPNVSITNSYGPTEAT 1793
Cdd:cd17635     79 TYKSLFKILTTNAVTTTCLVPTLLSKLV--SELKSANATVPSLRLIGYGGSRA-IAADVRFIEATGLTNTAQVYGLSETG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1794 veAAFFdCPPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgerm 1872
Cdd:cd17635    156 --TALC-LPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN----- 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1873 ykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELC-AYV---EGLQRNEVR 1948
Cdd:cd17635    228 --TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVgLAVvasAELDENAIR 305

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1678550997 1949 AQLERL---LPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd17635    306 ALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 470-949 4.71e-25

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: 113.88  E-value: 4.71e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVI------DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAI---MMERSAAFITGVLGIlkagGAI 540
Cdd:TIGR02188   64 DRHLEARPDKVAIIwegdepGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIympMIPEAAIAMLACARI----GAI 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  541 VPV-----DPHYPADRIryilHDCGCSHVVSQ--------------------AHLPSSLEDNYIITHP-EDIESKVDGSN 594
Cdd:TIGR02188  140 HSVvfggfSAEALADRI----NDAGAKLVITAdeglrggkviplkaivdealEKCPVSVEHVLVVRRTgNPVVPWVEGRD 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  595 ------IKSVN--------NADDLLYMIYTSGTTGKPKGVQfeHRNMANLLKFEYTHSGIdFE----------ADVLQFA 650
Cdd:TIGR02188  216 vwwhdlMAKASaycepepmDSEDPLFILYTSGSTGKPKGVL--HTTGGYLLYAAMTMKYV-FDikdgdifwctADVGWIT 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  651 TPSFdVCYqeifSALLKGGTLHI---VPeaikrDVPQ---LFAFINKHQTNIVFL-PTAfIKMIfseRELANSFPDgvKH 723
Cdd:TIGR02188  293 GHSY-IVY----GPLANGATTVMfegVP-----TYPDpgrFWEIIEKHKVTIFYTaPTA-IRAL---MRLGDEWVK--KH 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  724 liaageqlmisDLfqDVLRKRG-----IH------LHNHYGPSETHVVSTY--TIHPG---DPIPELPPIgKPIGCT--- 784
Cdd:TIGR02188  357 -----------DL--SSLRLLGsvgepINpeawmwYYKVVGKERCPIVDTWwqTETGGimiTPLPGATPT-KPGSATlpf 422

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  785 ---DLYIL-NHQKQLQPCGVPGELYISGA--SVARG-YVNHDKLTSDKFSsdPFKPdviMYRTGDLARRLEDGNIEYIGR 857
Cdd:TIGR02188  423 fgiEPAVVdEEGNPVEGPGEGGYLVIKQPwpGMLRTiYGDHERFVDTYFS--PFPG---YYFTGDGARRDKDGYIWITGR 497

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  858 ADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEhELCAYYCSVQKLNTID-----LRSYMASELPEYMIPA 931
Cdd:TIGR02188  498 VDDVINVSGHRLGTAEIESALVSHPAVAEAAVVgIPDDIKGQ-AIYAFVTLKDGYEPDDelrkeLRKHVRKEIGPIAKPD 576

                          570
                   ....*....|....*...
gi 1678550997  932 KWIWVDSIPLTPNGKVDR 949
Cdd:TIGR02188  577 KIRFVPGLPKTRSGKIMR 594
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 1494-1999 7.83e-25

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 112.16  E-value: 7.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1494 QTLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLP 1573
Cdd:PRK06155    21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1574 IDPDYPEERISFLLEDSGTNILLLQSAGLHV-------PEFTGEIVYLNQTNSGLAHR-----------LSNPNVDVLPQ 1635
Cdd:PRK06155   101 INTALRGPQLEHILRNSGARLLVVEAALLAAleaadpgDLPLPAVWLLDAPASVSVPAgwstaplppldAPAPAAAVQPG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1636 SLAYVIYTSGSTGMPKGVEIEH-------RSAVNFL-----------------NSLQSRYQLKHSDMIMHKTSySFDASi 1691
Cdd:PRK06155   181 DTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLeigaddvlyttlplfhtNALNAFFQALLAGATYVLEP-RFSAS- 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1692 weLFWwpyagasvyllpqggekepeviaKAIEEQKITAMHFVPSMLHAFLEhiKYRSVPIKTNRLKRVFSGG--EQLGTH 1769
Cdd:PRK06155   259 --GFW-----------------------PAVRRHGATVTYLLGAMVSILLS--QPARESDRAHRVRVALGPGvpAALHAA 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1770 LVSRFyellpNVSITNSYGPTEATveAAFFDCPPHEK---LERIpigKPVHHVRLylLNQNQRMLPVGCIGELYIAGA-- 1844
Cdd:PRK06155   312 FRERF-----GVDLLDGYGSTETN--FVIAVTHGSQRpgsMGRL---APGFEARV--VDEHDQELPDGEPGELLLRADep 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1845 -GVARGYLNRPALTEERFLEDPFYPGERmyktgdVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA 1923
Cdd:PRK06155   380 fAFATGYFGMPEKTVEAWRNLWFHTGDR------VVR-DADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAA 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1924 V-TVRTDSGEPELCAYV---EGLQRN--EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAAD-----A 1992
Cdd:PRK06155   453 VfPVPSELGEDEVMAAVvlrDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADtwdreA 532


                   ....*..
gi 1678550997 1993 ETYTAPR 1999
Cdd:PRK06155   533 AGVQLPR 539
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 488-889 9.49e-25

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 112.30  E-value: 9.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVS- 566
Cdd:PRK04319    73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITt 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  567 --------QAHLPS-----------SLEDNYIiTHPEDIESKVDGSNIKSVNnADDLLYMIYTSGTTGKPKGVQFEHRNM 627
Cdd:PRK04319   153 pallerkpADDLPSlkhvllvgedvEEGPGTL-DFNALMEQASDEFDIEWTD-REDGAILHYTSGSTGKPKGVLHVHNAM 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  628 anllkfeYTH--SG---IDFEADvlqfatpsfDV--CYQE----------IFSALLKGGTLhIVPEAiKRDVPQLFAFIN 690
Cdd:PRK04319   231 -------LQHyqTGkyvLDLHED---------DVywCTADpgwvtgtsygIFAPWLNGATN-VIDGG-RFSPERWYRILE 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  691 KHQTNIVF-LPTAFIKMIFSERELANSFP-DGVKHLIAAGEQLMISDLF--QDVLRKRgihLHNHYGPSET--HVVSTYT 764
Cdd:PRK04319   293 DYKVTVWYtAPTAIRMLMGAGDDLVKKYDlSSLRHILSVGEPLNPEVVRwgMKVFGLP---IHDNWWMTETggIMIANYP 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  765 ---IHPGDpipelppIGKPIGCTDLYILNHQKQLQPCGVPGELYISGA--SVARGYVNHDKLTSDKFSSDpfkpdviMYR 839
Cdd:PRK04319   370 amdIKPGS-------MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYFAGD-------WYV 435

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997  840 TGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAI 889
Cdd:PRK04319   436 SGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 473-953 1.31e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 111.24  E-value: 1.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:PRK13383    45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQ---AHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYmiyTSGTTGKPKGVQFEHRnman 629
Cdd:PRK13383   125 AAALRAHHISTVVADnefAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLL---TSGTTGKPKGVPRAPQ---- 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  630 llkfeyTHSGIDFEADVLQ-----------FATPSFD-VCYQEIFSALLKGGTL----HIVPEAIkrdvpqlFAFINKHQ 693
Cdd:PRK13383   198 ------LRSAVGVWVTILDrtrlrtgsrisVAMPMFHgLGLGMLMLTIALGGTVlthrHFDAEAA-------LAQASLHR 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  694 TN-IVFLPTAFIKMI-FSERELA-NSFPDgVKHLIAAGEQLMISdLFQDVLRKRGIHLHNHYGPSETHVVSTYTihPGDP 770
Cdd:PRK13383   265 ADaFTAVPVVLARILeLPPRVRArNPLPQ-LRVVMSSGDRLDPT-LGQRFMDTYGDILYNGYGSTEVGIGALAT--PADL 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  771 IPELPPIGKPIGCTDLYILNHQKQlqPCG--VPGELYISGasvargyvnhdKLTSDKFSSDPFKPDVI-MYRTGDLARRL 847
Cdd:PRK13383   341 RDAPETVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGG-----------ELAGTRYTDGGGKAVVDgMTSTGDMGYLD 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  848 EDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYY-----CSVqklNTIDLRSYMAS 922
Cdd:PRK13383   408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVvlhpgSGV---DAAQLRDYLKD 484

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1678550997  923 ELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:PRK13383   485 RVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 473-883 1.34e-24

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


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 111.56  E-value: 1.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAV--IDQAC----SLTYRELNKAANRLARHLRMKGVVRqEPVAIMMERSAAFITGVLGILKAGGAIVPV-DP 545
Cdd:cd05931      3 AAARPDRPAYtfLDDEGgreeTLTYAELDRRARAIAARLQAVGKPG-DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  546 HYP--ADRIRYILHDCGCSHVVSQA----------HLPSSLEDNYIITHPEDIESKVDGSNIKSVNnADDLLYMIYTSGT 613
Cdd:cd05931     82 TPGrhAERLAAILADAGPRVVLTTAaalaavrafaASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYLQYTSGS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  614 TGKPKGVQFEHRN-MANLLkfEYTHSGIDFEADVLQFATPsfdvCYQE------IFSALLKGGTLHIV-PEA-IKRdvP- 683
Cdd:cd05931    161 TGTPKGVVVTHRNlLANVR--QIRRAYGLDPGDVVVSWLP----LYHDmgliggLLTPLYSGGPSVLMsPAAfLRR--Pl 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  684 ---QLfafINKHQTNIVFLPT-AF---IKMIfSERELANSfpD--GVKHLIAAGEQLMISDL--FQDVLRKRGIH---LH 749
Cdd:cd05931    233 rwlRL---ISRYRATISAAPNfAYdlcVRRV-RDEDLEGL--DlsSWRVALNGAEPVRPATLrrFAEAFAPFGFRpeaFR 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  750 NHYGPSETHV-VST------YTIH----------------PGDPIPELPPIGKPIGCTDLYILN-HQKQLQPCGVPGELY 805
Cdd:cd05931    307 PSYGLAEATLfVSGgppgtgPVVLrvdrdalagravavaaDDPAARELVSCGRPLPDQEVRIVDpETGRELPDGEVGEIW 386

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  806 ISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLArRLEDGNIeYI-GRADNQVKIRGYRIEPQEIEVTLMNHPD 883
Cdd:cd05931    387 VRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 2674-3016 1.54e-24

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: 107.49  E-value: 1.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 HLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDI 2753
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2754 LAIkhqLSRQRITHMIIVPVLYRALLDVVQPEDvkTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVM 2833
Cdd:cd17633     81 IRK---INQYNATVIYLVPTMLQALARTLEPES--KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 RHMEKQAYvSIGQPIDGTQVLILNSNHqlqpiGVAGELCIAGTGLARGYVNLPELteraftqNPFKPearmYRTGDAARW 2913
Cdd:cd17633    156 NQESRPPN-SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFS-------NPDGW----MSVGDIGYV 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2914 MADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPV 2993
Cdd:cd17633    219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG-IPDARFGEIAVALYSGDKLTYKQLKRFLKQKLSR 297

                          330       340
                   ....*....|....*....|...
gi 1678550997 2994 FMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd17633    298 YEIPKKIIFVDSLPYTSSGKIAR 320
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
468-954 1.67e-24

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 111.13  E-value: 1.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  468 MFEKQAEKTPDAHAVI--DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDP 545
Cdd:PRK05852    21 LVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  546 HYPA----DR-----IRYILHDC------------------------GCSHVVSQAHLPSSLEDNYIITHPEDIeskvdg 592
Cdd:PRK05852   101 ALPIaeqrVRsqaagARVVLIDAdgphdraepttrwwpltvnvggdsGPSGGTLSVHLDAATEPTPATSTPEGL------ 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  593 sniksvnNADDLLYMiYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGI-DFEADVLQFATPSFDVCYQEIFSALLKGGTL 671
Cdd:PRK05852   175 -------RPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAIITGYRLsPRDATVAVMPLYHGHGLIAALLATLASGGAV 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  672 hIVPEAIKRDVPQLFAFINK-HQTNIVFLPTafIKMIFSERELANSFPDGVKHL--IAAGEQLMISDLFQDVLRKRGIHL 748
Cdd:PRK05852   247 -LLPARGRFSAHTFWDDIKAvGATWYTAVPT--IHQILLERAATEPSGRKPAALrfIRSCSAPLTAETAQALQTEFAAPV 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  749 HNHYGPSE-THVVSTYTI----HPGDPIPELPPIGKPIGcTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTS 823
Cdd:PRK05852   324 VCAFGMTEaTHQVTTTQIegigQTENPVVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITA 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  824 DKFSSDPFkpdvimyRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCA 903
Cdd:PRK05852   403 ANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAA 475

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  904 YYC--SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK05852   476 VIVprESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
468-952 2.13e-24

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 110.85  E-value: 2.13e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  468 MFEKQAEktPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGgaIVPVDPHY 547
Cdd:PRK10946    30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALF 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  548 ---------------PA--------------DRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEdieskvdGSNIKSV 598
Cdd:PRK10946   106 shqrselnayasqiePAlliadrqhalfsddDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPA-------EDFTATP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  599 NNADDLLYMIYTSGTTGKPKGVQFEHRnmanllkfEYTHSgIDFEADVLQF--------ATPS---FDVCYQEIFSALLK 667
Cdd:PRK10946   179 SPADEVAFFQLSGGSTGTPKLIPRTHN--------DYYYS-VRRSVEICGFtpqtrylcALPAahnYPMSSPGALGVFLA 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  668 GGTLHIV--PEAIkrdvpQLFAFINKHQTNIVFL-PTAFIKMIfserelansfpdgvKHLIAAGEQLMISDL-------- 736
Cdd:PRK10946   250 GGTVVLApdPSAT-----LCFPLIEKHQVNVTALvPPAVSLWL--------------QAIAEGGSRAQLASLkllqvgga 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  737 -FQDVLRKR-----GIHLHNHYGPSETHVvsTYTIHPGDPIPELPPIGKPIGCTD-LYILNHQKQLQPCGVPGELYISGA 809
Cdd:PRK10946   311 rLSETLARRipaelGCQLQQVFGMAEGLV--NYTRLDDSDERIFTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGP 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  810 SVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAI 889
Cdd:PRK10946   389 YTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAL 462

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  890 LIWQD-QNGEHElCAYYCSVQKLNTIDLRSYMASE-LPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK10946   463 VSMEDeLMGEKS-CAFLVVKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 1492-1983 2.79e-24

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 109.97  E-value: 2.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1492 MNQTLhYALEQQAEKTPDQAAVIFEDG-VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLgIY-GILKAGG 1569
Cdd:PRK07514     1 MNNNL-FDALRAAFADRDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALA-LYlATLRAGA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1570 AYLPIDPDYPEERISFLLEDSGTNILLLQSA------GLHVPEFTGEIVYLNQTNSG------LAHRLSNPNVDVLPQSL 1637
Cdd:PRK07514    79 VFLPLNTAYTLAELDYFIGDAEPALVVCDPAnfawlsKIAAAAGAPHVETLDADGTGslleaaAAAPDDFETVPRGADDL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1638 AYVIYTSGSTGMPKGVEIEHRsavNFL-NS--LQSRYQLKHSDMIMH-----KTSYSFDASIWELFwwpyAGASVYLLPQ 1709
Cdd:PRK07514   159 AAILYTSGTTGRSKGAMLSHG---NLLsNAltLVDYWRFTPDDVLIHalpifHTHGLFVATNVALL----AGASMIFLPK 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1710 ggeKEPEVIAKAIEEQkiTAMHFVPSMLHAFLEHIKYRSVPIKTNRLkrvF-SGGEQL--GTHlvSRFYELLPNvSITNS 1786
Cdd:PRK07514   232 ---FDPDAVLALMPRA--TVMMGVPTFYTRLLQEPRLTREAAAHMRL---FiSGSAPLlaETH--REFQERTGH-AILER 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATVEAAffdcPPHEKlERIP--IGKPVHHVRLYLLN-QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLE 1863
Cdd:PRK07514   301 YGMTETNMNTS----NPYDG-ERRAgtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRA 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1864 DPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV--TVRTDSGE-------PE 1934
Cdd:PRK07514   376 DGFF------ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVigVPHPDFGEgvtavvvPK 449

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997 1935 LCAYVEGlqrNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK07514   450 PGAALDE---AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
PRK09274 PRK09274
peptide synthase; Provisional
 2535-2987 3.03e-24

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 110.76  E-value: 3.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGD----------KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVW 2604
Cdd:PRK09274     8 IARHLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2605 KAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEADLG--------------VLAD----FEGEIL-TIESVEEDDKSP 2665
Cdd:PRK09274    88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLArrlfgwgkpsvrrlVTVGgrllWGGTTLaTLLRDGAAAPFP 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2666 LPQMSsAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAF--NETD-TILQLFSFsfdgfitsmFTPLLsGAKA 2742
Cdd:PRK09274   168 MADLA-PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIepGEIDlPTFPLFAL---------FGPAL-GMTS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2743 VLLHEEEAKDILA----IKHQLSRQRITHMIIVPVLYRALLDVVQPEDVK--TLRVVTLAGEAADRELIARSLAICPH-T 2815
Cdd:PRK09274   237 VIPDMDPTRPATVdpakLFAAIERYGVTNLFGSPALLERLGRYGEANGIKlpSLRRVISAGAPVPIAVIERFRAMLPPdA 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2816 ELANEYGPTEN-SVATTVMR--------HMEKQAYVSIGQPIDGTQVLILN---------SNHQLQPIGVAGELCIAGTG 2877
Cdd:PRK09274   317 EILTPYGATEAlPISSIESReilfatraATDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPM 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2878 LARGYVNLPELTERAftqnpfK-PEARM---YRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKD 2953
Cdd:PRK09274   397 VTRSYYNRPEATRLA------KiPDGQGdvwHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKR 470

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1678550997 2954 AAVVAHVTASGQT-----ELSAYVVTkpglSTNAVRSEL 2987
Cdd:PRK09274   471 SALVGVGVPGAQRpvlcvELEPGVAC----SKSALYQEL 505
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 1640-1978 3.33e-24

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: 106.82  E-value: 3.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 VIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSD--MIMHKTSYSFDasiwelfwwpYAGASVYLLPQGGEKEPEV 1717
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDryLIINPFFHTFG----------YKAGIVACLLTGATVVPVA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1718 ------IAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTE 1791
Cdd:cd17638     75 vfdvdaILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSS--LRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1792 ATVEAAffdCPPHEKLERIP--IGKPVHHVRLYLLNQnqrmlpvgciGELYIAGAGVARGYLNRPALTEERFLEDPFYpg 1869
Cdd:cd17638    153 AGVATM---CRPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL-- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1870 ermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL-CAYV-----EGLQ 1943
Cdd:cd17638    218 ----HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVgKAFVvarpgVTLT 293

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1678550997 1944 RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:cd17638    294 EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 1500-1983 4.11e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 110.04  E-value: 4.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PRK08162    24 LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLD 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNIL-------------LLQSAGLHVP------------EFTGEIVYLNQTNSGlahrlsNPNVD-VL 1633
Cdd:PRK08162   104 AASIAFMLRHGEAKVLivdtefaevareaLALLPGPKPLvidvddpeypggRFIGALDYEAFLASG------DPDFAwTL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQ------SLAYviyTSGSTGMPKGVEIEHRSAvnFLNSLQSryqLKHSDMIMHKTsYsfdasIWEL---------FWWP 1698
Cdd:PRK08162   178 PAdewdaiALNY---TSGTTGNPKGVVYHHRGA--YLNALSN---ILAWGMPKHPV-Y-----LWTLpmfhcngwcFPWT 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 Y---AGASVYLlpqggEK-EPEVIAKAIEEQKITamHF-----VPSML-HAFLEHIKYRSVPIKTNRL-----KRVFSGG 1763
Cdd:PRK08162   244 VaarAGTNVCL-----RKvDPKLIFDLIREHGVT--HYcgapiVLSALiNAPAEWRAGIDHPVHAMVAgaappAAVIAKM 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1764 EQLG---THLvsrfYELlpnvsiTNSYGPteATVeaaffdCPPHEKLERIPIGKPVHH-----VRLYLLNQ-----NQRM 1830
Cdd:PRK08162   317 EEIGfdlTHV----YGL------TETYGP--ATV------CAWQPEWDALPLDERAQLkarqgVRYPLQEGvtvldPDTM 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1831 LPVG----CIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 1906
Cdd:PRK08162   379 QPVPadgeTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYIKIKDRSKDIIISGGENISS 451

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1907 GEIEAALRSIEGVREAAVTVRTDS--GE-PelCAYVE---GLQ--RNEVRAQLERLLPGYMVPAyMIEMEQWPVTPSGKL 1978
Cdd:PRK08162   452 IEVEDVLYRHPAVLVAAVVAKPDPkwGEvP--CAFVElkdGASatEEEIIAHCREHLAGFKVPK-AVVFGELPKTSTGKI 528


                   ....*
gi 1678550997 1979 DRNAL 1983
Cdd:PRK08162   529 QKFVL 533
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 488-952 4.62e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 108.92  E-value: 4.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARhlRMKGVVRqepVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQ 567
Cdd:PRK07787    25 VLSRSDLAGAATAVAE--RVAGARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGP 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  568 AhlPSSLEDnyiITHpEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMAnllkfeythSGIDFEA--- 644
Cdd:PRK07787   100 A--PDDPAG---LPH-VPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIA---------ADLDALAeaw 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  645 -----DVLQFATPSFDV--CYQEIFSALLKGGTL-HIVpeaikRDVPQLFAFINKHQTNIVF-LPTAFIKmIFSERELAN 715
Cdd:PRK07787   165 qwtadDVLVHGLPLFHVhgLVLGVLGPLRIGNRFvHTG-----RPTPEAYAQALSEGGTLYFgVPTVWSR-IAADPEAAR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 SFpdgvkhliaAGEQLMISD-------LFQDVLRKRGIHLHNHYGPSEThVVSTYTIHPGDPIPELppIGKPIGCTDLYI 788
Cdd:PRK07787   239 AL---------RGARLLVSGsaalpvpVFDRLAALTGHRPVERYGMTET-LITLSTRADGERRPGW--VGLPLAGVETRL 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  789 LNHQKQLQPCGVP--GELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGR-ADNQVKIR 865
Cdd:PRK07787   307 VDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGReSTDLIKSG 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  866 GYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNG 945
Cdd:PRK07787   381 GYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMG 460


                   ....*..
gi 1678550997  946 KVDRAAL 952
Cdd:PRK07787   461 KVLKKQL 467
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 456-954 6.55e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 109.45  E-value: 6.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  456 TDQTPVYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILK 535
Cdd:PRK06164     3 HDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACAR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  536 AGGAIVPVDPHYPADRIRYILHDCGCSHVVSQAH-----LPSSLEDnyiITHPEDIESK----VDGSN------------ 594
Cdd:PRK06164    83 LGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAA---VPPDALPPLRaiavVDDAAdatpapapgarv 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  595 --------------IKSVNNADDLLYMIYTSGTTGKPKGVQfeHRNmANLLKfeytHSGIDFEA------DVLQFATPsf 654
Cdd:PRK06164   160 qlfalpdpappaaaGERAADPDAGALLFTTSGTTSGPKLVL--HRQ-ATLLR----HARAIARAygydpgAVLLAALP-- 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  655 dVC----YQEIFSALLKGGTLHIVPEAikrDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPdGVKHLIAAGEQ 730
Cdd:PRK06164   231 -FCgvfgFSTLLGALAGGAPLVCEPVF---DAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFP-SARLFGFASFA 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  731 LMISDLFQDVlRKRGIHLHNHYGPSEthVVSTYTIHPGDPiPELPPI---GKPI-GCTDLYILNHQK-QLQPCGVPGELY 805
Cdd:PRK06164   306 PALGELAALA-RARGVPLTGLYGSSE--VQALVALQPATD-PVSVRIeggGRPAsPEARVRARDPQDgALLPDGESGEIE 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  806 ISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDIS 885
Cdd:PRK06164   382 IRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVA 455

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997  886 EAAIlIWQDQNGEHELCAYYC--SVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLT--PNG-KVDRAALPE 954
Cdd:PRK06164   456 AAQV-VGATRDGKTVPVAFVIptDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLRE 528
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1634-1983 6.58e-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: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 106.41  E-value: 6.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTS-YSFDASIWELFWWPYAGASVYLLPQGGE 1712
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1713 KEPEVIA---KAIEEQKITAMHFVPSMLHAFLEhikyrsVPIKTN--RLKRVFSGGEQLGTHLVSRFyELLPNVSITNSY 1787
Cdd:cd05944     81 RNPGLFDnfwKLVERYRITSLSTVPTVYAALLQ------VPVNADisSLRFAMSGAAPLPVELRARF-EDATGLPVVEGY 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1788 GPTEATVEAAffdCPPHEKLERI-PIGKPVHH--VRLYLLNQNQRML---PVGCIGELYIAGAGVARGYL----NRPALT 1857
Cdd:cd05944    154 GLTEATCLVA---VNPPDGPKRPgSVGLRLPYarVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLytegNKNAFV 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1858 EERFLedpfypgermyKTGDVARWLPDGNVEFLGRTDDQVkIRG-YRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL- 1935
Cdd:cd05944    231 ADGWL-----------NTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELp 298

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1936 CAYVEGLQRNEVR-AQL-----ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05944    299 VAYVQLKPGAVVEeEELlawarDHVPERAAVPKHIEVLEELPVTAVGKVFKPAL 352
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2558-3019 8.89e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 107.93  E-value: 8.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2558 TLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTkllmti 2637
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP------ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2638 nEADLGVladfegeiltiesveeddksPLpqmssAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTI 2717
Cdd:cd05910     76 -DAFIGI--------------------PK-----ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2718 LQLFSfsfdgfITSMFTPLLSGAKAV--LLHEEEAKDILAIKHQLSRQ-RITHMIIVPVLYRALLDVVQPEDVK--TLRV 2792
Cdd:cd05910    130 LATFP------LFALFGPALGLTSVIpdMDPTRPARADPQKLVGAIRQyGVSIVFGSPALLERVARYCAQHGITlpSLRR 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2793 VTLAGEAADRELIAR-SLAICPHTELANEYGPTE---------NSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSN--- 2859
Cdd:cd05910    204 VLSAGAPVPIALAARlRKMLSDEAEILTPYGATEalpvssigsRELLATTTAATSGGAGTCVGRPIPGVRVRIIEIDdep 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2860 -------HQLqPIGVAGELCIAGTGLARGYVNLPELTerAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIR 2932
Cdd:cd05910    284 iaewddtLEL-PRGEIGEITVTGPTVTPTYVNRPVAT--ALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITT 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2933 GYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELsayVVTKPGLSTNAVRSELQNKL--------------PVFMHPA 2998
Cdd:cd05910    361 GGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPV---LCVEPLPGTITPRARLEQELralakdyphtqrigRFLIHPS 437

                          490       500
                   ....*....|....*....|...
gi 1678550997 2999 FiekldslPLSP--NGKLDRGAL 3019
Cdd:cd05910    438 F-------PVDIrhNAKIFREKL 453
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 2557-3016 1.14e-23

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: 109.26  E-value: 1.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI----DPEYPKERkryiLSDSGTK 2632
Cdd:TIGR02188   87 RKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVfggfSAEALADR----INDAGAK 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2633 LLMTINEA-------DLGVLAD--FEGEILTIESV--------------------------EEDDKSPLPQMSSAHHLaY 2677
Cdd:TIGR02188  163 LVITADEGlrggkviPLKAIVDeaLEKCPVSVEHVlvvrrtgnpvvpwvegrdvwwhdlmaKASAYCEPEPMDSEDPL-F 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMveHK------GIANTLQWrrnayAFNETDTilQLFSFSFD-GFITS----MFTPLLSGAkAVLLH 2746
Cdd:TIGR02188  242 ILYTSGSTGKPKGVL--HTtggyllYAAMTMKY-----VFDIKDG--DIFWCTADvGWITGhsyiVYGPLANGA-TTVMF 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2747 E-----EEAKDILAIkhqLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAADRE-------LIARSLa 2810
Cdd:TIGR02188  312 EgvptyPDPGRFWEI---IEKHKVTIFYTAPTAIRALMrlgdEWVKKHDLSSLRLLGSVGEPINPEawmwyykVVGKER- 387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2811 iCPhteLANEYGPTEN-SVATTVMRHMEKQAYVSIGQPIDGTQVLILNSN-HQLQPIGVAGELCIAGT--GLARGYVNLP 2886
Cdd:TIGR02188  388 -CP---IVDTWWQTETgGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEgNPVEGPGEGGYLVIKQPwpGMLRTIYGDH 463

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2887 ElterAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVA-HVTASGQ 2965
Cdd:TIGR02188  464 E----RFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGiPDDIKGQ 539

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 2966 tELSAYVVTKPGLSTNA-----VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:TIGR02188  540 -AIYAFVTLKDGYEPDDelrkeLRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMR 594
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1500-1983 1.33e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 108.44  E-value: 1.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDG--VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPD 1577
Cdd:PRK05852    22 VEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1578 YPEERISFLLEDSGTNILLLQSAGLH------VPEFTGEIVYLNQTNSGLA----HR--LSNPNVDV-LPQSL----AYV 1640
Cdd:PRK05852   102 LPIAEQRVRSQAAGARVVLIDADGPHdraeptTRWWPLTVNVGGDSGPSGGtlsvHLdaATEPTPATsTPEGLrpddAMI 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1641 IYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAK 1720
Cdd:PRK05852   182 MFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHTFWD 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1721 AIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQL----GTHLVSRFyeLLPNVSitnSYGPTEATVEA 1796
Cdd:PRK05852   262 DIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLtaetAQALQTEF--AAPVVC---AFGMTEATHQV 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1797 A-----FFDCPPHEKLERIPIGKPVHhVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypger 1871
Cdd:PRK05852   337 TttqieGIGQTENPVVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL----- 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 myKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYVE----GLQRN 1945
Cdd:PRK05852   411 --RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQlyGEAVAAVIVPresaPPTAE 488

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1678550997 1946 EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK05852   489 ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 462-955 1.47e-23

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 108.76  E-value: 1.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMK-GVVRQEPVAIMMERSAAFITGVLGILKAGGAI 540
Cdd:PRK12492    23 YKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  541 VPVDPHYPADRIRYILHDCGCSHVV--------SQAHLPSSLEDNYIITHPED---------IESKVD------------ 591
Cdd:PRK12492   103 VNTNPLYTAREMRHQFKDSGARALVylnmfgklVQEVLPDTGIEYLIEAKMGDllpaakgwlVNTVVDkvkkmvpayhlp 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  592 -------------GSNIKSVN-NADDLLYMIYTSGTTGKPKGVQFEHRNM-ANLLKF--------EYTHSGIDFEADVLQ 648
Cdd:PRK12492   183 qavpfkqalrqgrGLSLKPVPvGLDDIAVLQYTGGTTGLAKGAMLTHGNLvANMLQVraclsqlgPDGQPLMKEGQEVMI 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  649 FATPSFDVcYQeiFSA-----LLKGGtlHIVPEAIKRDVPQLFAFINKHQ-TNIVFLPTAFIKMI---------FSEREL 713
Cdd:PRK12492   263 APLPLYHI-YA--FTAncmcmMVSGN--HNVLITNPRDIPGFIKELGKWRfSALLGLNTLFVALMdhpgfkdldFSALKL 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  714 ANSfpdGVKHLIAAgeqlmISDLFQDVlrkRGIHLHNHYGPSETH-VVSTytiHPGDPIPELPPIGKPIGCTDLYILNHQ 792
Cdd:PRK12492   338 TNS---GGTALVKA-----TAERWEQL---TGCTIVEGYGLTETSpVAST---NPYGELARLGTVGIPVPGTALKVIDDD 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  793 KQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQ 872
Cdd:PRK12492   404 GNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPN 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  873 EIEVTLMNHPDISE-AAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAA 951
Cdd:PRK12492   478 EIEDVVMAHPKVANcAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRE 557


                   ....
gi 1678550997  952 LPEP 955
Cdd:PRK12492   558 LRDI 561
PRK07529 PRK07529
AMP-binding domain protein; Validated
 2524-3019 1.52e-23

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 108.89  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2524 TGQANQYGVQTISQLFEQQAARTPKASALV----SGDK----TLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFS 2595
Cdd:PRK07529    16 VPLAARDLPASTYELLSRAAARHPDAPALSflldADPLdrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2596 MIASILGVwKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT-------------------------INEADLG------- 2643
Cdd:PRK07529    96 THFALWGG-EAAGIANPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvaevlaalpelrtVVEVDLArylpgpk 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2644 -------------VLADFEGEIltieSVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKG-IANTlqWRRNAY 2709
Cdd:PRK07529   175 rlavplirrkahaRILDFDAEL----ARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNeVANA--WLGALL 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2710 AF-NETDTIL-QLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKH--QL-SRQRITHMIIVPVLYRALLDV-VQ 2783
Cdd:PRK07529   249 LGlGPGDTVFcGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVIANfwKIvERYRINFLSGVPTVYAALLQVpVD 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2784 PEDVKTLRVVtLAGEAA-DRELIARSLAicpHT--ELANEYGPTENSVATTVmrhmekqAYV-------SIGQPIDGTQV 2853
Cdd:PRK07529   329 GHDISSLRYA-LCGAAPlPVEVFRRFEA---ATgvRIVEGYGLTEATCVSSV-------NPPdgerrigSVGLRLPYQRV 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2854 LILNSN---HQLQPIGVA--GELCIAGTGLARGYVNlPELTERAFTqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQ 2928
Cdd:PRK07529   398 RVVILDdagRYLRDCAVDevGVLCIAGPNVFSGYLE-AAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDL 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2929 VkIR-GYRVETKEIESVIRCIKGVKDAAVV----AHvtaSGqtELS-AYVVTKPGLSTNAvrSELQNKLPVFMH-----P 2997
Cdd:PRK07529   471 I-IRgGHNIDPAAIEEALLRHPAVALAAAVgrpdAH---AG--ELPvAYVQLKPGASATE--AELLAFARDHIAeraavP 542

                          570       580
                   ....*....|....*....|..
gi 1678550997 2998 AFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK07529   543 KHVRILDALPKTAVGKIFKPAL 564
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 2540-3014 1.78e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 107.85  E-value: 1.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2540 EQQAARTPKASALV--SGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEY 2617
Cdd:PRK13391     4 GIHAQTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2618 PKERKRYILSDSGTKLLMT------INEADLG--------VLADFEGEILTIESVEEDDKS----PLPQMSSAHHLayiI 2679
Cdd:PRK13391    84 TPAEAAYIVDDSGARALITsaakldVARALLKqcpgvrhrLVLDGDGELEGFVGYAEAVAGlpatPIADESLGTDM---L 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2680 YTSGTTGRPKGVM--------VEHKGIANTLQwrrNAYAFNETDTILQ---LF---SFSFDGFITSMftpllsGAKAVLL 2745
Cdd:PRK13391   161 YSSGTTGRPKGIKrplpeqppDTPLPLTAFLQ---RLWGFRSDMVYLSpapLYhsaPQRAVMLVIRL------GGTVIVM 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2746 HEEEAKDILAIkhqLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGeaadreliarslAICP---HTELA 2818
Cdd:PRK13391   232 EHFDAEQYLAL---IEEYGVTHTQLVPTMFSRMLklpeEVRDKYDLSSLEVAIHAA------------APCPpqvKEQMI 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 NEYGP--------TENSVATTVMRHMEKQAYVSIGQPIDGTqVLILNSNHQLQPIGVAGELCIAGtGLARGYVNLPELTE 2890
Cdd:PRK13391   297 DWWGPiiheyyaaTEGLGFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTA 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2891 RAFTqnpfkPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSA 2970
Cdd:PRK13391   375 EARH-----PDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKA 449

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997 2971 YVVTKPGL-STNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:PRK13391   450 VVQPVDGVdPGPALAAELiafcRQRLSRQKCPRSIDFEDELPRLPTGKL 498
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 463-954 1.83e-23

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 108.22  E-value: 1.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVID------QACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKA 536
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  537 GGAIVPVDPHYPADRIRYILHDCGCSHVVS----------------QAHLPS-------------SLEDNYIITHPEDiE 587
Cdd:PRK13295   104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfdhaamarrlRPELPAlrhvvvvggdgadSFEALLITPAWEQ-E 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  588 SKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN-MANLLKF-EYTHSGIDfeaDVLQFATPsfdVCYQEIFsal 665
Cdd:PRK13295   183 PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTlMANIVPYaERLGLGAD---DVILMASP---MAHQTGF--- 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  666 LKGGTLHIV--PEAIKRDV--PQLFA-FINKHQTNIVFLPTAFI-KMIFSERELANSFPDgVKHLIAAGEQLMiSDLFQD 739
Cdd:PRK13295   254 MYGLMMPVMlgATAVLQDIwdPARAAeLIRTEGVTFTMASTPFLtDLTRAVKESGRPVSS-LRTFLCAGAPIP-GALVER 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  740 VLRKRGIHLHNHYGPSETHVVSTytIHPGDPiPELPPI--GKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVN 817
Cdd:PRK13295   332 ARAALGAKIVSAWGMTENGAVTL--TKLDDP-DERASTtdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLK 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  818 HDKLTSDKFSSdpfkpdviMYRTGDLARRLEDGNIEYIGRADNqVKIRG-YRIEPQEIEVTLMNHPDISEAAILIWQDQN 896
Cdd:PRK13295   409 RPQLNGTDADG--------WFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDER 479

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  897 GEHELCAyyCSVQKL-NTIDLRSyMASELPE------YmIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK13295   480 LGERACA--FVVPRPgQSLDFEE-MVEFLKAqkvakqY-IPERLVVRDALPRTPSGKIQKFRLRE 540
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 2663-3019 1.98e-23

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 110.01  E-value: 1.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2663 KSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSF--SFdGFITSMFTPLLSGA 2740
Cdd:PRK08633   772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSF-GLTVTLWLPLLEGI 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2741 KAVllHEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDV--VQPEDVKTLRVVtLAGEAADRELIARSLAICPHTELA 2818
Cdd:PRK08633   851 KVV--YHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNkkLHPLMFASLRLV-VAGAEKLKPEVADAFEEKFGIRIL 927

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 NEYGPTENS-VATTVMR-HMEKQAYV-------SIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARGYVNLPEL 2888
Cdd:PRK08633   928 EGYGATETSpVASVNLPdVLAADFKRqtgskegSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2889 TERAFTQNPFKpeaRMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIrcIKGVKDAAVVAHVTA---SGQ 2965
Cdd:PRK08633  1008 TAEVIKDIDGI---GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEEVVFAVTAvpdEKK 1082

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2966 TELSAYVVTKPGLSTNAVRSEL-QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK08633  1083 GEKLVVLHTCGAEDVEELKRAIkESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK07529 PRK07529
AMP-binding domain protein; Validated
 463-952 2.41e-23

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 108.50  E-value: 2.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVI--------DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGIL 534
Cdd:PRK07529    25 ASTYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  535 KAGgaIV-PVDPHYPADRIRYILHDCGCSHVVS----------------QAHLP------------------SSLEDNYI 579
Cdd:PRK07529   105 AAG--IAnPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvaevLAALPelrtvvevdlarylpgpkRLAVPLIR 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  580 ITHPEDI------------ESKVDGSNIksvnNADDLLYMIYTSGTTGKPKGVQFEHRNM------ANLLkfeythSGID 641
Cdd:PRK07529   183 RKAHARIldfdaelarqpgDRLFSGRPI----GPDDVAAYFHTGGTTGMPKLAQHTHGNEvanawlGALL------LGLG 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  642 fEADVLQFATPSFDV--CYQEIFSALLKGGTLHIVPEAIKRDvPQLFA----FINKHQTN-IVFLPTAFikmifseRELA 714
Cdd:PRK07529   253 -PGDTVFCGLPLFHVnaLLVTGLAPLARGAHVVLATPQGYRG-PGVIAnfwkIVERYRINfLSGVPTVY-------AALL 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  715 NSFPDG--VKHLIAA--GEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTytIHPGDPIPELPPIGKPIGCTDLYIL- 789
Cdd:PRK07529   324 QVPVDGhdISSLRYAlcGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSS--VNPPDGERRIGSVGLRLPYQRVRVVi 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  790 --NHQKQLQPCGV--PGELYISGASVARGYV----NHDKLTSDKFssdpfkpdvimYRTGDLARRLEDGNIEYIGRADNQ 861
Cdd:PRK07529   402 ldDAGRYLRDCAVdeVGVLCIAGPNVFSGYLeaahNKGLWLEDGW-----------LNTGDLGRIDADGYFWLTGRAKDL 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  862 VkIR-GYRIEPQEIEVTLMNHPDISEAAILiwqDQNGEH--EL-CAYycsVQ-----KLNTIDLRSYMASELPEYMIPAK 932
Cdd:PRK07529   471 I-IRgGHNIDPAAIEEALLRHPAVALAAAV---GRPDAHagELpVAY---VQlkpgaSATEAELLAFARDHIAERAAVPK 543

                          570       580
                   ....*....|....*....|.
gi 1678550997  933 WIW-VDSIPLTPNGKVDRAAL 952
Cdd:PRK07529   544 HVRiLDALPKTAVGKIFKPAL 564
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 12-328 3.56e-23

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: 105.62  E-value: 3.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNVSS-PQQVVLrERNVIVLE 90
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGePMQGVL-ASSPLRLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   91 -EDITHLNEAEQsQFieqwkEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASyvn 169
Cdd:cd19532     82 hVQISDEAEVEE-EF-----ERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG--- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  170 aSPITLEPVQpygkYIKWLMEQDKEQA-------VSYWDHYLSGHEQqtVLP-------KQKKTKGKSRQEHVTFSFSKE 235
Cdd:cd19532    153 -QPLLPPPLQ----YLDFAARQRQDYEsgaldedLAYWKSEFSTLPE--PLPllpfakvKSRPPLTRYDTHTAERRLDAA 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  236 ESSRLSELAAREEVtlsTIFH---TIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQ-GAKTPFL 311
Cdd:cd19532    226 LAARIKEASRKLRV---TPFHfylAALQVLLARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRrDPSQTFA 300

                          330
                   ....*....|....*..
gi 1678550997  312 QLIKDMQKDRLAAEAYS 328
Cdd:cd19532    301 DVLKETRDKAYAALAHS 317
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 478-954 3.85e-23

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: 106.84  E-value: 3.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  478 DAHAVIDqacsLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYpadRIRYILH 557
Cdd:cd17642     38 DAHTGVN----YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDH 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  558 DCGCSH--------------VVSQAHLP--------SSLED-------NYIITHPEDIESKVDGSNIKSVNNADDLLYMI 608
Cdd:cd17642    111 SLNISKptivfcskkglqkvLNVQKKLKiiktiiilDSKEDykgyqclYTFITQNLPPGFNEYDFKPPSFDRDEQVALIM 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  609 YTSGTTGKPKGVQFEHRNManLLKFEYT---------------------HSGIDFEAdVLQFATPSFDVCYQEIFSALLK 667
Cdd:cd17642    191 NSSGSTGLPKGVQLTHKNI--VARFSHArdpifgnqiipdtailtvipfHHGFGMFT-TLGYLICGFRVVLMYKFEEELF 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  668 GGTL--HIVPEAIKrdVPQLFAFINKHQtnivflptafikmIFSERELANSfpdgvkHLIAAGEQLMISDLFQDVLRKRG 745
Cdd:cd17642    268 LRSLqdYKVQSALL--VPTLFAFFAKST-------------LVDKYDLSNL------HEIASGGAPLSKEVGEAVAKRFK 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  746 IH-LHNHYGPSEThvVSTYTIHP-GDPIPELPPIGKPIGCTDLYILNHQKQLQPcGVPGELYISGASVARGYVNHDKLTS 823
Cdd:cd17642    327 LPgIRQGYGLTET--TSAILITPeGDDKPGAVGKVVPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATK 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  824 DKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGeHELCA 903
Cdd:cd17642    404 ALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA-GELPA 476

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  904 YYCSVQ---KLNTIDLRSYMASELPeymiPAKW-----IWVDSIPLTPNGKVDRAALPE 954
Cdd:cd17642    477 AVVVLEagkTMTEKEVMDYVASQVS----TAKRlrggvKFVDEVPKGLTGKIDRRKIRE 531
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 460-952 3.88e-23

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 107.24  E-value: 3.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  460 PVYETIHAMFEKQAEktPDAHAVIDQAC--SLTYRELNKAANRLARHLRMKGVVRQ-EPVAIMMERSAAFITGVLGILKA 536
Cdd:PLN02574    38 PNLDAVSFIFSHHNH--NGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVMGVRQgDVVLLLLPNSVYFPVIFLAVLSL 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  537 GGAIVPVDPHYPADRIRYILHDCGCSHV--------------VSQAHLPSSLEDNYIITHPEDIESKVDGSN---IKSVN 599
Cdd:PLN02574   116 GGIVTTMNPSSSLGEIKKRVVDCSVGLAftspenveklsplgVPVIGVPENYDFDSKRIEFPKFYELIKEDFdfvPKPVI 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 NADDLLYMIYTSGTTGKPKGVQFEHRN----MANLLKFE---YTHSGIDfeaDVLQFATPSFDVCYQEIF-SALLKGGTL 671
Cdd:PLN02574   196 KQDDVAAIMYSSGTTGASKGVVLTHRNliamVELFVRFEasqYEYPGSD---NVYLAALPMFHIYGLSLFvVGLLSLGST 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  672 HIVpeaIKR-DVPQLFAFINKHQ-TNIVFLPTAFIKMIFSEREL-ANSFpdGVKHLIAAGEQLMISDLFQDVLRK-RGIH 747
Cdd:PLN02574   273 IVV---MRRfDASDMVKVIDRFKvTHFPVVPPILMALTKKAKGVcGEVL--KSLKQVSCGAAPLSGKFIQDFVQTlPHVD 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  748 LHNHYGPSETHVVSTYTIHPgDPIPELPPIGkpigctdLYILNHQKQ--------LQPCGVPGELYISGASVARGYVNHD 819
Cdd:PLN02574   348 FIQGYGMTESTAVGTRGFNT-EKLSKYSSVG-------LLAPNMQAKvvdwstgcLLPPGNCGELWIQGPGVMKGYLNNP 419

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  820 KLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEH 899
Cdd:PLN02574   420 KATQSTIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGE 493

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  900 ELCAYYCSVQK--LNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PLN02574   494 IPVAFVVRRQGstLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1802-2070 4.19e-23

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 102.52  E-value: 4.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1802 PPHEKLERIPIGKPVHHVRLYLLNQ-NQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVAR 1880
Cdd:COG3433     10 PPTPDEPPPVIPPAIVQARALLLIVdLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1881 WLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEP--ELCAYVEGLQRNEVRAQLERLLPGY 1958
Cdd:COG3433     90 RRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGllLIVGAVAALDGLAAAAALAALDKVP 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1959 --MVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEM-----KLSQLWEDVLKNGP--VGIHDNFFDRG 2029
Cdd:COG3433    170 pdVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETalteeELRADVAELLGVDPeeIDPDDNLFDLG 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1678550997 2030 GHSLKATALVSRItKEFDVQVPLKDVFAHPTVEGLATVIRE 2070
Cdd:COG3433    250 LDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAA 289
PLN02479 PLN02479
acetate-CoA ligase
 1500-1985 6.35e-23

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 106.47  E-value: 6.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PLN02479    26 LERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNS-----------------GLAHRLS-------------NPN 1629
Cdd:PLN02479   106 APTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSfkppllivigdptcdpkSLQYALGkgaieyekfletgDPE 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1630 VDVLP-----QSLAyVIYTSGSTGMPKGVEIEHRSAvnFLNSLQsryqlkhsdmimhktsysfDASIWEL------FW-- 1696
Cdd:PLN02479   186 FAWKPpadewQSIA-LGYTSGTTASPKGVVLHHRGA--YLMALS-------------------NALIWGMnegavyLWtl 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1697 -------WPY-------AGASVYLLpqggEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVpIKTNRLKRVFSG 1762
Cdd:PLN02479   244 pmfhcngWCFtwtlaalCGTNICLR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI-LPLPRVVHVMTA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1763 GEQLGTHLVSRFYELLPNVS----ITNSYGPTEATVEAAFFDCPPHEKLERIPIGKPVHHVRLYLLN--QNQRMLPV--- 1833
Cdd:PLN02479   319 GAAPPPSVLFAMSEKGFRVThtygLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDvvDTKTMKPVpad 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1834 -GCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAA 1912
Cdd:PLN02479   399 gKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFH-------SGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENV 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1913 LRSIEGVREAAVTVRTDS--GEPElCAYV---EGLQRNEVRAQLERL-------LPGYMVPAYMIeMEQWPVTPSGKLDR 1980
Cdd:PLN02479   472 VYTHPAVLEASVVARPDErwGESP-CAFVtlkPGVDKSDEAALAEDImkfcrerLPAYWVPKSVV-FGPLPKTATGKIQK 549


                   ....*
gi 1678550997 1981 NALPA 1985
Cdd:PLN02479   550 HVLRA 554
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
434-952 9.02e-23

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 105.91  E-value: 9.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  434 NLP---PEEIDittdtekrqligeiTDQtpvYETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMK-G 509
Cdd:PRK08974     8 RYPadvPAEIN--------------PDR---YQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  510 VVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLE--------DNYIIT 581
Cdd:PRK08974    71 LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEkvvfktpvKHVILT 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  582 HPEDIESKVDGS-----------------------------------NIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN 626
Cdd:PRK08974   151 RMGDQLSTAKGTlvnfvvkyikrlvpkyhlpdaisfrsalhkgrrmqYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRN 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  627 M-ANLLKFEYTHSG-IDFEADVLQFATPSFdvcyqEIFS----ALL---KGGT-LHIV-PeaikRDVPQLFAFINKHQ-T 694
Cdd:PRK08974   231 MlANLEQAKAAYGPlLHPGKELVVTALPLY-----HIFAltvnCLLfieLGGQnLLITnP----RDIPGFVKELKKYPfT 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  695 NIVFLPTAFIKMIFSE--RELANSfpdGVKHLIAAGE--QLMISDLFQDVlrkRGIHLHNHYGPSE-THVVSTYTI---- 765
Cdd:PRK08974   302 AITGVNTLFNALLNNEefQELDFS---SLKLSVGGGMavQQAVAERWVKL---TGQYLLEGYGLTEcSPLVSVNPYdldy 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  766 HPGDpipelppIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDkfssdpfkpdVIM---YRTGD 842
Cdd:PRK08974   376 YSGS-------IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE----------VIKdgwLATGD 438

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  843 LARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISE-AAILIWQDQNGEhelCAYYCSVQK---LNTIDLRS 918
Cdd:PRK08974   439 IAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEvAAVGVPSEVSGE---AVKIFVVKKdpsLTEEELIT 515

                          570       580       590
                   ....*....|....*....|....*....|....
gi 1678550997  919 YMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK08974   516 HCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 603-949 9.81e-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: 102.72  E-value: 9.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  603 DLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATP-SFDVCYQEIFSALLKGGTLhivpeAIKRD 681
Cdd:cd17635      2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPaTHIGGLWWILTCLIHGGLC-----VTGGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  682 VPQLFAFINKHQTN----IVFLPTAFIKMIFSERELANSFPDgvKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSET 757
Cdd:cd17635     77 NTTYKSLFKILTTNavttTCLVPTLLSKLVSELKSANATVPS--LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSET 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  758 HVVSTytIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKpdvim 837
Cdd:cd17635    155 GTALC--LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN----- 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  838 yrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEHELCAYYCSVQKLNTI-- 914
Cdd:cd17635    228 --TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDENAir 305

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1678550997  915 DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd17635    306 ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK13382 PRK13382
bile acid CoA ligase;
1504-1986 1.13e-22

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 105.61  E-value: 1.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:PRK13382    53 AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNIL--------LLQSAGLHVPEFTGEIVYLNQTNSGLAHRLSNPNVDVLPQSLA----YVIYTSGSTGMPK 1651
Cdd:PRK13382   133 AEVVTREGVDTViydeefsaTVDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGrkgrVILLTSGTTGTPK 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1652 GVEIEHRSAVNFLNSLQSRYQLKHsdmimHKTSY----SFDAsiWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKI 1727
Cdd:PRK13382   213 GARRSGPGGIGTLKAILDRTPWRA-----EEPTVivapMFHA--WGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRA 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1728 TAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPTEATVEAAffdCPPhEKL 1807
Cdd:PRK13382   286 TGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIAT---ATP-ADL 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1808 ERIP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYlnRPALTEErfledpFYPGerMYKTGDVARWLPDG 1885
Cdd:PRK13382   361 RAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD------FHDG--FMASGDVGYLDENG 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1886 NVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---EGLQ------RNEVRAQLERll 1955
Cdd:PRK13382   431 RLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDEQYGQRLAAFVvlkPGASatpetlKQHVRDNLAN-- 508

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1678550997 1956 pgYMVPAYMIEMEQWPVTPSGKLDRNALPAP 1986
Cdd:PRK13382   509 --YKVPRDIVVLDELPRGATGKILRRELQAR 537
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 488-948 2.08e-22

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: 104.34  E-value: 2.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRmKGVVRQEPVAIMMERSAAFITGVLGILKAGGaiVPVDPHYPA--DRIRYILHDCGCSHVV 565
Cdd:cd05909      7 SLTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSGK--VPVMLNYTAglRELRACIKLAGIKTVL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  566 -SQA--------HLPSSLEDNYIItHPEDIESKVDGSN-----------------IKSVNN--ADDLLYMIYTSGTTGKP 617
Cdd:cd05909     84 tSKQfieklklhHLFDVEYDARIV-YLEDLRAKISKADkckaflagkfppkwllrIFGVAPvqPDDPAVILFTSGSEGLP 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  618 KGVQFEHRN-MANLlkfEYTHSGIDF-EADVLQFATPSF-----DVCyqeIFSALLKGGTLHIVPEAIkrDVPQLFAFIN 690
Cdd:cd05909    163 KGVVLSHKNlLANV---EQITAIFDPnPEDVVFGALPFFhsfglTGC---LWLPLLSGIKVVFHPNPL--DYKKIPELIY 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  691 KHQTNIVFLPTAFIkMIFSERELANSFPdGVKHLIAAGEQLMiSDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDP 770
Cdd:cd05909    235 DKKATILLGTPTFL-RGYARAAHPEDFS-SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPN 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  771 IPElpPIGKPIGCTDLYILNHQ-KQLQPCGVPGELYISGASVARGYVNHDKLTSdkfssdpFKPDVIMYRTGDLARRLED 849
Cdd:cd05909    312 KEG--TVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGE 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  850 GNIEYIGRADNQVKIRGYRIEPQEIEVTLMNH-PDISEAAILIWQD-QNGEHELCAYYCSVqkLNTIDLRSYM-ASELPE 926
Cdd:cd05909    383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDgRKGEKIVLLTTTTD--TDPSSLNDILkNAGISN 460

                          490       500
                   ....*....|....*....|..
gi 1678550997  927 YMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd05909    461 LAKPSYIHQVEEIPLLGTGKPD 482
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 2088-2484 2.32e-22

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: 103.16  E-value: 2.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2088 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEV--PFTL 2165
Cdd:cd19547      2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLapPWAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2166 ----------QTTVLGARTEQEAAAAFikpfDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNIL----IQEFGE 2231
Cdd:cd19547     82 ldwsgedpdrRAELLERLLADDRAAGL----SLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIwgdvFRVYEE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2232 LYNNR--KLPALRiQYKDYAVWQEGfKTGDAYKmQEAYWLKQLEgEL---PVLDLPADharppvRSFAGDKVSFTLEPEV 2306
Cdd:cd19547    158 LAHGRepQLSPCR-PYRDYVRWIRA-RTAQSEE-SERFWREYLR-DLtpsPFSTAPAD------REGEFDTVVHEFPEQL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2307 ASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHK--DLEPILGMFVNTLALRTRPEGGKPFVQYLQ 2384
Cdd:cd19547    228 TRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPEleGSEHMVGIFINTIPLRIRLDPDQTVTGLLE 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2385 EV-RETALEAfEHQNYPFEELVDKLELTRdMSRNPVFDAMLVVQNNDYEPLHLHDLQMK------PAQVSHLVSKFDLTL 2457
Cdd:cd19547    308 TIhRDLATTA-AHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQiidlhaQEKTEYPIGLIVLPL 385

                          410       420
                   ....*....|....*....|....*..
gi 1678550997 2458 QasegdgNIHFLFEYSTALFEKTTIER 2484
Cdd:cd19547    386 Q------KLAFHFNYDTTHFTRAQVDR 406
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 2844-3105 2.49e-22

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 100.59  E-value: 2.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2844 IGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPF-KPEARMYRTGDAARWMADGTLEYL 2922
Cdd:COG3433     20 IPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYpAQPGRQADDLRLLLRRGLGPGGGL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2923 GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIEK 3002
Cdd:COG3433    100 ERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3003 LDSLPLSPNGKLDRGALPKPVYN-----HEGERPFLPPSSKMEQILADiWKEVLG--AEKIGTADSFFELGGDSIKALQV 3075
Cdd:COG3433    180 ALDALLLLALKVVARAAPALAAAeallaAASPAPALETALTEEELRAD-VAELLGvdPEEIDPDDNLFDLGLDSIRLMQL 258

                          250       260       270
                   ....*....|....*....|....*....|
gi 1678550997 3076 SARLHRIGKQMAVKDLFSHPTIQELAAYIR 3105
Cdd:COG3433    259 VERWRKAGLDVSFADLAEHPTLAAWWALLA 288
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 1520-1983 3.98e-22

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 104.13  E-value: 3.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQ-ANRIAWELIGRGVKPETTVAIigkRSPEML---LGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNIL 1595
Cdd:PRK12492    50 LSYAELERHsAAFAAYLQQHTDLVPGDRIAV---QMPNVLqypIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1596 L-LQSAGLHVPEFTG--EIVYLNQTNSG-----LAHRLSNPNVDV---------LPQSLAY------------------- 1639
Cdd:PRK12492   127 VyLNMFGKLVQEVLPdtGIEYLIEAKMGdllpaAKGWLVNTVVDKvkkmvpayhLPQAVPFkqalrqgrglslkpvpvgl 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 -----VIYTSGSTGMPKGVEIEHRSAVnfLNSLQSRYQLKHSD-------------MIMHKTSYSFDASIWELFWWPYAG 1701
Cdd:PRK12492   207 ddiavLQYTGGTTGLAKGAMLTHGNLV--ANMLQVRACLSQLGpdgqplmkegqevMIAPLPLYHIYAFTANCMCMMVSG 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1702 ASVYLLpqggeKEPEVIAKAIEE---QKITAMHFVPSMLHAFLEHIKYRSVPIktNRLKRVFSGGEQLGTHLVSRfYELL 1778
Cdd:PRK12492   285 NHNVLI-----TNPRDIPGFIKElgkWRFSALLGLNTLFVALMDHPGFKDLDF--SALKLTNSGGTALVKATAER-WEQL 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1779 PNVSITNSYGPTEATVEAAffdCPPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALT 1857
Cdd:PRK12492   357 TGCTIVEGYGLTETSPVAS---TNPYGELARLgTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEAT 433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1858 EERFledpfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEPE- 1934
Cdd:PRK12492   434 AEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDerSGEAVk 507

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 1935 --LCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK12492   508 lfVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 1500-1998 4.28e-22

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 103.70  E-value: 4.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PRK07786    23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQS--AGLH------VPEFTGEIV-----------YLNQTNS-GLAHrlsnPNVDVLPQSLAY 1639
Cdd:PRK07786   103 PPEIAFLVSDCGAHVVVTEAalAPVAtavrdiVPLLSTVVVaggssddsvlgYEDLLAEaGPAH----APVDIPNDSPAL 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 VIYTSGSTGMPKGVEIEHRS----AVNFLNSlqSRYQLKHSdmIMHKTSYSFD-ASIWELFWWPYAGASVYLLPQGGeKE 1714
Cdd:PRK07786   179 IMYTSGTTGRPKGAVLTHANltgqAMTCLRT--NGADINSD--VGFVGVPLFHiAGIGSMLPGLLLGAPTVIYPLGA-FD 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1715 PEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrlkRVFSGGEQLGTH-LVSRFYELLPNVSITNSYGPTEAT 1793
Cdd:PRK07786   254 PGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAL----RVLSWGAAPASDtLLRQMAATFPEAQILAAFGQTEMS 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1794 VEAAFFDcpPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgerm 1872
Cdd:PRK07786   330 PVTCMLL--GEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH----- 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1873 ykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQRNEVRAQLE 1952
Cdd:PRK07786   403 --SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLE 480

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1953 RL-------LPGYMVPAYMIEMEQWPVTPSGKLD----RNALPAPGGAADAETYTAP 1998
Cdd:PRK07786   481 DLaefltdrLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGF 537
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 1620-1983 4.57e-22

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 103.69  E-value: 4.57e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1620 GLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNflNSLQSRyQLKHSDM------------IMHKTSYSF 1687
Cdd:PRK05677   192 AKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVA--NMLQCR-ALMGSNLnegceiliaplpLYHIYAFTF 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1688 DASIWELfwwpyAGASVYLLPQggEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIktNRLKRVFSGGEQLg 1767
Cdd:PRK05677   269 HCMAMML-----IGNHNILISN--PRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDF--SALKLTLSGGMAL- 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1768 THLVSRFYELLPNVSITNSYGPTEATVEAAFfdcPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVA 1847
Cdd:PRK05677   339 QLATAERWKEVTGCAICEGYGMTETSPVVSV---NPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVM 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1848 RGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE-AAVTV 1926
Cdd:PRK05677   416 KGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGV 489

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1927 RTD-SGEpELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK05677   490 PDEkSGE-AIKVFVvvkpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 2678-3016 4.65e-22

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 100.80  E-value: 4.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHKG-IANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLL-SGAKAVLLHEEEAKDILA 2755
Cdd:cd17635      6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIhGGLCVTGGENTTYKSLFK 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2756 IkhqLSRQRITHMIIVPVLYRALLDVVQP--EDVKTLRVVTLAGEAADRELIARSLAIcPHTELANEYGPTENSVATTVM 2833
Cdd:cd17635     86 I---LTTNAVTTTCLVPTLLSKLVSELKSanATVPSLRLIGYGGSRAIAADVRFIEAT-GLTNTAQVYGLSETGTALCLP 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 RHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFKpearmyrTGDAARW 2913
Cdd:cd17635    162 TDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN-------TGDLGER 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2914 MADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRS---ELQNK 2990
Cdd:cd17635    235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRAlkhTIRRE 314

                          330       340
                   ....*....|....*....|....*.
gi 1678550997 2991 LPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd17635    315 LEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 479-955 5.15e-22

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 103.24  E-value: 5.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  479 AHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHD 558
Cdd:PRK12406     2 YATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  559 CGCSHVVSQA--------HLPSSLEDNYIITHPEDIES-KVDGSNIKSVNNADDL--------LY----------MIYTS 611
Cdd:PRK12406    82 SGARVLIAHAdllhglasALPAGVTVLSVPTPPEIAAAyRISPALLTPPAGAIDWegwlaqqePYdgppvpqpqsMIYTS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  612 GTTGKPKGVQfehRNMANLlkfEYTHSGIDFEADVLQFATPSFDVC----YQE------IFSALLkGGTLHIVPeaiKRD 681
Cdd:PRK12406   162 GTTGHPKGVR---RAAPTP---EQAAAAEQMRALIYGLKPGIRALLtgplYHSapnaygLRAGRL-GGVLVLQP---RFD 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  682 VPQLFAFINKHQ-TNIVFLPTAFIKMIfserelanSFPDGVK---------HLIAAG-------EQLMIsDLFQDVlrkr 744
Cdd:PRK12406   232 PEELLQLIERHRiTHMHMVPTMFIRLL--------KLPEEVRakydvsslrHVIHAAapcpadvKRAMI-EWWGPV---- 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 gihLHNHYGPSETHVVSTYTI-----HPGDpipelppIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVAR-GYVNH 818
Cdd:PRK12406   299 ---IYEYYGSTESGAVTFATSedalsHPGT-------VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNK 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  819 D----KLTSDKFSSdpfkpdvimyrTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQD 894
Cdd:PRK12406   369 PekraEIDRGGFIT-----------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997  895 QNGEHELCAYycsVQ-----KLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEP 955
Cdd:PRK12406   438 AEFGEALMAV---VEpqpgaTLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2675-3019 7.04e-22

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 100.63  E-value: 7.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 LAYIIYTSGTTGRPKGVMVEHKG-IANTLQWRRNAyAFNETDTIL-QLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKD 2752
Cdd:cd05944      4 VAAYFHTGGTTGTPKLAQHTHSNeVYNAWMLALNS-LFDPDDVLLcGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2753 ILAIKH---QLSRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARslaICPHTELA--NEYGPTENS 2827
Cdd:cd05944     83 PGLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRAR---FEDATGLPvvEGYGLTEAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2828 VATTVMRHMEKQAYVSIGQPIDGTQVLILNSN---HQLQPIGV--AGELCIAGTGLARGYVNlPELTERAFTQNpfkpea 2902
Cdd:cd05944    160 CLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDgvgRLLRDCAPdeVGEICVAGPGVFGGYLY-TEGNKNAFVAD------ 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2903 RMYRTGDAARWMADGTLEYLGRIDDQVkIR-GYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLS-- 2979
Cdd:cd05944    233 GWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVve 311

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 2980 ----TNAVRSELQNKLPVfmhPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05944    312 eeelLAWARDHVPERAAV---PKHIEVLEELPVTAVGKVFKPAL 352
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
2527-3019 8.62e-22

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 102.82  E-value: 8.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2527 ANQYgvQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSR-GVKPDTPVGIMMHRSFSMIASILGVWK 2605
Cdd:PRK08974    19 PDRY--QSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2606 AGGCYVPIDPEY-PKERKrYILSDSGTKLLMtineadlgVLADFEGeilTIESVEEDD---------------------- 2662
Cdd:PRK08974    97 AGMIVVNVNPLYtPRELE-HQLNDSGAKAIV--------IVSNFAH---TLEKVVFKTpvkhviltrmgdqlstakgtlv 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2663 ------------KSPLPQ---MSSAHH----------------LAYIIYTSGTTGRPKGVMVEHKG-IANTLQWRRNAYA 2710
Cdd:PRK08974   165 nfvvkyikrlvpKYHLPDaisFRSALHkgrrmqyvkpelvpedLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAKAAYGP 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2711 FNETD-----TILQL---FSFSFDGFitsMFTPLlsGAKAVLLheEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDvv 2782
Cdd:PRK08974   245 LLHPGkelvvTALPLyhiFALTVNCL---LFIEL--GGQNLLI--TNPRDIPGFVKELKKYPFTAITGVNTLFNALLN-- 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2783 QPE----DVKTLRVVTLAGEAADRELIARSLAICpHTELANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNS 2858
Cdd:PRK08974   316 NEEfqelDFSSLKLSVGGGMAVQQAVAERWVKLT-GQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDD 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2859 NHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVET 2938
Cdd:PRK08974   395 DGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2939 KEIESVIRCIKGVKDAAV--VAHvTASGQTeLSAYVVTK-PGLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:PRK08974   468 NEIEDVVMLHPKVLEVAAvgVPS-EVSGEA-VKIFVVKKdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKIL 545


                   ....
gi 1678550997 3016 RGAL 3019
Cdd:PRK08974   546 RREL 549
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 470-947 8.69e-22

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: 102.38  E-value: 8.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA 549
Cdd:cd12118     11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  550 DRIRYILHDCGCSHVvsqahlpsslednyIITHPEDIESKVDGSN----IKSVNNADDLLYMIYTSGTTGKPKGVQFEHR 625
Cdd:cd12118     91 EEIAFILRHSEAKVL--------------FVDREFEYEDLLAEGDpdfeWIPPADEWDPIALNYTSGTTGRPKGVVYHHR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  626 N-----MANLLKFEYTHSGidfeadVLQFATPSFDV---CYQEIFSALlkGGTlHIVPEAIkrDVPQLFAFINKHQ-TNI 696
Cdd:cd12118    157 GaylnaLANILEWEMKQHP------VYLWTLPMFHCngwCFPWTVAAV--GGT-NVCLRKV--DAKAIYDLIEKHKvTHF 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  697 VFLPTAFIKMIFSERELANSFPDGVK----------HLIAAGEQLmisdlfqdvlrkrGIHLHNHYGPSET---HVVSTY 763
Cdd:cd12118    226 CGAPTVLNMLANAPPSDARPLPHRVHvmtagapppaAVLAKMEEL-------------GFDVTHVYGLTETygpATVCAW 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  764 TihpgDPIPELPP---------IGKP-IGCTDLYILNHQKQlQPcgVP------GELYISGASVARGYVNHDKLTSDKFS 827
Cdd:cd12118    293 K----PEWDELPTeerarlkarQGVRyVGLEEVDVLDPETM-KP--VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAFR 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  828 SDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEhELCAYyc 906
Cdd:cd12118    366 GG-------WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGE-VPCAF-- 435

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1678550997  907 sV-----QKLNTIDLRSYMASELPEYMIPaKWIWVDSIPLTPNGKV 947
Cdd:cd12118    436 -VelkegAKVTEEEIIAFCREHLAGFMVP-KTVVFGELPKTSTGKI 479
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2677-3015 1.09e-21

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 100.15  E-value: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 YIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTP-------------LLSGAKAV 2743
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPplmhgtgswtafgGLLGGQTV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2744 LLHEEE--AKDILAIKHqlsRQRITHMIIV-PVLYRALLDVVQ---PEDVKTLRVVTLAGEAADRELIARSLAICPHTEL 2817
Cdd:cd05924     87 VLPDDRfdPEEVWRTIE---KHKVTSMTIVgDAMARPLIDALRdagPYDLSSLFAISSGGALLSPEVKQGLLELVPNITL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2818 ANEYGPTENSvatTVMRHMEKQAYVSIG--QPIDGTQVLILNSNHQLQPiGVAGELCIAGTGL-ARGYVNLPELTERAFt 2894
Cdd:cd05924    164 VDAFGSSETG---FTGSGHSAGSGPETGpfTRANPDTVVLDDDGRVVPP-GSGGVGWIARRGHiPLGYYGDEAKTAETF- 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2895 qnPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVT 2974
Cdd:cd05924    239 --PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 2975 KPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:cd05924    317 REGagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1493-1977 1.20e-21

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 102.58  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1493 NQTLHYALEQQAEKTPDQAAVIFED-GV-MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:PRK08315    15 EQTIGQLLDRTAARYPDREALVYRDqGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYPEERISFLLEDSGTNILL----------------------------LQSAGLhvPEFTgEIVYLNQTNSG-- 1620
Cdd:PRK08315    95 LVTINPAYRLSELEYALNQSGCKALIaadgfkdsdyvamlyelapelatcepgqLQSARL--PELR-RVIFLGDEKHPgm 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1621 --------LAHRLSNPNVDVLPQSLAY--VI---YTSGSTGMPKGVEIEHRsavNFLN---SLQSRYQLKHSD------- 1677
Cdd:PRK08315   172 lnfdellaLGRAVDDAELAARQATLDPddPIniqYTSGTTGFPKGATLTHR---NILNngyFIGEAMKLTEEDrlcipvp 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1678 ------MIM-------HktsysfdasiwelfwwpyaGAS-VYLLPqggEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEH 1743
Cdd:PRK08315   249 lyhcfgMVLgnlacvtH-------------------GATmVYPGE---GFDPLATLAAVEEERCTALYGVPTMFIAELDH 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1744 IKYRS---------------VPIKTnrLKRVfsggeqlgthlVSRFYelLPNVSItnSYGPTEAT-VeaaFFDCPPHEKL 1807
Cdd:PRK08315   307 PDFARfdlsslrtgimagspCPIEV--MKRV-----------IDKMH--MSEVTI--AYGMTETSpV---STQTRTDDPL 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1808 ER--IPIGKPVHHVRLYLLN-QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFypgerMYkTGDVARWLPD 1884
Cdd:PRK08315   367 EKrvTTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----MH-TGDLAVMDEE 440

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1885 GNVEFLGRTDDQVkIR-GYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRA----QLE 1952
Cdd:PRK08315   441 GYVNIVGRIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVGVPDEkyGE-EVCAWIilrPGatLTEEDVRDfcrgKIA 518

                          570       580
                   ....*....|....*....|....*
gi 1678550997 1953 RllpgYMVPAYMIEMEQWPVTPSGK 1977
Cdd:PRK08315   519 H----YKIPRYIRFVDEFPMTVTGK 539
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 2559-2930 1.37e-21

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: 102.29  E-value: 1.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVK--PDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMt 2636
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 ineADLGVladfegEILTIESVEE---DDKSPLPQmSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTL-----QWRRnA 2708
Cdd:cd05927     85 ---CDAGV------KVYSLEEFEKlgkKNKVPPPP-PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfkILEI-L 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2709 YAFNETDTilqLFSF-----SFDGFITSMFtpLLSGAK---------------AVL--------------LHE-----EE 2749
Cdd:cd05927    154 NKINPTDV---YISYlplahIFERVVEALF--LYHGAKigfysgdirlllddiKALkptvfpgvprvlnrIYDkifnkVQ 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2750 AKDIL-------AIKHQLSRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELI--ARSLAICPHTElanE 2820
Cdd:cd05927    229 AKGPLkrklfnfALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLefLRVALGCPVLE---G 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2821 YGPTENSVATTVMRHMEKqAYVSIGQPIDGTQV-LI----LNSNHQLQPigVAGELCIAGTGLARGYVNLPELTERAFTQ 2895
Cdd:cd05927    306 YGQTECTAGATLTLPGDT-SVGHVGGPLPCAEVkLVdvpeMNYDAKDPN--PRGEVCIRGPNVFSGYYKDPEKTAEALDE 382

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1678550997 2896 NPFkpearmYRTGDAARWMADGTLeylgRIDDQVK 2930
Cdd:cd05927    383 DGW------LHTGDIGEWLPNGTL----KIIDRKK 407
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 489-890 1.55e-21

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: 100.72  E-value: 1.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRyilhdcgcSHVVSQA 568
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLR--------DRVDRGG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDNyiiTHpedieskvdgsniksvnnADDLLYMIYTSGTTGKPKGVQFEHRNM-ANLLKFEYtHSGIDfEADV- 646
Cdd:cd05974     73 AVYAAVDEN---TH------------------ADDPMLLYFTSGTTSKPKLVEHTHRSYpVGHLSTMY-WIGLK-PGDVh 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  647 LQFATPSF-DVCYQEIFSALLKGGTLHIVPEAiKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSErELAnSFPDGVKHLI 725
Cdd:cd05974    130 WNISSPGWaKHAWSCFFAPWNAGATVFLFNYA-RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-DLA-SFDVKLREVV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  726 AAGEQLMiSDLFQDVLRKRGIHLHNHYGPSETHVVSTYTihPGDPIpELPPIGKPIGCTDLYILNhqkqlqPCGVP---G 802
Cdd:cd05974    207 GAGEPLN-PEVIEQVRRAWGLTIRDGYGQTETTALVGNS--PGQPV-KAGSMGRPLPGYRVALLD------PDGAPateG 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  803 ELYIS-----GASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVT 877
Cdd:cd05974    277 EVALDlgdtrPVGLMKGYAGDPDKTAHAMRGG-------YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESV 349

                          410
                   ....*....|...
gi 1678550997  878 LMNHPDISEAAIL 890
Cdd:cd05974    350 LIEHPAVAEAAVV 362
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 2533-3021 2.36e-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: 101.59  E-value: 2.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKA----SALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGG 2608
Cdd:cd05906     10 RTLLELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2609 --CYVPIDPEYPKERKR--------------YILSDSGTKLLMTINEADLGVLADfegEILTIESVEEDDKSPLPQMSSA 2672
Cdd:cd05906     90 vpAPLTVPPTYDEPNARlrklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGI---RVLSIEELLDTAADHDLPQSRP 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2673 HHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDGFITSM-FTPLLSGAKAVLLHEEEak 2751
Cdd:cd05906    167 DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEE-- 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2752 dILAIKHQ----LSRQRITHMIIVPVLYRALLDVV-----QPEDVKTLRVVTLAGEAADRELIARSLAI-----CPHTEL 2817
Cdd:cd05906    245 -ILADPLRwldlIDRYRVTITWAPNFAFALLNDLLeeiedGTWDLSSLRYLVNAGEAVVAKTIRRLLRLlepygLPPDAI 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2818 ANEYGPTENSVATTVMRHMEKQA------YVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTER 2891
Cdd:cd05906    324 RPAFGMTETCSGVIYSRSFPTYDhsqaleFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAE 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2892 AFTqnpfkpEARMYRTGDAArWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKD--AAVVAHVTASGQTE-- 2967
Cdd:cd05906    404 AFT------EDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEel 476

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2968 ----LSAYVVTKPGLSTN-AVRSELQNKLPVfmHPAFIEKL--DSLPLSPNGKLDRGALPK 3021
Cdd:cd05906    477 aiffVPEYDLQDALSETLrAIRSVVSREVGV--SPAYLIPLpkEEIPKTSLGKIQRSKLKA 535
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 1635-1983 2.40e-21

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 101.46  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 QSLAYVIYTSGSTGMPKGVEIEHRsavNFLNSLQ-------SRYQLKHSDMIMHKTSYSFDASIWELFWWPYA--GASVY 1705
Cdd:PLN02574   198 DDVAAIMYSSGTTGASKGVVLTHR---NLIAMVElfvrfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLslGSTIV 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1706 LLPQGGEKEpevIAKAIEEQKITAMHFVPSMLHAFLEHIK-YRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLPNVSIT 1784
Cdd:PLN02574   275 VMRRFDASD---MVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKS--LKQVSCGAAPLSGKFIQDFVQTLPHVDFI 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1785 NSYGPTEAT-VEAAFFDCPPHEKLERIPIGKPVHHVRLYLLNQNQrMLPVGCIGELYIAGAGVARGYLNRPALTEERFLE 1863
Cdd:PLN02574   350 QGYGMTESTaVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGC-LLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1864 DPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL-CAYV--- 1939
Cdd:PLN02574   429 DGWL------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIpVAFVvrr 502

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1678550997 1940 --EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PLN02574   503 qgSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 2675-3019 3.42e-21

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: 101.06  E-value: 3.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 LAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRN---AYAFNETDTILQLFSFsFDGFitSMFTPL---LSGAKAVLLHEE 2748
Cdd:cd17642    186 VALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQIIPDTAILTVIPF-HHGF--GMFTTLgylICGFRVVLMYKF 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2749 EAKDILAikhQLSRQRITHMIIVPVLYRALL--DVVQPEDVKTLRVVTLAGEAADREL---IARSLAIcphTELANEYGP 2823
Cdd:cd17642    263 EEELFLR---SLQDYKVQSALLVPTLFAFFAksTLVDKYDLSNLHEIASGGAPLSKEVgeaVAKRFKL---PGIRQGYGL 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2824 TENSVATTVMRHME-KQAYVSIGQPIDGTQVLILNSNHQLQPiGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpea 2902
Cdd:cd17642    337 TETTSAILITPEGDdKPGAVGKVVPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKALIDKDGW---- 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2903 rmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAvVAHVTASGQTEL-SAYVVTKPGLSTN 2981
Cdd:cd17642    412 --LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAG-VAGIPDEDAGELpAAVVVLEAGKTMT 488

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 2982 avRSELQNKLPVFMHPAF-----IEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd17642    489 --EKEVMDYVASQVSTAKrlrggVKFVDEVPKGLTGKIDRRKI 529
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 2556-3016 3.83e-21

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 101.13  E-value: 3.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2556 DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI----DPEYPKERkryiLSDSGT 2631
Cdd:PRK04319    71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDR----LEDSEA 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2632 KLLMTINEADLGVLAD----FEGEILTIESVEEDDKS-PLPQ-MSSAHH-----------LAYIIYTSGTTGRPKGVMVE 2694
Cdd:PRK04319   147 KVLITTPALLERKPADdlpsLKHVLLVGEDVEEGPGTlDFNAlMEQASDefdiewtdredGAILHYTSGSTGKPKGVLHV 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2695 HKgiANTLQWRRNAYA--FNETDtilqLFSFSFD-GFITSM----FTPLLSGAKAVLLHEE-EAKDILAIkhqLSRQRIT 2766
Cdd:PRK04319   227 HN--AMLQHYQTGKYVldLHEDD----VYWCTADpGWVTGTsygiFAPWLNGATNVIDGGRfSPERWYRI---LEDYKVT 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2767 HMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAADRELI---ARSLAICPH-----TE-----LANEYGptensva 2829
Cdd:PRK04319   298 VWYTAPTAIRMLMgagdDLVKKYDLSSLRHILSVGEPLNPEVVrwgMKVFGLPIHdnwwmTEtggimIANYPA------- 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2830 ttvmrhME-KQAyvSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAgTG---LARGYVNLPELTERAFTQNpfkpearMY 2905
Cdd:PRK04319   371 ------MDiKPG--SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAGD-------WY 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2906 RTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAH---VTasGQTeLSAYVVTKPGL-STN 2981
Cdd:PRK04319   435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKpdpVR--GEI-IKAFVALRPGYePSE 511

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1678550997 2982 AVRSELQN----KLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:PRK04319   512 ELKEEIRGfvkkGLGAHAAPREIEFKDKLPKTRSGKIMR 550
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 1496-1983 4.04e-21

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: 100.68  E-value: 4.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LHYALEQQAeKTPDqaAVIFEDGV----MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAY 1571
Cdd:cd17642     20 LHKAMKRYA-SVPG--TIAFTDAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1572 LPIDPDYPEERISFLLEDSGTNILLLQSAGLH--------VPeFTGEIVYLN--------QTNSGLAHRLSNPNVDVLP- 1634
Cdd:cd17642     97 APTNDIYNERELDHSLNISKPTIVFCSKKGLQkvlnvqkkLK-IIKTIIILDskedykgyQCLYTFITQNLPPGFNEYDf 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 --------QSLAYVIYTSGSTGMPKGVEIEHRsavNFLNSLQSRYQLKHSDMIMHKTS--------YSFdaSIWELFWWP 1698
Cdd:cd17642    176 kppsfdrdEQVALIMNSSGSTGLPKGVQLTHK---NIVARFSHARDPIFGNQIIPDTAiltvipfhHGF--GMFTTLGYL 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 YAGASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHI---KYrsvpiKTNRLKRVFSGGEQL----GTHLV 1771
Cdd:cd17642    251 ICGFRVVLMYK---FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlvdKY-----DLSNLHEIASGGAPLskevGEAVA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1772 SRFYelLPnvSITNSYGPTEATVEAAFF---DCPPHEkleripIGK--PVHHVRLY------LLNQNQRmlpvgciGELY 1840
Cdd:cd17642    323 KRFK--LP--GIRQGYGLTETTSAILITpegDDKPGA------VGKvvPFFYAKVVdldtgkTLGPNER-------GELC 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1841 IAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 1920
Cdd:cd17642    386 VKGPMIMKGYVNNPEATKALIDKDGWL------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1921 EAAVTVRTDSGEPELCAYV----EGLQRNE------VRAQL---ERLLPGymvpayMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd17642    460 DAGVAGIPDEDAGELPAAVvvleAGKTMTEkevmdyVASQVstaKRLRGG------VKFVDEVPKGLTGKIDRRKI 529
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 3151-3566 5.44e-21

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: 98.99  E-value: 5.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3151 SVQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQYNRPLSHSDDALyglqmIDLSAPDGtdgnrPYEPLIKRHVLDIQQ 3230
Cdd:cd19539     35 PLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEV-----RDLSDPDS-----DRERRLEELLRERES 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3231 K-MDLKNGPLLQAGLF-HTIDGDFLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYAKKLSDYAE 3308
Cdd:cd19539    105 RgFDLDEEPPIRAVLGrFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPELRQQYKEYAAWQREALA 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3309 SQQLMKQLKYWREA-EEYQTEALPFDQidgTRAHEGQRST--ISFTLNDKETAALLKDANSAYNTDTQdMLLASVILALR 3385
Cdd:cd19539    185 APRAAELLDFWRRRlRGAEPTALPTDR---PRPAGFPYPGadLRFELDAELVAALRELAKRARSSLFM-VLLAAYCVLLR 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3386 HWTNQSafklsleghgreDVLKGIDVS--------RTIGWFTAIYPLLIKLNaDLPDSEESMVHVLKTTKDTLR--RVPd 3455
Cdd:cd19539    261 RYTGQT------------DIVVGTPVAgrnhprfeSTVGFFVNLLPLRVDVS-DCATFRDLIARVRKALVDAQRhqELP- 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3456 kgfgygvIKYLTPPGKKDINFTGAP--EISFnylgQFESGRTAEVPEEDAFSFSPlgaGGDISTTwnreQSLDISAIAAE 3533
Cdd:cd19539    327 -------FQQLVAELPVDRDAGRHPlvQIVF----QVTNAPAGELELAGGLSYTE---GSDIPDG----AKFDLNLTVTE 388

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1678550997 3534 --GKLTVNMTYDNARFQRKTIEQLSETCRQFLLQL 3566
Cdd:cd19539    389 egTGLRGSLGYATSLFDEETIQGFLADYLQVLRQL 423
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 463-949 5.87e-21

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 100.46  E-value: 5.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVP 542
Cdd:PRK05605    32 TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  543 VDPHYPADRIRYILHDCGC----------------------SHVVS---------------QAHLPSSLEDNYIITHP-- 583
Cdd:PRK05605   112 HNPLYTAHELEHPFEDHGArvaivwdkvaptverlrrttplETIVSvnmiaampllqrlalRLPIPALRKARAALTGPap 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  584 --EDIESKVDGSNIKSVN-------NADDLLYMIYTSGTTGKPKGVQFEHRN-MANLLKFEYTHSGIDFEADVLQFATPS 653
Cdd:PRK05605   192 gtVPWETLVDAAIGGDGSdvshprpTPDDVALILYTSGTTGKPKGAQLTHRNlFANAAQGKAWVPGLGDGPERVLAALPM 271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  654 FDV-----CyqeIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIV-FLPTAFIKMIFSERE-------LANSFpDG 720
Cdd:PRK05605   272 FHAygltlC---LTLAVSIGGELVLLP---APDIDLILDAMKKHPPTWLpGVPPLYEKIAEAAEErgvdlsgVRNAF-SG 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  721 VKHLIAAgeqlmISDLFQDVlrkRGIHLHNHYGPSETHVVSTytihpGDPI-PELPP--IGKPIGCTDLYILNHQK--QL 795
Cdd:PRK05605   345 AMALPVS-----TVELWEKL---TGGLLVEGYGLTETSPIIV-----GNPMsDDRRPgyVGVPFPDTEVRIVDPEDpdET 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  796 QPCGVPGELYISGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:PRK05605   412 MPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVE 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  876 VTLMNHPDISEAAILIWQDQNGEHELCAyyCSVqkLN---TID---LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:PRK05605   485 EVLREHPGVEDAAVVGLPREDGSEEVVA--AVV--LEpgaALDpegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 1495-1892 6.82e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 100.51  E-value: 6.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIFEDGV------MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAG 1568
Cdd:PRK12582    50 SIPHLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1569 GAYLPIDPDYP-----EERISFLLEDSGTNILLLQSA-----GLHVPEFTG-EIVYLNQTNSG-----LAHRLSNPNVD- 1631
Cdd:PRK12582   130 VPAAPVSPAYSlmshdHAKLKHLFDLVKPRVVFAQSGapfarALAALDLLDvTVVHVTGPGEGiasiaFADLAATPPTAa 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1632 -------VLPQSLAYVIYTSGSTGMPKGVEIEHRS-AVNFLNSLQSRYQL---KHSD----MIMHKTS---YSFDASIWE 1693
Cdd:PRK12582   210 vaaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMmCANIAMQEQLRPREpdpPPPVsldwMPWNHTMggnANFNGLLWG 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1694 lfwwpyaGASVYLlpQGGEKEPEVIAKAIE---EQKITAMHFVPSMLHAFLEHIKYRSVPIKT--NRLKRVFSGGEQLGT 1768
Cdd:PRK12582   290 -------GGTLYI--DDGKPLPGMFEETIRnlrEISPTVYGNVPAGYAMLAEAMEKDDALRRSffKNLRLMAYGGATLSD 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1769 HLVSRFYELL-----PNVSITNSYGPTeatvEAAFFDCPPHEKLERIP-IGKPVHHVRLyllnqnqRMLPVGCIGELYIA 1842
Cdd:PRK12582   361 DLYERMQALAvrttgHRIPFYTGYGAT----ETAPTTTGTHWDTERVGlIGLPLPGVEL-------KLAPVGDKYEVRVK 429

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1843 GAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWL-PDGNVE---FLGR 1892
Cdd:PRK12582   430 GPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdPDDPEKgliFDGR 477
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1493-1983 7.21e-21

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 99.76  E-value: 7.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1493 NQTLHYALEQQAEKTPDQAAVIFED--GVM---TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKA 1567
Cdd:PRK08008     6 GQHLRQMWDDLADVYGHKTALIFESsgGVVrrySYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1568 GGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGL----------------------HVPEFTGEIVY---LNQTNSGLA 1622
Cdd:PRK08008    86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYpmyrqiqqedatplrhicltrvALPADDGVSSFtqlKAQQPATLC 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1623 HR--LSNPNVdvlpqslAYVIYTSGSTGMPKGVEIEHrsaVNFLNS-LQSRYQ--LKHSDMIMH-KTSYSFDASIWELFW 1696
Cdd:PRK08008   166 YAppLSTDDT-------AEILFTSGTTSRPKGVVITH---YNLRFAgYYSAWQcaLRDDDVYLTvMPAFHIDCQCTAAMA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1697 WPYAGASVYLLpqggEK-EPEVIAKAIEEQKITAMHFVPSMLHAFLehIKYRSVPIKTNRLKRVF-----SGGEQLGthL 1770
Cdd:PRK08008   236 AFSAGATFVLL----EKySARAFWGQVCKYRATITECIPMMIRTLM--VQPPSANDRQHCLREVMfylnlSDQEKDA--F 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1771 VSRFyellpNVSITNSYGPTEaTVEAAFFDCPPHEKleRIP-IGKPVHHVRLYLLNQNQRMLPVGCIGELYI---AGAGV 1846
Cdd:PRK08008   308 EERF-----GVRLLTSYGMTE-TIVGIIGDRPGDKR--RWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTI 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1847 ARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTV 1926
Cdd:PRK08008   380 FKEYYLDPKATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVG 453

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1927 RTDSGEPE-LCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK08008   454 IKDSIRDEaIKAFVvlnegETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK08315 PRK08315
AMP-binding domain protein; Validated
 463-947 1.45e-20

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 99.11  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKTPDAHAVI--DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAI----------MMERSAafitgv 530
Cdd:PRK08315    16 QTIGQLLDRTAARYPDREALVyrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIwapnvpewvlTQFATA------ 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  531 lgilKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSledNYIIT-----------HPEDIESK---------- 589
Cdd:PRK08315    90 ----KIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDS---DYVAMlyelapelatcEPGQLQSArlpelrrvif 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  590 ----------------VDGSN--------IKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMAN-------LLKFEyths 638
Cdd:PRK08315   163 lgdekhpgmlnfdellALGRAvddaelaaRQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNngyfigeAMKLT---- 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  639 gidfEADVLQFATPSFDvCyqeiF-------SALLKGGTLHIVPEAIkrDVPQLFAFINKHQTNIVF-LPTAFIKMI--- 707
Cdd:PRK08315   239 ----EEDRLCIPVPLYH-C----FgmvlgnlACVTHGATMVYPGEGF--DPLATLAAVEEERCTALYgVPTMFIAELdhp 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  708 -FSERELAnSFPDGvkhlIAAG----EQLMisdlfQDVLRKrgIHLHN---HYGPSETHVVSTYTiHPGDPI-------- 771
Cdd:PRK08315   308 dFARFDLS-SLRTG----IMAGspcpIEVM-----KRVIDK--MHMSEvtiAYGMTETSPVSTQT-RTDDPLekrvttvg 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  772 ---PEL------PPIGKPIgctdlyilnhqkqlqPCGVPGELYISGASVARGYVNhdkltsdkfssDPFKP-DVI----- 836
Cdd:PRK08315   375 ralPHLevkivdPETGETV---------------PRGEQGELCTRGYSVMKGYWN-----------DPEKTaEAIdadgw 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  837 MyRTGDLARRLEDGNIEYIGRADNQVkIR-GYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEhELCAYycsV-----Q 909
Cdd:PRK08315   429 M-HTGDLAVMDEEGYVNIVGRIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVGVPDEKyGE-EVCAW---IilrpgA 502

                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1678550997  910 KLNTIDLRSYMASELPEYMIPaKWIW-VDSIPLTPNGKV 947
Cdd:PRK08315   503 TLTEEDVRDFCRGKIAHYKIP-RYIRfVDEFPMTVTGKI 540
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 470-960 1.85e-20

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 98.51  E-value: 1.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVIDQAcsLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA 549
Cdd:PLN02330    39 ELYADKVAFVEAVTGKA--VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  550 DRIRYILHDCGCSHVVSQA---HLPSSLEDNYIITHPEDIESKVDGSNIksVNNAD--------------DLLYMIYTSG 612
Cdd:PLN02330   117 SEIKKQAEAAGAKLIVTNDtnyGKVKGLGLPVIVLGEEKIEGAVNWKEL--LEAADragdtsdneeilqtDLCALPFSSG 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  613 TTGKPKGVQFEHRNM-ANLLKfeyTHSGIDFEAdVLQFAT----PSFDV------CyqeiFSALLKGGTLHIVPEAIKRD 681
Cdd:PLN02330   195 TTGISKGVMLTHRNLvANLCS---SLFSVGPEM-IGQVVTlgliPFFHIygitgiC----CATLRNKGKVVVMSRFELRT 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  682 VpqLFAFINKHQTNIVFLPTAFIKM----IFSERELANSfpdGVKHLIAAGEQLMiSDLFQDVLRK-RGIHLHNHYGPSE 756
Cdd:PLN02330   267 F--LNALITQEVSFAPIVPPIILNLvknpIVEEFDLSKL---KLQAIMTAAAPLA-PELLTAFEAKfPGVQVQEAYGLTE 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  757 tHvvSTYTIHPGDP-----IPELPPIGKPIGCTDLYILNHQKQLQ-PCGVPGELYISGASVARGYVNHDKLTSDKFSSDP 830
Cdd:PLN02330   341 -H--SCITLTHGDPekghgIAKKNSVGFILPNLEVKFIDPDTGRSlPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDG 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  831 FkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GE-HELCAYYCSV 908
Cdd:PLN02330   418 W------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEaGEiPAACVVINPK 491

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997  909 QKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASIS 960
Cdd:PLN02330   492 AKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2110-2496 1.85e-20

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: 97.32  E-value: 1.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2110 YNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGdPVQRIHDEV--PFTLQTTVLGARTEQEAAAAFI---- 2183
Cdd:cd19534     22 FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGG-WQQRIRGDVeeLFRLEVVDLSSLAQAAAIEALAaeaq 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2184 KPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFGELYNN---RKLPAL--RIQYKDYAVWQEGFKTG 2258
Cdd:cd19534    101 SSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQalaGEPIPLpsKTSFQTWAELLAEYAQS 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2259 DAYKMQEAYWLKQLEGELPvlDLPADHarpPVRSFAGDKVSFTLEPE-VASGLHKLARENGSTLYMVLLAAYTAFLSRLS 2337
Cdd:cd19534    181 PALLEELAYWRELPAADYW--GLPKDP---EQTYGDARTVSFTLDEEeTEALLQEANAAYRTEINDLLLAALALAFQDWT 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2338 GQEDIIVGSPIAGR----PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRE----------------------TAL 2391
Cdd:cd19534    256 GRAPPAIFLEGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEqlrripnkgigygilryltpegTKR 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2392 EAFEHQ-----NYpfeelvdkLELTRDMSRNPVFDAMLVVQnndyePLHLHDLQMKpaqvshLVSKFDLTLQASegDGNI 2466
Cdd:cd19534    336 LAFHPQpeisfNY--------LGQFDQGERDDALFVSAVGG-----GGSDIGPDTP------RFALLDINAVVE--GGQL 394

                          410       420       430
                   ....*....|....*....|....*....|
gi 1678550997 2467 HFLFEYSTALFEKTTIERWASHLTNVLSII 2496
Cdd:cd19534    395 VITVSYSRNMYHEETIQQLADSYKEALEAL 424
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 2556-3006 2.16e-20

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: 97.42  E-value: 2.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2556 DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDpeypkerkryilsdsgTKLlm 2635
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN----------------YNL-- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2636 tineadlgvladfEGEILTiESVeeddksplpQMSSAHHL----AYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAF 2711
Cdd:cd05940     63 -------------RGESLA-HCL---------NVSSAKHLvvdaALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGA 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2712 NETDTI---LQLFSFSfdGFITSMFTPLLSGAKAVLLHEEEAKDIL--AIKHQlsrqrITHMIIVPVLYRALLDVVQPED 2786
Cdd:cd05940    120 LPSDVLytcLPLYHST--ALIVGWSACLASGATLVIRKKFSASNFWddIRKYQ-----ATIFQYIGELCRYLLNQPPKPT 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2787 VK--TLRVVTLAGEAAD--RELIARsLAICPHTELaneYGPTENSVAT--------TVMRHMEKQAYVS----------I 2844
Cdd:cd05940    193 ERkhKVRMIFGNGLRPDiwEEFKER-FGVPRIAEF---YAATEGNSGFinffgkpgAIGRNPSLLRKVAplalvkydleS 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2845 GQPIDGTQVLILNSnhqlqPIGVAGELCIAGTGLAR--GYVNlPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYL 2922
Cdd:cd05940    269 GEPIRDAEGRCIKV-----PRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFV 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2923 GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV--VAHVTASGQTELSAyVVTKPGLSTN--AVRSELQNKLPVFMHPA 2998
Cdd:cd05940    343 DRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAA-IVLQPNEEFDlsALAAHLEKNLPGYARPL 421


                   ....*...
gi 1678550997 2999 FIEKLDSL 3006
Cdd:cd05940    422 FLRLQPEM 429
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 1517-1961 2.45e-20

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: 97.42  E-value: 2.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1517 DGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAylpidpdypeerisflledsgtnill 1596
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-------------------------- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1597 lqsaglhvpefTGEIVYlNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHS 1676
Cdd:cd05940     55 -----------AALINY-NLRGESLAHCLNVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1677 DMIM------HKTS--YSFDASIwelfwwpYAGASVyllpqggekepeVIAKaieeqKITAMHFVPsmlhaflEHIKYRS 1748
Cdd:cd05940    123 DVLYtclplyHSTAliVGWSACL-------ASGATL------------VIRK-----KFSASNFWD-------DIRKYQA 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1749 VPI-------------------KTNRLKRVFSGGeqLGTHLVSRFYELLPNVSITNSYGPTEATVE---------AAFFD 1800
Cdd:cd05940    172 TIFqyigelcryllnqppkpteRKHKVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATEGNSGfinffgkpgAIGRN 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1801 CPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVG------CIGElyIAGAGVARGYLNrPALTEERFLEDPFYPGERMYK 1874
Cdd:cd05940    250 PSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPrgepglLISR--INPLEPFDGYTD-PAATEKKILRDVFKKGDAWFN 326

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1875 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA---AVTVRTDSGEPELCAYV----EGLQRNEV 1947
Cdd:cd05940    327 TGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEAnvyGVQVPGTDGRAGMAAIVlqpnEEFDLSAL 406

                          490
                   ....*....|....
gi 1678550997 1948 RAQLERLLPGYMVP 1961
Cdd:cd05940    407 AAHLEKNLPGYARP 420
PLN02246 PLN02246
4-coumarate--CoA ligase
 2541-3016 2.56e-20

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 98.13  E-value: 2.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2541 QQAARTPKASALVSGD--KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEY- 2617
Cdd:PLN02246    31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2618 PKERKRYILSdSGTKLLMTiNEADLGVLADFEGE----ILTIESVEE----------DDKSPLPQMS-SAHHLAYIIYTS 2682
Cdd:PLN02246   111 PAEIAKQAKA-SGAKLIIT-QSCYVDKLKGLAEDdgvtVVTIDDPPEgclhfseltqADENELPEVEiSPDDVVALPYSS 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2683 GTTGRPKGVMVEHKGIANTLQWR-----RNAYaFNETDTI---LQLFS-FSFDgfiTSMFTPLLSGAKAVLLHEEEakdI 2753
Cdd:PLN02246   189 GTTGLPKGVMLTHKGLVTSVAQQvdgenPNLY-FHSDDVIlcvLPMFHiYSLN---SVLLCGLRVGAAILIMPKFE---I 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2754 LAIKHQLSRQRITHMIIVP--VLYRALLDVVQPEDVKTLRVVtLAGEAA-DRELIARSLAICPHTELANEYGPTEN---- 2826
Cdd:PLN02246   262 GALLELIQRHKVTIAPFVPpiVLAIAKSPVVEKYDLSSIRMV-LSGAAPlGKELEDAFRAKLPNAVLGQGYGMTEAgpvl 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2827 --SVA-------------TTVMRHMEkqayVSIGQPIDGTQVlilnsnhqlqPIGVAGELCIAGTGLARGYVNLPELTER 2891
Cdd:PLN02246   341 amCLAfakepfpvksgscGTVVRNAE----LKIVDPETGASL----------PRNQPGEICIRGPQIMKGYLNDPEATAN 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2892 AFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHV-TASGQTELsA 2970
Cdd:PLN02246   407 TIDKDGW------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKdEVAGEVPV-A 479

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2971 YVVTKPG--LSTNAVRsELQNKLPVF---MHPAFIekLDSLPLSPNGKLDR 3016
Cdd:PLN02246   480 FVVRSNGseITEDEIK-QFVAKQVVFykrIHKVFF--VDSIPKAPSGKILR 527
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2559-2977 2.70e-20

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


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 96.87  E-value: 2.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPidpeypkerkryilsdsGTKLLmtiN 2638
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-----------------ATTLL---T 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 EADLGVLADFEGEilTIESVEEDDKSPLPQMssahhlayIIYTSGTTGRPKGVMVEHK----GIANTLQW---RRNAYAF 2711
Cdd:cd05974     61 PDDLRDRVDRGGA--VYAAVDENTHADDPML--------LYFTSGTTSKPKLVEHTHRsypvGHLSTMYWiglKPGDVHW 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2712 NETDTILQLFSFSfdgfitSMFTPLLSGAKAVLLHEE--EAKDILAikhQLSRQRITHMIIVPVLYRALLDvvqpEDVKT 2789
Cdd:cd05974    131 NISSPGWAKHAWS------CFFAPWNAGATVFLFNYArfDAKRVLA---ALVRYGVTTLCAPPTVWRMLIQ----QDLAS 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2790 LRV----VTLAGEAADRELIARSLAICPHTeLANEYGPTENsvaTTVMRHMEKQAYV--SIGQPIDGTQVLILNsnhqlq 2863
Cdd:cd05974    198 FDVklreVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTET---TALVGNSPGQPVKagSMGRPLPGYRVALLD------ 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2864 PIGVA---GELCIA-----GTGLARGYVNLPELTERAFtqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYR 2935
Cdd:cd05974    268 PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR 340

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 2936 VETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG 2977
Cdd:cd05974    341 ISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG 382
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1493-1985 2.79e-20

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 98.95  E-value: 2.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1493 NQTLHYALEQQAEKT--PDQAAVIFEDgVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:PRK06060     3 NGNLAGLLAEQASEAgwYDRPAFYAAD-VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYPEERISFLLEDsgTNILLLQSAGLHVPEFTGEIVYLNQTNSGLAHRLSNPNVDVLP-QSLAYVIYTSGSTGM 1649
Cdd:PRK06060    82 AFLANPELHRDDHALAARN--TEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGgDALAYATYTSGTTGP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1650 PKGVEIEHRSAVNFLNSL-QSRYQLKHSDMIMHKTSYSFDASIWELFWWPYA---GASVYLLPQGGEKEPEVIAKaieeq 1725
Cdd:PRK06060   160 PKAAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLAtggSAVINSAPVTPEAAAILSAR----- 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1726 kitamhFVPSMLHA---FLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEAT---VEAAFF 1799
Cdd:PRK06060   235 ------FGPSVLYGvpnFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGqtfVSNRVD 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1800 DCPPHEkleripIGK--PVHHVRLylLNQNQRMLPVGCIGELYIAGAGVARGYLNRPalteerfleDPFYPGERMYKTGD 1877
Cdd:PRK06060   309 EWRLGT------LGRvlPPYEIRV--VAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRD 371

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1878 VARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV-----EGLQRNEVRAQL 1951
Cdd:PRK06060   372 RVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVaVRESTGASTLQAFLvatsgATIDGSVMRDLH 451

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1678550997 1952 ERL---LPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:PRK06060   452 RGLlnrLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 1500-1983 2.89e-20

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 98.17  E-value: 2.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PLN03102    20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLL-----------------QSAGLHVPeftgeIVYLNQTNSglAHRLSNPNVDV---------L 1633
Cdd:PLN03102   100 ATSIAAILRHAKPKILFVdrsfeplarevlhllssEDSNLNLP-----VIFIHEIDF--PKRPSSEELDYecliqrgepT 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQSLAYVI------------YTSGSTGMPKGVEIEHRSAvnFLNSLQS--RYQLKHSDMIMHkTSYSFDASIWELFWWPY 1699
Cdd:PLN03102   173 PSLVARMFriqdehdpislnYTSGTTADPKGVVISHRGA--YLSTLSAiiGWEMGTCPVYLW-TLPMFHCNGWTFTWGTA 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1700 A--GASVYLLPQGGekePEvIAKAIEEQKITAMHFVPSMLHAFLE----HIKYRSVPIKtnrlkrVFSGGEQLGTHLVSR 1773
Cdd:PLN03102   250 ArgGTSVCMRHVTA---PE-IYKNIEMHNVTHMCCVPTVFNILLKgnslDLSPRSGPVH------VLTGGSPPPAALVKK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1774 FYELlpNVSITNSYGPTEATVEAAFFD-------CPPHEKLErIPIGKPVHHVRLYLLN----QNQRMLPVG--CIGELY 1840
Cdd:PLN03102   320 VQRL--GFQVMHAYGLTEATGPVLFCEwqdewnrLPENQQME-LKARQGVSILGLADVDvknkETQESVPRDgkTMGEIV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1841 IAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 1920
Cdd:PLN03102   397 IKGSSIMKGYLKNPKATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVL 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1921 EAAVT--------------VRTDSGEPELCAYVEGLQRNEvRAQLERL---LPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PLN03102   470 ETAVVamphptwgetpcafVVLEKGETTKEDRVDKLVTRE-RDLIEYCrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PLN02246 PLN02246
4-coumarate--CoA ligase
 454-952 2.90e-20

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 98.13  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  454 EITDQTPVYETIhamFEKQAEkTPDAHAVIDQAC--SLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVL 531
Cdd:PLN02246    18 YIPNHLPLHDYC---FERLSE-FSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  532 GILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA----HLPSSLEDN--YIITHPEDIE--------SKVDGSNIKS 597
Cdd:PLN02246    94 GASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQScyvdKLKGLAEDDgvTVVTIDDPPEgclhfselTQADENELPE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  598 VN-NADDLLYMIYTSGTTGKPKGVQFEHRNM----ANLLKFE----YTHSGidfeaDVLQFATPSFDV-CYQEI-FSALL 666
Cdd:PLN02246   174 VEiSPDDVVALPYSSGTTGLPKGVMLTHKGLvtsvAQQVDGEnpnlYFHSD-----DVILCVLPMFHIySLNSVlLCGLR 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  667 KGGTLHIVPeaiKRDVPQLFAFINKHQTNIV-FLPTAFIkmifserELANSfPDGVKH------LIAAGEQLMISDLfQD 739
Cdd:PLN02246   249 VGAAILIMP---KFEIGALLELIQRHKVTIApFVPPIVL-------AIAKS-PVVEKYdlssirMVLSGAAPLGKEL-ED 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  740 VLRKR--GIHLHNHYGPSETH-VVSTYTIHPGDPIPElppigKPIGC------TDLYILNHQKQLQ-PCGVPGELYISGA 809
Cdd:PLN02246   317 AFRAKlpNAVLGQGYGMTEAGpVLAMCLAFAKEPFPV-----KSGSCgtvvrnAELKIVDPETGASlPRNQPGEICIRGP 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  810 SVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAI 889
Cdd:PLN02246   392 QIMKGYLNDPEATANTIDKDGW------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV 465

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  890 LIWQDQNGEHELCAYYCSVQ--KLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PLN02246   466 VPMKDEVAGEVPVAFVVRSNgsEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 11-433 3.14e-20

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: 96.67  E-value: 3.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   11 YPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFISQNvSSPQQVVLRERnvivlE 90
Cdd:cd19533      2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-GEPYQWIDPYT-----P 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   91 EDITHLN---EAEQSQFIEQWKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASY 167
Cdd:cd19533     76 VPIRHIDlsgDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  168 VNASPItlePVQPYGKYIKWLMEQDK-------EQAVSYW-DHYlsGHEQQTVLPKQKKTKGKSRQEHVTFSFSKEESSR 239
Cdd:cd19533    156 LKGRPA---PPAPFGSFLDLVEEEQAyrqserfERDRAFWtEQF--EDLPEPVSLARRAPGRSLAFLRRTAELPPELTRT 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  240 LSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGR--PAEIegieHMVGLFINTMPVRVQGA-KTPFLQLIKD 316
Cdd:cd19533    231 LLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDpQQTFAELVAQ 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  317 MQKDRLAAEAYSYHPLYEIQ---SRSAVKQGLIDHILVFENYPVQQEIqmlnkqehASDLFQIHNFTVADETNYSFYLM- 392
Cdd:cd19533    307 VSRELRSLLRHQRYRYEDLRrdlGLTGELHPLFGPTVNYMPFDYGLDF--------GGVVGLTHNLSSGPTNDLSIFVYd 378

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1678550997  393 VAPGEEIHIKMNYDAEQHDRSFVLSVKEHLLNAVSQILNNP 433
Cdd:cd19533    379 RDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2559-3024 3.83e-20

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 98.57  E-value: 3.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTIn 2638
Cdd:PRK06060    31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 eadlGVLAD-FE-------GEILTIES-VEEDDKSPLpqmsSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWR-RNA 2708
Cdd:PRK06060   110 ----DALRDrFQpsrvaeaAELMSEAArVAPGGYEPM----GGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKA 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2709 YAFNETDTILQLFSFSFD-GFITSMFTPLLSGAKAVLLHEEEAKDILAIKHqlSRQRITHMIIVPVLYRALLDVVQPEDV 2787
Cdd:PRK06060   182 LRLTPEDTGLCSARMYFAyGLGNSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFARVIDSCSPDSF 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2788 KTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSvATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGV 2867
Cdd:PRK06060   260 RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVG-QTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGV 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2868 AGELCIAGTGLARGYVNLPElteraftqnPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRC 2947
Cdd:PRK06060   339 EGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2948 IKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNA-----VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL--- 3019
Cdd:PRK06060   410 DEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkq 489


                   ....*..
gi 1678550997 3020 --PKPVY 3024
Cdd:PRK06060   490 spTKPIW 496
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
462-952 3.91e-20

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 97.64  E-value: 3.91e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  462 YETIHAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHL----RMKgvvRQEPVAIMMERSAAFITGVLGILKAG 537
Cdd:PRK08751    24 FRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlgelQLK---KGDRVALMMPNCLQYPIATFGVLRAG 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  538 GAIVPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLED---------------------------NYIITHPEDI--ES 588
Cdd:PRK08751   101 LTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQviadtpvkqvittglgdmlgfpkaalvNFVVKYVKKLvpEY 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  589 KVDGS-------------NIKSVNNA-DDLLYMIYTSGTTGKPKGVQFEHRNM-ANLLKFEY---THSGIDFEADVLQFA 650
Cdd:PRK08751   181 RINGAirfrealalgrkhSMPTLQIEpDDIAFLQYTGGTTGVAKGAMLTHRNLvANMQQAHQwlaGTGKLEEGCEVVITA 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  651 TPSFdvcyqEIFS------ALLK-GGTLHIVPEAikRDVPQLFAFINKHQ-TNIVFLPTAFIKMI----FSERELANsfp 718
Cdd:PRK08751   261 LPLY-----HIFAltanglVFMKiGGCNHLISNP--RDMPGFVKELKKTRfTAFTGVNTLFNGLLntpgFDQIDFSS--- 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  719 dgVKHLIAAGE--QLMISDLFQDVlrkRGIHLHNHYGPSETHVVSTytIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQ 796
Cdd:PRK08751   331 --LKMTLGGGMavQRSVAERWKQV---TGLTLVEAYGLTETSPAAC--INPLTLKEYNGSIGLPIPSTDACIKDDAGTVL 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  797 PCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEV 876
Cdd:PRK08751   404 AIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIED 477

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  877 TLMNHPDISE-AAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK08751   478 VIAMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 2549-3030 4.17e-20

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 97.28  E-value: 4.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2549 ASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSD 2628
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2629 SGTKLLMT-------------INEADLGVLADFEGEILTIESVEE--DDKS--PLPQMSSAHHLAyiiYTSGTTGRPKGV 2691
Cdd:PRK08276    82 SGAKVLIVsaaladtaaelaaELPAGVPLLLVVAGPVPGFRSYEEalAAQPdtPIADETAGADML---YSSGTTGRPKGI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2692 MVEhkgiantLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGA-------------KAVLLHEEEAKDILAikh 2758
Cdd:PRK08276   159 KRP-------LPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVVVMEKFDAEEALA--- 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2759 QLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGeaadreliarslAICP-HTELA---------NE-YGP 2823
Cdd:PRK08276   229 LIERYRVTHSQLVPTMFVRMLklpeEVRARYDVSSLRVAIHAA------------APCPvEVKRAmidwwgpiiHEyYAS 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2824 TENSVATTV-----MRHMEkqayvSIGQPIDGtQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAftQNPf 2898
Cdd:PRK08276   297 SEGGGVTVItsedwLAHPG-----SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA--RNP- 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2899 kpeARMYRTGDAARWMADGTLeYL-GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG 2977
Cdd:PRK08276   368 ---HGWVTVGDVGYLDEDGYL-YLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADG 443

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2978 -LSTNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPKPVYNHEGER 3030
Cdd:PRK08276   444 aDAGDALAAELiawlRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 1500-1983 4.21e-20

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 97.78  E-value: 4.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIgkrSPEML---LGIYGILKAGGAYLPIDP 1576
Cdd:PRK07059    29 LEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIM---MPNVLqypVAIAAVLRAGYVVVNVNP 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1577 DYPEERISFLLEDSGTN--ILL------LQSAGLHVP-------------EFTGEIVYL-----------------NQTN 1618
Cdd:PRK07059   106 LYTPRELEHQLKDSGAEaiVVLenfattVQQVLAKTAvkhvvvasmgdllGFKGHIVNFvvrrvkkmvpawslpghVRFN 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1619 SGLAH--RLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAV-NFLNS---LQSRYQLK-HSDMIMHKTS---YSFD 1688
Cdd:PRK07059   186 DALAEgaRQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQMeawLQPAFEKKpRPDQLNFVCAlplYHIF 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1689 ASIWELFWWPYAGASVYLLPQggekePEVIAKAIEEQKITAMHFVP---SMLHAFLEHIKYRSVPIKtnRLKRVFSGGEQ 1765
Cdd:PRK07059   266 ALTVCGLLGMRTGGRNILIPN-----PRDIPGFIKELKKYQVHIFPavnTLYNALLNNPDFDKLDFS--KLIVANGGGMA 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1766 LGTHLVSRFYELLpNVSITNSYGPTEATVEAAffdCPPHEKLERI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGA 1844
Cdd:PRK07059   339 VQRPVAERWLEMT-GCPITEGYGLSETSPVAT---CNPVDATEFSgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP 414

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1845 GVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:PRK07059   415 QVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAA 488

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1925 TVRTD--SGEpELCAYV----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK07059   489 VGVPDehSGE-AVKLFVvkkdPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 1630-1979 4.31e-20

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: 97.02  E-value: 4.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1630 VDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HktSYSFDASIWELFwwpYAGAS 1703
Cdd:cd05909    142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFgalpffH--SFGLTGCLWLPL---LSGIK 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1704 VYLLPQggEKEPEVIAKAIEEQKITAMHFVPSmlhaFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLpNVSI 1783
Cdd:cd05909    217 VVFHPN--PLDYKKIPELIYDKKATILLGTPT----FLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRI 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1784 TNSYGPTEAtveaaffdCPPheklerIPIGKPVHH-----VRLYLLNQNQRMLPV--------GCIGELYIAGAGVARGY 1850
Cdd:cd05909    290 LEGYGTTEC--------SPV------ISVNTPQSPnkegtVGRPLPGMEVKIVSVetheevpiGEGGLLLVRGPNVMLGY 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1851 LNRPALTEerfledpFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV-REAAVTVRTD 1929
Cdd:cd05909    356 LNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPD 428

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1930 S--GEPE-LCAYVEGLQRNEVRAQL-ERLLPGYMVPAYMIEMEQWPVTPSGKLD 1979
Cdd:cd05909    429 GrkGEKIvLLTTTTDTDPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 1495-1998 5.42e-20

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: 97.77  E-value: 5.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEK-TPDQAAVIFEDGV------MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKA 1567
Cdd:cd05967     51 TCYNALDRHVEAgRGDQIALIYDSPVtgtertYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARI 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1568 GGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLhvpEFTGEIVY-------LNQTNSGLAH-----------RLSNPN 1629
Cdd:cd05967    131 GAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGI---EPGKVVPYkplldkaLELSGHKPHHvlvlnrpqvpaDLTKPG 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1630 VDVLPQSL-----------------AYVIYTSGSTGMPKGVEIE---HRSAVNFlnSLQSRYQLKHSDMimhktsysfda 1689
Cdd:cd05967    208 RDLDWSELlakaepvdcvpvaatdpLYILYTSGTTGKPKGVVRDnggHAVALNW--SMRNIYGIKPGDV----------- 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1690 siwelfWWpyaGAS-----------VY---------LLPQG---GEKEPEVIAKAIEEQKITAMHFVPSMLHA---FLEH 1743
Cdd:cd05967    275 ------WW---AASdvgwvvghsyiVYgpllhgattVLYEGkpvGTPDPGAFWRVIEKYQVNALFTAPTAIRAirkEDPD 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1744 IKY-RSVPIktNRLKRVFSGGEqlgtHLVSRFYELLPN---VSITNSYGPTEATVEAAffdCPPhEKLERIPI-----GK 1814
Cdd:cd05967    346 GKYiKKYDL--SSLRTLFLAGE----RLDPPTLEWAENtlgVPVIDHWWQTETGWPIT---ANP-VGLEPLPIkagspGK 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1815 PVHHVRLYLLNQNQRMLPVGCIGELYIAGAgVARGYLNRPALTEERFLEDPF--YPGerMYKTGDVARWLPDGNVEFLGR 1892
Cdd:cd05967    416 PVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKNDERFKKLYLskFPG--YYDTGDAGYKDEDGYLFIMGR 492

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYV--------EGLQRNEVRAQLERLLPGYMVPA 1962
Cdd:cd05967    493 TDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDElkGQVPLGLVVlkegvkitAEELEKELVALVREQIGPVAAFR 572

                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1678550997 1963 YMIEMEQWPVTPSGKLDRNALPApggAADAETYTAP 1998
Cdd:cd05967    573 LVIFVKRLPKTRSGKILRRTLRK---IADGEDYTIP 605
PRK05857 PRK05857
fatty acid--CoA ligase;
1502-1996 6.89e-20

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 97.00  E-value: 6.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1502 QQAEKTPDQAAVIFEDGV--MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYP 1579
Cdd:PRK05857    22 EQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1580 EERISFLLEDSGTNILLLQSAG----LHVPEFTGEIVYLN-QTNSGLAHRLSNPNVDVLPQSLAY-------VIYTSGST 1647
Cdd:PRK05857   102 IAAIERFCQITDPAAALVAPGSkmasSAVPEALHSIPVIAvDIAAVTRESEHSLDAASLAGNADQgsedplaMIFTSGTT 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1648 GMPKGVEIEHRSAVNFLNSLQSRyQLKHSDMIMHKTSYS-FDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQK 1726
Cdd:PRK05857   182 GEPKAVLLANRTFFAVPDILQKE-GLNWVTWVVGETTYSpLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNA 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1727 ITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKrVFSGGEQLGTHLvsRFYELlPNVSITNSYGPTEATVEAAffdCPPHE- 1805
Cdd:PRK05857   261 VATTCLVPTLLSKLVSELKSANATVPSLRLV-GYGGSRAIAADV--RFIEA-TGVRTAQVYGLSETGCTAL---CLPTDd 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1806 ----KLERIPIGKPVHHVRLYLLNQN------QRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDpfypgerMYKT 1875
Cdd:PRK05857   334 gsivKIEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG-------WVNT 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1876 GDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDsgePELCAYVeGLQ------------ 1943
Cdd:PRK05857   407 GDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD---EEFGALV-GLAvvasaeldesaa 482

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1944 ---RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYT 1996
Cdd:PRK05857   483 ralKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVV 538
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 1511-1978 7.49e-20

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 96.51  E-value: 7.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1511 AAVIFEDG-VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLED 1589
Cdd:PRK08276     2 AVIMAPSGeVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1590 SGTNIL------------LLQSAGLHVPEFT---GEIVYLNQTNSGLAHRLSNPNVDVLPQSLayVIYTSGSTGMPKGVe 1654
Cdd:PRK08276    82 SGAKVLivsaaladtaaeLAAELPAGVPLLLvvaGPVPGFRSYEEALAAQPDTPIADETAGAD--MLYSSGTTGRPKGI- 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1655 iehrsavnflnslqsRYQLKHSDMIMhktsySFDASIWELFWWPYAGA-SVYLLP----------------QGGEK---- 1713
Cdd:PRK08276   159 ---------------KRPLPGLDPDE-----APGMMLALLGFGMYGGPdSVYLSPaplyhtaplrfgmsalALGGTvvvm 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1714 ---EPEVIAKAIEEQKITAMHFVPSMLHAFL---EHIKYR----SvpiktnrLKRVFSGGEQLGTHLVSRFYELLPNVsI 1783
Cdd:PRK08276   219 ekfDAEEALALIERYRVTHSQLVPTMFVRMLklpEEVRARydvsS-------LRVAIHAAAPCPVEVKRAMIDWWGPI-I 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1784 TNSYGPTEA---TVeaaffdCPPHEKLERiP--IGKPVHHVrLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTE 1858
Cdd:PRK08276   291 HEYYASSEGggvTV------ITSEDWLAH-PgsVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTA 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1859 ERfledpfYPGERMYKTGDVArWL-PDGnveFLGRTD---DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE 1932
Cdd:PRK08276   363 AA------RNPHGWVTVGDVG-YLdEDG---YLYLTDrksDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEemGE 432

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1933 pELCAYVEGLQ--------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:PRK08276   433 -RVKAVVQPADgadagdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 465-963 8.08e-20

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 97.18  E-value: 8.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  465 IHAMFEKQAEKTPDAHAVI-----DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGA 539
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRwegedGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  540 IVPVDPHYPADRIRYILHDCG--------------------------CSH--------VVSQAHLPSSLEDNYIITHPED 585
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEakalitadgftrrgrevnlkeeadkaCAQcptvekvvVVRHLGNDFTPAKGRDLSYDEE 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  586 IESKVDGSnikSVNNADDLLYMIYTSGTTGKPKGVQfeHRNMANLLK--FEYTHsGIDF-EADVLQFATpsfDVCYQE-- 660
Cdd:cd05968    223 KETAGDGA---ERTESEDPLMIIYTSGTTGKPKGTV--HVHAGFPLKaaQDMYF-QFDLkPGDLLTWFT---DLGWMMgp 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  661 --IFSALLKGGTLHIVPEAIKRDVP-QLFAFINKHQTNIVFLPTAFIK--MIFSERELANSFPDGVKHLIAAGEQLMISD 735
Cdd:cd05968    294 wlIFGGLILGATMVLYDGAPDHPKAdRLWRMVEDHEITHLGLSPTLIRalKPRGDAPVNAHDLSSLRVLGSTGEPWNPEP 373

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  736 ---LFQDVLRKRgIHLHNHYGPSEthvVSTyTIHPGDPIPELPPIG--KPIGCTDLYILNHQKQLQPCGVpGELYISGA- 809
Cdd:cd05968    374 wnwLFETVGKGR-NPIINYSGGTE---ISG-GILGNVLIKPIKPSSfnGPVPGMKADVLDESGKPARPEV-GELVLLAPw 447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  810 -SVARGYVNHDKLTSDKFSSDpfKPDVIMYrtGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISE-A 887
Cdd:cd05968    448 pGMTRGFWRDEDRYLETYWSR--FDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsA 523

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  888 AILIWQDQNGEHELCAyycSVQKLNTI-------DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR-----AALPEP 955
Cdd:cd05968    524 AIGVPHPVKGEAIVCF---VVLKPGVTptealaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRrviraAYLGKE 600

                          570
                   ....*....|
gi 1678550997  956 DASISG--NP 963
Cdd:cd05968    601 LGDLSSleNP 610
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 1489-1985 8.15e-20

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 97.18  E-value: 8.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1489 GYSMNqTLHYALEQQAEKTPDQAAVIF--EDG---VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYG 1563
Cdd:cd05968     57 GGRMN-IVEQLLDKWLADTRTRPALRWegEDGtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLA 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1564 ILKAGGAYLPIDPDYPEERISFLLEDSGTNILL-----------------LQSAGLHVPEFTGEIVYLNQTNSGLAHR-- 1624
Cdd:cd05968    136 VARIGGIVVPIFSGFGKEAAATRLQDAEAKALItadgftrrgrevnlkeeADKACAQCPTVEKVVVVRHLGNDFTPAKgr 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1625 -LSNPNVDVLPQSLA---------YVIYTSGSTGMPKGVEieHRSAVNFLNSLQSRY---QLKHSDMIMHKTSYSFDASI 1691
Cdd:cd05968    216 dLSYDEEKETAGDGAertesedplMIIYTSGTTGKPKGTV--HVHAGFPLKAAQDMYfqfDLKPGDLLTWFTDLGWMMGP 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1692 WELFWWPYAGASVYLLpQG--GEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHikyRSVPIKTNRLK--RVF-SGGEQL 1766
Cdd:cd05968    294 WLIFGGLILGATMVLY-DGapDHPKADRLWRMVEDHEITHLGLSPTLIRALKPR---GDAPVNAHDLSslRVLgSTGEPW 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1767 GTHLVSRFYE--LLPNVSITNSYGPTEatVEAAFFDCPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPvGCIGELYIAGA 1844
Cdd:cd05968    370 NPEPWNWLFEtvGKGRNPIINYSGGTE--ISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAP 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1845 --GVARGYLNrpalTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE- 1921
Cdd:cd05968    447 wpGMTRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEs 522

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1922 AAVTVRTD-SGEPELCAYV--------EGLqRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:cd05968    523 AAIGVPHPvKGEAIVCFVVlkpgvtptEAL-AEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 2533-3000 1.02e-19

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 96.87  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGC--- 2609
Cdd:PRK08279    37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2610 --------------------YVPIDPEYpkeRKRYILSDSGTKLLMTINEADLGVLADFEGEI-LTIESVEEDDKSP-LP 2667
Cdd:PRK08279   117 lntqqrgavlahslnlvdakHLIVGEEL---VEAFEEARADLARPPRLWVAGGDTLDDPEGYEdLAAAAAGAPTTNPaSR 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2668 QMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTI---LQLFSFSfdGFITSMFTPLLSGAKavl 2744
Cdd:PRK08279   194 SGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLyccLPLYHNT--GGTVAWSSVLAAGAT--- 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2745 lheeeakdiLAIKHQLS---------RQRITHMIIVPVLYRALLDvvQPEDVK----TLRVVTLAG-------EAADREL 2804
Cdd:PRK08279   269 ---------LALRRKFSasrfwddvrRYRATAFQYIGELCRYLLN--QPPKPTdrdhRLRLMIGNGlrpdiwdEFQQRFG 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2805 IARslaICphtELaneYGPTE------------NSVATTVMRHMEKQAYVSI----GQPIDGTQVLilnsnhqLQPIGvA 2868
Cdd:PRK08279   338 IPR---IL---EF---YAASEgnvgfinvfnfdGTVGRVPLWLAHPYAIVKYdvdtGEPVRDADGR-------CIKVK-P 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2869 GE--LCIAG-TGLAR--GYVNlPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIES 2943
Cdd:PRK08279   401 GEvgLLIGRiTDRGPfdGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVEN 479

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2944 VIRCIKGVKDAAV--VAHVTASGQTELSAYVVTK-PGLSTNAVRSELQNKLPVFMHPAFI 3000
Cdd:PRK08279   480 ALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVPLFV 539
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 2557-3019 1.81e-19

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 95.43  E-value: 1.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:PLN02330    54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 --------------------------INEADLGVLADFEGEILTIESVEEDDKSPLPqmssahhlayiiYTSGTTGRPKG 2690
Cdd:PLN02330   134 ndtnygkvkglglpvivlgeekiegaVNWKELLEAADRAGDTSDNEEILQTDLCALP------------FSSGTTGISKG 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2691 VMVEHKG-IANTLQ--WRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILaikHQLSRQRITH 2767
Cdd:PLN02330   202 VMLTHRNlVANLCSslFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFL---NALITQEVSF 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2768 MIIVPVLYRALLD--VVQPEDVKTLRVVTLAGEAAD--RELIARSLAICPHTELANEYGPTENSVATTVMRHMEKQAYV- 2842
Cdd:PLN02330   279 APIVPPIILNLVKnpIVEEFDLSKLKLQAIMTAAAPlaPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIa 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2843 ---SIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGT 2918
Cdd:PLN02330   359 kknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW------LHTGDIGYIDDDGD 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2919 LEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPglstNAVRSE------LQNKLP 2992
Cdd:PLN02330   433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINP----KAKESEedilnfVAANVA 508

                          490       500
                   ....*....|....*....|....*..
gi 1678550997 2993 VFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PLN02330   509 HYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 1501-1983 2.21e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 95.14  E-value: 2.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1501 EQQAEKTPDQAAVIF--EDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:PRK13391     4 GIHAQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSAGL--------HVPEFTGEIVYLNQTNS----GLAHRLSNPNVDVLP-QSL-AYVIYTS 1644
Cdd:PRK13391    84 TPAEAAYIVDDSGARALITSAAKLdvarallkQCPGVRHRLVLDGDGELegfvGYAEAVAGLPATPIAdESLgTDMLYSS 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1645 GSTGMPKGV-----EIEHRSAVNFLNSLQSRYQLKhSDMIM-------HKTSYSFDASIWELfwwpyaGASVYLLpqggE 1712
Cdd:PRK13391   164 GTTGRPKGIkrplpEQPPDTPLPLTAFLQRLWGFR-SDMVYlspaplyHSAPQRAVMLVIRL------GGTVIVM----E 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1713 K-EPEVIAKAIEEQKITAMHFVPSMLHAFL---EHIKYRsvpIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYG 1788
Cdd:PRK13391   233 HfDAEQYLALIEEYGVTHTQLVPTMFSRMLklpEEVRDK---YDLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1789 PTEAtveAAFFDCPPHEKLE-RIPIGKPVHHVrLYLLNQNQRMLPVGCIGELYIAGaGVARGYLNRPALTEERFLEDPfy 1867
Cdd:PRK13391   309 ATEG---LGFTACDSEEWLAhPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-- 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 pgeRMYKTGDVARWLPDGnveFLGRTDDQVKI---RGYRIEPGEIEAALRSIEGVREAAV--TVRTDSGEpELCAYV--- 1939
Cdd:PRK13391   382 ---TWSTVGDIGYVDEDG---YLYLTDRAAFMiisGGVNIYPQEAENLLITHPKVADAAVfgVPNEDLGE-EVKAVVqpv 454

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997 1940 EGLQRN-----EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK13391   455 DGVDPGpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 602-952 3.47e-19

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: 92.54  E-value: 3.47e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDLLYMIYTSGTTGKPKGVQFEHRN-------MANLLKFEythsgidfEADVLQFATPSFDV--CYQEIFSALLKGGTLH 672
Cdd:cd05944      2 DDVAAYFHTGGTTGTPKLAQHTHSNevynawmLALNSLFD--------PDDVLLCGLPLFHVngSVVTLLTPLASGAHVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  673 IVPEAIKRD---VPQLFAFINKHQ-TNIVFLPTAFIKMIfserelanSFPDGVK----HLIAAGEQLMISDLFQDVLRKR 744
Cdd:cd05944     74 LAGPAGYRNpglFDNFWKLVERYRiTSLSTVPTVYAALL--------QVPVNADisslRFAMSGAAPLPVELRARFEDAT 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 GIHLHNHYGPSETHVVSTYTiHPGDPIpELPPIGKPIGCTDLYILNHQ---KQLQPCGVP--GELYISGASVARGYVNhD 819
Cdd:cd05944    146 GLPVVEGYGLTEATCLVAVN-PPDGPK-RPGSVGLRLPYARVRIKVLDgvgRLLRDCAPDevGEICVAGPGVFGGYLY-T 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  820 KLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVkIR-GYRIEPQEIEVTLMNHPDISEAAILIWQDQNGE 898
Cdd:cd05944    223 EGNKNAFVADGW------LNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  899 HELCAYYCSVQ--KLNTIDLRSYMASELPEYMIPAKWIWV-DSIPLTPNGKVDRAAL 952
Cdd:cd05944    296 ELPVAYVQLKPgaVVEEEELLAWARDHVPERAAVPKHIEVlEELPVTAVGKVFKPAL 352
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1519-1983 3.58e-19

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 94.56  E-value: 3.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1519 VMTYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLL 1597
Cdd:PRK08751    50 TITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1598 Q--------------------SAGLH---------------------VPEFT--GEIVYLNQTNSGLAHRLsnPNVDVLP 1634
Cdd:PRK08751   130 IdnfgttvqqviadtpvkqviTTGLGdmlgfpkaalvnfvvkyvkklVPEYRinGAIRFREALALGRKHSM--PTLQIEP 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 QSLAYVIYTSGSTGMPKGVEIEHRSAVnfLNSLQSRYQLKHSDMIMHKTSYSFDA-SIWELFwwPYAGASVYLLPQGG-- 1711
Cdd:PRK08751   208 DDIAFLQYTGGTTGVAKGAMLTHRNLV--ANMQQAHQWLAGTGKLEEGCEVVITAlPLYHIF--ALTANGLVFMKIGGcn 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1712 -----EKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRfYELLPNVSITNS 1786
Cdd:PRK08751   284 hlisnPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSS--LKMTLGGGMAVQRSVAER-WKQVTGLTLVEA 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATVEAAF--FDCPPHEKleriPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLED 1864
Cdd:PRK08751   361 YGLTETSPAACInpLTLKEYNG----SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDAD 436

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1865 PFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE-AAVTVRTD-SGEPELCAYVE-- 1940
Cdd:PRK08751   437 GWL------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAVGVPDEkSGEIVKVVIVKkd 510

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 1941 -GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK08751   511 pALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 1499-1961 3.61e-19

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 94.94  E-value: 3.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGA-------- 1570
Cdd:PRK08279    42 VFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVvallntqq 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 ---------------YLPIDPDYPE--ERISFLLEDSGTnILLLQSAGLHVPEFTGEivyLNQTNSGLAHRlsNPNV--D 1631
Cdd:PRK08279   122 rgavlahslnlvdakHLIVGEELVEafEEARADLARPPR-LWVAGGDTLDDPEGYED---LAAAAAGAPTT--NPASrsG 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1632 VLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HKTSY------------------SF 1687
Cdd:PRK08279   196 VTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYcclplyHNTGGtvawssvlaagatlalrrKF 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1688 DASiweLFWwpyagasvyllpqggekePEVIAkaieeQKITAMHFVPSMLHAFLEHikyrsvPIKT----NRLKRVFSGG 1763
Cdd:PRK08279   276 SAS---RFW------------------DDVRR-----YRATAFQYIGELCRYLLNQ------PPKPtdrdHRLRLMIGNG 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1764 ----------EQLGthlVSRFYELlpnvsitnsYGPTEATVeaAFFD----------CPPHEKleripigKPVHHVRL-- 1821
Cdd:PRK08279   324 lrpdiwdefqQRFG---IPRILEF---------YAASEGNV--GFINvfnfdgtvgrVPLWLA-------HPYAIVKYdv 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1822 ----YLLNQNQRMLPVG------CIGElyIAGAGVARGYlNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLG 1891
Cdd:PRK08279   383 dtgePVRDADGRCIKVKpgevglLIGR--ITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVD 459

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1892 RTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV---------------TVRTDSGepelcayvEGLQRNEVRAQLERLLP 1956
Cdd:PRK08279   460 RLGDTFRWKGENVATTEVENALSGFPGVEEAVVygvevpgtdgragmaAIVLADG--------AEFDLAALAAHLYERLP 531


                   ....*
gi 1678550997 1957 GYMVP 1961
Cdd:PRK08279   532 AYAVP 536
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 472-952 3.75e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 94.31  E-value: 3.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  472 QAEKTPDAHAVI--DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA 549
Cdd:PRK13390     6 HAQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  550 DRIRYILHDCGCSHVVSQAHLpssleDNYIITHPEDIESKVD-GSNIKSVNNADDLL--------------YMIYTSGTT 614
Cdd:PRK13390    86 PEADYIVGDSGARVLVASAAL-----DGLAAKVGADLPLRLSfGGEIDGFGSFEAALagagprlteqpcgaVMLYSSGTT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  615 GKPKGVQ--FEHRN----------MANLLkFEYTHSGIDFEADVLQFATPsfdVCYQEIFSALlkGGTLHIvpeAIKRDV 682
Cdd:PRK13390   161 GFPKGIQpdLPGRDvdapgdpivaIARAF-YDISESDIYYSSAPIYHAAP---LRWCSMVHAL--GGTVVL---AKRFDA 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  683 PQLFAFINKHQTNIV-FLPTAFIKMIFSERELANSFP-DGVKHLIAAGEQLMIsDLFQDVLRKRGIHLHNHYGPSETHVV 760
Cdd:PRK13390   232 QATLGHVERYRITVTqMVPTMFVRLLKLDADVRTRYDvSSLRAVIHAAAPCPV-DVKHAMIDWLGPIVYEYYSSTEAHGM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  761 StyTIHPGDPIPELPPIGKPIgCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNH-DKLTSDKFSSDPFKPDVimyr 839
Cdd:PRK13390   311 T--FIDSPDWLAHPGSVGRSV-LGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDpEKTAAAQHPAHPFWTTV---- 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  840 tGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTID---- 915
Cdd:PRK13390   384 -GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelar 462

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1678550997  916 -LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK13390   463 eLIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 601-948 3.76e-19

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: 92.45  E-value: 3.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  601 ADDLlYMIYTSGTTGKPKGVQFEHRNM-------ANLLKFEYTHSGIDFEADVLQFATPSFDVC-------YQEIFSALL 666
Cdd:cd05924      3 ADDL-YILYTGGTTGMPKGVMWRQEDIfrmlmggADFGTGEFTPSEDAHKAAAAAAGTVMFPAPplmhgtgSWTAFGGLL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  667 KGGTLhIVPEaIKRDVPQLFAFINKHQTN-IVFLPTAFIKMIFSERELANSFPDGVKHLIAAGEQLMISDLFQDVLR-KR 744
Cdd:cd05924     82 GGQTV-VLPD-DRFDPEEVWRTIEKHKVTsMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLElVP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 GIHLHNHYGPSETHvvSTYTIHPGDPIPELPPIGKPIGCTDLyILNHQKQLQP-CGVPGELYISGaSVARGYVNHDKLTS 823
Cdd:cd05924    160 NITLVDAFGSSETG--FTGSGHSAGSGPETGPFTRANPDTVV-LDDDGRVVPPgSGGVGWIARRG-HIPLGYYGDEAKTA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  824 DKFssdPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCA 903
Cdd:cd05924    236 ETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA 312

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  904 yycsVQKLNTI------DLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd05924    313 ----VVQLREGagvdleELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 466-1041 6.67e-19

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: 94.77  E-value: 6.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  466 HAMFEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDP 545
Cdd:COG3319      4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  546 HYPADRIRYILHDCGCSHVVSQ----AHLPSSLEDNYIITHPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQ 621
Cdd:COG3319     84 LALALAAAAAALLLAALALLLAllaaLALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  622 FEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPT 701
Cdd:COG3319    164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  702 AFIkmIFSERELANSFPDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYT---IHPGDPIPELPPIG 778
Cdd:COG3319    244 LAA--LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAaaaAPGVAGALGPIGGG 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  779 KPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRA 858
Cdd:COG3319    322 PGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRL 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  859 DNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDS 938
Cdd:COG3319    402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  939 IPLTPNGKVDRAALPEPDASISGNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQ 1018
Cdd:COG3319    482 LLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561

                          570       580
                   ....*....|....*....|...
gi 1678550997 1019 VSLKDIFAHPTVEGLALIIREAE 1041
Cdd:COG3319    562 LLLLALLLAPTLAALAAALAAAA 584
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 1504-1924 6.93e-19

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 93.01  E-value: 6.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1504 AEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLqsaglhvpeFTGEIVYLNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVeiEHrSAVNF 1663
Cdd:PRK09029    93 EELLPSLTLDFALV---------LEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAA--VH-TAQAH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1664 LNSLQSRYQLkhsdmiMHktsysFDAS-IW----ELF--------W-WPYAGASVYLlpqgGEKEPevIAKAIeeQKITA 1729
Cdd:PRK09029   161 LASAEGVLSL------MP-----FTAQdSWllslPLFhvsgqgivWrWLYAGATLVV----RDKQP--LEQAL--AGCTH 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1730 MHFVPSMLHAFLEhikYRSVPIktnRLKRVFSGGEQLGTHLVSRFYELlpnvSITN--SYGPTEA--TVEAaffdcpphE 1805
Cdd:PRK09029   222 ASLVPTQLWRLLD---NRSEPL---SLKAVLLGGAAIPVELTEQAEQQ----GIRCwcGYGLTEMasTVCA--------K 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1806 KLERIP-IGKPVHHVRLYLLNqnqrmlpvgciGELYIAGAGVARGYLNRPALTeerfledPFYPGERMYKTGDVARWLpD 1884
Cdd:PRK09029   284 RADGLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-N 344

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1678550997 1885 GNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:PRK09029   345 GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 2535-2957 7.30e-19

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 93.71  E-value: 7.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2535 ISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPID 2614
Cdd:PLN02860     9 ICQCLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2615 PEYP-KERKRYILS--------DSGTK---LLMTIN-----------EADLGVLADFEGEILTIESVEEDD-KSPLPQMS 2670
Cdd:PLN02860    89 YRWSfEEAKSAMLLvrpvmlvtDETCSswyEELQNDrlpslmwqvflESPSSSVFIFLNSFLTTEMLKQRAlGTTELDYA 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2671 SA-HHLAYIIYTSGTTGRPKGVMVEHKG-IANTLQwRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEE 2748
Cdd:PLN02860   169 WApDDAVLICFTSGTTGRPKGVTISHSAlIVQSLA-KIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKF 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2749 EAKDIL-AIKHqlsrQRITHMIIVPVLYRALLDVVQPEDV----KTLRVVTLAGEAADRELIARSLAICPHTELANEYGP 2823
Cdd:PLN02860   248 DAKAALqAIKQ----HNVTSMITVPAMMADLISLTRKSMTwkvfPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGM 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2824 TENSVATTVMR-HMEKQAyvSIGQPIDGTQVLILNSNHQLQPIGVAG-----ELCIA-------GTGLARGyvnlPELTE 2890
Cdd:PLN02860   324 TEACSSLTFMTlHDPTLE--SPKQTLQTVNQTKSSSVHQPQGVCVGKpaphvELKIGldessrvGRILTRG----PHVML 397

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 2891 RAFTQNPFKPEARM----YRTGDAArWMAD-GTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVV 2957
Cdd:PLN02860   398 GYWGQNSETASVLSndgwLDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1058-1456 1.04e-18

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: 91.93  E-value: 1.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1058 PVSSAQKRiYVLQQLDEGVAYNMPAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSgADDEPVQRIH--TEVPFTL-- 1133
Cdd:cd19534      3 PLTPIQRW-FFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRR-EDGGWQQRIRgdVEELFRLev 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1134 ------SKETTIEGFV----RPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQL----- 1198
Cdd:cd19534     81 vdlsslAQAAAIEALAaeaqSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAgepip 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1199 KPLRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPilELPTDkrrPAERQFIGGKVTFQLDKEITARIkrLAHKNR 1278
Cdd:cd19534    161 LPSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKD---PEQTYGDARTVSFTLDEEETEAL--LQEANA 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1279 StlYMT-----LL-ALYSAFlSRLSGQDDIVIGSPIAGR----PHADLEAVLGMFVNTLALRTRPAGNKTFEEFLKEVRQ 1348
Cdd:cd19534    234 A--YRTeindlLLaALALAF-QDWTGRAPPAIFLEGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1349 TA---------------LEAYEHQDYPF----EELVDKLGVQREMSRNPLFDTTLVLQNMEQQKLKMndvqlqwnDLEHP 1409
Cdd:cd19534    311 QLrripnkgigygilryLTPEGTKRLAFhpqpEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDT--------PRFAL 382

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 1410 iskFDISLYVteHDSELFCQFEYSTALFEKETIQRWASLF----TTLVEHT 1456
Cdd:cd19534    383 ---LDINAVV--EGGQLVITVSYSRNMYHEETIQQLADSYkealEALIEHC 428
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 2554-2963 1.07e-18

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: 92.66  E-value: 1.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2554 SGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGgcyVPIDPEYPKerkryiLSDSGtkL 2633
Cdd:cd17639      1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT------LGEDA--L 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2634 LMTINEADLGVLadfegeiltIESVEEDDksplpqmssahhLAYIIYTSGTTGRPKGVMVEHKGIANTL--QWRRNAYAF 2711
Cdd:cd17639     70 IHSLNETECSAI---------FTDGKPDD------------LACIMYTSGSTGNPKGVMLTHGNLVAGIagLGDRVPELL 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2712 NETDTIL------QLFSFSFD----------GFIT----------------SMFTP-LLSGAKAVLlhEEEAKDILA--- 2755
Cdd:cd17639    129 GPDDRYLaylplaHIFELAAEnvclyrggtiGYGSprtltdkskrgckgdlTEFKPtLMVGVPAIW--DTIRKGVLAkln 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2756 ----IKHQL------SRQ-RITHMIIVPVLYRALLdvvqpedvKTLRVVT-------LAGEAA----DRELIarSLAICP 2813
Cdd:cd17639    207 pmggLKRTLfwtayqSKLkALKEGPGTPLLDELVF--------KKVRAALggrlrymLSGGAPlsadTQEFL--NIVLCP 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2814 hteLANEYGPTENSVATTVMRHMEkQAYVSIGQPIDGTQVLILN------SNHQLQPigvAGELCIAGTGLARGYVNLPE 2887
Cdd:cd17639    277 ---VIQGYGLTETCAGGTVQDPGD-LETGRVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPE 349

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2888 LTERAFTqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIR-GYRVETKEIESVIRCIKGVKDAAVVAHVTAS 2963
Cdd:cd17639    350 KTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS 420
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 3123-3362 1.27e-18

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: 91.65  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQK--WFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQgkwdqynRPLSH-SDDALYG 3199
Cdd:cd19531      5 SFAQQrlWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-------EPVQViLPPLPLP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3200 LQMIDLSAPDGTDGnrpyEPLIKRHVLD-IQQKMDLKNGPLLQAGLFHTIDGDF-LFLSAHHLVVDGISWRVLLEDLALG 3277
Cdd:cd19531     78 LPVVDLSGLPEAER----EAEAQRLAREeARRPFDLARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAAL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3278 YRQAAGGEDIKLPPktssfkayakkLS----DYAESQQ-------LMKQLKYWRE--AEEYQTEALPFDqidgtRAHEGQ 3344
Cdd:cd19531    154 YAAFLAGRPSPLPP-----------LPiqyaDYAVWQRewlqgevLERQLAYWREqlAGAPPVLELPTD-----RPRPAV 217

                          250       260
                   ....*....|....*....|..
gi 1678550997 3345 RS----TISFTLnDKETAALLK 3362
Cdd:cd19531    218 QSfrgaRVRFTL-PAELTAALR 238
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 1520-1939 1.38e-18

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: 92.28  E-value: 1.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGgaylpidpdypeerisflledsgtnilllqs 1599
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN------------------------------- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1600 aglhvpeFTGEIVYLNQTNSGLAHRLSNPNVDVL-----PQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSR-YQL 1673
Cdd:cd17639     55 -------IPIVTVYATLGEDALIHSLNETECSAIftdgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvPEL 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1674 KHSD--MImhktSYSFDASIWE-------LFWWPYAG-ASVYLL-------PQGGEKE---------PEV---IAKAIEE 1724
Cdd:cd17639    128 LGPDdrYL----AYLPLAHIFElaaenvcLYRGGTIGyGSPRTLtdkskrgCKGDLTEfkptlmvgvPAIwdtIRKGVLA 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1725 qKITAMHFVPSML--HAFLEHIKYRSVPIKT----------------NRLKRVFSGGEQLG--THlvsRFYELL--Pnvs 1782
Cdd:cd17639    204 -KLNPMGGLKRTLfwTAYQSKLKALKEGPGTplldelvfkkvraalgGRLRYMLSGGAPLSadTQ---EFLNIVlcP--- 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1783 ITNSYGPTEaTVEAAFFDCPPHEKLERIpiGKPVHHVRLYLLN-----------QNQrmlpvgciGELYIAGAGVARGYL 1851
Cdd:cd17639    277 VIQGYGLTE-TCAGGTVQDPGDLETGRV--GPPLPCCEIKLVDweeggystdkpPPR--------GEILIRGPNVFKGYY 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1852 NRPALTEERFLEDpfypgeRMYKTGDVARWLPDGNVEFLGRTDDQVKIR-GYRIEPGEIEAALRSIEGVreAAVTVRTDS 1930
Cdd:cd17639    346 KNPEKTKEAFDGD------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV--NNICVYADP 417


                   ....*....
gi 1678550997 1931 GEPELCAYV 1939
Cdd:cd17639    418 DKSYPVAIV 426
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 1497-1983 1.43e-18

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: 92.53  E-value: 1.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1497 HYALEQQAEKTPDQAAVIFEDG----VM-TYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:cd05928     14 QWADKEKAGKRPPNPALWWVNGkgdeVKwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYPEERISFLLEDSGTNILL--------LQSAGLHVPEFTGEIVYLNQTNSG------LAHRLSNPNVDVLPQS 1636
Cdd:cd05928     94 FIPGTIQLTAKDILYRLQASKAKCIVtsdelapeVDSVASECPSLKTKLLVSEKSRDGwlnfkeLLNEASTEHHCVETGS 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1637 L-AYVIY-TSGSTGMPKGVEIEHRSAVNFLnSLQSRY--QLKHSDmIMHKTSYS--FDASIWELFW-WPyAGASVY--LL 1707
Cdd:cd05928    174 QePMAIYfTSGTTGSPKMAEHSHSSLGLGL-KVNGRYwlDLTASD-IMWNTSDTgwIKSAWSSLFEpWI-QGACVFvhHL 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1708 PQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRsvpIKTNRLKRVFSGGEQLGTHLVSRFYELlPNVSITNSY 1787
Cdd:cd05928    251 PR---FDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS---YKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGY 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1788 GPTEATVEAAFFDcppHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYI-----AGAGVARGYLNRPALTEERFL 1862
Cdd:cd05928    324 GQTETGLICANFK---GMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIR 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1863 EDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELC-AYV-- 1939
Cdd:cd05928    401 GD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVkAFVvl 473

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1940 ---------EGLQRnEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05928    474 apqflshdpEQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 2544-3019 2.03e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 91.99  E-value: 2.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2544 ART-PKASALVSGD--KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKE 2620
Cdd:PRK13390     7 AQIaPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2621 RKRYILSDSGTKLLMTINEADlGVLAD----------FEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKG 2690
Cdd:PRK13390    87 EADYIVGDSGARVLVASAALD-GLAAKvgadlplrlsFGGEIDGFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKG 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2691 VM-------VEHKGiANTLQWRRNAYAFNETDT------ILQLFSFSFDGFITSMftpllsGAKAVLLHEEEAKDILAik 2757
Cdd:PRK13390   166 IQpdlpgrdVDAPG-DPIVAIARAFYDISESDIyyssapIYHAAPLRWCSMVHAL------GGTVVLAKRFDAQATLG-- 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2758 hQLSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAgeAADRELIARSLAICPHTELANEYGPTENSVATTVM 2833
Cdd:PRK13390   237 -HVERYRITVTQMVPTMFVRLLkldaDVRTRYDVSSLRAVIHA--AAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFI 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2834 RHMEKQAYV-SIGQPIDGTQVLILNSNHQLqPIGVAGELCIAGTGLARGYVNLPELTERAftQNPFKPearMYRT-GDAA 2911
Cdd:PRK13390   314 DSPDWLAHPgSVGRSVLGDLHICDDDGNEL-PAGRIGTVYFERDRLPFRYLNDPEKTAAA--QHPAHP---FWTTvGDLG 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2912 RWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLS-TNAVRSEL--- 2987
Cdd:PRK13390   388 SVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRgSDELARELidy 467

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1678550997 2988 -QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK13390   468 tRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1496-1985 2.19e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 91.98  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPID 1575
Cdd:PRK13383    37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPEERISFLLEDSGTNILLLQSAGLHVPEFTGE-IVYLNQTNSGLAHRLSNPNVdvlPQSLAYVIYTSGSTGMPKGV- 1653
Cdd:PRK13383   117 TEFRSDALAAALRAHHISTVVADNEFAERIAGADDaVAVIDPATAGAEESGGRPAV---AAPGRIVLLTSGTTGKPKGVp 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1654 -EIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVyLLPQGGEKEPEVIAKAIeeQKITAMHF 1732
Cdd:PRK13383   194 rAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTV-LTHRHFDAEAALAQASL--HRADAFTA 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1733 VPSMLHAFLE---HIKYRSvPIKtnRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPTEATVEAAffdCPPHEkLER 1809
Cdd:PRK13383   271 VPVVLARILElppRVRARN-PLP--QLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGAL---ATPAD-LRD 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1810 IP--IGKPVHHVRLYLLNQNQRmlPVG--CIGELYIAGAGVARGYLNRPAlteeRFLEDPfypgerMYKTGDVARWLPDG 1885
Cdd:PRK13383   343 APetVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRYTDGGG----KAVVDG------MTSTGDMGYLDNAG 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1886 NVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYM 1959
Cdd:PRK13383   411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIgVPDERFGHRLAAFVvlhpgSGVDAAQLRDYLKDRVSRFE 490

                          490       500
                   ....*....|....*....|....*.
gi 1678550997 1960 VPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:PRK13383   491 QPRDINIVSSIPRNPTGKVLRKELPG 516
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 2556-3016 2.26e-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: 2.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2556 DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI----DPEYPKERkryiLSDSGT 2631
Cdd:cd05966     82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfagfSAESLADR----INDAQC 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2632 KLLMTINEA-------DLGVLADfegEIL----TIESV-------------------------EEDDKSPLPQMSSAHHL 2675
Cdd:cd05966    158 KLVITADGGyrggkviPLKEIVD---EALekcpSVEKVlvvkrtggevpmtegrdlwwhdlmaKQSPECEPEWMDSEDPL 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 aYIIYTSGTTGRPKGVMVEHKG----IANTLQWrrnayAFNETDTilQLFSFSFD-GFIT----SMFTPLLSGAKAVLLh 2746
Cdd:cd05966    235 -FILYTSGSTGKPKGVVHTTGGyllyAATTFKY-----VFDYHPD--DIYWCTADiGWITghsyIVYGPLANGATTVMF- 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2747 eEEAK---------DILAiKHqlsrqRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAAD-------RELIA 2806
Cdd:cd05966    306 -EGTPtypdpgrywDIVE-KH-----KVTIFYTAPTAIRALMkfgdEWVKKHDLSSLRVLGSVGEPINpeawmwyYEVIG 378

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2807 RSLaiCP------HTE-----LANEYG--PTENSVATTvmrhmekqayvsigqPIDGTQVLILNSNHQLQPIGVAGELCI 2873
Cdd:cd05966    379 KER--CPivdtwwQTEtggimITPLPGatPLKPGSATR---------------PFFGIEPAILDEEGNEVEGEVEGYLVI 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2874 AGT--GLARGYVNLPELTERAFtqnpFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGV 2951
Cdd:cd05966    442 KRPwpGMARTIYGDHERYEDTY----FSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAV 517

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 2952 KDAAVVAH---VTasGQTeLSAYVVTKPGLSTN-AVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:cd05966    518 AEAAVVGRphdIK--GEA-IYAFVTLKDGEEPSdELRKELrkhvRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
PLN02246 PLN02246
4-coumarate--CoA ligase
 1496-1932 3.20e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 91.58  E-value: 3.20e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1496 LH-YALEQQAEkTPDQAAVIfeDG----VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:PLN02246    25 LHdYCFERLSE-FSDRPCLI--DGatgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYPEERISFLLEDSGTNILLLQSAGL-HVPEFTGE----IVYLNQTNSGLAH--RLSN------PNVDVLPQSL 1637
Cdd:PLN02246   102 TTTANPFYTPAEIAKQAKASGAKLIITQSCYVdKLKGLAEDdgvtVVTIDDPPEGCLHfsELTQadenelPEVEISPDDV 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1638 AYVIYTSGSTGMPKGVEIEHRSAVNflnslqSRYQ----------LKHSDMIM------HktSYSFDaSIweLFWWPYAG 1701
Cdd:PLN02246   182 VALPYSSGTTGLPKGVMLTHKGLVT------SVAQqvdgenpnlyFHSDDVILcvlpmfH--IYSLN-SV--LLCGLRVG 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1702 ASVYLLPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHikyrsvPIKTNR----LKRVFSGGEQLGTHLVSRFYEL 1777
Cdd:PLN02246   251 AAILIMPK---FEIGALLELIQRHKVTIAPFVPPIVLAIAKS------PVVEKYdlssIRMVLSGAAPLGKELEDAFRAK 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1778 LPNVSITNSYGPTEA-TVEAAffdCPPHEKlERIPI-----GKPVHHVRLYLLNQNQRM-LPVGCIGELYIAGAGVARGY 1850
Cdd:PLN02246   322 LPNAVLGQGYGMTEAgPVLAM---CLAFAK-EPFPVksgscGTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGY 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1851 LNRPALTEErfledpfypgermykTGDVARWLPDGNVEFLGRTD-----DQV----KIRGYRIEPGEIEAALRSIEGVRE 1921
Cdd:PLN02246   398 LNDPEATAN---------------TIDKDGWLHTGDIGYIDDDDelfivDRLkeliKYKGFQVAPAELEALLISHPSIAD 462

                          490
                   ....*....|...
gi 1678550997 1922 AAVTVRTD--SGE 1932
Cdd:PLN02246   463 AAVVPMKDevAGE 475
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 2543-3019 9.44e-18

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: 89.74  E-value: 9.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERK 2622
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 R---YILSDSGTKLLMTINEAdLGVLADFEgeiltiESVEEDDKSPLPQMSSAHhlaYIIYTSGTTGRPKGVMVEHKGIA 2699
Cdd:cd05929     82 CaiiEIKAAALVCGLFTGGGA-LDGLEDYE------AAEGGSPETPIEDEAAGW---KMLYSGGTTGRPKGIKRGLPGGP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2700 NTLQWRRNAyafnetdtiLQLFSFSFD-------------GFITSMfTPLLSGAKAVLLHEEEAKDILAIkhqLSRQRIT 2766
Cdd:cd05929    152 PDNDTLMAA---------ALGFGPGADsvylspaplyhaaPFRWSM-TALFMGGTLVLMEKFDPEEFLRL---IERYRVT 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2767 HMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGEAADRELIARSLAICPhtELANE-YGPTEnSVATTVMRHMEKQAY 2841
Cdd:cd05929    219 FAQFVPTMFVRLLklpeAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG--PIIWEyYGGTE-GQGLTIINGEEWLTH 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2842 V-SIGQPIDGtQVLILNSNHQLQPIGVAGELCIAGtGLARGYVNLPELTERAFtqnpfkpEARMYRT-GDAARWMADGTL 2919
Cdd:cd05929    296 PgSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAAR-------NEGGWSTlGDVGYLDEDGYL 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2920 EYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVV-AHVTASGQtELSAYVVTKPGLSTNAVRSE-----LQNKLPV 2993
Cdd:cd05929    367 YLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVgVPDEELGQ-RVHAVVQPAPGADAGTALAEeliafLRDRLSR 445

                          490       500
                   ....*....|....*....|....*.
gi 1678550997 2994 FMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05929    446 YKCPRSIEFVAELPRDDTGKLYRRLL 471
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1520-1924 1.16e-17

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


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 88.78  E-value: 1.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLP----IDPDYPEERIsflleDSGTNIL 1595
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRV-----DRGGAVY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1596 LLQSAGLHVpeftgeivylnqtnsglahrlSNPnvdvlpqSLAYviYTSGSTGMPKGVEIEHRS-AVNFLNSLqsrY--Q 1672
Cdd:cd05974     76 AAVDENTHA---------------------DDP-------MLLY--FTSGTTSKPKLVEHTHRSyPVGHLSTM---YwiG 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1673 LKHSDMIMHKTSYSFDASIWELFWWPY-AGASVYLLPQGgEKEPEVIAKAIEEQKITAMHFVPSMLHAFL-EHIKYRSVP 1750
Cdd:cd05974    123 LKPGDVHWNISSPGWAKHAWSCFFAPWnAGATVFLFNYA-RFDAKRVLAALVRYGVTTLCAPPTVWRMLIqQDLASFDVK 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1751 iktnrLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAffdCPPHEKLERIPIGKPVHHVRLYLLNQNQRM 1830
Cdd:cd05974    202 -----LREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVG---NSPGQPVKAGSMGRPLPGYRVALLDPDGAP 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1831 LPVGCIGELYIAG--AGVARGYLNRPALTEERfLEDPFYPgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGE 1908
Cdd:cd05974    273 ATEGEVALDLGDTrpVGLMKGYAGDPDKTAHA-MRGGYYR------TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE 345

                          410
                   ....*....|....*.
gi 1678550997 1909 IEAALRSIEGVREAAV 1924
Cdd:cd05974    346 LESVLIEHPAVAEAAV 361
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 470-949 1.25e-17

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: 89.93  E-value: 1.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  470 EKQAEKTPDAHAVI------DQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGgAIVPV 543
Cdd:cd05966     60 DRHLKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG-AVHSV 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  544 -----DPHYPADRIryilHDCGCS--------------------------------HVVSQAHLPSSLEDNYIITHP-ED 585
Cdd:cd05966    139 vfagfSAESLADRI----NDAQCKlvitadggyrggkviplkeivdealekcpsveKVLVVKRTGGEVPMTEGRDLWwHD 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  586 IESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQfeHRNMANLLKFEYTHSGI-DFEADvlqfatpsfDV--CYQEI- 661
Cdd:cd05966    215 LMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVV--HTTGGYLLYAATTFKYVfDYHPD---------DIywCTADIg 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  662 ---------FSALLKGGTLHI---VPeaikrDVPQ---LFAFINKHQTNIVFL-PTAfIKMifserelansfpdgvkhLI 725
Cdd:cd05966    284 witghsyivYGPLANGATTVMfegTP-----TYPDpgrYWDIVEKHKVTIFYTaPTA-IRA-----------------LM 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  726 AAGEQ-LMISDLFQdvLRKRG-----IH------LHNHYGPSETHVVSTY----------TihpgdPIPELPPIgKPIGC 783
Cdd:cd05966    341 KFGDEwVKKHDLSS--LRVLGsvgepINpeawmwYYEVIGKERCPIVDTWwqtetggimiT-----PLPGATPL-KPGSA 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  784 T------DLYILNHQKQLQPCGVPGELYISGA--SVARG-YVNHDKLTSDKFSsdPFKPdviMYRTGDLARRLEDGNIEY 854
Cdd:cd05966    413 TrpffgiEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTiYGDHERYEDTYFS--KFPG---YYFTGDGARRDEDGYYWI 487

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  855 IGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEhelcAYYCSV---------QKLNTiDLRSYMASEL 924
Cdd:cd05966    488 TGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVgRPHDIKGE----AIYAFVtlkdgeepsDELRK-ELRKHVRKEI 562

                          570       580
                   ....*....|....*....|....*
gi 1678550997  925 PEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd05966    563 GPIATPDKIQFVPGLPKTRSGKIMR 587
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 473-952 1.41e-17

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: 88.97  E-value: 1.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQAHLPSSLEdnyiitHPEDIESKVDGSN---IKSVNNADDllyMIYTSGTTGKPKGVQ--FEHRNM 627
Cdd:cd05929     82 CAIIEIKAAALVCGLFTGGGALD------GLEDYEAAEGGSPetpIEDEAAGWK---MLYSGGTTGRPKGIKrgLPGGPP 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  628 ANLLKFEYThSGIDFEADVLQF-------ATPsFDVCyqeiFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQ-TNIVFL 699
Cdd:cd05929    153 DNDTLMAAA-LGFGPGADSVYLspaplyhAAP-FRWS----MTALFMGGTLVLME---KFDPEEFLRLIERYRvTFAQFV 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  700 PTAFIKMIFSERELANSFP-DGVKHLIAAG-------EQLMIsDLFQDVLrkrgihlHNHYGPSE----THVVST-YTIH 766
Cdd:cd05929    224 PTMFVRLLKLPEAVRNAYDlSSLKRVIHAAapcppwvKEQWI-DWGGPII-------WEYYGGTEgqglTIINGEeWLTH 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  767 PGDpipelppIGKPIGcTDLYILNHQKQLQPCGVPGELYISGASvARGYVNHDKLTSDKFSSDPFkpdvimyRT-GDLAR 845
Cdd:cd05929    296 PGS-------VGRAVL-GKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGW-------STlGDVGY 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  846 RLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEHELCAyycsVQKLNTIDLRSYMASEL 924
Cdd:cd05929    360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVgVPDEELGQRVHAV----VQPAPGADAGTALAEEL 435

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1678550997  925 PE--------YMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05929    436 IAflrdrlsrYKCPRSIEFVAELPRDDTGKLYRRLL 471
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 517-953 1.45e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 88.17  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  517 AIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQahlpsslEDNYIITHpedieskvdgsnIK 596
Cdd:PRK08308    36 AVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYG-------ESDFTKLE------------AV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  597 SVNNADDLLYMiYTSGTTGKPKGVqfehrnmanllkfEYTHSGIDFEAD--VLQFATPSFDV----C-----YQEI---F 662
Cdd:PRK08308    97 NYLAEEPSLLQ-YSSGTTGEPKLI-------------RRSWTEIDREIEayNEALNCEQDETpivaCpvthsYGLIcgvL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  663 SALLKGGTLHIV----PE---AIKRDVPQlfafinkhqtNIVFLPTAFIKMIfserelaNSFPDGVK--HLIAAGEQLMI 733
Cdd:PRK08308   163 AALTRGSKPVIItnknPKfalNILRNTPQ----------HILYAVPLMLHIL-------GRLLPGTFqfHAVMTSGTPLP 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  734 SDLFQDvLRKRGIHLHNHYGPSETHVVStytIHPgdPIPELPPIGKPigctdlyiLNHqkqlqpcgvpgelyisgASVAR 813
Cdd:PRK08308   226 EAWFYK-LRERTTYMMQQYGCSEAGCVS---ICP--DMKSHLDLGNP--------LPH-----------------VSVSA 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GyvnhdkltsdkfsSDPFKPDVIMYR-------TGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISE 886
Cdd:PRK08308   275 G-------------SDENAPEEIVVKmgdkeifTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE 341

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  887 AAILIWQDQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALP 953
Cdd:PRK08308   342 AVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 1492-1978 1.91e-17

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 88.94  E-value: 1.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1492 MNqtLHYALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAY 1571
Cdd:PRK07470     7 MN--LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1572 LPIDPDYPEERISFLLEDSGTNILLLQSA-GLHV-------PEFTGEIV---------YLNQTNSGLAHRLSNPNVDvlP 1634
Cdd:PRK07470    85 VPTNFRQTPDEVAYLAEASGARAMICHADfPEHAaavraasPDLTHVVAiggaragldYEALVARHLGARVANAAVD--H 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 QSLAYVIYTSGSTGMPKGVEIEHRS----AVNFLNSLQSryQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVyLLPqg 1710
Cdd:PRK07470   163 DDPCWFFFTSGTTGRPKAAVLTHGQmafvITNHLADLMP--GTTEQDASLVVAPLSHGAGIHQLCQVARGAATV-LLP-- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1711 GEK-EPEVIAKAIEEQKITAMHFVPSML-------------HAFLEHIKYRSVPIKTNRLKRVFsggEQLGTHLVSRFye 1776
Cdd:PRK07470   238 SERfDPAEVWALVERHRVTNLFTVPTILkmlvehpavdrydHSSLRYVIYAGAPMYRADQKRAL---AKLGKVLVQYF-- 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1777 llpnvsitnsyGPTEATVEAAFFdcPPHEKLE------RI-PIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARG 1849
Cdd:PRK07470   313 -----------GLGEVTGNITVL--PPALHDAedgpdaRIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAG 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1850 YLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD 1929
Cdd:PRK07470   380 YYNNPEANAKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPD 452

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1930 S--GEP--ELCAYVEGLQRN--EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 1978
Cdd:PRK07470   453 PvwGEVgvAVCVARDGAPVDeaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1483-1983 2.06e-17

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 88.89  E-value: 2.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1483 HLFEETGYSMNQTLHYALEQQAEktPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIY 1562
Cdd:PRK10946    14 RRYREKGYWQDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1563 GILKAGGAylPIDPDYPEERI--------------------SFLLEDSGTNILLLQSAGLHVPEFTGEivylnQTNSGLA 1622
Cdd:PRK10946    92 ALLKLGVA--PVNALFSHQRSelnayasqiepalliadrqhALFSDDDFLNTLVAEHSSLRVVLLLND-----DGEHSLD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1623 HRLSNPNVDVLPQS-----LAYVIYTSGSTGMPK---------------GVEI-EHRSAVNFLNSLQSryqlkhsdmiMH 1681
Cdd:PRK10946   165 DAINHPAEDFTATPspadeVAFFQLSGGSTGTPKliprthndyyysvrrSVEIcGFTPQTRYLCALPA----------AH 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1682 KTSYSFDASIWELfwwpYAGASVYLLPqggEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIK---YRSvPIKTNRLKR 1758
Cdd:PRK10946   235 NYPMSSPGALGVF----LAGGTVVLAP---DPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAeggSRA-QLASLKLLQ 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1759 VfsGGEQLGTHLVSRFYELLpNVSITNSYGPTEATVEAAFFDCPPheklERI------PIgKPVHHVRLylLNQNQRMLP 1832
Cdd:PRK10946   307 V--GGARLSETLARRIPAEL-GCQLQQVFGMAEGLVNYTRLDDSD----ERIfttqgrPM-SPDDEVWV--ADADGNPLP 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1833 VGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAA 1912
Cdd:PRK10946   377 QGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFY------CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENL 450

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 1913 LRSIEGVREAAVTVRTDS--GEPElCAYVegLQRNEVRA-QLERLLPG-----YMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK10946   451 LLRHPAVIHAALVSMEDElmGEKS-CAFL--VVKEPLKAvQLRRFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQL 526
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 1499-1981 3.51e-17

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 88.32  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDY 1578
Cdd:PLN02860    12 CLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRW 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1579 PEERISFLLEDSGTNILLLQSAGLHVPE--FTGEI------VYLNQTNSGLAHRLSN----------------PNVDVLP 1634
Cdd:PLN02860    92 SFEEAKSAMLLVRPVMLVTDETCSSWYEelQNDRLpslmwqVFLESPSSSVFIFLNSflttemlkqralgtteLDYAWAP 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 QSLAYVIYTSGSTGMPKGVEIEHRSAVnflnsLQSRYQLK-----HSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQ 1709
Cdd:PLN02860   172 DDAVLICFTSGTTGRPKGVTISHSALI-----VQSLAKIAivgygEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPK 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1710 ggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGP 1789
Cdd:PLN02860   247 ---FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGM 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1790 TEATVEAAFFdcPPHEKLERIPIGKPVHHVRLYLLNQNQrmlPVG-CIG------ELYIAGAGVAR--GYLNRPALTEER 1860
Cdd:PLN02860   324 TEACSSLTFM--TLHDPTLESPKQTLQTVNQTKSSSVHQ---PQGvCVGkpaphvELKIGLDESSRvgRILTRGPHVMLG 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1861 FL-EDPFYPGERM----YKTGDVArWLPD-GNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPE 1934
Cdd:PLN02860   399 YWgQNSETASVLSndgwLDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTE 477

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 1935 LCAYV----EGLQRNEVRAQLERL-----------------LPGYMVP-AYMIEMEQWPVTPSGKLDRN 1981
Cdd:PLN02860   478 MVVACvrlrDGWIWSDNEKENAKKnltlssetlrhhcreknLSRFKIPkLFVQWRKPFPLTTTGKIRRD 546
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 12-304 3.57e-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: 87.48  E-value: 3.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVERHDIFRTIFIS------QNVSSPQQVVLRERN 85
Cdd:cd19540      3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEddggpyQVVLPAAEARPDLTV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   86 VIVLEEDITHLNEAEQSqfieqwkekdrdRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYA 165
Cdd:cd19540     83 VDVTEDELAARLAEAAR------------RGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  166 SYVNASPITLEP--VQpYGKYIKW---LM--EQDKEQAVS----YWDHYLSGHEQQTVLP--KQKKTKGKSRQEHVTFSF 232
Cdd:cd19540    151 ARRAGRAPDWAPlpVQ-YADYALWqreLLgdEDDPDSLAArqlaYWRETLAGLPEELELPtdRPRPAVASYRGGTVEFTI 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997  233 SKEESSRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAeiEGIEHMVGLFINTMPVRVQ 304
Cdd:cd19540    230 DAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD--EALDDLVGMFVNTLVLRTD 299
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 469-625 4.14e-17

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 88.39  E-value: 4.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  469 FEKQAEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGG---------- 538
Cdd:PRK08279    43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvallntqqr 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  539 ------AIVPVDPhypadriRYILHDCGCSHVVSQA------HLPSSLEDNYIITHPEDIESKVDGSNIKSVNN------ 600
Cdd:PRK08279   123 gavlahSLNLVDA-------KHLIVGEELVEAFEEAradlarPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNpasrsg 195

                          170       180
                   ....*....|....*....|....*..
gi 1678550997  601 --ADDLLYMIYTSGTTGKPKGVQFEHR 625
Cdd:PRK08279   196 vtAKDTAFYIYTSGTTGLPKAAVMSHM 222
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 761-1043 5.06e-17

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 84.80  E-value: 5.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  761 STYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPcgVPGELYISGASVARGYVNHDKLTsDKFSSDPFKPDVI---- 836
Cdd:COG3433      2 AIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQG--YFGGFGGEGGLLGAGLLLRIRLL-AAAARAPFIPVPYpaqp 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  837 --MYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHP-DISEAAILIWQDQNGEHELCAYYCsVQKLNT 913
Cdd:COG3433     79 grQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAvVRVAVLAALRGAGVGLLLIVGAVA-ALDGLA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  914 IDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASISGNPYTAPRN-----LLEAKLSQLFEDVLKNG-- 986
Cdd:COG3433    158 AAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaletaLTEEELRADVAELLGVDpe 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  987 HIGIQDNFFDNGGHSLKATVLMSRiAKEFHVQVSLKDIFAHPTVEGLALIIREAEQN 1043
Cdd:COG3433    238 EIDPDDNLFDLGLDSIRLMQLVER-WRKAGLDVSFADLAEHPTLAAWWALLAAAQAA 293
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 489-902 6.04e-17

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 87.14  E-value: 6.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVV--- 565
Cdd:cd05932      7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgk 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  566 -----SQAH-LPSSLEDNYIITHP--------EDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMANLL 631
Cdd:cd05932     87 lddwkAMAPgVPEGLISISLPPPSaancqyqwDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  632 KFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAI-------KRDVPQLFAFI----NKHQTNI---- 696
Cdd:cd05932    167 QAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLdtfvedvQRARPTLFFSVprlwTKFQQGVqdki 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  697 ------VFLPTAFIKMIFSERELANSFPDGVKhlIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTiHPGDp 770
Cdd:cd05932    247 pqqklnLLLKIPVVNSLVKRKVLKGLGLDQCR--LAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLN-YPGR- 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  771 iPELPPIGKPIGCTDLYIlnhqkqlqpcGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDG 850
Cdd:cd05932    323 -DKIGTVGNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGF------LRTGDKGELDADG 385

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  851 NIEYIGRADNQVKI-RGYRIEPQEIEVTLMNHPDIsEAAILIWQDQNGEHELC 902
Cdd:cd05932    386 NLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAPLALV 437
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 2559-2991 7.86e-17

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 87.14  E-value: 7.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2559 LTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMtin 2638
Cdd:cd05932      7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2639 eadLGVLADFE-------GEILTIESveeddkSPLPQMSS---------------------AHHLAYIIYTSGTTGRPKG 2690
Cdd:cd05932     84 ---VGKLDDWKamapgvpEGLISISL------PPPSAANCqyqwddliaqhppleerptrfPEQLATLIYTSGTTGQPKG 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2691 VMVEHKGIANTLQWRRNAYAFNETDtilQLFSFSFDGFITS-MFTPLLSGAKAVLLHEEEAKDILAikHQLSRQRITHMI 2769
Cdd:cd05932    155 VMLTFGSFAWAAQAGIEHIGTEEND---RMLSYLPLAHVTErVFVEGGSLYGGVLVAFAESLDTFV--EDVQRARPTLFF 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2770 IVPVLY----RALLDVVQPEDVKTLRVVTLAGEAADRELIA-------------------------RSLAIcphtELANE 2820
Cdd:cd05932    230 SVPRLWtkfqQGVQDKIPQQKLNLLLKIPVVNSLVKRKVLKglgldqcrlagcgsapvppallewyRSLGL----NILEA 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2821 YGPTENSVATTVMRHMEKQAYvSIGQPIDGTQVlilnsnhqlqPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkp 2900
Cdd:cd05932    306 YGMTENFAYSHLNYPGRDKIG-TVGNAGPGVEV----------RISEDGEILVRSPALMMGYYKDPEATAEAFTADGF-- 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2901 earmYRTGDAARWMADGTLEYLGRIDDQVKI-RGYRVETKEIESvirciKGVKDAAVVAH-VTASGQTELSAYVVTKPG- 2977
Cdd:cd05932    373 ----LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIEN-----KLAEHDRVEMVcVIGSGLPAPLALVVLSEEa 443

                          490
                   ....*....|....*.
gi 1678550997 2978 --LSTNAVRSELQNKL 2991
Cdd:cd05932    444 rlRADAFARAELEASL 459
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 2678-3021 8.66e-17

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: 87.14  E-value: 8.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKgvMVEHK----GIANTLQWRRnAYAFNETDTIlqlFSFSFDGFI----TSMFTPLLSGAkAVLLHEEE 2749
Cdd:cd05928    179 IYFTSGTTGSPK--MAEHShsslGLGLKVNGRY-WLDLTASDIM---WNTSDTGWIksawSSLFEPWIQGA-CVFVHHLP 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2750 AKDILAIKHQLSRQRITHMIIVPVLYRALLDvvqpEDVKTLRVVTL-----AGEAADRELIARSLAicpHT--ELANEYG 2822
Cdd:cd05928    252 RFDPLVILKTLSSYPITTFCGAPTVYRMLVQ----QDLSSYKFPSLqhcvtGGEPLNPEVLEKWKA---QTglDIYEGYG 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2823 PTENSVATTVMRHMEKQAYvSIGQPIDGTQVLILNSNHQLQPIGVAGELCI-----AGTGLARGYVNLPELTERAFTQNp 2897
Cdd:cd05928    325 QTETGLICANFKGMKIKPG-SMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD- 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2898 fkpearMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPG 2977
Cdd:cd05928    403 ------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQ 476

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2978 LSTN---AVRSELQ----NKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPK 3021
Cdd:cd05928    477 FLSHdpeQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 1624-1983 1.18e-16

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 87.67  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1624 RLSNPNVDvlPQSLAYVIYTSGSTGMPKGVEIEHRsavNFL-NSLQSR--YQLKHSDMIM------HktSYSFDASiwel 1694
Cdd:PRK08633   773 RLYGPTFK--PDDTATIIFSSGSEGEPKGVMLSHH---NILsNIEQISdvFNLRNDDVILsslpffH--SFGLTVT---- 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1695 FWWPYA-GASVYLLPqggekEP---EVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRsvPIKTNRLKRVFSGGEQLGTHL 1770
Cdd:PRK08633   842 LWLPLLeGIKVVYHP-----DPtdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLH--PLMFASLRLVVAGAEKLKPEV 914

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1771 VSRFyELLPNVSITNSYGPTEaTVEAAFFDCPPHEKLERIP--------IGKPVHHVRLYLLN-QNQRMLPVGCIGELYI 1841
Cdd:PRK08633   915 ADAF-EEKFGIRILEGYGATE-TSPVASVNLPDVLAADFKRqtgskegsVGMPLPGVAVRIVDpETFEELPPGEDGLILI 992

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1842 AGAGVARGYLNRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSI--EGV 1919
Cdd:PRK08633   993 GGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEE 1069

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 1920 REAAVTVRTDS--GEPELCAYVEGLQRNE--VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK08633  1070 VVFAVTAVPDEkkGEKLVVLHTCGAEDVEelKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 3123-3569 1.23e-16

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: 85.72  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQKWFLSQDIKEKH---HFNQSVM-LHRStsVQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQY---NRPLShsdd 3195
Cdd:cd19543      5 SPMQEGMLFHSLLDPGsgaYVEQMVItLEGP--LDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVvlkDRKLP---- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3196 alygLQMIDLSAPDGTDGNRPYEPLIKRhvlDIQQKMDLKNGPLLQAGLFHTIDGDF-LFLSAHHLVVDGISWRVLLEDL 3274
Cdd:cd19543     79 ----WRELDLSHLSEAEQEAELEALAEE---DRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKEL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3275 ALGYRQAAGGEDIKLPPkTSSFKAYAKKLS--DYAESQQlmkqlkYWRE--AEEYQTEALPFDQIDGTrAHEGQRSTISF 3350
Cdd:cd19543    152 FAIYAALGEGQPPSLPP-VRPYRDYIAWLQrqDKEAAEA------YWREylAGFEEPTPLPKELPADA-DGSYEPGEVSF 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3351 TLNDKETAALLKDANSAYNTdtqdmlLASVIlalrhwtnQSAFKLSLEGH-GREDVLKGIDVS----------RTIGWFT 3419
Cdd:cd19543    224 ELSAELTARLQELARQHGVT------LNTVV--------QGAWALLLSRYsGRDDVVFGTTVSgrpaelpgieTMVGLFI 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3420 AIYPLLIKLNADlpdseesmvhvlKTTKDTLRRVpdkgfgygvikyltppgKKDINFTgapeISFNYLGQFESGRTAEV- 3498
Cdd:cd19543    290 NTLPVRVRLDPD------------QTVLELLKDL-----------------QAQQLEL----REHEYVPLYEIQAWSEGk 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3499 -------------PEEDAFSFSPLGAGGDISTTWNREQS-LDISAIAAEGK-LTVNMTYDNARFQRKTIEQLSETCRQFL 3563
Cdd:cd19543    337 qalfdhllvfenyPVDESLEEEQDEDGLRITDVSAEEQTnYPLTVVAIPGEeLTIKLSYDAEVFDEATIERLLGHLRRVL 416


                   ....*.
gi 1678550997 3564 LQLIEH 3569
Cdd:cd19543    417 EQVAAN 422
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 2556-3025 1.31e-16

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: 85.94  E-value: 1.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2556 DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLM 2635
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2636 TINEADLgvLADFEGEILTIESVEEDDKsplpqmssahhLAYiIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETD 2715
Cdd:cd05939     81 FNLLDPL--LTQSSTEPPSQDDVNFRDK-----------LFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPED 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2716 TI---LQLFSFSfdGFITSMFTPLLSGAKAVLLHEEEAKDILA--IKHQLS-RQRITHMIivpvlyRALLDVVQPEDVKT 2789
Cdd:cd05939    147 VVydcLPLYHSA--GGIMGVGQALLHGSTVVIRKKFSASNFWDdcVKYNCTiVQYIGEIC------RYLLAQPPSEEEQK 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2790 LRVVTLAG---------EAADRELIARslaicphteLANEYGPTE-NSVATTVMRHMEKQAYVSIG----QPI------D 2849
Cdd:cd05939    219 HNVRLAVGnglrpqiweQFVRRFGIPQ---------IGEFYGATEgNSSLVNIDNHVGACGFNSRIlpsvYPIrlikvdE 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2850 GTQVLILNSNHQLQPI--GVAGELC---IAGTGLAR--GYVNLPElTERAFTQNPFKPEARMYRTGDAARWMADGTLEYL 2922
Cdd:cd05939    290 DTGELIRDSDGLCIPCqpGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFK 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2923 GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV----VAHVtaSGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPA 2998
Cdd:cd05939    369 DRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGV--EGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQ 446

                          490       500
                   ....*....|....*....|....*..
gi 1678550997 2999 FIEKLDSLPLSPNGKLDRGALPKPVYN 3025
Cdd:cd05939    447 FIRLLPEVDKTGTFKLQKTDLQKEGYD 473
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 1497-1985 1.85e-16

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 86.10  E-value: 1.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1497 HYALEQQAEKT-PDQAAVIFEDGV----MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAY 1571
Cdd:PRK04319    46 YEAIDRHADGGrKDKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1572 LPIDPDYPEERISFLLEDSGTNILLLQSAGL------------HV------PEFTGEIVYLNQTNSGLAHRLSNPNVDvl 1633
Cdd:PRK04319   126 GPLFEAFMEEAVRDRLEDSEAKVLITTPALLerkpaddlpslkHVllvgedVEEGPGTLDFNALMEQASDEFDIEWTD-- 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQSLAYVIYTSGSTGMPKGVEieHrsaVnflnslqsryqlkHSDMIMHKTS--YSFDASIWELFW------W-------- 1697
Cdd:PRK04319   204 REDGAILHYTSGSTGKPKGVL--H---V-------------HNAMLQHYQTgkYVLDLHEDDVYWctadpgWvtgtsygi 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1698 --PY-AGASvyLLPQGGEKEPEVIAKAIEEQKITAMHFVPS---ML-HAFLEHIKYRSVPiktnRLKRVFSGGEQLGTHL 1770
Cdd:PRK04319   266 faPWlNGAT--NVIDGGRFSPERWYRILEDYKVTVWYTAPTairMLmGAGDDLVKKYDLS----SLRHILSVGEPLNPEV 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1771 VSRFYELLpNVSITNSYGPTE--ATVEAAF--FDCPPHEkleripIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAgAG- 1845
Cdd:PRK04319   340 VRWGMKVF-GLPIHDNWWMTEtgGIMIANYpaMDIKPGS------MGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGw 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1846 --VARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA 1923
Cdd:PRK04319   412 psMMRGIWNNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAG 484

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 1924 VTVRTDSGEPELC-AYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:PRK04319   485 VIGKPDPVRGEIIkAFValrPGYEpseelKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 600-967 2.07e-16

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: 86.22  E-value: 2.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 NADDLLYMIYTSGTTGKPKGVQFE--------HRNMANLlkfeY-THSGIDFEA--DVLQFATPSFdVCYqeifSALLKG 668
Cdd:cd05967    228 AATDPLYILYTSGTTGKPKGVVRDngghavalNWSMRNI----YgIKPGDVWWAasDVGWVVGHSY-IVY----GPLLHG 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  669 GTlHIVPEAIKRDVP---QLFAFINKHQTNIVF-LPTAFikmifseRELANSFPDG----------VKHLIAAGEQLMiS 734
Cdd:cd05967    299 AT-TVLYEGKPVGTPdpgAFWRVIEKYQVNALFtAPTAI-------RAIRKEDPDGkyikkydlssLRTLFLAGERLD-P 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  735 DLFQDVLRKRGIHLHNHYGPSETH--VVSTYTIHPGDPIPELPPiGKPIGCTDLYILNHQKQLQPCGVPGELYISG---- 808
Cdd:cd05967    370 PTLEWAENTLGVPVIDHWWQTETGwpITANPVGLEPLPIKAGSP-GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLplpp 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  809 ASVARGYVNHDKLTSDKFSSDPfkpdvIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAA 888
Cdd:cd05967    449 GCLLTLWKNDERFKKLYLSKFP-----GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECA 523

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  889 ILIWQDQ-NGEHELCayYCSVQKLNTID-------LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALpepDASIS 960
Cdd:cd05967    524 VVGVRDElKGQVPLG--LVVLKEGVKITaeelekeLVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL---RKIAD 598


                   ....*..
gi 1678550997  961 GNPYTAP 967
Cdd:cd05967    599 GEDYTIP 605
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 607-947 2.52e-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: 2.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  607 MIYTSGTTGKPKGVQFEHRNMANLLKfEYTHSGIDFEADVLQFATPSF-DVCYQE-IFSALLKGGTlhIVPEAIkRDVPQ 684
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAA-AWADCADLTEDDRYLIINPFFhTFGYKAgIVACLLTGAT--VVPVAV-FDVDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  685 LFAFINKHQtnIVFLP---TAFIKMI---------FSERELANSfpdGVKHLIAAGEQLMISDL-FQDVLrkrgihlhNH 751
Cdd:cd17638     81 ILEAIERER--ITVLPgppTLFQSLLdhpgrkkfdLSSLRAAVT---GAATVPVELVRRMRSELgFETVL--------TA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  752 YGPSETHVVSTytIHPGDPIPELP-PIGKPIGCTDLYilnhqkqlqpCGVPGELYISGASVARGYVNHDKLTSDKFSSDP 830
Cdd:cd17638    148 YGLTEAGVATM--CRPGDDAETVAtTCGRACPGFEVR----------IADDGEVLVRGYNVMQGYLDDPEATAEAIDADG 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  831 FkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSV-- 908
Cdd:cd17638    216 W------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARpg 289

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1678550997  909 QKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKV 947
Cdd:cd17638    290 VTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 489-889 3.52e-16

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


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 84.43  E-value: 3.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHypadriryilhdcgcshvVSQA 568
Cdd:cd05910      3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGRK 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDnyiithpedieskVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMA---NLLK--FEYTHSGIDFe 643
Cdd:cd05910     65 NLKQCLQE-------------AEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAaqiDALRqlYGIRPGEVDL- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  644 ADVLQFAtpsfdvcyqeIFSALLkgGTLHIVPE-----AIKRDVPQLFAFINKHQTNIVFLPTAFIKMIfSERELANSFP 718
Cdd:cd05910    131 ATFPLFA----------LFGPAL--GLTSVIPDmdptrPARADPQKLVGAIRQYGVSIVFGSPALLERV-ARYCAQHGIT 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  719 -DGVKHLIAAGEQLMISDLfqDVLRK---RGIHLHNHYGPSE--------THVVSTYTIHP---------GDPIPelPPI 777
Cdd:cd05910    198 lPSLRRVLSAGAPVPIALA--ARLRKmlsDEAEILTPYGATEalpvssigSRELLATTTAAtsggagtcvGRPIP--GVR 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  778 GKPIGCTDLYILNHQKQLQ-PCGVPGELYISGASVARGYVNHDKLTSDKFSSDPfkPDVIMYRTGDLARRLEDGNIEYIG 856
Cdd:cd05910    274 VRIIEIDDEPIAEWDDTLElPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRLWFCG 351

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1678550997  857 RADNQVKIRGYRIEPQEIEVTLMNHPDISEAAI 889
Cdd:cd05910    352 RKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 2678-3015 3.86e-16

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: 82.73  E-value: 3.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 IIYTSGTTGRPKGVMVEHKGI---ANTLQWRRNAyafNETDTILQ---LFSFsfdGFITSMFTPLLSGAKAVLLHEEEAK 2751
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQAI---DEGTVFLNsgpLFHI---GTLMFTLATFHAGGTNVFVRRVDAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2752 DILAIkhqLSRQRITHMIIVPVLYRALLDVVQ--PEDVKTLRVVTLAGE-----AADRELIARSLAicphtelanEYGPT 2824
Cdd:cd17636     79 EVLEL---IEAERCTHAFLLPPTIDQIVELNAdgLYDLSSLRSSPAAPEwndmaTVDTSPWGRKPG---------GYGQT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2825 ENSvATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTqnpfkpeARM 2904
Cdd:cd17636    147 EVM-GLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGW 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2905 YRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLStnAVR 2984
Cdd:cd17636    219 HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS--VTE 296

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1678550997 2985 SEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:cd17636    297 AELiehcRARIASYKKPKSVEFADALPRTAGGADD 331
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 1502-1936 5.33e-16

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 84.65  E-value: 5.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1502 QQAEKTPDQAAviFEDGV----MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPD 1577
Cdd:PLN02330    36 QDAELYADKVA--FVEAVtgkaVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPT 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1578 YPEERISFLLEDSGTNILLLQSA------GLHVPEFT-GEIVYLNQTN----SGLAHRLSNPNV--DVLPQSLAYVIYTS 1644
Cdd:PLN02330   114 ALESEIKKQAEAAGAKLIVTNDTnygkvkGLGLPVIVlGEEKIEGAVNwkelLEAADRAGDTSDneEILQTDLCALPFSS 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1645 GSTGMPKGVEIEHRSAV-NFLNSLQSryqlKHSDMIMHKTSYSFdasIWELFWWPYAGASVYLLPQGGEK------EPEV 1717
Cdd:PLN02330   194 GTTGISKGVMLTHRNLVaNLCSSLFS----VGPEMIGQVVTLGL---IPFFHIYGITGICCATLRNKGKVvvmsrfELRT 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1718 IAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAA 1797
Cdd:PLN02330   267 FLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITL 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1798 FFDCPP--HEKLERIPIGKPVHHVRLYLLN-QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyK 1874
Cdd:PLN02330   347 THGDPEkgHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWL------H 420

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1875 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGE-PELC 1936
Cdd:PLN02330   421 TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDeeAGEiPAAC 485
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 489-954 6.07e-16

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 84.16  E-value: 6.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVV--- 565
Cdd:PRK07514    29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVcdp 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  566 SQAHLPSSLEDNYIITHPEDIESKVDGSNIKS-----------VNNADDLLYMIYTSGTTGKPKGVQFEHRNMA-NLLKF 633
Cdd:PRK07514   109 ANFAWLSKIAAAAGAPHVETLDADGTGSLLEAaaaapddfetvPRGADDLAAILYTSGTTGRSKGAMLSHGNLLsNALTL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  634 -EYTHSGIDfeaDVLQFATPSFDVcyQEIFSA----LLKGGTLHIVPeaiKRDVPQLFAfinkhqtnivFLPTAFIKM-- 706
Cdd:PRK07514   189 vDYWRFTPD---DVLIHALPIFHT--HGLFVAtnvaLLAGASMIFLP---KFDPDAVLA----------LMPRATVMMgv 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 -IFSERELANsfpDGVKHLIAAGEQLMIS-------DLFQDVLRKRGIHLHNHYGPSEThVVSTYTIHPGDPIPElpPIG 778
Cdd:PRK07514   251 pTFYTRLLQE---PRLTREAAAHMRLFISgsapllaETHREFQERTGHAILERYGMTET-NMNTSNPYDGERRAG--TVG 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  779 KPIGCTDLYILNHQ--KQLqPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIG 856
Cdd:PRK07514   325 FPLPGVSLRVTDPEtgAEL-PPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYVHIVG 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  857 RADNQVKIRGYRIEPQEIEVTL-------------MNHPDISEAAILIWQDQNGehelcayycsvQKLNTIDLRSYMASE 923
Cdd:PRK07514   398 RGKDLIISGGYNVYPKEVEGEIdelpgvvesavigVPHPDFGEGVTAVVVPKPG-----------AALDEAAILAALKGR 466

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1678550997  924 LPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK07514   467 LARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 490-952 6.60e-16

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 84.05  E-value: 6.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMK-GVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA 568
Cdd:cd05928     43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDnyIITHPEDIESKV-------DG-SNIKS-VNNAD-----------DLLYMIYTSGTTGKPKgvqfehrnMA 628
Cdd:cd05928    123 ELAPEVDS--VASECPSLKTKLlvseksrDGwLNFKElLNEAStehhcvetgsqEPMAIYFTSGTTGSPK--------MA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  629 nllkfEYTHS--GIDFEADVLQFA--TPSfDVCYQ------------EIFSALLKGGTL--HIVPeaiKRDVPQLFAFIN 690
Cdd:cd05928    193 -----EHSHSslGLGLKVNGRYWLdlTAS-DIMWNtsdtgwiksawsSLFEPWIQGACVfvHHLP---RFDPLVILKTLS 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  691 KHQ-TNIVFLPTAFiKMIFSERELANSFPdGVKHLIAAGEQLMiSDLFQDVLRKRGIHLHNHYGPSETHVV----STYTI 765
Cdd:cd05928    264 SYPiTTFCGAPTVY-RMLVQQDLSSYKFP-SLQHCVTGGEPLN-PEVLEKWKAQTGLDIYEGYGQTETGLIcanfKGMKI 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  766 HPGDpipelppIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVA-----RGYVNHDKLTSDKFSSDpfkpdviMYRT 840
Cdd:cd05928    341 KPGS-------MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRpfglfSGYVDNPEKTAATIRGD-------FYLT 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  841 GDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQ-NGEH-----ELCAYYCS--VQKLn 912
Cdd:cd05928    407 GDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPiRGEVvkafvVLAPQFLShdPEQL- 485

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997  913 TIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05928    486 TKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 1520-1885 9.14e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 83.80  E-value: 9.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELIGRGVK--PETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLL 1597
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1598 QsAGLHVPEFTgEIVYLNQTNSGlahrlsnPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVN----FLNSLQSRYQL 1673
Cdd:cd05927     86 D-AGVKVYSLE-EFEKLGKKNKV-------PPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNKI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1674 KHSDMIMhktSY-----SFDASIWELFWwpYAGASVYLLpQGgekEPEVIAKAIEEQKITAMHFVP-------------- 1734
Cdd:cd05927    157 NPTDVYI---SYlplahIFERVVEALFL--YHGAKIGFY-SG---DIRLLLDDIKALKPTVFPGVPrvlnriydkifnkv 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 ---SMLHAFLEHIKYRSvpiKTNRLKR------------VF---------------SGGEQLGTHlVSRFYELLPNVSIT 1784
Cdd:cd05927    228 qakGPLKRKLFNFALNY---KLAELRSgvvraspfwdklVFnkikqalggnvrlmlTGSAPLSPE-VLEFLRVALGCPVL 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1785 NSYGPTEaTVEAAFFDCPPheklERIP--IGKPV--HHVRL-------YL-LNQNQRmlpvgciGELYIAGAGVARGYLN 1852
Cdd:cd05927    304 EGYGQTE-CTAGATLTLPG----DTSVghVGGPLpcAEVKLvdvpemnYDaKDPNPR-------GEVCIRGPNVFSGYYK 371

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1678550997 1853 RPALTEERFLEDPFypgermYKTGDVARWLPDG 1885
Cdd:cd05927    372 DPEKTAEALDEDGW------LHTGDIGEWLPNG 398
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 2534-2912 1.39e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 83.56  E-value: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAARTPKASALVSGD------KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAG 2607
Cdd:PRK12582    50 SIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2608 GCYVPIDPEYP--------------KERKRYILSDSG---TKLLMTINEAD---LGVLADFEGeiltIESVEEDD---KS 2664
Cdd:PRK12582   130 VPAAPVSPAYSlmshdhaklkhlfdLVKPRVVFAQSGapfARALAALDLLDvtvVHVTGPGEG----IASIAFADlaaTP 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2665 PLPQMSSAHH------LAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQL-----FSFSFDGFITsmF 2733
Cdd:PRK12582   206 PTAAVAAAIAaitpdtVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSldwmpWNHTMGGNAN--F 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2734 TPLLSGAKAvlLHEEEAKDILAIKHQLSR--QRI--THMIIVPVLYRALLDVVQPEDV------KTLRVVTLAGEAADRE 2803
Cdd:PRK12582   284 NGLLWGGGT--LYIDDGKPLPGMFEETIRnlREIspTVYGNVPAGYAMLAEAMEKDDAlrrsffKNLRLMAYGGATLSDD 361

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2804 LIAR--SLAICPHTE---LANEYGPTENSvATTVMRHMEKQAYVSIGQPIDGTQVlilnsnhQLQPIGVAGELCIAGTGL 2878
Cdd:PRK12582   362 LYERmqALAVRTTGHripFYTGYGATETA-PTTTGTHWDTERVGLIGLPLPGVEL-------KLAPVGDKYEVRVKGPNV 433

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1678550997 2879 ARGYVNLPELTERAFTQNPFkpearmYRTGDAAR 2912
Cdd:PRK12582   434 TPGYHKDPELTAAAFDEEGF------YRLGDAAR 461
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1500-1983 1.50e-15

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 83.18  E-value: 1.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELI-GRGVKPETTVAIIgkrSPEML---LGIYGILKAGGAYLPID 1575
Cdd:PRK08974    29 FEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALM---MPNLLqypIALFGILRAGMIVVNVN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1576 PDYPEERISFLLEDSGTNILLLQSAGLHVPEftgEIVYLNQTNS----GLAHRLSNP-----NVDV-----------LPQ 1635
Cdd:PRK08974   106 PLYTPRELEHQLNDSGAKAIVIVSNFAHTLE---KVVFKTPVKHviltRMGDQLSTAkgtlvNFVVkyikrlvpkyhLPD 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1636 S------------------------LAYVIYTSGSTGMPKGVEIEHRSAVNflNSLQSRYqlKHSDMIMHKTSYSFDA-S 1690
Cdd:PRK08974   183 AisfrsalhkgrrmqyvkpelvpedLAFLQYTGGTTGVAKGAMLTHRNMLA--NLEQAKA--AYGPLLHPGKELVVTAlP 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1691 IWELFwwpyaGASV---YLLPQGGEK----EPEVIAKAIEEQK---ITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKrvf 1760
Cdd:PRK08974   259 LYHIF-----ALTVnclLFIELGGQNllitNPRDIPGFVKELKkypFTAITGVNTLFNALLNNEEFQELDFSSLKLS--- 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1761 SGGEQLGTHLVSRFYELLPNVSITNSYGPTEAT--VEAAFFDCPPHEKleriPIGKPVHHVRLYLLNQNQRMLPVGCIGE 1838
Cdd:PRK08974   331 VGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplVSVNPYDLDYYSG----SIGLPVPSTEIKLVDDDGNEVPPGEPGE 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1839 LYIAGAGVARGYLNRPALTEErFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEG 1918
Cdd:PRK08974   407 LWVKGPQVMLGYWQRPEATDE-VIKDGW------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 1919 VRE-AAVTVRTD-SGEpELCAYV----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK08974   480 VLEvAAVGVPSEvSGE-AVKIFVvkkdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 489-887 1.74e-15

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: 82.40  E-value: 1.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVsqa 568
Cdd:cd05940      4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV--- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslednyiithpedieskvdgsniksvnnADDLLYmIYTSGTTGKPKGVQFEHRNMANLLKFEYtHSGIDFEADVLQ 648
Cdd:cd05940     81 --------------------------------VDAALY-IYTSGTTGLPKAAIISHRRAWRGGAFFA-GSGGALPSDVLY 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  649 FATPSFD-----VCyqeIFSALLKGGTLHIvpeAIKRDVPQLFAFINKHQTNIVflptAFIKMIFseRELANS--FPDGV 721
Cdd:cd05940    127 TCLPLYHstaliVG---WSACLASGATLVI---RKKFSASNFWDDIRKYQATIF----QYIGELC--RYLLNQppKPTER 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  722 KHLI--AAGEQLM--ISDLFQDvlRKRGIHLHNHYGPSEThvVSTYTIHPGDP-----IPELPPIGKPIGC------TDL 786
Cdd:cd05940    195 KHKVrmIFGNGLRpdIWEEFKE--RFGVPRIAEFYAATEG--NSGFINFFGKPgaigrNPSLLRKVAPLALvkydleSGE 270

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  787 YILNHQKQLQPCGV--PGEL--YISGASVARGYVNHDKlTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQV 862
Cdd:cd05940    271 PIRDAEGRCIKVPRgePGLLisRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349

                          410       420
                   ....*....|....*....|....*
gi 1678550997  863 KIRGYRIEPQEIEVTLMNHPDISEA 887
Cdd:cd05940    350 RWKGENVSTTEVAAVLGAFPGVEEA 374
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 1514-1980 2.64e-15

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: 82.15  E-value: 2.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1514 IFEDGV---MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEds 1590
Cdd:cd05908      7 ILGDKKekfVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLKLNK-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1591 gtnilllqsaglhvpeftgeivylnqtnsgLAHRLSNPNV-------DVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNF 1663
Cdd:cd05908     85 ------------------------------VWNTLKNPYLiteeevlCELADELAFIQFSSGSTGDPKGVMLTHENLVHN 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1664 LNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWP-YAGASVYLLPQGGE-KEPEVIAKAIEEQKITAM---HFVPSMLH 1738
Cdd:cd05908    135 MFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPlIAGMNQYLMPTRLFiRRPILWLKKASEHKATIVsspNFGYKYFL 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1739 AFLEHIKYRSVPIKTNRLkrVFSGGEQLGTHLVSRF------YELLPNvSITNSYGPTEATVEAAFFDCPPHEKL----- 1807
Cdd:cd05908    215 KTLKPEKANDWDLSSIRM--ILNGAEPIDYELCHEFldhmskYGLKRN-AILPVYGLAEASVGASLPKAQSPFKTitlgr 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1808 ------ERIP--------------IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFy 1867
Cdd:cd05908    292 rhvthgEPEPevdkkdsecltfveVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW- 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 pgermYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV---REAAVTV-RTDSGEPELCAYVEGlq 1943
Cdd:cd05908    371 -----LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVelgRVVACGVnNSNTRNEEIFCFIEH-- 442

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997 1944 rnevRAQLERLLP-GYMVPAYMIEMEQW-----------PVTPSGKLDR 1980
Cdd:cd05908    443 ----RKSEDDFYPlGKKIKKHLNKRGGWqinevlpirriPKTTSGKVKR 487
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 3123-3569 3.37e-15

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: 81.26  E-value: 3.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQK--WFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQYNrplshsDDALYGL 3200
Cdd:cd19533      5 TSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWID------PYTPVPI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3201 QMIDLSA---PDGTdgnrpYEPLIKRhvlDIQQKMDLKNGPLLQAGLFHtIDGD--FLFLSAHHLVVDGISWRVLLEDLA 3275
Cdd:cd19533     79 RHIDLSGdpdPEGA-----AQQWMQE---DLRKPLPLDNDPLFRHALFT-LGDNrhFWYQRVHHIVMDGFSFALFGQRVA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3276 LGYRQAAGGEDIKLPPKTsSFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEGQRSTISFTLNDK 3355
Cdd:cd19533    150 EIYTALLKGRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3356 ETaalLKDANSAYNTDTQDMLLASVILALRHWTnqsafklsleghGREDVLKGIDVSR--------TIGWFTAIYPLLIK 3427
Cdd:cd19533    229 RT---LLEAAEAHGASWPSFFIALVAAYLHRLT------------GANDVVLGVPVMGrlgaaarqTPGMVANTLPLRLT 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3428 LNADLPDSEesMV-HVLKTTKDTLR----RVPDKGFGYGVIKYLTPPGKKDIN---FTGAPEISFNYlgqfesGRTAevp 3499
Cdd:cd19533    294 VDPQQTFAE--LVaQVSRELRSLLRhqryRYEDLRRDLGLTGELHPLFGPTVNympFDYGLDFGGVV------GLTH--- 362

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3500 eedafsfsplgaggDISTTWNREQSLDISAIAAEGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEH 3569
Cdd:cd19533    363 --------------NLSSGPTNDLSIFVYDRDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 3123-3569 4.28e-15

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: 80.43  E-value: 4.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNE-QGKWDQ--YNRP------LSHS 3193
Cdd:cd19542      5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSaEGTFLQvvLKSLdppieeVETD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3194 DDALyglqmidlsapdgtdgnrpyepliKRHVLDIQQKMDLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLE 3272
Cdd:cd19542     85 EDSL------------------------DALTRDLLDDPTLFGQPPHRLTLLETSSGEvYLVLRISHALYDGVSLPIILR 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3273 DLALGYRQaaggediKLPPKTSSFKAYAkklsDYAESQQLMKQLKYWREA-EEYQTEALPFdqidgTRAHEGQRSTISFT 3351
Cdd:cd19542    141 DLAAAYNG-------QLLPPAPPFSDYI----SYLQSQSQEESLQYWRKYlQGASPCAFPS-----LSPKRPAERSLSST 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3352 LNDKETaalLKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREDVLKGIDvsRTIGWFTAIYPLLIKLNAD 3431
Cdd:cd19542    205 RRSLAK---LEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGID--DIVGPCINTLPVRVKLDPD 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3432 LPDSE----------ESMVHV---LKTTKDTLRRVPDKG-FGYGVIkYLtppgkkdiNFTGAPEISFNYLGQFEsGRTAE 3497
Cdd:cd19542    280 WTVLDllrqlqqqylRSLPHQhlsLREIQRALGLWPSGTlFNTLVS-YQ--------NFEASPESELSGSSVFE-LSAAE 349

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 3498 VPEEDAFSfsplgaggdisttwnreqsldISAIAAEGKLTVNMTYDNARFQRKTIEQLSETCRQFLLQLIEH 3569
Cdd:cd19542    350 DPTEYPVA---------------------VEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
489-952 7.01e-15

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 81.62  E-value: 7.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQA 568
Cdd:PRK06060    31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDNYIItHPEDIES---KVDGSNIKSVNnADDLLYMIYTSGTTGKPKGVQFEHRNMANLLK------FEYTHSG 639
Cdd:PRK06060   111 ALRDRFQPSRVA-EAAELMSeaaRVAPGGYEPMG-GDALAYATYTSGTTGPPKAAIHRHADPLTFVDamcrkaLRLTPED 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  640 IDFEADVLQFAtpsfdvcY---QEIFSALLKGGTLHIVPEAIKRDVPQLFAfiNKHQTNIVF-LPTAFIKMIFSERelAN 715
Cdd:PRK06060   189 TGLCSARMYFA-------YglgNSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYgVPNFFARVIDSCS--PD 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 SFpDGVKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSE---THVVSTY-TIHPGDPIPELPP----IGKPIGCTdly 787
Cdd:PRK06060   258 SF-RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvgqTFVSNRVdEWRLGTLGRVLPPyeirVVAPDGTT--- 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  788 ilnhqkqlQPCGVPGELYISGASVARGYVNHdkltsdkfsSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGY 867
Cdd:PRK06060   334 --------AGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  868 RIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYC---------SVQKlntiDLRSYMASELPEYMIPAKWIWVDS 938
Cdd:PRK06060   397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVatsgatidgSVMR----DLHRGLLNRLSAFKVPHRFAVVDR 472

                          490
                   ....*....|....
gi 1678550997  939 IPLTPNGKVDRAAL 952
Cdd:PRK06060   473 LPRTPNGKLVRGAL 486
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 1499-1980 9.24e-15

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: 80.68  E-value: 9.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1499 ALEQQAEKTPDQAAVIFE--DGVM----TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPE----ML----LG-IYG 1563
Cdd:cd05966     58 CLDRHLKERGDKVAIIWEgdEPDQsrtiTYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPElviaMLacarIGaVHS 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1564 ILKAGGAylpidPDYPEERIsfllEDSGTNILLLQSAGLHvpefTGEIVYLNQT------------NSGLAHRLSNPNV- 1630
Cdd:cd05966    138 VVFAGFS-----AESLADRI----NDAQCKLVITADGGYR----GGKVIPLKEIvdealekcpsveKVLVVKRTGGEVPm 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1631 ---------DVLPQSLAY-------------VIYTSGSTGMPKGVEieHRSAVNFLnslqsryqlkHSDMIMHktsYSFD 1688
Cdd:cd05966    205 tegrdlwwhDLMAKQSPEcepewmdsedplfILYTSGSTGKPKGVV--HTTGGYLL----------YAATTFK---YVFD 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1689 ASIWELFW------W----------P---------YAGASVYllPQggekePEVIAKAIEEQKITAMHFVPSMLHAFleh 1743
Cdd:cd05966    270 YHPDDIYWctadigWitghsyivygPlangattvmFEGTPTY--PD-----PGRYWDIVEKHKVTIFYTAPTAIRAL--- 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1744 IKY-RSVPIKTNR--LKRVFSGGEQLGTHLVSRFYELLPN--VSITNSYGPTE------ATVEAAffdcppheklerIPI 1812
Cdd:cd05966    340 MKFgDEWVKKHDLssLRVLGSVGEPINPEAWMWYYEVIGKerCPIVDTWWQTEtggimiTPLPGA------------TPL 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1813 -----GKPVHHVRLYLLNQNQRMLPVGCIGELYIAGA--GVARGYLNRPalteERFLEDPF--YPGerMYKTGDVARWLP 1883
Cdd:cd05966    408 kpgsaTRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFskFPG--YYFTGDGARRDE 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1884 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEpELCAYV---EGLQ-----RNEVRAQLER 1953
Cdd:cd05966    482 DGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHdiKGE-AIYAFVtlkDGEEpsdelRKELRKHVRK 560

                          570       580
                   ....*....|....*....|....*..
gi 1678550997 1954 LLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd05966    561 EIGPIATPDKIQFVPGLPKTRSGKIMR 587
PRK09274 PRK09274
peptide synthase; Provisional
 473-888 1.26e-14

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 80.33  E-value: 1.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQA----------CSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGgaIVP 542
Cdd:PRK09274    16 AQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAG--AVP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  543 V--DPHYPADRIRYILhdcgcSHV-------VSQAHLPSSL--------------EDNYII--THPEDIESKVDGSNIKS 597
Cdd:PRK09274    94 VlvDPGMGIKNLKQCL-----AEAqpdafigIPKAHLARRLfgwgkpsvrrlvtvGGRLLWggTTLATLLRDGAAAPFPM 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  598 VN-NADDLLYMIYTSGTTGKPKGVQFEHRN---MANLLKFEY--THSGIDFeadvlqfAT-PSFDVcyqeiFSALLKGGT 670
Cdd:PRK09274   169 ADlAPDDMAAILFTSGSTGTPKGVVYTHGMfeaQIEALREDYgiEPGEIDL-------PTfPLFAL-----FGPALGMTS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  671 lhIVPEA-----IKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSE-RELANSFPdGVKHLIAAGEQLMISDL--FQDVLR 742
Cdd:PRK09274   237 --VIPDMdptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYgEANGIKLP-SLRRVISAGAPVPIAVIerFRAMLP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  743 KrGIHLHNHYGPSETHVVST------------YTiHPGDPIPelppIGKPIGCTDLYILN---------HQKQLQPCGVP 801
Cdd:PRK09274   314 P-DAEILTPYGATEALPISSiesreilfatraAT-DNGAGIC----VGRPVDGVEVRIIAisdapipewDDALRLATGEI 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  802 GELYISGASVARGYVNHDKLTSDKFSSDPfKPDViMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNH 881
Cdd:PRK09274   388 GEIVVAGPMVTRSYYNRPEATRLAKIPDG-QGDV-WHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465


                   ....*..
gi 1678550997  882 PDISEAA 888
Cdd:PRK09274   466 PGVKRSA 472
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 1520-1982 1.40e-14

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 80.17  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1520 MTYKELNEQANRIAWELiGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI-DPDYP--EERISFLLEDSGTNILL 1596
Cdd:PRK12476    69 LTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1597 LQSAGLH-VPEFTGE--------IVYLNQTNSGLAHRLSNPNVDVlpQSLAYVIYTSGSTGMPKGVEIEHRSAVNflNSL 1667
Cdd:PRK12476   148 TTTAAAEaVEGFLRNlprlrrprVIAIDAIPDSAGESFVPVELDT--DDVSHLQYTSGSTRPPVGVEITHRAVGT--NLV 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1668 QSRYQLKHSDMIMHKTSysfdasiwelfWWP---------------YAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHF 1732
Cdd:PRK12476   224 QMILSIDLLDRNTHGVS-----------WLPlyhdmglsmigfpavYGGHSTLMSPTAFVRRPQRWIKALSEGSRTGRVV 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1733 VPSMLHAFlEHIKYRSVPIKTNRLK----RVFSGGEQLGTHLVSRFYEL-----LPNVSITNSYGPTEATV--------- 1794
Cdd:PRK12476   293 TAAPNFAY-EWAAQRGLPAEGDDIDlsnvVLIIGSEPVSIDAVTTFNKAfapygLPRTAFKPSYGIAEATLfvatiapda 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1795 --EAAFFDcppHEKLE-----RIPIGKP--VHHVRLYLLNQNQRM----------LPVGCIGELYIAGAGVARGYLNRPA 1855
Cdd:PRK12476   372 epSVVYLD---REQLGagravRVAADAPnaVAHVSCGQVARSQWAvivdpdtgaeLPDGEVGEIWLHGDNIGRGYWGRPE 448

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1856 LTEERF---LEDPFYPGERMYKTGDVARWLP--------DGNVEFLGRTDDQVKIRGYRIEPGEIEA-ALRSIEGVREAA 1923
Cdd:PRK12476   449 ETERTFgakLQSRLAEGSHADGAADDGTWLRtgdlgvylDGELYITGRIADLIVIDGRNHYPQDIEAtVAEASPMVRRGY 528

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1924 VTVRTDSGE--PELCAYVE---GLQRNE-------VRAQLERL--LPGY---MVPAYMIemeqwPVTPSGKLDRNA 1982
Cdd:PRK12476   529 VTAFTVPAEdnERLVIVAEraaGTSRADpapaidaIRAAVSRRhgLAVAdvrLVPAGAI-----PRTTSGKLARRA 599
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 1639-1983 1.57e-14

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: 79.34  E-value: 1.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1639 YVIYTSGSTGMPKGVEIEHrSAVNFlnslqsryqlkHSDMIMhktsysfdasIWELFWWPYAGaSVYLLP---------- 1708
Cdd:cd05929    129 KMLYSGGTTGRPKGIKRGL-PGGPP-----------DNDTLM----------AAALGFGPGAD-SVYLSPaplyhaapfr 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1709 -------QGG-----EK-EPEVIAKAIEEQKITAMHFVPSMLHAFLEhiKYRSVPIKTN--RLKRVFSGGEQLGTHLVSR 1773
Cdd:cd05929    186 wsmtalfMGGtlvlmEKfDPEEFLRLIERYRVTFAQFVPTMFVRLLK--LPEAVRNAYDlsSLKRVIHAAAPCPPWVKEQ 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1774 FYELLPNVsITNSYGPTEATveaAFFDCPPHEKLE-RIPIGKPVHHvRLYLLNQNQRMLPVGCIGELYIAGAGvARGYLN 1852
Cdd:cd05929    264 WIDWGGPI-IWEYYGGTEGQ---GLTIINGEEWLThPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTN 337

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1853 RPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV--TVRTDS 1930
Cdd:cd05929    338 DPEKTAAARNEGGW------STLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvgVPDEEL 411

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1931 GE-------PELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05929    412 GQrvhavvqPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 1640-1980 1.84e-14

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: 77.70  E-value: 1.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 VIYTSGSTGMPKGVEIEHRsavnflNSLQSRYQLKHSdmiMHKTSYSFDASIWELFWWPYAGASVYLLPQGG-----EK- 1713
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHG------NLIAANLQLIHA---MGLTEADVYLNMLPLFHIAGLNLALATFHAGGanvvmEKf 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1714 EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFsgG-------EQLGTHLVSRFYELlpnvsitns 1786
Cdd:cd17637     76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSS--LRHVL--GldapetiQRFEETTGATFWSL--------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATVEAAFfdCPPHEKleriP--IGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLED 1864
Cdd:cd17637    143 YGQTETSGLVTL--SPYRER----PgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1865 pfypgerMYKTGDVARWLPDGNVEFLGRT--DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE--PELCAY 1938
Cdd:cd17637    217 -------WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwGEgiKAVCVL 289

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1678550997 1939 VEG--LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 1980
Cdd:cd17637    290 KPGatLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 3128-3364 1.86e-14

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: 78.65  E-value: 1.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3128 WFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNE------QGKWDQ-----YNRPLSHSDDA 3196
Cdd:cd19532     12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPedgepmQGVLASsplrlEHVQISDEAEV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3197 LYGLQmidlsapdgtdgnrpyepLIKRHVLDiqqkmdLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLA 3275
Cdd:cd19532     92 EEEFE------------------RLKNHVYD------LESGETMRIVLLSLSPTEhYLIFGYHHIAMDGVSFQIFLRDLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3276 LGYRQAaggediKLPPKTSSFKAYAKKLSDYAESQQLMKQLKYWReaEEYQTEA-----LPFdqidgtrAHEGQRS---- 3346
Cdd:cd19532    148 RAYNGQ------PLLPPPLQYLDFAARQRQDYESGALDEDLAYWK--SEFSTLPeplplLPF-------AKVKSRPpltr 212

                          250       260
                   ....*....|....*....|..
gi 1678550997 3347 ----TISFTLnDKETAALLKDA 3364
Cdd:cd19532    213 ydthTAERRL-DAALAARIKEA 233
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
2676-3019 2.19e-14

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 77.78  E-value: 2.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 AYIIYTSGTTGRPKGVMVE-----------HKGIANTLQWrrnayafnetdtILQLFSFSFDGfITSMFTPLLSGAKAVL 2744
Cdd:PRK07824    38 ALVVATSGTTGTPKGAMLTaaaltasadatHDRLGGPGQW------------LLALPAHHIAG-LQVLVRSVIAGSEPVE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2745 LHEEEAKDILAIK---HQLSRQRiTHMIIVPV-LYRALLDVVQPEDVKTLRVVTLAGEAADRELI--ARSLAIcphtELA 2818
Cdd:PRK07824   105 LDVSAGFDPTALPravAELGGGR-RYTSLVPMqLAKALDDPAATAALAELDAVLVGGGPAPAPVLdaAAAAGI----NVV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 NEYGPTENSVATtvmrhmekqayVSIGQPIDGTQVLILNsnhqlqpigvaGELCIAGTGLARGYVNLPElteraftqNPF 2898
Cdd:PRK07824   180 RTYGMSETSGGC-----------VYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD--------PDP 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2899 KPEARMYRTGDAARwMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS-GQTELSAYVVT-KP 2976
Cdd:PRK07824   230 FAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVAAVVGDgGP 308

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1678550997 2977 GLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK07824   309 APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 488-945 2.55e-14

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: 79.42  E-value: 2.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQEP-VAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHV-V 565
Cdd:cd17632     67 TITYAELWERVGAVAAAHDPEQPVRPGDfVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLaV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  566 SQAHLPSSLE--------------DNY--IITHPEDIESKVD------------------------GSNIKSVNNADDLL 605
Cdd:cd17632    147 SAEHLDLAVEavleggtpprlvvfDHRpeVDAHRAALESARErlaavgipvttltliavrgrdlppAPLFRPEPDDDPLA 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  606 YMIYTSGTTGKPKGVQFEHRNMANL-LKFEYTHSGIDFEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEAikrDVPQ 684
Cdd:cd17632    227 LLIYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAAS---DMST 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  685 LFAFINKHQTNIVFLPTAFIKMIFSE--RELANSFPDGVKHLIAAGEqlMISDLFQDVLRKR------------------ 744
Cdd:cd17632    304 LFDDLALVRPTELFLVPRVCDMLFQRyqAELDRRSVAGADAETLAER--VKAELRERVLGGRllaavcgsaplsaemkaf 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 -----GIHLHNHYGPSETHVVSTytihpgDPIPELPPI--GKPIGCTDL-YILN---HQKqlqpcgvpGELYISGASVAR 813
Cdd:cd17632    382 mesllDLDLHDGYGSTEAGAVIL------DGVIVRPPVldYKLVDVPELgYFRTdrpHPR--------GELLVKTDTLFP 447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKI-RGYRIEPQEIEVTLMNHPDI-------- 884
Cdd:cd17632    448 GYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVrqifvygn 521

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  885 SEAAILIW--------QDQNGEHEL-CAYYCSVQklntidlRSYMASELPEYMIPAKWIwVDSIPLTP-NG 945
Cdd:cd17632    522 SERAYLLAvvvptqdaLAGEDTARLrAALAESLQ-------RIAREAGLQSYEIPRDFL-IETEPFTIaNG 584
PRK09192 PRK09192
fatty acyl-AMP ligase;
1519-1980 2.68e-14

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 79.28  E-value: 2.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1519 VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGG--AYLPIdpdyPE---------ERISFLL 1587
Cdd:PRK09192    49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPL----PMgfggresyiAQLRGML 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1588 EDSGTNILLlqsAGLHVPEFTGEIVYLNQTNSGLAHRLSN--PNVDV-LPQ----SLAYVIYTSGSTGMPKGVEIEHRSA 1660
Cdd:PRK09192   125 ASAQPAAII---TPDELLPWVNEATHGNPLLHVLSHAWFKalPEADVaLPRptpdDIAYLQYSSGSTRFPRGVIITHRAL 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1661 VNFLNSLqSRY--QLKHSDMIMHKTSYSFDASIWELFWWPYA-GASVYLLPQGG-EKEPEVIAKAIEEQKITaMHFVP-- 1734
Cdd:PRK09192   202 MANLRAI-SHDglKVRPGDRCVSWLPFYHDMGLVGFLLTPVAtQLSVDYLPTRDfARRPLQWLDLISRNRGT-ISYSPpf 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 ----------SMLHAFLEHIKYRSVPIktnrlkrvfsGGEQLGTHLVSRFYELLPNV-----SITNSYGPTEATVEAAFf 1799
Cdd:PRK09192   280 gyelcarrvnSKDLAELDLSCWRVAGI----------GADMIRPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLAVSF- 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1800 dcPPH-----------EKLERIPI-----------------GKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYL 1851
Cdd:PRK09192   349 --SPLgsgivveevdrDRLEYQGKavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1852 NRP----ALTEERFLEdpfypgermykTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR--EAAVT 1925
Cdd:PRK09192   427 RDEesqdVLAADGWLD-----------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAF 494

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 1926 VRTDSGEPELCAYVEG-LQRNEVRAQLERLLPGY------------MVPAYMIemeqwPVTPSGKLDR 1980
Cdd:PRK09192   495 SIAQENGEKIVLLVQCrISDEERRGQLIHALAALvrsefgveaaveLVPPHSL-----PRTSSGKLSR 557
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 1493-1928 2.86e-14

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 79.39  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1493 NQTLHYALEQQAEKTPDQAAVIFEDgvmTYKELNEQANRIAWELIG---RGV--------KPETTVAIIGKRSPEMLLGI 1561
Cdd:PRK07769    20 NTNLVRHVERWAKVRGDKLAYRFLD---FSTERDGVARDLTWSQFGarnRAVgarlqqvtKPGDRVAILAPQNLDYLIAF 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1562 YGILKAGGAYLPI-DPDYP--EERISFLLED-SGTNILLLQSAGLHVPEF--------TGEIVYLNQTNSGLAHRLSNPN 1629
Cdd:PRK07769    97 FGALYAGRIAVPLfDPAEPghVGRLHAVLDDcTPSAILTTTDSAEGVRKFfrarpakeRPRVIAVDAVPDEVGATWVPPE 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1630 VDVlpQSLAYVIYTSGSTGMPKGVEIEHRSAVNflNSLQsryqlkhsdMImhkTSYSFDASIWELFWWPY---AGASVYL 1706
Cdd:PRK07769   177 ANE--DTIAYLQYTSGSTRIPAGVQITHLNLPT--NVLQ---------VI---DALEGQEGDRGVSWLPFfhdMGLITVL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1707 LPQGGEKEPEVIAKAIEEQK----ITAMHFVPSMLH---------AFlEHIKYRSVP------IKTNRLKRVFSGGEQLG 1767
Cdd:PRK07769   241 LPALLGHYITFMSPAAFVRRpgrwIRELARKPGGTGgtfsaapnfAF-EHAAARGLPkdgeppLDLSNVKGLLNGSEPVS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1768 THLVSRFYEL-----LPNVSITNSYGPTEATVeaaFFDCPPHEKLERipigkpVHHVRLYLLNqNQRM------------ 1830
Cdd:PRK07769   320 PASMRKFNEAfapygLPPTAIKPSYGMAEATL---FVSTTPMDEEPT------VIYVDRDELN-AGRFvevpadapnava 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1831 -----------------------LPVGCIGELYIAGAGVARGYLNRPALTEERF---LEDPFYP--------GERMYKTG 1876
Cdd:PRK07769   390 qvsagkvgvsewavivdpetaseLPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdDALWVRTG 469

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1877 DVARWLpDGNVEFLGRTDDQVKIRGYRIEPGEIEAAlrsiegVREAAVTVRT 1928
Cdd:PRK07769   470 DYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEYT------AQEATKALRT 514
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 1503-1983 2.91e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 78.90  E-value: 2.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1503 QAEKTPDQAAVIF-EDG-VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPE 1580
Cdd:PRK13390     6 HAQIAPDRPAVIVaETGeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1581 ERISFLLEDSGTNIL--------LLQSAGLHVP---EFTGEIVYLNQTNSGLAHrlSNPNVDVLPQSlAYVIYTSGSTGM 1649
Cdd:PRK13390    86 PEADYIVGDSGARVLvasaaldgLAAKVGADLPlrlSFGGEIDGFGSFEAALAG--AGPRLTEQPCG-AVMLYSSGTTGF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1650 PKGVEIEhrsavnflnsLQSRYQLKHSDMIMHKTSYSFDASIWELFwwpYAGASVY----------LLPQGGEKepeVIA 1719
Cdd:PRK13390   163 PKGIQPD----------LPGRDVDAPGDPIVAIARAFYDISESDIY---YSSAPIYhaaplrwcsmVHALGGTV---VLA 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1720 KA---------IEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVsITNSYGPT 1790
Cdd:PRK13390   227 KRfdaqatlghVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSST 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1791 EATvEAAFFDCP---PHEKleriPIGKPVHHVrLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERflEDPFY 1867
Cdd:PRK13390   306 EAH-GMTFIDSPdwlAHPG----SVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAA--QHPAH 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 PgerMYKT-GDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDsgePEL-------CAYV 1939
Cdd:PRK13390   378 P---FWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPD---PEMgeqvkavIQLV 451

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1940 EGLQRNEvraQLERLL--------PGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK13390   452 EGIRGSD---ELARELidytrsriAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
PRK05857 PRK05857
fatty acid--CoA ligase;
471-952 3.40e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 78.90  E-value: 3.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  471 KQAEKTPDAHAV--IDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYP 548
Cdd:PRK05857    22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 ADRI-RY--------ILHDCGCShvVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSV-------NNADDLLYMIYTSG 612
Cdd:PRK05857   102 IAAIeRFcqitdpaaALVAPGSK--MASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslagnadQGSEDPLAMIFTSG 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  613 TTGKPKGVQFEHRN---MANLLKFEYThSGIDFEADVLQF----ATPSFDVCYqeIFSALLKGGTLHIVPEaikrDVPQL 685
Cdd:PRK05857   180 TTGEPKAVLLANRTffaVPDILQKEGL-NWVTWVVGETTYsplpATHIGGLWW--ILTCLMHGGLCVTGGE----NTTSL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  686 FAFINKHQTNIVFL-PTAFIKMIfSERELANSFPDGVKHLIAAGEQLMISDLfqDVLRKRGIHLHNHYGPSETHVVSTYT 764
Cdd:PRK05857   253 LEILTTNAVATTCLvPTLLSKLV-SELKSANATVPSLRLVGYGGSRAIAADV--RFIEATGVRTAQVYGLSETGCTALCL 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  765 IHPGDPIP--ELPPIGKPIGCTDLYIL--NHQKQLQPCGVP----GELYISGASVARGYVNHDKLTSDKFSSDpfkpdvi 836
Cdd:PRK05857   330 PTDDGSIVkiEAGAVGRPYPGVDVYLAatDGIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLIDG------- 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  837 MYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQKLN---T 913
Cdd:PRK05857   403 WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDesaA 482

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1678550997  914 IDLRSYMAS----ELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK05857   483 RALKHTIAArfrrESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 2676-3019 3.74e-14

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 78.70  E-value: 3.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 AYIIYTSGTTGRPKGVMVEHkgiANTLQWRRNAYAF---NETDTILQ-LFSFSFDGFITSMFTPLLSGAKAVLLHEE-EA 2750
Cdd:PRK06334   186 AVILFTSGTEKLPKGVPLTH---ANLLANQRACLKFfspKEDDVMMSfLPPFHAYGFNSCTLFPLLSGVPVVFAYNPlYP 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2751 KDILAIkhqLSRQRITHMIIVPVLYRALLDVV--QPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANEYGPTENSV 2828
Cdd:PRK06334   263 KKIVEM---IDEAKVTFLGSTPVFFDYILKTAkkQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSP 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2829 ATTVMRHMEKQAYVSIGQPIDGTQVLILN-SNHQLQPIGVAGELCIAGTGLARGYvnLPELTERAFTQnpfKPEARMYRT 2907
Cdd:PRK06334   340 VITINTVNSPKHESCVGMPIRGMDVLIVSeETKVPVSSGETGLVLTRGTSLFSGY--LGEDFGQGFVE---LGGETWYVT 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2908 GDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAA-----VVAHVtaSGQTELSAYVVTKPgLSTNA 2982
Cdd:PRK06334   415 GDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADhagplVVCGL--PGEKVRLCLFTTFP-TSISE 491

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1678550997 2983 VRSELQN-KLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06334   492 VNDILKNsKTSSILKISYHHQVESIPMLGTGKPDYCSL 529
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 1515-1964 3.91e-14

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: 78.24  E-value: 3.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1515 FEDGVMTYKELNEQANRIA-WELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAylpidpdypeerisflledsgtn 1593
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAhWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA----------------------- 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1594 illlqsaglhvPEFtgeIVYlNQTNSGLAH--RLSNPN-VDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSR 1670
Cdd:cd05937     58 -----------PAF---INY-NLSGDPLIHclKLSGSRfVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHD 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1671 YQLKHSDM------IMHKTSYSFdasiwelfwwpyagASVYLLPQGGekepeVIAKAieeQKITAMHFVPSMLHAFLEHI 1744
Cdd:cd05937    123 LNLKNGDRtytcmpLYHGTAAFL--------------GACNCLMSGG-----TLALS---RKFSASQFWKDVRDSGATII 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1745 KY--------RSVPI----KTNRLKRVFSGGeqLGTHLVSRFYELLpNVS-ITNSYGPTEATveAAFFdcppheKLERIP 1811
Cdd:cd05937    181 QYvgelcrylLSTPPspydRDHKVRVAWGNG--LRPDIWERFRERF-NVPeIGEFYAATEGV--FALT------NHNVGD 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1812 --IGKPVHH---VRLYLLNQ--------NQRM------------LPVGCIGELYIA----GAGVARGYLNRPALTEERFL 1862
Cdd:cd05937    250 fgAGAIGHHgliRRWKFENQvvlvkmdpETDDpirdpktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLV 329

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1863 EDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA---AVTVRTDSGEPElCAYV 1939
Cdd:cd05937    330 RDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVPGHDGRAG-CAAI 408

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1678550997 1940 EGLQRNEVR--------AQLERL-LPGYMVPAYM 1964
Cdd:cd05937    409 TLEESSAVPteftksllASLARKnLPSYAVPLFL 442
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1997-2070 4.92e-14

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


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 69.88  E-value: 4.92e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1997 APRNVTEMKLSQLWEDVLKNGP--VGIHDNFF-DRGGHSLKATALVSRITKEFDVQVPLKDVFAHPTVEGLATVIRE 2070
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 463-952 5.58e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 78.14  E-value: 5.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  463 ETIHAMFEKQAEKtpDAHAVIDQACSLTYRE-LNKAANR--LARHLRMKGvvRQEPVAIMMERSAAFITGVLGILKAGGA 539
Cdd:PRK13388     3 DTIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARaaALIALADPD--RPLHVGVLLGNTPEMLFWLAAAALGGYV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  540 IVPVDP-HYPADRIRYILH-DCGCShVVSQAHLP--SSLE---DNYIIT----HPEDIESKVDGSNIKSVNnADDLLYMI 608
Cdd:PRK13388    79 LVGLNTtRRGAALAADIRRaDCQLL-VTDAEHRPllDGLDlpgVRVLDVdtpaYAELVAAAGALTPHREVD-AMDPFMLI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  609 YTSGTTGKPKGVQFEHRNMANL---LKFEYTHSgidfEADVLQFATPSF--DVCYQEIFSALLKGGTLHIVPE------- 676
Cdd:PRK13388   157 FTSGTTGAPKAVRCSHGRLAFAgraLTERFGLT----RDDVCYVSMPLFhsNAVMAGWAPAVASGAAVALPAKfsasgfl 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  677 -AIKRDVPQLFAFINKhqtnivflPTAFIkMIFSERelansfPDGVKH--LIAAGEQLMISDLfQDVLRKRGIHLHNHYG 753
Cdd:PRK13388   233 dDVRRYGATYFNYVGK--------PLAYI-LATPER------PDDADNplRVAFGNEASPRDI-AEFSRRFGCQVEDGYG 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  754 PSETHVVSTytihpgdPIPELPP--IGKPIgcTDLYILNHQKqLQPCGVP---------------GELY-ISGASVARGY 815
Cdd:PRK13388   297 SSEGAVIVV-------REPGTPPgsIGRGA--PGVAIYNPET-LTECAVArfdahgallnadeaiGELVnTAGAGFFEGY 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  816 VNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQ 895
Cdd:PRK13388   367 YNNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997  896 -NGEHELCAyycsvqkLNTIDLRSYMASELPEYM-----IPAKW----IWV-DSIPLTPNGKVDRAAL 952
Cdd:PRK13388   440 rVGDQVMAA-------LVLRDGATFDPDAFAAFLaaqpdLGTKAwpryVRIaADLPSTATNKVLKREL 500
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 1521-1924 5.67e-14

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 77.87  E-value: 5.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNIL----- 1595
Cdd:PRK06018    41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVitdlt 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1596 ---LLQSAGLHVPEFTGEIVYlnqtnSGLAHRLSNpnvdVLPQSLAY-----------------------VIYTSGSTGM 1649
Cdd:PRK06018   121 fvpILEKIADKLPSVERYVVL-----TDAAHMPQT----TLKNAVAYeewiaeadgdfawktfdentaagMCYTSGTTGD 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1650 PKGVEIEHRSavNFLNSLQSRYQ----LKHSDMIMHKTSYsFDASIWEL-FWWPYAGASVyLLPqGGEKEPEVIAKAIEE 1724
Cdd:PRK06018   192 PKGVLYSHRS--NVLHALMANNGdalgTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKL-VMP-GAKLDGASVYELLDT 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1725 QKITAMHFVPSMLHAFLEHIkyRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELlpNVSITNSYGPTE-------ATVEAA 1797
Cdd:PRK06018   267 EKVTFTAGVPTVWLMLLQYM--EKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEmsplgtlAALKPP 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1798 FFDCPPHEKLE-RIPIGKPVHHVRLYLLNQNQRMLPVG--CIGELYIAGAGVARGYLNrpalTEERFLEDpfypgERMYK 1874
Cdd:PRK06018   343 FSKLPGDARLDvLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR----VDGEILDD-----DGFFD 413

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1875 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:PRK06018   414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 1521-1980 6.76e-14

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 77.73  E-value: 6.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSA 1600
Cdd:PRK07768    31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 GLHVPEFTGEIVYLNQTNSGLAHRLSN-------PNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQL 1673
Cdd:PRK07768   111 AVVVGEPFLAAAPVLEEKGIRVLTVADllaadpiDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEF 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1674 KHSDMIMhktsysfdasiweLFWWP---------------YAGAS-VYLLPQGGEKEPEVIAKAIEEQKIT---AMHFVP 1734
Cdd:PRK07768   191 DVETDVM-------------VSWLPlfhdmgmvgfltvpmYFGAElVKVTPMDFLRDPLLWAELISKYRGTmtaAPNFAY 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHAFLEH-IKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYEL-----LPNVSITNSYGPTEATVEAAFFDC------- 1801
Cdd:PRK07768   258 ALLARRLRRqAKPGAFDLSS--LRFALNGAEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEATLAVSFSPCgaglvvd 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1802 --------------PPHEKLER--IPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLnrpalTEERFLE-- 1863
Cdd:PRK07768   336 evdadllaalrravPATKGNTRrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFIPaq 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1864 DPfypgERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA-AVTVRTDSG----------- 1931
Cdd:PRK07768   411 DA----DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGnAVAVRLDAGhsregfavave 486

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1932 -----EPELCAYVEGLQRNEVRAQLE------RLLPGYMVPAymiemeqwpvTPSGKLDR 1980
Cdd:PRK07768   487 snafeDPAEVRRIRHQVAHEVVAEVGvrprnvVVLGPGSIPK----------TPSGKLRR 536
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 2560-3019 6.92e-14

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 77.87  E-value: 6.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2560 TYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTine 2639
Cdd:PRK06018    41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT--- 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2640 aDLGVLADFEGEILTIESVEE----DDKSPLPQMSSAHHLAY-----------------------IIYTSGTTGRPKGVM 2692
Cdd:PRK06018   118 -DLTFVPILEKIADKLPSVERyvvlTDAAHMPQTTLKNAVAYeewiaeadgdfawktfdentaagMCYTSGTTGDPKGVL 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2693 VEHKgiANTLQW----RRNAYAFNETDTILQLFS-FSFDGFITSMFTPlLSGAKAVLlheEEAK-DILAIKHQLSRQRIT 2766
Cdd:PRK06018   197 YSHR--SNVLHAlmanNGDALGTSAADTMLPVVPlFHANSWGIAFSAP-SMGTKLVM---PGAKlDGASVYELLDTEKVT 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2767 HMIIVPVLYRALLDVVQPEDVK--TLRVVTLAGEAADRELIARSLAIcpHTELANEYGPTENSVATTV------------ 2832
Cdd:PRK06018   271 FTAGVPTVWLMLLQYMEKEGLKlpHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEMSPLGTLaalkppfsklpg 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2833 ---MRHMEKQAYvsigqPIDGTQVLILNSNHQLQPI-GVA-GELCIAGTGLARGYVNLPE--LTERAFtqnpfkpearmY 2905
Cdd:PRK06018   349 darLDVLQKQGY-----PPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------F 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2906 RTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVV-AHVTASGQTELsAYVVTKPGlsTNAVR 2984
Cdd:PRK06018   413 DTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIgVYHPKWDERPL-LIVQLKPG--ETATR 489

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1678550997 2985 SE----LQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK06018   490 EEilkyMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 1640-1924 1.11e-13

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: 75.42  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 VIYTSGSTGMPKGVEIEHRS----AVN------------FLNSLQsryqLKHSDMIMHkTSYSFDAsiwelfwwpyAGAS 1703
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQAllaqALVlavlqaidegtvFLNSGP----LFHIGTLMF-TLATFHA----------GGTN 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1704 VYLlPQggeKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPnvsi 1783
Cdd:cd17636     70 VFV-RR---VDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG---- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1784 tnSYGPTEATVEAAFfdcpPHEKLERIPI-GKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFl 1862
Cdd:cd17636    142 --GYGQTEVMGLATF----AALGGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT- 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1863 edpfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:cd17636    215 ------RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 603-949 1.37e-13

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: 75.00  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  603 DLLYMIYTSGTTGKPKGVQFEHRNM-ANLLKFEYTHsGIDfEADVLQFATPSFDVCYQEIFSALLKGGTLHIVPEaiKRD 681
Cdd:cd17637      1 DPFVIIHTAAVAGRPRGAVLSHGNLiAANLQLIHAM-GLT-EADVYLNMLPLFHIAGLNLALATFHAGGANVVME--KFD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  682 VPQLFAFINKHQTNIV--FLPTAFikMIFSERELANSFPDGVKHLiaAGeqLMISDLFQDVLRKRGIHLHNHYGPSETHV 759
Cdd:cd17637     77 PAEALELIEEEKVTLMgsFPPILS--NLLDAAEKSGVDLSSLRHV--LG--LDAPETIQRFEETTGATFWSLYGQTETSG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  760 VSTYTihpgdPIPELP-PIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDpfkpdviMY 838
Cdd:cd17637    151 LVTLS-----PYRERPgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WH 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  839 RTGDLARRLEDGNIEYIGRADNQ--VKIRGYRIEPQEIEVTLMNHPDISEAAILIWQD-QNGE--HELCAYYCSvQKLNT 913
Cdd:cd17637    219 HTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDpKWGEgiKAVCVLKPG-ATLTA 297

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1678550997  914 IDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:cd17637    298 DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 3035-3106 1.47e-13

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


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 68.34  E-value: 1.47e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 3035 PSSKMEQILADIWKEVLG--AEKIGTADSFF-ELGGDSIKALQVSARLH-RIGKQMAVKDLFSHPTIQELAAYIRD 3106
Cdd:COG0236      2 PREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLADYLEE 77
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 2594-3016 1.53e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 75.84  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2594 FSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTineadlgvladFEGEILTIESVEEDDKSP-LPQmssa 2672
Cdd:PRK08308    43 FDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLY-----------GESDFTKLEAVNYLAEEPsLLQ---- 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2673 hhlayiiYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDT--ILQLFSFSFdGFITSMFTPLLSGAKAVLLHEEEA 2750
Cdd:PRK08308   108 -------YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETpiVACPVTHSY-GLICGVLAALTRGSKPVIITNKNP 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2751 KDILAIkhqlSRQRITHMII-VPVLYRALLDVVqPEDVKTLRVVT---LAGEAADRELIARSlaicphTELANEYGPTEn 2826
Cdd:PRK08308   180 KFALNI----LRNTPQHILYaVPLMLHILGRLL-PGTFQFHAVMTsgtPLPEAWFYKLRERT------TYMMQQYGCSE- 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2827 svATTVMRHMEKQAYVSIGQPIdgtqvlilnSNHQLQpigvagelciAGTGlargyvnlpelterafTQNP----FKPEA 2902
Cdd:PRK08308   248 --AGCVSICPDMKSHLDLGNPL---------PHVSVS----------AGSD----------------ENAPeeivVKMGD 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2903 RMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNA 2982
Cdd:PRK08308   291 KEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQ 370

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1678550997 2983 VRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDR 3016
Cdd:PRK08308   371 LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
602-952 1.56e-13

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 75.08  E-value: 1.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDLLYMIYTSGTTGKPKGVQFehrNMANLL-KFEYTHSGIDFEADVLqFATPSFDVC-YQEIFSALLKGgtlhIVPEAIk 679
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAML---TAAALTaSADATHDRLGGPGQWL-LALPAHHIAgLQVLVRSVIAG----SEPVEL- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  680 rDVPQLFafinkhqtNIVFLPTAFIKMIFSER-------ELANSFPDgvkhlIAAGEQLMISD--------LFQDVLRKR 744
Cdd:PRK07824   106 -DVSAGF--------DPTALPRAVAELGGGRRytslvpmQLAKALDD-----PAATAALAELDavlvgggpAPAPVLDAA 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  745 ---GIHLHNHYGPSETHVVSTYTihpgdpipelppiGKPIGCTDLYILNhqkqlqpcgvpGELYISGASVARGYVNHDkl 821
Cdd:PRK07824   172 aaaGINVVRTYGMSETSGGCVYD-------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV-- 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  822 tsdkfSSDPFKpDVIMYRTGDLARrLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN-GEHE 900
Cdd:PRK07824   226 -----DPDPFA-EPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRV 298

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  901 LCAYYCSVQKLNTID-LRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK07824   299 VAAVVGDGGPAPTLEaLRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PLN02479 PLN02479
acetate-CoA ligase
 2526-3019 3.16e-13

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 75.65  E-value: 3.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2526 QANqYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWK 2605
Cdd:PLN02479    14 AAN-YTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2606 AGGCYVPIDPEYPKERKRYILSDSGTKLLM------TINEADLGVLAD-----FEGEILTIESVEEDDKSPLPQMSSAHH 2674
Cdd:PLN02479    93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVMvdqeffTLAEEALKILAEkkkssFKPPLLIVIGDPTCDPKSLQYALGKGA 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 LAY------------------------IIYTSGTTGRPKGVMVEHKG-----IANTLQWRRNAYAFnetdTILQLFSFSF 2725
Cdd:PLN02479   173 IEYekfletgdpefawkppadewqsiaLGYTSGTTASPKGVVLHHRGaylmaLSNALIWGMNEGAV----YLWTLPMFHC 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2726 DGFITSMFTPLLSGaKAVLLHEEEAKdilAIKHQLSRQRITHMIIVPVLYRALLDVVQPEDVKTL-RVVTL--AGEAADR 2802
Cdd:PLN02479   249 NGWCFTWTLAALCG-TNICLRQVTAK---AIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLpRVVHVmtAGAAPPP 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2803 ELIArSLAI----CPHTE-LANEYGPT---------ENSVATTVMRHMEKQAYVSIGqpIDGTQVLILNSNHQLQPIG-V 2867
Cdd:PLN02479   325 SVLF-AMSEkgfrVTHTYgLSETYGPStvcawkpewDSLPPEEQARLNARQGVRYIG--LEGLDVVDTKTMKPVPADGkT 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2868 AGELCIAGTGLARGYVNLPELTERAFtqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRC 2947
Cdd:PLN02479   402 MGEIVMRGNMVMKGYLKNPKANEEAF-------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2948 IKGVKDAAVVAHVTASGQTELSAYVVTKPGLST---NAVRSEL----QNKLPVFMHPAFIeKLDSLPLSPNGKLDRGAL 3019
Cdd:PLN02479   475 HPAVLEASVVARPDERWGESPCAFVTLKPGVDKsdeAALAEDImkfcRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 514-952 4.86e-13

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 75.06  E-value: 4.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  514 EPVAIMMERS-AAFITGVLGILkaggaivPVDPHYPADRIRYIlhdcgcsHVVSQAHLPSSLEDNY--IITHPEDIESKV 590
Cdd:PLN03102   111 KPKILFVDRSfEPLAREVLHLL-------SSEDSNLNLPVIFI-------HEIDFPKRPSSEELDYecLIQRGEPTPSLV 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  591 dgSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN-----MANLLKFEYthsGIdfeADVLQFATPSFDvC--YQEIFS 663
Cdd:PLN03102   177 --ARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGaylstLSAIIGWEM---GT---CPVYLWTLPMFH-CngWTFTWG 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  664 ALLKGGTlhivpEAIKRDV--PQLFAFINKHQ-TNIVFLPTAFiKMIFSERELANSFPDGVKHLIAAGEQlMISDLFQDV 740
Cdd:PLN03102   248 TAARGGT-----SVCMRHVtaPEIYKNIEMHNvTHMCCVPTVF-NILLKGNSLDLSPRSGPVHVLTGGSP-PPAALVKKV 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  741 lRKRGIHLHNHYGPSETH--VVSTYTIHPGDPIPELPPIG-------KPIGCTDLYILNHQKQLQpcgVP------GELY 805
Cdd:PLN03102   321 -QRLGFQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMElkarqgvSILGLADVDVKNKETQES---VPrdgktmGEIV 396

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  806 ISGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDIS 885
Cdd:PLN03102   397 IKGSSIMKGYLKNPKATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVL 469

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  886 EAAIL-----IWQD--------QNGEHELCAYYCSVQKlNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PLN03102   470 ETAVVamphpTWGEtpcafvvlEKGETTKEDRVDKLVT-RERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 1500-1892 5.85e-13

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 74.92  E-value: 5.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDG-----VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI 1574
Cdd:PRK08180    45 LVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1575 DPDYpeeriSFLLEDSG---TNILLLQSAGLHV--------------PEFTGEIVYLNQTNSGLAHRLS-------NPNV 1630
Cdd:PRK08180   125 SPAY-----SLVSQDFGklrHVLELLTPGLVFAddgaafaralaavvPADVEVVAVRGAVPGRAATPFAallatppTAAV 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1631 D-----VLPQSLAYVIYTSGSTGMPKGVEIEHRS-AVNFLNSLQSRYQLKHSDMIMhktsysfdasiweLFWWP------ 1698
Cdd:PRK08180   200 DaahaaVGPDTIAKFLFTSGSTGLPKAVINTHRMlCANQQMLAQTFPFLAEEPPVL-------------VDWLPwnhtfg 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 ---------YAGASVYLlpQGGEKEPEVIAKAIEEQK--ITAMHF-VPS---MLHAFLEhikyRSVPIKTN---RLKRVF 1760
Cdd:PRK08180   267 gnhnlgivlYNGGTLYI--DDGKPTPGGFDETLRNLReiSPTVYFnVPKgweMLVPALE----RDAALRRRffsRLKLLF 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1761 SGGEQLGTHLVSRFYELLPN-----VSITNSYGPTEATVEAAFFdcppHEKLERI-PIGKPVHHVRLyllnqnqRMLPVG 1834
Cdd:PRK08180   341 YAGAALSQDVWDRLDRVAEAtcgerIRMMTGLGMTETAPSATFT----TGPLSRAgNIGLPAPGCEV-------KLVPVG 409

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 1835 CIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWL----PDGNVEFLGR 1892
Cdd:PRK08180   410 GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRFVdpadPERGLMFDGR 465
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 473-890 7.66e-13

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 74.14  E-value: 7.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSniksvnnADDLLYMIYTSGTTGKPKGVQFEHRN-MAN-- 629
Cdd:PRK09029    93 EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQ-------PQRLATMTLTSGSTGLPKAAVHTAQAhLASae 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  630 -LLkfeythSGIDFEA-DVLQFATPSFDVCYQEIF-SALLKGGTLHIvpeaikRDVPQLFAFINKhQTNIVFLPTAFikm 706
Cdd:PRK09029   166 gVL------SLMPFTAqDSWLLSLPLFHVSGQGIVwRWLYAGATLVV------RDKQPLEQALAG-CTHASLVPTQL--- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 ifsERELANS-FPDGVKHLIAAGEqlMISDLFQDVLRKRGIHLHNHYGPSEthVVSTYTIHPGDpipELPPIGKPIGctd 785
Cdd:PRK09029   230 ---WRLLDNRsEPLSLKAVLLGGA--AIPVELTEQAEQQGIRCWCGYGLTE--MASTVCAKRAD---GLAGVGSPLP--- 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  786 lyilNHQKQLqpcgVPGELYISGASVARGYVNHDKLTsdkfssdPFKPDVIMYRTGDLArRLEDGNIEYIGRADNQVKIR 865
Cdd:PRK09029   297 ----GREVKL----VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRG-EWQNGELTILGRLDNLFFSG 360

                          410       420
                   ....*....|....*....|....*
gi 1678550997  866 GYRIEPQEIEVTLMNHPDISEAAIL 890
Cdd:PRK09029   361 GEGIQPEEIERVINQHPLVQQVFVV 385
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 12-304 9.13e-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: 73.37  E-value: 9.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEGMLFHSLLQKDSQA----YVeqasFTIEGKVNPQFFQNSINALVERHDIFRTIFI--------SQNVSSPQQV 79
Cdd:cd19537      3 ALSPIEREWWHKYQLSTGTSSfnvsFA----CRLSGDVDRDRLASAWNTVLARHRILRSRYVprdgglrrSYSSSPPRVQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   80 VLRERNVivleedithlneaeqsqfieqWKEKDRDrgFHLQKDVLMRIALiqtgeSQYSCIWTFHHIMMDGWCLSIVLKE 159
Cdd:cd19537     79 RVDTLDV---------------------WKEINRP--FDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLRE 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  160 FLHIYASyvnaspITLEPVQPygKYIKWLMEQDK--EQAVSYWDHYLSGHeQQTVLPKQKKTK---GKSRqehvTFSFSK 234
Cdd:cd19537    131 VSAAYNG------KLLPPVRR--EYLDSTAWSRPasPEDLDFWSEYLSGL-PLLNLPRRTSSKsyrGTSR----VFQLPG 197

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  235 EESSRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEgiEHMVGLFINTMPVRVQ 304
Cdd:cd19537    198 SLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEED--METVGLFLEPLPIRIR 265
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 1643-1955 9.63e-13

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 73.26  E-value: 9.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1643 TSGSTGMPKGV-----EIEhRSAVNFLNSLQSrYQLKHSDMIMHKTSYS-------FDASIWELfwwpyaGASVylLPQG 1710
Cdd:COG1541     91 SSGTTGKPTVVgytrkDLD-RWAELFARSLRA-AGVRPGDRVQNAFGYGlftgglgLHYGAERL------GATV--IPAG 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1711 GEKePEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPT 1790
Cdd:COG1541    161 GGN-TERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERW-GIKAYDIYGLT 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1791 EATVEAAFfDCPPHEKL-----ERIP-I-----GKPVhhvrlyllnqnqrmlPVGCIGELYIAGagvargylnrpaLTEE 1859
Cdd:COG1541    239 EVGPGVAY-ECEAQDGLhiwedHFLVeIidpetGEPV---------------PEGEEGELVVTT------------LTKE 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1860 -----RfledpfypgermYKTGDVARWLPD-----------GNVefLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR-EA 1922
Cdd:COG1541    291 ampliR------------YRTGDLTRLLPEpcpcgrthpriGRI--LGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpEY 356

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1678550997 1923 AVTVRTDSGEPELCAYVE---GLQRNEVRAQLERLL 1955
Cdd:COG1541    357 QIVVDREGGLDELTVRVElapGASLEALAEAIAAAL 392
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 1500-1940 1.34e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 73.82  E-value: 1.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFED------GV---MTYKELNEQANRIAWELIGRGVkPETTVAIIGKRSPEMLLGIYGILKAGGA 1570
Cdd:PRK05850     7 LRERASLQPDDAAFTFIDyeqdpaGVaetLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1571 YLPIDPDYP---EERISFLLEDSGTNILLLQSAglhvpeFTGEIV-YLNQTNSGLAHRL---------SNPNVDVLPQSL 1637
Cdd:PRK05850    86 AVPLSVPQGgahDERVSAVLRDTSPSVVLTTSA------VVDDVTeYVAPQPGQSAPPVievdlldldSPRGSDARPRDL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1638 ---AYVIYTSGSTGMPKGVEIEHRSA-VNFLNSLQSRYQLKHSDMIMHKTSYSfdasiwelfWWP--------------- 1698
Cdd:PRK05850   160 pstAYLQYTSGSTRTPAGVMVSHRNViANFEQLMSDYFGDTGGVPPPDTTVVS---------WLPfyhdmglvlgvcapi 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 YAGASVYLL-PQGGEKEPE--VIAKAIEEQKITAmhfVPSMlhAF----------------LEHIKyrsvpiktnrlkRV 1759
Cdd:PRK05850   231 LGGCPAVLTsPVAFLQRPArwMQLLASNPHAFSA---APNF--AFelavrktsdddmagldLGGVL------------GI 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1760 FSGGEQLGTHLVSRF------YELLPNVsITNSYGPTEATV-----------EAAFFDcppHEKL-----ERIPIGKPVH 1817
Cdd:PRK05850   294 ISGSERVHPATLKRFadrfapFNLRETA-IRPSYGLAEATVyvatrepgqppESVRFD---YEKLsaghaKRCETGGGTP 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1818 HVRlYLLNQNQ----------RMLPVGCIGELYIAGAGVARGYLNRPALTEERF---LEDPF--YPGERMYKTGDVArWL 1882
Cdd:PRK05850   370 LVS-YGSPRSPtvrivdpdtcIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSpgTPEGPWLRTGDLG-FI 447

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 1883 PDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEpELCAYVE 1940
Cdd:PRK05850   448 SEGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGGRVAAISVPDDGTE-KLVAIIE 504
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 1521-1983 1.67e-12

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 73.20  E-value: 1.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAII---GKRSPEMLLGIYGIlkagGAYL-PIDPDYPEERISFLLEDSGTNILL 1596
Cdd:PRK07008    41 TYRDCERRAKQLAQALAALGVEPGDRVGTLawnGYRHLEAYYGVSGS----GAVChTINPRLFPEQIAYIVNHAEDRYVL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1597 LQSAGL-----------------------HVPEFTGEIVYLNQTNSGLAHRLSNPNVDvlPQSLAYVIYTSGSTGMPKGV 1653
Cdd:PRK07008   117 FDLTFLplvdalapqcpnvkgwvamtdaaHLPAGSTPLLCYETLVGAQDGDYDWPRFD--ENQASSLCYTSGTTGNPKGA 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1654 EIEHRSAV--NFLNSLQSRYQLKHSDMIMHKTSYsFDASIWELfwwPYAGASV---YLLPqGGEKEPEVIAKAIEEQKIT 1728
Cdd:PRK07008   195 LYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGL---PYSAPLTgakLVLP-GPDLDGKSLYELIEAERVT 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1729 AMHFVPSMLHAFLEHIKYRSVPIKTnrLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTE-------ATVEAAFFDC 1801
Cdd:PRK07008   270 FSAGVPTVWLGLLNHMREAGLRFST--LRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEmsplgtlCKLKWKHSQL 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1802 PPHEKLE-RIPIGKPVHHVRLYLLNQNQRMLPVG--CIGELYIAGAGVARGYLNRpaltEERFLEDPFYPgermykTGDV 1878
Cdd:PRK07008   347 PLDEQRKlLEKQGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWVIDRYFRG----DASPLVDGWFP------TGDV 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1879 ARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA---------------VTVRTDSGEpelcayvegLQ 1943
Cdd:PRK07008   417 ATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAciacahpkwderpllVVVKRPGAE---------VT 487

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997 1944 RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK07008   488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 600-954 1.70e-12

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: 73.29  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  600 NADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDV----CYqeiFSALLKGGTLHIVP 675
Cdd:cd05908    104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMgliaFH---LAPLIAGMNQYLMP 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  676 EA--IKRdvPQLFAF-INKHQTNIVFLPTAFIKMIFS--ERELANSFPDGVKHLIAAGEQLMISDL---FQDVLRKRGIH 747
Cdd:cd05908    181 TRlfIRR--PILWLKkASEHKATIVSSPNFGYKYFLKtlKPEKANDWDLSSIRMILNGAEPIDYELcheFLDHMSKYGLK 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  748 ---LHNHYGPSETHV----------VSTYTIH-----PGDPIPE----------LPPIGKPIGCTDLYILNHQKQLQPCG 799
Cdd:cd05908    259 rnaILPVYGLAEASVgaslpkaqspFKTITLGrrhvtHGEPEPEvdkkdsecltFVEVGKPIDETDIRICDEDNKILPDG 338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  800 VPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLArRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLM 879
Cdd:cd05908    339 YIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAE 411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  880 NHPDISE---AAILIWQDQNGEHELCAYYCSVQKLNT-IDLRSYMASELPEYmipAKW-----IWVDSIPLTPNGKVDRA 950
Cdd:cd05908    412 ELEGVELgrvVACGVNNSNTRNEEIFCFIEHRKSEDDfYPLGKKIKKHLNKR---GGWqinevLPIRRIPKTTSGKVKRY 488


                   ....
gi 1678550997  951 ALPE 954
Cdd:cd05908    489 ELAQ 492
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 458-948 2.51e-12

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 73.42  E-value: 2.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  458 QTPVYETIHAMFEKQAEKTPDAHAVIDQ-ACSLTYRELNKAANRLARHLRmKGVVRQEPVAIMMERSAAFITGVLGILKA 536
Cdd:PRK08633   610 RKEALPPLAEAWIDTAKRNWSRLAVADStGGELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  537 GgaIVPVDPHYPA--DRIRYILHDCGCSHVV-SQAHL---------PSSLEDNYIItHPEDIE---SKVDG--------- 592
Cdd:PRK08633   689 G--KVPVNLNYTAseAALKSAIEQAQIKTVItSRKFLeklknkgfdLELPENVKVI-YLEDLKakiSKVDKltallaarl 765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  593 --------SNIKSVNNaDDLLYMIYTSGTTGKPKGVQFEHRN-MANllkfeythsgIDFEADVLQFAtpSFDVcyqeIFS 663
Cdd:PRK08633   766 lparllkrLYGPTFKP-DDTATIIFSSGSEGEPKGVMLSHHNiLSN----------IEQISDVFNLR--NDDV----ILS 828

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  664 AL-------LKGGTLHIVPEAIK-------RDVPQLFAFINKHQTNIVF-LPT---AFIKMIFSERELANSFpdgvkHLI 725
Cdd:PRK08633   829 SLpffhsfgLTVTLWLPLLEGIKvvyhpdpTDALGIAKLVAKHRATILLgTPTflrLYLRNKKLHPLMFASL-----RLV 903

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  726 AAG-EQLM--ISDLFQDvlrKRGIHLHNHYGPSETHVVST----------YTIHPGDpipELPPIGKPIGCTDLYILnHQ 792
Cdd:PRK08633   904 VAGaEKLKpeVADAFEE---KFGIRILEGYGATETSPVASvnlpdvlaadFKRQTGS---KEGSVGMPLPGVAVRIV-DP 976

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  793 KQLQPC--GVPGELYISGASVARGYVNHDKLTSdkfssdpfkpDVIM-------YRTGDLARRLEDGNIEYIGRADNQVK 863
Cdd:PRK08633   977 ETFEELppGEDGLILIGGPQVMKGYLGDPEKTA----------EVIKdidgigwYVTGDKGHLDEDGFLTITDRYSRFAK 1046

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  864 IRG-------------YRIEPQEIEVTLMNHPDiseaailiwqDQNGEHELCAYYCSVQKLNTIdLRSYMASELPEYMIP 930
Cdd:PRK08633  1047 IGGemvplgaveeelaKALGGEEVVFAVTAVPD----------EKKGEKLVVLHTCGAEDVEEL-KRAIKESGLPNLWKP 1115

                          570
                   ....*....|....*...
gi 1678550997  931 AKWIWVDSIPLTPNGKVD 948
Cdd:PRK08633  1116 SRYFKVEALPLLGSGKLD 1133
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1632-1994 2.93e-12

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 72.51  E-value: 2.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1632 VLPQSLAYVI-YTSGSTGMPKGVEIEHRSAvnFLNSLQSRyqLKHSDMIMHKTSYSFDASIWELFWW--PYAG--ASVYL 1706
Cdd:PRK05620   177 ELDETTAAAIcYSTGTTGAPKGVVYSHRSL--YLQSLSLR--TTDSLAVTHGESFLCCVPIYHVLSWgvPLAAfmSGTPL 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1707 LPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHikYRSVPIKTNRLKRVFSGGEQLGTHLVsRFYELLPNVSITNS 1786
Cdd:PRK05620   253 VFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVH--YLKNPPERMSLQEIYVGGSAVPPILI-KAWEERYGVDVVHV 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATveaaffdcpPHEKLERIPIGKPVHHVRLYLLNQ-------NQRMLPVGCI--------GELYIAGAGVARGYL 1851
Cdd:PRK05620   330 WGMTETS---------PVGTVARPPSGVSGEARWAYRVSQgrfpaslEYRIVNDGQVmestdrneGEIQVRGNWVTASYY 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1852 NRPALTE----------------ERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRS 1915
Cdd:PRK05620   401 HSPTEEGggaastfrgedvedanDRFTADGW------LRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMA 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1916 IEGVREAAVTVRTDS--GEPELCAYV--EGLQRN-----EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN----- 1981
Cdd:PRK05620   475 APEVVECAVIGYPDDkwGERPLAVTVlaPGIEPTretaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKdlrqh 554

                          410       420
                   ....*....|....*....|..
gi 1678550997 1982 ---------ALPAPGGAADAET 1994
Cdd:PRK05620   555 ladgdfeiiKLKGPGESGESDS 576
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2845-3019 3.30e-12

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 72.33  E-value: 3.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2845 GQPI-DGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLG 2923
Cdd:PRK10946   356 GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVG 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2924 RIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELS-AYVVTKPGLSTNAVRSELQN------KLpvfmh 2996
Cdd:PRK10946   430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVS-MEDELMGEKScAFLVVKEPLKAVQLRRFLREqgiaefKL----- 503

                          170       180
                   ....*....|....*....|...
gi 1678550997 2997 PAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK10946   504 PDRVECVDSLPLTAVGKVDKKQL 526
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 490-954 4.99e-12

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 71.71  E-value: 4.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVS--- 566
Cdd:PRK06018    41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITdlt 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  567 -----------------------QAHLPSSLEDNYIIThpEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFE 623
Cdd:PRK06018   121 fvpilekiadklpsveryvvltdAAHMPQTTLKNAVAY--EEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYS 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  624 HRnmANLLkfeytHSGIDFEADVLqfATPSFDVCYQEI-----------FSALLKGGTLhIVPEAiKRDVPQLFAFINKH 692
Cdd:PRK06018   199 HR--SNVL-----HALMANNGDAL--GTSAADTMLPVVplfhanswgiaFSAPSMGTKL-VMPGA-KLDGASVYELLDTE 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  693 Q-TNIVFLPTAFIKMIFSERELANSFPDGVKHLI--AAGEQLMISdLFQDVlrkrGIHLHNHYGPSETHVVSTYTIHPGd 769
Cdd:PRK06018   268 KvTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCggSAMPRSMIK-AFEDM----GVEVRHAWGMTEMSPLGTLAALKP- 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  770 PIPELPPIGKPigctdlyilnHQKQLQ---PCGV------------------PGELYISGASVARGYVnhdKLTSDKFSS 828
Cdd:PRK06018   342 PFSKLPGDARL----------DVLQKQgypPFGVemkitddagkelpwdgktFGRLKVRGPAVAAAYY---RVDGEILDD 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  829 DPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAI-------------LIWQDQ 895
Cdd:PRK06018   409 DGF------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVigvyhpkwderplLIVQLK 482

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  896 NGEhelcayycSVQKLNTIDlrsYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK06018   483 PGE--------TATREEILK---YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
PLN02479 PLN02479
acetate-CoA ligase
 609-952 6.46e-12

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 71.41  E-value: 6.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  609 YTSGTTGKPKGVQFEHRN-----MANLLKFEYThsgidfEADVLQFATPSFDV---CYQEIFSALLkgGT----LHIVPE 676
Cdd:PLN02479   202 YTSGTTASPKGVVLHHRGaylmaLSNALIWGMN------EGAVYLWTLPMFHCngwCFTWTLAALC--GTniclRQVTAK 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  677 AIKRdvpqlfAFINKHQTNIVFLPTAFIKMIFSER-ELANSFPDGVkHLIAAGEQLMISDLFQdvLRKRGIHLHNHYGPS 755
Cdd:PLN02479   274 AIYS------AIANYGVTHFCAAPVVLNTIVNAPKsETILPLPRVV-HVMTAGAAPPPSVLFA--MSEKGFRVTHTYGLS 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  756 ETHVVSTYTIHPgdpiPE---LPPIGKP----------IGCTDLYILNhQKQLQPcgVP------GELYISGASVARGYV 816
Cdd:PLN02479   345 ETYGPSTVCAWK----PEwdsLPPEEQArlnarqgvryIGLEGLDVVD-TKTMKP--VPadgktmGEIVMRGNMVMKGYL 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  817 NHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQN 896
Cdd:PLN02479   418 KNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997  897 GEHELCAYYC-------SVQKLNTIDLRSYMASELPEYMIPaKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PLN02479   491 WGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKIQKHVL 552
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 3128-3449 6.65e-12

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


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 70.75  E-value: 6.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3128 WFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQN----EQgkwdqynRPLshsDDALYGLQMI 3203
Cdd:cd20483     12 WFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGddfgEQ-------QVL---DDPSFHLIVI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3204 DLS-APDgtdgnrpYEPLIKRHVLDIQQK-MDLKNGPLLQAGLFHTIDGDF-LFLSAHHLVVDGISWRVLLEDLALGYRQ 3280
Cdd:cd20483     82 DLSeAAD-------PEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTALYDA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3281 -AAGGEDIKLPPKTSSFKAYAKKLSDYAESQQLMKQLKYWREAEEYQTEA---LPFDQIDGTRAHEGQRSTISFTLnDKE 3356
Cdd:cd20483    155 lRAGRDLATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDAsklLPFAKAERPPVKDYERSTVEATL-DKE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3357 TAALLKDANSAYNTdTQDMLLASVILALRH-WTnqsafklsleghGREDVLKGI--------DVSRTIGWFTAIYPLLIK 3427
Cdd:cd20483    234 LLARMKRICAQHAV-TPFMFLLAAFRAFLYrYT------------EDEDLTIGMvdgdrphpDFDDLVGFFVNMLPIRCR 300

                          330       340
                   ....*....|....*....|..
gi 1678550997 3428 LnadlpDSEESMVHVLKTTKDT 3449
Cdd:cd20483    301 M-----DCDMSFDDLLESTKTT 317
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 2543-3018 7.82e-12

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 71.18  E-value: 7.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKAsaLVSGD----KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYP 2618
Cdd:PRK07768    12 ARTSPRG--MVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTP 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2619 KERKRYILSDSGTKLLMTinEADLGVLAD-FE----------GEILTI-ESVEEDDKSPLPQMSSAhhLAYIIYTSGTTG 2686
Cdd:PRK07768    90 RTDLAVWAEDTLRVIGMI--GAKAVVVGEpFLaaapvleekgIRVLTVaDLLAADPIDPVETGEDD--LALMQLTSGSTG 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2687 RPKGVMVEHKGIANTLQWRRNAYAFN-ETDTILQLFSFSFD----GFITsmfTPLLSGAKAVLLHEEE-AKDILAIKHQL 2760
Cdd:PRK07768   166 SPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDmgmvGFLT---VPMYFGAELVKVTPMDfLRDPLLWAELI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2761 SRQRIThMIIVP-----VLYRALLDVVQPE--DVKTLRVVTLAGEAADRELIARSLAI-----CPHTELANEYGPTENSV 2828
Cdd:PRK07768   243 SKYRGT-MTAAPnfayaLLARRLRRQAKPGafDLSSLRFALNGAEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEATL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2829 ATTVMR-------------------------HMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLARGYV 2883
Cdd:PRK07768   322 AVSFSPcgaglvvdevdadllaalrravpatKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2884 nlpelterafTQNPFKPearmyrTGDAARWMADGTLEYL---------GRIDDQVKIRGYRVETKEIESVIRCIKGVKDA 2954
Cdd:PRK07768   402 ----------TMDGFIP------AQDADGWLDTGDLGYLteegevvvcGRVKDVIIMAGRNIYPTDIERAAARVEGVRPG 465

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2955 AVVA-HVTASGQTELSAYVVTKPGLS------------TNAVRSElqnklpVFMHPAFIEKLD--SLPLSPNGKLDRGA 3018
Cdd:PRK07768   466 NAVAvRLDAGHSREGFAVAVESNAFEdpaevrrirhqvAHEVVAE------VGVRPRNVVVLGpgSIPKTPSGKLRRAN 538
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 489-863 9.12e-12

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 70.71  E-value: 9.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHvvsqa 568
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA----- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslednyIIThpedieskvdgsniksVNNADDLLYMIYTSGTTGKPKGVQFEHRNMAnllkfeythSGI-DFEADVL 647
Cdd:cd17639     81 ----------IFT----------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLV---------AGIaGLGDRVP 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  648 QFATPS------------FDVCYQEIFsaLLKGG--------TLHivpEAIKRD---------------VPQLFAFINKH 692
Cdd:cd17639    126 ELLGPDdrylaylplahiFELAAENVC--LYRGGtigygsprTLT---DKSKRGckgdltefkptlmvgVPAIWDTIRKG 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  693 QTNIVFLPTAFIKMIFS---ERELANsfpdgVKHL-------------------------------IAAGEQLMISDLFQ 738
Cdd:cd17639    201 VLAKLNPMGGLKRTLFWtayQSKLKA-----LKEGpgtplldelvfkkvraalggrlrymlsggapLSADTQEFLNIVLC 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  739 DVLrkrgihlhNHYGPSETHVVSTYTiHPGDPIPELppIGKPIGCTDLYILN-----HQKQLQPCgvPGELYISGASVAR 813
Cdd:cd17639    276 PVI--------QGYGLTETCAGGTVQ-DPGDLETGR--VGPPLPCCEIKLVDweeggYSTDKPPP--RGEILIRGPNVFK 342

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997  814 GYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVK 863
Cdd:cd17639    343 GYYKNPEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRKKDLVK 386
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 966-1040 1.23e-11

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: 62.95  E-value: 1.23e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997  966 APRNLLEAKLSQLFEDVLK--NGHIGIQDNFFDN-GGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLALIIREA 1040
Cdd:COG0236      1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 2771-3021 1.25e-11

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 70.02  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2771 VPVLYRALLDVVqPEDVKTLRVVTLAGEAADRELI--ARSLAICphteLANEYGPTENS--VATtvmrhMEKQAYV---- 2842
Cdd:PRK07445   214 VPTQLQRLLQLR-PQWLAQFRTILLGGAPAWPSLLeqARQLQLR----LAPTYGMTETAsqIAT-----LKPDDFLagnn 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2843 SIGQPIDGTQVLILNSNhqlqpigvAGELCIAGTGLARGYVnlPelteraftqnPFKPEARMYRTGDAARWMADGTLEYL 2922
Cdd:PRK07445   284 SSGQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--P----------QILDSQGIFETDDLGYLDAQGYLHIL 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2923 GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS-GQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFIE 3001
Cdd:PRK07445   344 GRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWI 423

                          250       260
                   ....*....|....*....|
gi 1678550997 3002 KLDSLPLSPNGKLDRGALPK 3021
Cdd:PRK07445   424 PVPQLPRNPQGKINRQQLQQ 443
PLN02654 PLN02654
acetate-CoA ligase
 2677-3021 1.38e-11

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 70.70  E-value: 1.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2677 YIIYTSGTTGRPKGVMVEHKG----IANTLQwrrnaYAFNETDTilQLFSFSFD-GFITS----MFTPLLSGAkAVLLHE 2747
Cdd:PLN02654   279 FLLYTSGSTGKPKGVLHTTGGymvyTATTFK-----YAFDYKPT--DVYWCTADcGWITGhsyvTYGPMLNGA-TVLVFE 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2748 EEAK--------DILaikhqlSRQRITHMIIVPVLYRALL----DVVQPEDVKTLRVVTLAGE----AADR---ELIARS 2808
Cdd:PLN02654   351 GAPNypdsgrcwDIV------DKYKVTIFYTAPTLVRSLMrdgdEYVTRHSRKSLRVLGSVGEpinpSAWRwffNVVGDS 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2809 LaiCPhteLANEYGPTENS-VATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGT--GLARGYVNL 2885
Cdd:PLN02654   425 R--CP---ISDTWWQTETGgFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFRTLYGD 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2886 PELTERAFtqnpFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVA---HVTA 2962
Cdd:PLN02654   500 HERYETTY----FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGiehEVKG 575

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2963 SGqteLSAYVVTKPGLS-TNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKLDRGALPK 3021
Cdd:PLN02654   576 QG---IYAFVTLVEGVPySEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 1521-1983 1.47e-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: 70.19  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLL--- 1597
Cdd:cd05932      8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgkl 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1598 -----QSAGlhVPEftGEIVYLNQTNSGL-AHR-------LSNPNVDVL---PQSLAYVIYTSGSTGMPKGVEIEHRSAV 1661
Cdd:cd05932     88 ddwkaMAPG--VPE--GLISISLPPPSAAnCQYqwddliaQHPPLEERPtrfPEQLATLIYTSGTTGQPKGVMLTFGSFA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1662 NFLNSLQSRYQLKHSDMIMhktSYSFDASIWELFW----WPYAGASVYLlpqggekePEVIAKAIEEQKI---TAMHFVP 1734
Cdd:cd05932    164 WAAQAGIEHIGTEENDRML---SYLPLAHVTERVFveggSLYGGVLVAF--------AESLDTFVEDVQRarpTLFFSVP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1735 SMLHAFLEHIKYRSVPIKTNRL-----------KRVF------------SGGEQLGTHLVSRFYELlpNVSITNSYGPTE 1791
Cdd:cd05932    233 RLWTKFQQGVQDKIPQQKLNLLlkipvvnslvkRKVLkglgldqcrlagCGSAPVPPALLEWYRSL--GLNILEAYGMTE 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1792 ATVEAAFfdCPPHEKLERIpIGKPVHHVRLYLLNQnqrmlpvgciGELYIAGAGVARGYLNRPALTEERFLEDPFYpger 1871
Cdd:cd05932    311 NFAYSHL--NYPGRDKIGT-VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFL---- 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 myKTGDVARWLPDGNVEFLGRTDDQVKI-RGYRIEPGEIEAALRSIEGVrEAAVTVRTDSGEP-ELCAYVEGLQ------ 1943
Cdd:cd05932    374 --RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAPlALVVLSEEARlradaf 450

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 1944 -RNEVRAQLERLL--------PGYMVPAYMIEMEQWPV-----TPSGKLDRNAL 1983
Cdd:cd05932    451 aRAELEASLRAHLarvnstldSHEQLAGIVVVKDPWSIdngilTPTLKIKRNVL 504
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 2556-2989 1.59e-11

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 70.55  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2556 DKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMhrsfSMI--ASI--LGVWKAG--------GcyvpIDPEYPKERkr 2623
Cdd:PRK00174    96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYM----PMIpeAAVamLACARIGavhsvvfgG----FSAEALADR-- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2624 yiLSDSGTKLLMTineADLGV---------------LADFEgeilTIESV-------------------------EEDDK 2663
Cdd:PRK00174   166 --IIDAGAKLVIT---ADEGVrggkpiplkanvdeaLANCP----SVEKVivvrrtggdvdwvegrdlwwhelvaGASDE 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2664 SPlPQMSSAHHLAYIIYTSGTTGRPKGVMveHK------GIANTLQWrrnAYAFNETDTilqlFSFSFD-GFIT----SM 2732
Cdd:PRK00174   237 CE-PEPMDAEDPLFILYTSGSTGKPKGVL--HTtggylvYAAMTMKY---VFDYKDGDV----YWCTADvGWVTghsyIV 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2733 FTPLLSGAKaVLLHE------EEAK--DILAiKHQlsrqrithmiiVPVLY------RALL----DVVQPEDVKTLRVVT 2794
Cdd:PRK00174   307 YGPLANGAT-TLMFEgvpnypDPGRfwEVID-KHK-----------VTIFYtaptaiRALMkegdEHPKKYDLSSLRLLG 373

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2795 LAGEAAD-------RELIARSLaiCP------HTELaneyG-----PTENSVATtvmrhmeKQAyvSIGQPIDGTQVLIL 2856
Cdd:PRK00174   374 SVGEPINpeawewyYKVVGGER--CPivdtwwQTET----GgimitPLPGATPL-------KPG--SATRPLPGIQPAVV 438

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2857 NSNHQLQPIGVAGELCIAGT--GLARGYVNLPElteRaFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGY 2934
Cdd:PRK00174   439 DEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE---R-FVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGH 514

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2935 RVETKEIESVIRCIKGVKDAAVV--AHVTaSGQtELSAYVVTKPGLSTN-AVRSELQN 2989
Cdd:PRK00174   515 RLGTAEIESALVAHPKVAEAAVVgrPDDI-KGQ-GIYAFVTLKGGEEPSdELRKELRN 570
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 602-949 1.84e-11

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 70.21  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDLLYMIYTSGTTGKPKGVQFEHRNMA--NLLKFEYTHSGidfEADVLQFATPsfdVCYQEIFS---ALLKGGTLHI-VP 675
Cdd:PLN02860   172 DDAVLICFTSGTTGRPKGVTISHSALIvqSLAKIAIVGYG---EDDVYLHTAP---LCHIGGLSsalAMLMVGACHVlLP 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  676 eaiKRDVPQLFAFINKHQ-TNIVFLPTAFIKMIFSERELAN--SFPdGVKHLIAAGEQLMiSDLFQDVL----RKRgihL 748
Cdd:PLN02860   246 ---KFDAKAALQAIKQHNvTSMITVPAMMADLISLTRKSMTwkVFP-SVRKILNGGGSLS-SRLLPDAKklfpNAK---L 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  749 HNHYGPSETHVVSTY-TIHpgDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVP----------------GELYISGASV 811
Cdd:PLN02860   318 FSAYGMTEACSSLTFmTLH--DPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPaphvelkigldessrvGRILTRGPHV 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  812 ARGYVNHDKLTSDKFSSDpfkpdvIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL- 890
Cdd:PLN02860   396 MLGYWGQNSETASVLSND------GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVg 469

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  891 --------------------IWQDQNGEHelcayYCSVQKLNTIDLRSYMASE-LPEYMIPAKWI-WVDSIPLTPNGKVD 948
Cdd:PLN02860   470 vpdsrltemvvacvrlrdgwIWSDNEKEN-----AKKNLTLSSETLRHHCREKnLSRFKIPKLFVqWRKPFPLTTTGKIR 544


                   .
gi 1678550997  949 R 949
Cdd:PLN02860   545 R 545
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 1492-1996 2.13e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 69.67  E-value: 2.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1492 MNQTLHYALEQQAEKtpDQAAVIFEDGVMTYKELNEQANRIAWELIG--RGVKPeTTVAIIGKRSPEMLLGIYGILKAG- 1568
Cdd:PRK13388     1 MRDTIAQLLRDRAGD--DTIAVRYGDRTWTWREVLAEAAARAAALIAlaDPDRP-LHVGVLLGNTPEMLFWLAAAALGGy 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1569 ----------GAYLPIDPDYPEERIsfLLEDSGTNILLlqsAGLHVPEFTGEIV----YLNQTNsglAHRLSNPNVDVLP 1634
Cdd:PRK13388    78 vlvglnttrrGAALAADIRRADCQL--LVTDAEHRPLL---DGLDLPGVRVLDVdtpaYAELVA---AAGALTPHREVDA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1635 QSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSD-----MIMhktsysFDASIWELFWWPY--AGASVYLL 1707
Cdd:PRK13388   150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDvcyvsMPL------FHSNAVMAGWAPAvaSGAAVALP 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1708 PqggekepeviakaieeqKITAMHFVPSMLHAFLEHIKYRSVPI------------KTNRLKRVF--SGGEQLGTHLVSR 1773
Cdd:PRK13388   224 A-----------------KFSASGFLDDVRRYGATYFNYVGKPLayilatperpddADNPLRVAFgnEASPRDIAEFSRR 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1774 FyellpNVSITNSYGPTE-ATVEAAFFDCPPHEkleripIGKPVHHVRLY-----------LLNQNQRML-PVGCIGELY 1840
Cdd:PRK13388   287 F-----GCQVEDGYGSSEgAVIVVREPGTPPGS------IGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELV 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1841 -IAGAGVARGYLNRPALTEERFledpfypgeR--MYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 1917
Cdd:PRK13388   356 nTAGAGFFEGYYNNPEATAERM---------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHP 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1918 GVREAAVTVRTD--SGEPELCAYV----EGLQRNEVRAQL--ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGA 1989
Cdd:PRK13388   427 AINRVAVYAVPDerVGDQVMAALVlrdgATFDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGWA 506


                   ....*..
gi 1678550997 1990 ADAETYT 1996
Cdd:PRK13388   507 TGDPVTL 513
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 2647-3019 2.23e-11

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 69.66  E-value: 2.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2647 DFEGEILTIEsveeddksPLPQMSSA-------HHLAYIIYTSGTTGRPKGVMVEHKG-----IANTLQWRRNAYAFnet 2714
Cdd:PLN03102   161 DYECLIQRGE--------PTPSLVARmfriqdeHDPISLNYTSGTTADPKGVVISHRGaylstLSAIIGWEMGTCPV--- 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2715 dTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKdilaIKHQLSRQRITHMIIVPVLYRALLD---VVQPEDVKTLR 2791
Cdd:PLN03102   230 -YLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPE----IYKNIEMHNVTHMCCVPTVFNILLKgnsLDLSPRSGPVH 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2792 VVTlAGEAADRELIARSLAICPHteLANEYGPTEnsvATTVMRHMEKQayvSIGQPIDGTQVLILNSNHQLQPIGVA--- 2868
Cdd:PLN03102   305 VLT-GGSPPPAALVKKVQRLGFQ--VMHAYGLTE---ATGPVLFCEWQ---DEWNRLPENQQMELKARQGVSILGLAdvd 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2869 -----------------GELCIAGTGLARGYVNLPELTERAFTQNpfkpearMYRTGDAARWMADGTLEYLGRIDDQVKI 2931
Cdd:PLN03102   376 vknketqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIIS 448

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2932 RGYRVETKEIESVIRCIKGVKDAAVVA--HVTAsGQTElSAYVVTKPGLSTNAVRSEL------------QNKLPVFMHP 2997
Cdd:PLN03102   449 GGENISSVEVENVLYKYPKVLETAVVAmpHPTW-GETP-CAFVVLEKGETTKEDRVDKlvtrerdlieycRENLPHFMCP 526

                          410       420
                   ....*....|....*....|..
gi 1678550997 2998 AFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PLN03102   527 RKVVFLQELPKNGNGKILKPKL 548
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 2655-2945 3.32e-11

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 69.39  E-value: 3.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2655 IESVEEDDKSP----LPQMSSahHLAYIIYTSGTTGRPKGVmVEHKGiANTLQWRRNAYAFNETDTILQLFSFSFDGFIT 2730
Cdd:PTZ00237   234 IKKIKENNQSPfyeyVPVESS--HPLYILYTSGTTGNSKAV-VRSNG-PHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2731 --SMFTPLLSGAKAVLLHEeeaKDILAIKHQ-------LSRQRITHMIIVPVLYRALLDvVQPE--------DVKTLRVV 2793
Cdd:PTZ00237   310 fhGFLYGSLSLGNTFVMFE---GGIIKNKHIeddlwntIEKHKVTHTLTLPKTIRYLIK-TDPEatiirskyDLSNLKEI 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2794 TLAGEAADR---ELIARSLAICPhtelANEYGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGE 2870
Cdd:PTZ00237   386 WCGGEVIEEsipEYIENKLKIKS----SRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGE 461

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2871 LCIA---GTGLARGYVNLPELTERAFTQNPfkpeaRMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVI 2945
Cdd:PTZ00237   462 VAFKlpmPPSFATTFYKNDEKFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSI 534
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 3139-3566 3.69e-11

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


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 68.49  E-value: 3.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3139 HFNQSVmLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQYNRplshsDDALYGLQMIDLSapdGTDGNRPYE 3218
Cdd:cd19547     24 YFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVR-----DDLAPPWALLDWS---GEDPDRRAE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3219 PLIKRHVLDIQQKMDLKNGPLLQAGLFHTIDG-DFLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPkTSSFK 3297
Cdd:cd19547     95 LLERLLADDRAAGLSLADCPLYRLTLVRLGGGrHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSP-CRPYR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3298 AYAKKLSdyAESQQLMKQLKYWREAEEYQTEAlPFDQIDGTRahEGQRSTISFTLNDKETaALLKDANSAYNTDTQDMLL 3377
Cdd:cd19547    174 DYVRWIR--ARTAQSEESERFWREYLRDLTPS-PFSTAPADR--EGEFDTVVHEFPEQLT-RLVNEAARGYGVTTNAISQ 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3378 A--SVILALRHWTNQSAFKLSLEghGREDVLKGIDVsrTIGWFTAIYPLLIKLnadlpDSEESMVHVLKTTKDTLRRVPD 3455
Cdd:cd19547    248 AawSMLLALQTGARDVVHGLTIA--GRPPELEGSEH--MVGIFINTIPLRIRL-----DPDQTVTGLLETIHRDLATTAA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3456 KGFgygvikyltPPGKKDINFTGAPEIS----FNYLGQFESGRTAEVPEEDaFSFSPLgaggDISTTWNREQSLDISAIA 3531
Cdd:cd19547    319 HGH---------VPLAQIKSWASGERLSggrvFDNLVAFENYPEDNLPGDD-LSIQII----DLHAQEKTEYPIGLIVLP 384

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1678550997 3532 AEgKLTVNMTYDNARFQRKTIEQLSETCRQFLLQL 3566
Cdd:cd19547    385 LQ-KLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQL 418
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2005-2062 3.91e-11

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


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 60.65  E-value: 3.91e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2005 KLSQLWEDVLK--NGPVGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKDVFAHPTVE 2062
Cdd:pfam00550    2 RLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 489-949 4.17e-11

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 69.01  E-value: 4.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSaafITGVLGILKAG--GAIVPV-----DPHYPADRIRyilhDCGC 561
Cdd:PRK00174    99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMI---PEAAVAMLACAriGAVHSVvfggfSAEALADRII----DAGA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  562 SHVVS-----QAHLPSSLEDNY--IITHPEDIES----KVDGSNIKSVN----------------------NADDLLYMI 608
Cdd:PRK00174   172 KLVITadegvRGGKPIPLKANVdeALANCPSVEKvivvRRTGGDVDWVEgrdlwwhelvagasdecepepmDAEDPLFIL 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  609 YTSGTTGKPKGVQfeHRNMANLLKFEYTHSGIdfeadvlqfatpsFDVCYQEIF--SA---------------LLKGGTL 671
Cdd:PRK00174   252 YTSGSTGKPKGVL--HTTGGYLVYAAMTMKYV-------------FDYKDGDVYwcTAdvgwvtghsyivygpLANGATT 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  672 HI---VPeaikrDVPQ---LFAFINKHQTNIVFL-PTAfIKMifserelansfpdgvkhLIAAGEQLMI-SDLfqDVLRK 743
Cdd:PRK00174   317 LMfegVP-----NYPDpgrFWEVIDKHKVTIFYTaPTA-IRA-----------------LMKEGDEHPKkYDL--SSLRL 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  744 RG-----IH------LHNHYGPSETHVVSTY--T------IhpgDPIPELPPIgKPIGCT------DLYILNHQKQLQPC 798
Cdd:PRK00174   372 LGsvgepINpeawewYYKVVGGERCPIVDTWwqTetggimI---TPLPGATPL-KPGSATrplpgiQPAVVDEEGNPLEG 447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  799 GVPGELYI--SGASVARG-YVNHDKLTSDKFSsdPFKPdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:PRK00174   448 GEGGNLVIkdPWPGMMRTiYGDHERFVKTYFS--TFKG---MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  876 VTLMNHPDISEAAIL-IWQDQNGEhELCAY------YCSVQKLNTiDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:PRK00174   523 SALVAHPKVAEAAVVgRPDDIKGQ-GIYAFvtlkggEEPSDELRK-ELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIM 600


                   .
gi 1678550997  949 R 949
Cdd:PRK00174   601 R 601
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 1500-1880 4.35e-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: 69.00  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDG-----VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPI 1574
Cdd:cd05921      1 LAHWARQAPDRTWLAEREGnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1575 DPDYP-----EERISFLLEDSGTNILLLQSA-----GLHVPEFTGE--IVYLNQ-------TNSGLAHRLSNPNVD---- 1631
Cdd:cd05921     81 SPAYSlmsqdLAKLKHLFELLKPGLVFAQDAapfarALAAIFPLGTplVVSRNAvagrgaiSFAELAATPPTAAVDaafa 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1632 -VLPQSLAYVIYTSGSTGMPKGVEIEHRS-AVNFLNSLQSRYQLKHSDMIMhktsysfdasiweLFWWP----------- 1698
Cdd:cd05921    161 aVGPDTVAKFLFTSGSTGLPKAVINTQRMlCANQAMLEQTYPFFGEEPPVL-------------VDWLPwnhtfggnhnf 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 ----YAGASVYLlpQGGEKEPEVIAKAI---EEQKITAMHFVP---SMLHAFLEH---IKYRSVpiktNRLKRVFSGGEQ 1765
Cdd:cd05921    228 nlvlYNGGTLYI--DDGKPMPGGFEETLrnlREISPTVYFNVPagwEMLVAALEKdeaLRRRFF----KRLKLMFYAGAG 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1766 LGTHLVSRFYELL-----PNVSITNSYGPTEATveAAFFDCppHEKLERIP-IGKPVHHVRLyllnqnqRMLPVGCIGEL 1839
Cdd:cd05921    302 LSQDVWDRLQALAvatvgERIPMMAGLGATETA--PTATFT--HWPTERSGlIGLPAPGTEL-------KLVPSGGKYEV 370

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1678550997 1840 YIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVAR 1880
Cdd:cd05921    371 RVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAK 405
prpE PRK10524
propionyl-CoA synthetase; Provisional
 2674-3019 4.35e-11

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 68.82  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 HLAYIIYTSGTTGRPKGVMVEHKGIANTLQwrrnayafNETDTIlqlfsfsFDG------FITS-----------MFTPL 2736
Cdd:PRK10524   234 EPSYILYTSGTTGKPKGVQRDTGGYAVALA--------TSMDTI-------FGGkagetfFCASdigwvvghsyiVYAPL 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2737 LSGAKAVLLheeEAKDIL---AIKHQLSRQ-RITHMIIVPVLYRAL----LDVVQPEDVKTLRVVTLAGEAADR---ELI 2805
Cdd:PRK10524   299 LAGMATIMY---EGLPTRpdaGIWWRIVEKyKVNRMFSAPTAIRVLkkqdPALLRKHDLSSLRALFLAGEPLDEptaSWI 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2806 ARSLAIcPhteLANEYGPTENS-VATTVMRHMEKQA--YVSIGQPIDGTQVLILNSNhqlqpigvAGELCIAGTglaRGY 2882
Cdd:PRK10524   376 SEALGV-P---VIDNYWQTETGwPILAIARGVEDRPtrLGSPGVPMYGYNVKLLNEV--------TGEPCGPNE---KGV 440

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2883 VN----LPE--LT------ERaFTQNPFKPEARM-YRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIK 2949
Cdd:PRK10524   441 LViegpLPPgcMQtvwgddDR-FVKTYWSLFGRQvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHP 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2950 GVKDAAVVAHVTA-SGQTELsAYVVTKPG--LSTNAVRSELQ--------NKLPVFMHPAFIEKLDSLPLSPNGKLDRGA 3018
Cdd:PRK10524   520 AVAEVAVVGVKDAlKGQVAV-AFVVPKDSdsLADREARLALEkeimalvdSQLGAVARPARVWFVSALPKTRSGKLLRRA 598


                   .
gi 1678550997 3019 L 3019
Cdd:PRK10524   599 I 599
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 1491-1924 4.90e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 68.55  E-value: 4.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1491 SMNQTLHYALEQQAEKtpDQAAVIFEDGVMTYKE-LNEQANRIAW--ELIGRGVKPEttVAIIGKRSPEMLL-----GIY 1562
Cdd:PRK07867     2 SSAPTVAELLLPLAED--DDRGLYFEDSFTSWREhIRGSAARAAAlrARLDPTRPPH--VGVLLDNTPEFSLllgaaALS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1563 GILKAG------GAYLPIDPDYPEERisFLLEDSGtNILLLQSAGLHVPEFTGEIVYLNQTNSGLAHRLSNPnVDVLPQS 1636
Cdd:PRK07867    78 GIVPVGlnptrrGAALARDIAHADCQ--LVLTESA-HAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPF-RVADPDD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1637 LAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLK------------HSDMIMHKtsysfdasiwelfWWP--YAGA 1702
Cdd:PRK07867   154 LFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGpddvcyvsmplfHSNAVMAG-------------WAValAAGA 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1703 SVYLlpqggekepeviakaieEQKITAMHFVPSMLHAFLEHIKYRSVPI------------KTNRLKRVFsgGEQLGTHL 1770
Cdd:PRK07867   221 SIAL-----------------RRKFSASGFLPDVRRYGATYANYVGKPLsyvlatperpddADNPLRIVY--GNEGAPGD 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1771 VSRFYELLpNVSITNSYGPTEATVE-AAFFDCPPHEkleripIGKPVHHVRLY-----------LLNQNQRMLPVGCIGE 1838
Cdd:PRK07867   282 IARFARRF-GCVVVDGFGSTEGGVAiTRTPDTPPGA------LGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGE 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1839 LY-IAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 1917
Cdd:PRK07867   355 LVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427


                   ....*..
gi 1678550997 1918 GVREAAV 1924
Cdd:PRK07867   428 DATEVAV 434
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 30-319 4.94e-11

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 67.90  E-value: 4.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   30 SQAYVEqasftIEGK-VNPQFFQNSINALVERHDIFRTIFISQNvsspQQVVLRERNVIVLE-EDITHLNEAEQSQFIEQ 107
Cdd:cd19535     26 CHAYLE-----FDGEdLDPDRLERAWNKLIARHPMLRAVFLDDG----TQQILPEVPWYGITvHDLRGLSEEEAEAALEE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  108 WKEK------DRDRG--FHLQkdvlmrIALIQTGEsqysciwTFHHI-----MMDGWCLSIVLKEFLHIYASyvnaSPIT 174
Cdd:cd19535     97 LRERlshrvlDVERGplFDIR------LSLLPEGR-------TRLHLsidllVADALSLQILLRELAALYED----PGEP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  175 LEPVQP-YGKYIKW---LMEQDKEQAVSYWDHYLSgheqqtVLP--------KQKKTKGKSRQEHVTFSFSKEESSRLSE 242
Cdd:cd19535    160 LPPLELsFRDYLLAeqaLRETAYERARAYWQERLP------TLPpapqlplaKDPEEIKEPRFTRREHRLSAEQWQRLKE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  243 LAAREEVTLSTIFHTIWGILLQKYNNNDD-----AVFgsvisGRPAEIEGIEHMVGLFINTMPVRVQG-AKTPFLQLIKD 316
Cdd:cd19535    234 RARQHGVTPSMVLLTAYAEVLARWSGQPRfllnlTLF-----NRLPLHPDVNDVVGDFTSLLLLEVDGsEGQSFLERARR 308


                   ...
gi 1678550997  317 MQK 319
Cdd:cd19535    309 LQQ 311
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 3123-3452 6.41e-11

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: 67.86  E-value: 6.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3123 SPVQKWFLsqdikeKHHFNQ---SVMLHRST-----SVQEDALRKTLKAITCHHDALRMVFTqneqgkWDQYNRP----L 3190
Cdd:cd19536      5 SSLQEGML------FHSLLNpggSVYLHNYTytvgrRLNLDLLLEALQVLIDRHDILRTSFI------EDGLGQPvqvvH 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3191 SHSDdalyglqmIDLSAPDGTDGNRPYEPLIKRHVLDIQQKMDLKNGPLLQAGLFH-TIDGDFLF-LSAHHLVVDGISWR 3268
Cdd:cd19536     73 RQAQ--------VPVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRkDERERFLLvISDHHSILDGWSLY 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3269 VLLEDLALGYRQAAGGEDIKLPPkTSSFKAYAKKLSDYAESQQLmkqLKYWREAeeyqtealpFDQIDGTRAHEGQRSTI 3348
Cdd:cd19536    145 LLVKEILAVYNQLLEYKPLSLPP-AQPYRDFVAHERASIQQAAS---ERYWREY---------LAGATLATLPALSEAVG 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3349 SFTLNDKETA-ALLKDANSAYNTDTQDMLLASVILA-----LRHWTNQSAFKLSLEGHGREDVLKGIDvsRTIGWFTAIY 3422
Cdd:cd19536    212 GGPEQDSELLvSVPLPVRSRSLAKRSGIPLSTLLLAawalvLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTL 289

                          330       340       350
                   ....*....|....*....|....*....|
gi 1678550997 3423 PLLIKLnadlpdSEESMVHVLKTTKDTLRR 3452
Cdd:cd19536    290 PLRVTL------SEETVEDLLKRAQEQELE 313
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 1643-1919 7.42e-11

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 67.65  E-value: 7.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1643 TSGSTGMPKGVEIEHRSAVNFLNsLQSRY----QLKHSDMIMHKTSYS-------FDASIWELfwwpyaGASVylLPQG- 1710
Cdd:cd05913     86 SSGTTGKPTVVGYTKNDLDVWAE-LVARCldaaGVTPGDRVQNAYGYGlftgglgFHYGAERL------GALV--IPAGg 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1711 GEKEPEViaKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFyELLPNVSITNSYGPT 1790
Cdd:cd05913    157 GNTERQL--QLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRI-ERRLGIKAYDIYGLT 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1791 EATVEAAFFDCP---------PHEKLERI-P-IGKPVhhvrlyllnqnqrmlPVGCIGELYIAGagvargyLNRPALtee 1859
Cdd:cd05913    234 EIIGPGVAFECEekdglhiweDHFIPEIIdPeTGEPV---------------PPGEVGELVFTT-------LTKEAM--- 288

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 1860 rfledpfyPGERmYKTGDVARWLPDGNVE---------FLGRTDDQVKIRGYRIEPGEIEAALRSIEGV 1919
Cdd:cd05913    289 --------PLIR-YRTRDITRLLPGPCPCgrthrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 490-890 7.95e-11

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: 67.83  E-value: 7.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVS--- 566
Cdd:cd17641     13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAede 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  567 ---------QAHLPS---------------------SLED------NYIITHPEDIESKVDGSNiksvnnADDLLYMIYT 610
Cdd:cd17641     93 eqvdklleiADRIPSvryviycdprgmrkyddprliSFEDvvalgrALDRRDPGLYEREVAAGK------GEDVAVLCTT 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  611 SGTTGKPKGVQFEHRNM----ANLLKFEYTHSGIDFEAdVLQFATpsfdvCYQEIFS---ALLKGGTLHIV--PEAIKRD 681
Cdd:cd17641    167 SGTTGKPKLAMLSHGNFlghcAAYLAADPLGPGDEYVS-VLPLPW-----IGEQMYSvgqALVCGFIVNFPeePETMMED 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  682 VPQLfafinkhQTNIVFLP-------TAFI--KMIFSERELANSFPDGVKHLIAAGEQLM-----------ISDLFQDV- 740
Cdd:cd17641    241 LREI-------GPTFVLLPprvwegiAADVraRMMDATPFKRFMFELGMKLGLRALDRGKrgrpvslwlrlASWLADALl 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  741 ---LRKR---------------------------GIHLHNHYGPSETHVVstYTIHPGDPIPElPPIGKPIGCTDLYILN 790
Cdd:cd17641    314 frpLRDRlgfsrlrsaatggaalgpdtfrffhaiGVPLKQLYGQTELAGA--YTVHRDGDVDP-DTVGVPFPGTEVRIDE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  791 HqkqlqpcgvpGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRA-DNQVKIRGYRI 869
Cdd:cd17641    391 V----------GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRF 454

                          490       500
                   ....*....|....*....|.
gi 1678550997  870 EPQEIEVTLMNHPDISEAAIL 890
Cdd:cd17641    455 SPQFIENKLKFSPYIAEAVVL 475
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 3041-3099 8.15e-11

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


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 59.88  E-value: 8.15e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997 3041 QILADIWKEVLG--AEKIGTADSFFELGGDSIKALQVSARLHR-IGKQMAVKDLFSHPTIQE 3099
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEeFGVEIPPSDLFEHPTLAE 62
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 2543-2997 1.17e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 67.20  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2543 AARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPkERK 2622
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP-QPL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2623 RyilsdsgTKLLMTINeADLGVLADFEGEILTIESVEEDDKSPLPQMS-SAHHLAYIIYTSGTTGRPKGVMVEHKG-IAN 2700
Cdd:PRK09029    92 L-------EELLPSLT-LDFALVLEGENTFSALTSLHLQLVEGAHAVAwQPQRLATMTLTSGSTGLPKAAVHTAQAhLAS 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2701 T---LQWrrnaYAFNETDT---ILQLFSFSFDGFItsmFTPLLSGAKAVLLHEEEAKDILaikhqlsrQRITHMIIVPV- 2773
Cdd:PRK09029   164 AegvLSL----MPFTAQDSwllSLPLFHVSGQGIV---WRWLYAGATLVVRDKQPLEQAL--------AGCTHASLVPTq 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2774 LYRaLLDvvQPEDVKTLRVVTLAGEAADRELI--ARSLAICphTELAneYGPTEnsVATTVmrhMEKQAYVS--IGQPID 2849
Cdd:PRK09029   229 LWR-LLD--NRSEPLSLKAVLLGGAAIPVELTeqAEQQGIR--CWCG--YGLTE--MASTV---CAKRADGLagVGSPLP 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2850 GTQVLIlnsnhqlqpigVAGELCIAGTGLARGYVNLPELTeraftqnPFKPEARMYRTGDAARWmADGTLEYLGRIDDQV 2929
Cdd:PRK09029   297 GREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEW-QNGELTILGRLDNLF 357

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2930 KIRGYRVETKEIESVIRCIKGVKDAAVVAHVTAS-GQTELsAYVVTKPGLSTNAVRSELQNKLPVFMHP 2997
Cdd:PRK09029   358 FSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfGQRPV-AVVESDSEAAVVNLAEWLQDKLARFQQP 425
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 2555-3019 1.20e-10

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: 67.07  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2555 GDKTLTYQELDEWSNGIARALRS-RGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDpeypkerkrYILSdsGTKL 2633
Cdd:cd05937      2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLS--GDPL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2634 LMTINeadlgvladfegeILTIESVEEDDKSPlpqmssahhlAYIIYTSGTTGRPKGVMVehkgiantlQWRRN------ 2707
Cdd:cd05937     71 IHCLK-------------LSGSRFVIVDPDDP----------AILIYTSGTTGLPKAAAI---------SWRRTlvtsnl 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2708 -AYAFNETDTiLQLFS----FSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAikhQLSRQRITHMIIVPVLYRALLDV- 2781
Cdd:cd05937    119 lSHDLNLKNG-DRTYTcmplYHGTAAFLGACNCLMSGGTLALSRKFSASQFWK---DVRDSGATIIQYVGELCRYLLSTp 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2782 VQPEDVK-TLRVVTLAGEAAD-----RELIARSlaicphtELANEYGPTENSVATT----------VMRHmekqaYVSIG 2845
Cdd:cd05937    195 PSPYDRDhKVRVAWGNGLRPDiwerfRERFNVP-------EIGEFYAATEGVFALTnhnvgdfgagAIGH-----HGLIR 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2846 QPIDGTQVLILNSNHQLQ--------------PIGVAGELCIAGT----GLARGYVNLPELTERAFTQNPFKPEARMYRT 2907
Cdd:cd05937    263 RWKFENQVVLVKMDPETDdpirdpktgfcvraPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2908 GDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQ--------TELSAYVVTKPGLS 2979
Cdd:cd05937    343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG-VKVPGHdgragcaaITLEESSAVPTEFT 421

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1678550997 2980 TNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:cd05937    422 KSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 605-948 1.49e-10

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: 65.79  E-value: 1.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  605 LYMIYTSGTTGKPKGVQFEHR-------NMANLLK----FEYTHSGIDFEADVLQFATPSFdvcyqeifsalLKGGTLHI 673
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQallaqalVLAVLQAidegTVFLNSGPLFHIGTLMFTLATF-----------HAGGTNVF 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  674 VPEAIKRDVPQLfafINKHQTNIVFLPTAFIKMIfseREL------------ANSFPDGVKHLIAAGEQLMISDLFQdvl 741
Cdd:cd17636     72 VRRVDAEEVLEL---IEAERCTHAFLLPPTIDQI---VELnadglydlsslrSSPAAPEWNDMATVDTSPWGRKPGG--- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  742 rkrgihlhnhYGPSEthvVSTYTIHPGDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKL 821
Cdd:cd17636    143 ----------YGQTE---VMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEV 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  822 TSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAIL-----IWqDQN 896
Cdd:cd17636    210 NARRTRGG-------WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIgvpdpRW-AQS 281

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997  897 -------------GEHELCAyYCsvqklntidlRSYMASelpeYMIPAKWIWVDSIPLTPNGKVD 948
Cdd:cd17636    282 vkaivvlkpgasvTEAELIE-HC----------RARIAS----YKKPKSVEFADALPRTAGGADD 331
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 3155-3435 1.64e-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: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3155 DALRKTLKAITCHHDALRMVFTQneqgkwDQYNRPLSHSddALYGLQMIDLSAPDGTDgnrpyeplIKRHVLDI-----Q 3229
Cdd:cd19535     40 DRLERAWNKLIARHPMLRAVFLD------DGTQQILPEV--PWYGITVHDLRGLSEEE--------AEAALEELrerlsH 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3230 QKMDLKNGPL--LQAGLFHTiDGDFLFLSAHHLVVDGISWRVLLEDLALGYRQAaggeDIKLPPKTSSFKAY-----AKK 3302
Cdd:cd19535    104 RVLDVERGPLfdIRLSLLPE-GRTRLHLSIDLLVADALSLQILLRELAALYEDP----GEPLPPLELSFRDYllaeqALR 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3303 LSDYAESQQlmkqlkYWREaeeyQTEALPF----------DQIDGTRAHegQRstiSFTLnDKETAALLKDANSAYNTdT 3372
Cdd:cd19535    179 ETAYERARA------YWQE----RLPTLPPapqlplakdpEEIKEPRFT--RR---EHRL-SAEQWQRLKERARQHGV-T 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 3373 QDMLLASV---ILALrhWTNQSAFKLSLEGHGREDVLKGIDvsRTIGWFTAIypLLIKLNADLPDS 3435
Cdd:cd19535    242 PSMVLLTAyaeVLAR--WSGQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSL--LLLEVDGSEGQS 301
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 1564-1990 1.80e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 66.21  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1564 ILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSaglhvPEFTGEIVylnqtNSGLAHrlsnpnvdvlPQSLayVIYT 1643
Cdd:PRK08308    52 LKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYGE-----SDFTKLEA-----VNYLAE----------EPSL--LQYS 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1644 SGSTGMPKGVEiehRSAVNFLNSLQSRYQLKHSDMIM---------HktSYSFdasIWELFWWPYAGASVYLLpqgGEKE 1714
Cdd:PRK08308   110 SGTTGEPKLIR---RSWTEIDREIEAYNEALNCEQDEtpivacpvtH--SYGL---ICGVLAALTRGSKPVII---TNKN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1715 PEVIAKAIEEQKITAMHFVPSMLHAflehikyrsvpiktnrLKRVFSGGEQL------GTHLVSRFYELLPNVS--ITNS 1786
Cdd:PRK08308   179 PKFALNILRNTPQHILYAVPLMLHI----------------LGRLLPGTFQFhavmtsGTPLPEAWFYKLRERTtyMMQQ 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATVEAAFFDCPPHEKLeripiGKPVHHVRLyllnqnqrmlpvgcigelyiaGAGVARgylNRPaltEERFLEDpf 1866
Cdd:PRK08308   243 YGCSEAGCVSICPDMKSHLDL-----GNPLPHVSV---------------------SAGSDE---NAP---EEIVVKM-- 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1867 ypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG 1941
Cdd:PRK08308   289 --GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvaGE-RVKAKVishEE 365

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1678550997 1942 LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAA 1990
Cdd:PRK08308   366 IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 489-875 2.77e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 66.08  E-value: 2.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEP--VAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVS 566
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  567 QAHLPsslednyIITHpEDIEsKVDGSNIKSVN--NADDLLYMIYTSGTTGKPKGVQFEHRNMANLLkfeythSGIDFEA 644
Cdd:cd05927     86 DAGVK-------VYSL-EEFE-KLGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSNV------AGVFKIL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  645 DVLQFATPSF-DVCY---QEIFSALLKGGTLHI-------------VPEAIKR-------DVPQLFAFI-NKHQTNIVFL 699
Cdd:cd05927    151 EILNKINPTDvYISYlplAHIFERVVEALFLYHgakigfysgdirlLLDDIKAlkptvfpGVPRVLNRIyDKIFNKVQAK 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  700 PTaFIKMIFS------ERELAN--SFPDG---------VKHLIAAGEQLMISD---LFQDVLRK-R---GIHLHNHYGPS 755
Cdd:cd05927    231 GP-LKRKLFNfalnykLAELRSgvVRASPfwdklvfnkIKQALGGNVRLMLTGsapLSPEVLEFlRvalGCPVLEGYGQT 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  756 ETHVVSTYTiHPGDPIPElpPIGKPIGC-----TDLYILN-HQKQLQPcgvPGELYISGASVARGYVNHDKLTSDKFSSD 829
Cdd:cd05927    310 ECTAGATLT-LPGDTSVG--HVGGPLPCaevklVDVPEMNyDAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEALDED 383

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997  830 PFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKI-RGYRIEPQEIE 875
Cdd:cd05927    384 GW------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIE 424
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1509-1983 5.41e-10

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: 65.14  E-value: 5.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1509 DQAAVIFE-----DGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERI 1583
Cdd:cd05915      9 GRKEVVSRlhtgeVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1584 SFLLEDSGTNILLLQSAGLHVPEFTGEI---VYLNQTNSGLAHRLS------NPNVDVL-------PQSLAYviyTSGST 1647
Cdd:cd05915     89 AYILNHAEDKVLLFDPNLLPLVEAIRGElktVQHFVVMDEKAPEGYlayeeaLGEEADPvrvperaACGMAY---TTGTT 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1648 GMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHK-TSYSFDASIWELFWWPYAGASVYLLPQGGEKEpEVIAKAIEEQK 1726
Cdd:cd05915    166 GLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLpVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDP-ASLVELFDGEG 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1727 ITAMHFVPSMLHAFL---EHIKyRSVPIKTnrlkRVFSGG----------EQLGTHLVSRFYellpnvSITNSYGPTEAT 1793
Cdd:cd05915    245 VTFTAGVPTVWLALAdylESTG-HRLKTLR----RLVVGGsaaprsliarFERMGVEVRQGY------GLTETSPVVVQN 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1794 VEAAFFDCPPHEKLERIPIGKPVHHVR--LYLLNQNQRMLPVG--CIGELYIAGAGVARGYLNRPALTEERFLEDPFYpg 1869
Cdd:cd05915    314 FVKSHLESLSEEEKLTLKAKTGLPIPLvrLRVADEEGRPVPKDgkALGEVQLKGPWITGGYYGNEEATRSALTPDGFF-- 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1870 ermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVEgLQRNEV 1947
Cdd:cd05915    392 ----RTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPkwQE-RPLAVVV-PRGEKP 465

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 1948 RAQ------LERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05915    466 TPEelnehlLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 973-1031 5.65e-10

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: 57.57  E-value: 5.65e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  973 AKLSQLFEDVLK--NGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVE 1031
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
2786-3016 6.25e-10

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 64.79  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2786 DVKTLRVVTLAGEAADRELIARSL-AICPH----TELANEYGPTENSVATTVMRHME--------------KQAYVSIGQ 2846
Cdd:PRK05851   270 DLGALRVALNGGEPVDCDGFERFAtAMAPFgfdaGAAAPSYGLAESTCAVTVPVPGIglrvdevttddgsgARRHAVLGN 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2847 PIDGTQVLILNSNHqlqPIGVA----GELCIAGTGLARGYVNlpelteraftQNPFKPEArMYRTGDAArWMADGTLEYL 2922
Cdd:PRK05851   350 PIPGMEVRISPGDG---AAGVAgreiGEIEIRGASMMSGYLG----------QAPIDPDD-WFPTGDLG-YLVDGGLVVC 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2923 GRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQtelsayvvTKPGLSTNA---------VRSELQNKLP- 2992
Cdd:PRK05851   415 GRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--------ARPGLVIAAefrgpdeagARSEVVQRVAs 486

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1678550997 2993 ---------VFMHPAfiekldSLPLSPNGKLDR 3016
Cdd:PRK05851   487 ecgvvpsdvVFVAPG------SLPRTSSGKLRR 513
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 2540-2982 8.66e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 64.58  E-value: 8.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2540 EQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPK 2619
Cdd:PRK08162    25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2620 ERKRYILSDSGTKLLMTINE-ADLGVLADFEGEILTIESVEEDDKsPLPQMSSAHHLAY--------------------- 2677
Cdd:PRK08162   105 ASIAFMLRHGEAKVLIVDTEfAEVAREALALLPGPKPLVIDVDDP-EYPGGRFIGALDYeaflasgdpdfawtlpadewd 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2678 ---IIYTSGTTGRPKGVMVEHKG-----IANTLQW---RRNAYAFnetdtILQLF-----SFSfdgfitsmFTPLLSGAK 2741
Cdd:PRK08162   184 aiaLNYTSGTTGNPKGVVYHHRGaylnaLSNILAWgmpKHPVYLW-----TLPMFhcngwCFP--------WTVAARAGT 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2742 AVLLHEEEAKDIL-AIKhqlsRQRITHMIIVPVLYRALLDVvqPEDVK---TLRVVTL-AGEAADRELIARSLAIcpHTE 2816
Cdd:PRK08162   251 NVCLRKVDPKLIFdLIR----EHGVTHYCGAPIVLSALINA--PAEWRagiDHPVHAMvAGAAPPAAVIAKMEEI--GFD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2817 LANEYGPTEN-SVATTVMRH-------MEKQAYVSIGQPI-----DGTQVLilnSNHQLQPI----GVAGELCIAGTGLA 2879
Cdd:PRK08162   323 LTHVYGLTETyGPATVCAWQpewdalpLDERAQLKARQGVryplqEGVTVL---DPDTMQPVpadgETIGEIMFRGNIVM 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2880 RGYVNLPELTERAFtqnpfkpEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAH 2959
Cdd:PRK08162   400 KGYLKNPKATEEAF-------AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472

                          490       500
                   ....*....|....*....|...
gi 1678550997 2960 VTASGQTELSAYVVTKPGLSTNA 2982
Cdd:PRK08162   473 PDPKWGEVPCAFVELKDGASATE 495
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1837-1983 1.52e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 62.76  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1837 GELYIAGAGVARGYLNRPalteerflEDPFYPGERMYKTGDVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSI 1916
Cdd:PRK07824   208 GRIALGGPTLAKGYRNPV--------DPDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATH 278

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1917 EGVREAAVTVRTDS--GEPELCAYVEGLQRNEV----RAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:PRK07824   279 PAVADCAVFGLPDDrlGQRVVAAVVGDGGPAPTlealRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 2534-3014 1.58e-09

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 63.57  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQqAAR----TPKASALVSGD-KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGG 2608
Cdd:PRK07008    11 LISSLIAH-AARhagdTEIVSRRVEGDiHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2609 CYVPIDPEYPKERKRYILSDSGTKLLMTineaDLGVLADFEGEILTIESVEE----DDKSPLPQMS----------SAHH 2674
Cdd:PRK07008    90 VCHTINPRLFPEQIAYIVNHAEDRYVLF----DLTFLPLVDALAPQCPNVKGwvamTDAAHLPAGStpllcyetlvGAQD 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2675 LAY------------IIYTSGTTGRPKGVMVEHKgiANTLqwrrNAYA--------FNETDTILQlfsfsfdgfITSMF- 2733
Cdd:PRK07008   166 GDYdwprfdenqassLCYTSGTTGNPKGALYSHR--STVL----HAYGaalpdamgLSARDAVLP---------VVPMFh 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2734 --------TPLLSGAKAVLlhEEEAKDILAIKHQLSRQRITHMIIVPVLYRALLDVVQPEDVK--TLRVVTLAGEAADRE 2803
Cdd:PRK07008   231 vnawglpySAPLTGAKLVL--PGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRfsTLRRTVIGGSACPPA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2804 LIaRSLAICPHTELANEYGPTENSVATTV---------------MRHMEKQayvsiGQPIDGTQVLILNSNHQLQPI-GV 2867
Cdd:PRK07008   309 MI-RTFEDEYGVEVIHAWGMTEMSPLGTLcklkwkhsqlpldeqRKLLEKQ-----GRVIYGVDMKIVGDDGRELPWdGK 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2868 A-GELCIAGTGLARGYvnlpelteraftqnpFKPEA-----RMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEI 2941
Cdd:PRK07008   383 AfGDLQVRGPWVIDRY---------------FRGDAsplvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDI 447

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997 2942 ESVIRCIKGVKDAAVVAhVTASGQTELSAYVVT-KPGlsTNAVRSEL----QNKLPVFMHPAFIEKLDSLPLSPNGKL 3014
Cdd:PRK07008   448 ENVAVAHPAVAEAACIA-CAHPKWDERPLLVVVkRPG--AEVTREELlafyEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 1633-1913 1.93e-09

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


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 63.60  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1633 LPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRY-QLKHSDMIMhktSYSFDASIWELfwwpyaGASVYLLPQG- 1710
Cdd:PLN02387   248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYL---AYLPLAHILEL------AAESVMAAVGa 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1711 --GEKEPEV-------IAKA----IEEQKITAMHFVPS------------------------------------------ 1735
Cdd:PLN02387   319 aiGYGSPLTltdtsnkIKKGtkgdASALKPTLMTAVPAildrvrdgvrkkvdakgglakklfdiaykrrlaaiegswfga 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1736 -----MLHAFLEHIKYRSVpiKTNRLKRVFSGGEQLGTHlVSRFYELLPNVSITNSYGPTEATVEAAF--FDCPpheKLE 1808
Cdd:PLN02387   399 wglekLLWDALVFKKIRAV--LGGRIRFMLSGGAPLSGD-TQRFINICLGAPIGQGYGLTETCAGATFseWDDT---SVG 472

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1809 RIpiGKPVHHVRLYLLNQNQ-------RMLPVGcigELYIAGAGVARGYLNRPALTEERFLEDPfyPGERMYKTGDVARW 1881
Cdd:PLN02387   473 RV--GPPLPCCYVKLVSWEEggylisdKPMPRG---EIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGMRWFYTGDIGQF 545

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1678550997 1882 LPDGNVEFLGRTDDQVKIR-GYRIEPGEIEAAL 1913
Cdd:PLN02387   546 HPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 605-949 1.99e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 63.61  E-value: 1.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  605 LYMIYTSGTTGKPKGVQfeHRNMANLLKFEYTHSGIDFEADVLQFATP------SFdvcYQEIFSALLKGGTL------H 672
Cdd:PTZ00237   257 LYILYTSGTTGNSKAVV--RSNGPHLVGLKYYWRSIIEKDIPTVVFSHssigwvSF---HGFLYGSLSLGNTFvmfeggI 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  673 IVPEAIKRDvpqLFAFINKHQTNIVF-LPTAF---IKM------IFSERELANsfpdgVKHLIAAGEQL--MISDLFQDV 740
Cdd:PTZ00237   332 IKNKHIEDD---LWNTIEKHKVTHTLtLPKTIrylIKTdpeatiIRSKYDLSN-----LKEIWCGGEVIeeSIPEYIENK 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  741 LRKRGIHLhnhYGPSETHVVSTYTIHP--------GDPIPELPPI-----GKPIGCTDLYILNHQKQLQPcgvpgelyis 807
Cdd:PTZ00237   404 LKIKSSRG---YGQTEIGITYLYCYGHinipynatGVPSIFIKPSilsedGKELNVNEIGEVAFKLPMPP---------- 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  808 gaSVARGYVNHDKLTSDKFSSDPFkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEA 887
Cdd:PTZ00237   471 --SFATTFYKNDEKFKQLFSKFPG-----YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLEC 543

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997  888 AILIWQDQNGEHELCAYYC-----SVQKLNTIDLRS----YMASELPEYMIPAKWIWVDSIPLTPNGKVDR 949
Cdd:PTZ00237   544 CSIGIYDPDCYNVPIGLLVlkqdqSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 588-870 2.70e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 63.20  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  588 SKVDGSNIKSVNNADDLLYMI-YTSGTTGKPKGVQFEHRNMANLLKFEYTHSgidfeadVLQFATPSFDVCYQEI----- 661
Cdd:PTZ00342   289 TKNKTTNYKIQNEDPDFITSIvYTSGTSGKPKGVMLSNKNLYNTVVPLCKHS-------IFKKYNPKTHLSYLPIshiye 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  662 ----FSALLKGGTLHIVPEAIK---RD-----------VPQLFafiNKHQTNIV-------FLPTAFIKMIFSERELAN- 715
Cdd:PTZ00342   362 rviaYLSFMLGGTINIWSKDINyfsKDiynskgnilagVPKVF---NRIYTNIMteinnlpPLKRFLVKKILSLRKSNNn 438

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  716 ----SFPDGVKHL--------------IAAGEQLMISDLFQDVLRKRGIHLHNHYGPSEThvvsTYTI---HPGDPIPEl 774
Cdd:PTZ00342   439 ggfsKFLEGITHIsskikdkvnpnlevILNGGGKLSPKIAEELSVLLNVNYYQGYGLTET----TGPIfvqHADDNNTE- 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  775 pPIGKPIGCTDLYILNHQKQLQPCGVP--GELYISGASVARGYVNHDKLTSDKFSSDPFkpdvimYRTGDLARRLEDGNI 852
Cdd:PTZ00342   514 -SIGGPISPNTKYKVRTWETYKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSL 586

                          330
                   ....*....|....*....
gi 1678550997  853 EYIGRADNQVKI-RGYRIE 870
Cdd:PTZ00342   587 TFLDRSKGLVKLsQGEYIE 605
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 488-625 3.17e-09

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: 62.69  E-value: 3.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  488 SLTYRELNKAANRLARHLRMKGVVRQ-EPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYpadRIRYILHDCGCSH--- 563
Cdd:cd05938      5 TYTYRDVDRRSNQAARALLAHAGLRPgDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNI---RSKSLLHCFRCCGakv 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  564 -VVS-------QAHLPSSLEDNYII------THPEDIES---KVDGSNIKSV--------NNADDLLYmIYTSGTTGKPK 618
Cdd:cd05938     82 lVVApelqeavEEVLPALRADGVSVwylshtSNTEGVISlldKVDAASDEPVpaslrahvTIKSPALY-IYTSGTTGLPK 160


                   ....*..
gi 1678550997  619 GVQFEHR 625
Cdd:cd05938    161 AARISHL 167
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 601-889 3.30e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 62.78  E-value: 3.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  601 ADDLLYMIYTSGTTGKPKGVQFEHRNMAnllkfeythsgidFEADVL--QFATPSFDVCY--QEIFS----------ALL 666
Cdd:PRK07867   151 PDDLFMLIFTSGTSGDPKAVRCTHRKVA-------------SAGVMLaqRFGLGPDDVCYvsMPLFHsnavmagwavALA 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  667 KGGTLhivpeAIKR--DVPQLFAFINKHQT---NIVFLPTAFIkMIFSERelansfPDGVKH--LIAAGEQLMISDLfQD 739
Cdd:PRK07867   218 AGASI-----ALRRkfSASGFLPDVRRYGAtyaNYVGKPLSYV-LATPER------PDDADNplRIVYGNEGAPGDI-AR 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  740 VLRKRGIHLHNHYGPSETHVVSTYTihpgdpiPELPP--IGKPIGctDLYILNHQKqLQPCGVP--------------GE 803
Cdd:PRK07867   285 FARRFGCVVVDGFGSTEGGVAITRT-------PDTPPgaLGPLPP--GVAIVDPDT-GTECPPAedadgrllnadeaiGE 354

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  804 LY-ISGASVARGYVNHDKLTSDKFSSDpfkpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHP 882
Cdd:PRK07867   355 LVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427


                   ....*..
gi 1678550997  883 DISEAAI 889
Cdd:PRK07867   428 DATEVAV 434
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3152-3393 3.78e-09

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 63.14  E-value: 3.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3152 VQEDALRKTLKAITCHHDALRMVFTQNEQGKWDQYNRPLshsddALYGLQMIDLS-APDGTDGNRPyepLIKRhvlDIQQ 3230
Cdd:PRK10252    42 LDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPAL-----TFPLPEIIDLRtQPDPHAAAQA---LMQA---DLQQ 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3231 KMDLKNG-PLLQAGLFHTIDGDFL-FLSAHHLVVDGISWRVLLEDLALGYRQAAGGEdiklPPKTSSFKAYAKKLSDYA- 3307
Cdd:PRK10252   111 DLRVDSGkPLVFHQLIQLGDNRWYwYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGE----PTPASPFTPFADVVEEYQr 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3308 --ESQQLMKQLKYWREaeeyQTEALP-FDQIDGTRAhEGQRSTISFtLNDK---ETAALLKDANSAYNTDTQDMLLASVI 3381
Cdd:PRK10252   187 yrASEAWQRDAAFWAE----QRRQLPpPASLSPAPL-PGRSASADI-LRLKlefTDGAFRQLAAQASGVQRPDLALALVA 260

                          250
                   ....*....|..
gi 1678550997 3382 LALRHWTNQSAF 3393
Cdd:PRK10252   261 LWLGRLCGRMDY 272
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 2557-2956 3.83e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 62.65  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVgIMMHRSFSMIASILGVWKAGGCYVPIDPEYP---KERKRYILSDSGTKL 2633
Cdd:PRK05850    34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2634 LMTINeADLGVLADFEGE--------ILTIESVEEDdkSPLPQMSSAHHL---AYIIYTSGTTGRPKGVMVEHKG-IANT 2701
Cdd:PRK05850   113 VLTTS-AVVDDVTEYVAPqpgqsappVIEVDLLDLD--SPRGSDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNvIANF 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2702 LQWRRNAYAFNET-----DTILQLFSFSFD-GFITSMFTPLLSGAKAVLLH-----EEEAKDI--LAIKHQ--------- 2759
Cdd:PRK05850   190 EQLMSDYFGDTGGvpppdTTVVSWLPFYHDmGLVLGVCAPILGGCPAVLTSpvaflQRPARWMqlLASNPHafsaapnfa 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2760 --LSRQRITH--MiivpvlyrALLDV------------VQPEDVK-------------------------TLRVVT-LAG 2797
Cdd:PRK05850   270 feLAVRKTSDddM--------AGLDLggvlgiisgserVHPATLKrfadrfapfnlretairpsyglaeaTVYVATrEPG 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2798 EAAD-RELIARSLAicphtelANEYGPTENSVATtvmrhmekqAYVSIGQPiDGTQVLILNSNHQLQ-PIGVAGELCIAG 2875
Cdd:PRK05850   342 QPPEsVRFDYEKLS-------AGHAKRCETGGGT---------PLVSYGSP-RSPTVRIVDPDTCIEcPAGTVGEIWVHG 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2876 TGLARGYVNLPELTERAF-----TQNPFKPEARMYRTGDAArWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKG 2950
Cdd:PRK05850   405 DNVAAGYWQKPEETERTFgatlvDPSPGTPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITG 483


                   ....*.
gi 1678550997 2951 VKDAAV 2956
Cdd:PRK05850   484 GRVAAI 489
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 464-630 3.96e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 62.65  E-value: 3.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  464 TIHAMFEKQAEKTPD--AHAVID-------QACSLTYRELNKAANRLARHLRMKGVVRqEPVAIMMERSAAFITGVLGIL 534
Cdd:PRK05850     2 SVPSLLRERASLQPDdaAFTFIDyeqdpagVAETLTWSQLYRRTLNVAEELRRHGSTG-DRAVILAPQGLEYIVAFLGAL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  535 KAGGAIVPVD-PHYPA--DRIRYILHDCGCSHVVSQahlpSSLEDN---YIITHPEDIESKV-----------DGSNIKS 597
Cdd:PRK05850    81 QAGLIAVPLSvPQGGAhdERVSAVLRDTSPSVVLTT----SAVVDDvteYVAPQPGQSAPPVievdlldldspRGSDARP 156

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1678550997  598 VNnADDLLYMIYTSGTTGKPKGVQFEHRN-MANL 630
Cdd:PRK05850   157 RD-LPSTAYLQYTSGSTRTPAGVMVSHRNvIANF 189
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 3033-3106 4.00e-09

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 56.10  E-value: 4.00e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  3033 LPPSSKMEQILADI---WKEVLG---AEKIGTADSFFELGGDSIKALQVSARLHR-IGKQMAVKDLFSHPTIQELAAYIR 3105
Cdd:smart00823    4 LPPAERRRLLLDLVreqVAAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAaTGLRLPATLVFDHPTPAALAEHLA 83


                    .
gi 1678550997  3106 D 3106
Cdd:smart00823   84 A 84
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1836-1980 4.07e-09

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 62.48  E-value: 4.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1836 IGELYIAGAGVARGYLNrpalteerflEDPFYPGErMYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRS 1915
Cdd:PRK05851   372 IGEIEIRGASMMSGYLG----------QAPIDPDD-WFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQ 439

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1916 IEGVREAAV-TVRTDSG--EPELCAYVE--GLQRNEVRAQL-ERLLP--GyMVPAYMIEME--QWPVTPSGKLDR 1980
Cdd:PRK05851   440 VRGVREGAVvAVGTGEGsaRPGLVIAAEfrGPDEAGARSEVvQRVASecG-VVPSDVVFVApgSLPRTSSGKLRR 513
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 489-930 4.35e-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: 62.06  E-value: 4.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQa 568
Cdd:cd05939      4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 HLPSSLEDNYiiTHPEDIESKvdgsniksvnNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDfEADVLQ 648
Cdd:cd05939     83 LLDPLLTQSS--TEPPSQDDV----------NFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR-PEDVVY 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  649 FATPSFD-----VCyqeIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVflptAFIKMIFSERELANSFPDGVKH 723
Cdd:cd05939    150 DCLPLYHsaggiMG---VGQALLHGSTVVIRK---KFSASNFWDDCVKYNCTIV----QYIGEICRYLLAQPPSEEEQKH 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  724 LI--AAGEQLMISdLFQDVLRKRGI-HLHNHYGPSE---------THV-----VSTY--TIHPGDPIPELPPIGKPIGCT 784
Cdd:cd05939    220 NVrlAVGNGLRPQ-IWEQFVRRFGIpQIGEFYGATEgnsslvnidNHVgacgfNSRIlpSVYPIRLIKVDEDTGELIRDS 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  785 DlyilnhqKQLQPCGvPGElyiSGASVAR-----------GYVNhDKLTSDKFSSDPFKPDVIMYRTGDLARRLEDGNIE 853
Cdd:cd05939    299 D-------GLCIPCQ-PGE---PGLLVGKiiqndplrrfdGYVN-EGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLY 366

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  854 YIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQ--DQNGEHELCAYYCSVQKLNTIDLRSYMASELPEYMIP 930
Cdd:cd05939    367 FKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvpGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARP 445
PRK09192 PRK09192
fatty acyl-AMP ligase;
489-898 6.62e-09

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 61.94  E-value: 6.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGgaIVPVDPHYPA---------DRIRYILHDC 559
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAG--LVPVPLPLPMgfggresyiAQLRGMLASA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  560 GCSHVVSQAHL-------PSSLEDNYIIThPEDIESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRN-MANLL 631
Cdd:PRK09192   128 QPAAIITPDELlpwvneaTHGNPLLHVLS-HAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAlMANLR 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  632 KfeYTHSGIDFEA------------------------------DVL---QFA-------------------TPSF--DVC 657
Cdd:PRK09192   207 A--ISHDGLKVRPgdrcvswlpfyhdmglvgflltpvatqlsvDYLptrDFArrplqwldlisrnrgtisySPPFgyELC 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  658 YQEIFSALLKGGTLH------IVPEAIKRDVPQLFA--FINKHqtnivFLPTAFIKMI-FSERELANSFPDgvkhlIAAG 728
Cdd:PRK09192   285 ARRVNSKDLAELDLScwrvagIGADMIRPDVLHQFAeaFAPAG-----FDDKAFMPSYgLAEATLAVSFSP-----LGSG 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  729 EQLMISDLfqDVLRKRGIHLHNhygPSETHVVSTYTIhpgdpipelppIGKPIGCTDLYILNHQKQLQPCGVPGELYISG 808
Cdd:PRK09192   355 IVVEEVDR--DRLEYQGKAVAP---GAETRRVRTFVN-----------CGKALPGHEIEIRNEAGMPLPERVVGHICVRG 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  809 ASVARGYVNhDKLTSDKFSSDPFkpdvimYRTGDLARrLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDI--SE 886
Cdd:PRK09192   419 PSLMSGYFR-DEESQDVLAADGW------LDTGDLGY-LLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGD 490

                          490
                   ....*....|..
gi 1678550997  887 AAILIWQDQNGE 898
Cdd:PRK09192   491 AAAFSIAQENGE 502
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 1859-1939 7.19e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 61.70  E-value: 7.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1859 ERFLEDPF--YPGerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpE 1934
Cdd:PRK00174   471 ERFVKTYFstFKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDikGQ-G 547


                   ....*
gi 1678550997 1935 LCAYV 1939
Cdd:PRK00174   548 IYAFV 552
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 2557-2972 9.04e-09

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: 61.28  E-value: 9.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:cd17641     10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 INEADLGVLADFEGEILTIESVEEDDKSPL-----PQMSS---------AHH------------------LAYIIYTSGT 2684
Cdd:cd17641     90 EDEEQVDKLLEIADRIPSVRYVIYCDPRGMrkyddPRLISfedvvalgrALDrrdpglyerevaagkgedVAVLCTTSGT 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2685 TGRPKGVMVEHKGIANTLQWRRNAYAFNETDTILQLFSFSFDG-FITSMFTPLLSGAKAVLLHEEEA--KDILAI----- 2756
Cdd:cd17641    170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGeQMYSVGQALVCGFIVNFPEEPETmmEDLREIgptfv 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2757 -------KHQLSRQRITHMIIVPV---LYRALLDVVQP--EDVKTLRVVTLAGEAAD---RELIARSL------------ 2809
Cdd:cd17641    250 llpprvwEGIAADVRARMMDATPFkrfMFELGMKLGLRalDRGKRGRPVSLWLRLASwlaDALLFRPLrdrlgfsrlrsa 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2810 -----AICPHT---------ELANEYGPTENSVATTVmrHMEKQA-YVSIGQPIDGTQVLILNsnhqlqpigvAGELCIA 2874
Cdd:cd17641    330 atggaALGPDTfrffhaigvPLKQLYGQTELAGAYTV--HRDGDVdPDTVGVPFPGTEVRIDE----------VGEILVR 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2875 GTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKI-RGYRVETKEIESVIRCIKGVKD 2953
Cdd:cd17641    398 SPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAE 471

                          490
                   ....*....|....*....
gi 1678550997 2954 AAVVAHvtasGQTELSAYV 2972
Cdd:cd17641    472 AVVLGA----GRPYLTAFI 486
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1603-1979 1.08e-08

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 61.26  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1603 HVPEFTGEI--VYLNQTNSG---------LAHRLSnPNVDVLPQS---LAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQ 1668
Cdd:PRK08043   320 HLPEQLTQVrwVYLEDLKDDvttadklwiFAHLLM-PRLAQVKQQpedAALILFTSGSEGHPKGVVHSHKSLLANVEQIK 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1669 SRYQLKHSDMIMHKTS--YSFDASIwELFWWPYAGASVYLLPQggekeP---EVIAKAIEEQKITAMhFVPSmlhAFLEH 1743
Cdd:PRK08043   399 TIADFTPNDRFMSALPlfHSFGLTV-GLFTPLLTGAEVFLYPS-----PlhyRIVPELVYDRNCTVL-FGTS---TFLGN 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1744 IKYRSVPIKTNRLKRVFSGGEQLGTHlVSRFYELLPNVSITNSYGPTEatveaaffdCPPHEKLErIPIGKPVHHVRLYL 1823
Cdd:PRK08043   469 YARFANPYDFARLRYVVAGAEKLQES-TKQLWQDKFGLRILEGYGVTE---------CAPVVSIN-VPMAAKPGTVGRIL 537

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1824 LNQNQRMLPVGCI---GELYIAGAGVARGYL--NRPALTEERFLEDPfyPGER---MYKTGDVARWLPDGNVEFLGRTDD 1895
Cdd:PRK08043   538 PGMDARLLSVPGIeqgGRLQLKGPNIMNGYLrvEKPGVLEVPTAENA--RGEMergWYDTGDIVRFDEQGFVQIQGRAKR 615

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1896 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPElcAYV-----EGLQRNEVRAQLERL-LPGYMVPAYMIEMEQ 1969
Cdd:PRK08043   616 FAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE--ALVlfttdSELTREKLQQYAREHgVPELAVPRDIRYLKQ 693

                          410
                   ....*....|
gi 1678550997 1970 WPVTPSGKLD 1979
Cdd:PRK08043   694 LPLLGSGKPD 703
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 60-314 1.77e-08

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


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 60.19  E-value: 1.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   60 RHDIFRTIFISQNVSSPQQVVLRERNVIVLEedITHLNEAEQSQFIEQwkekDRDRGFHLQKDVLMRIALIQTGESQYSC 139
Cdd:cd19546     54 RHEILRTTFPGDGGDVHQRILDADAARPELP--VVPATEEELPALLAD----RAAHLFDLTRETPWRCTLFALSDTEHVL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  140 IWTFHHIMMDGWCLSIVLKEFLHIYASYVNA-----SPITLEpvqpYGKYIKW---LM--EQDKE----QAVSYWDHYLS 205
Cdd:cd19546    128 LLVVHRIAADDESLDVLVRDLAAAYGARREGraperAPLPLQ----FADYALWereLLagEDDRDsligDQIAYWRDALA 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  206 GHEQQTVLPKQKKTKGKS--RQEHVTFSFSKEESSRLSELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISgRPA 283
Cdd:cd19546    204 GAPDELELPTDRPRPVLPsrRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDD 282

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1678550997  284 EIEGIEHMVGLFINTMPVRVQGAKTP-FLQLI 314
Cdd:cd19546    283 EEGDLEGMVGPFARPLALRTDLSGDPtFRELL 314
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 1813-1984 1.91e-08

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 60.01  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1813 GKPVHHVRLYLLNQNqrmlpvgcIGELYIAGAGVARGYLnrPALTEERfledpfypgeRMYKTGDVARWLPDGNVEFLGR 1892
Cdd:PRK07445   286 GQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQILDSQ----------GIFETDDLGYLDAQGYLHILGR 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1893 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEM 1967
Cdd:PRK07445   346 NSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPhwGEVVTAIYVpkdPSISLEELKTAIKDQLSPFKQPKHWIPV 425

                          170
                   ....*....|....*..
gi 1678550997 1968 EQWPVTPSGKLDRNALP 1984
Cdd:PRK07445   426 PQLPRNPQGKINRQQLQ 442
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 12-324 1.98e-08

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: 59.96  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   12 PLSYMQEgMLFHslLQKDSQAYVEQA-SFTIEGKVNPQFFQNSINALVERHDIFRTIFiSQNVSSPQQVVLR-ERNVIVL 89
Cdd:cd19534      3 PLTPIQR-WFFE--QNLAGRHHFNQSvLLRVPQGLDPDALRQALRALVEHHDALRMRF-RREDGGWQQRIRGdVEELFRL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997   90 E-EDITHLNEAEQsqfIEQwKEKDRDRGFHLQKDVLMRIALIQTGESQYSCIWTFHHIMMDG--WclSIVLKEFLHIYAS 166
Cdd:cd19534     79 EvVDLSSLAQAAA---IEA-LAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDLEAAYEQ 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  167 YVNASPITLEPVQPYGKYIKWLMEQDKEQAVS----YWDHYLSGHEQQtvLPK-QKKTKGKSRQehVTFSFSKEESSRL- 240
Cdd:cd19534    153 ALAGEPIPLPSKTSFQTWAELLAEYAQSPALLeelaYWRELPAADYWG--LPKdPEQTYGDART--VSFTLDEEETEALl 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  241 SELAAReevtLST----IFHTIWGILLQKYNNNDDavfgSVIS----GRPAEIEGIEHM--VGLFiNTM-PVRVQ-GAKT 308
Cdd:cd19534    229 QEANAA----YRTeindLLLAALALAFQDWTGRAP----PAIFleghGREEIDPGLDLSrtVGWF-TSMyPVVLDlEASE 299

                          330
                   ....*....|....*.
gi 1678550997  309 PFLQLIKDMqKDRLAA 324
Cdd:cd19534    300 DLGDTLKRV-KEQLRR 314
prpE PRK10524
propionyl-CoA synthetase; Provisional
 1497-1985 2.59e-08

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 59.96  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1497 HYALEQQAEKTPDQAAVIF------EDGVMTYKELNEQANRIAWELIGRGVKPETTVAI----IGKRSPEML----LG-- 1560
Cdd:PRK10524    56 HNAVDRHLAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIympmIAEAAFAMLacarIGai 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1561 ---IYGILKAGGAYLPIDPDYPEERISfllEDSGT---NIL----LLQSAgLHVPEFTGEIVYLnqTNSGLAHRLSNPNV 1630
Cdd:PRK10524   136 hsvVFGGFASHSLAARIDDAKPVLIVS---ADAGSrggKVVpykpLLDEA-IALAQHKPRHVLL--VDRGLAPMARVAGR 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1631 DVLPQSL-------------------AYVIYTSGSTGMPKGVEiehRS----AVNFLNSLQsryqlkhsdmimhktsYSF 1687
Cdd:PRK10524   210 DVDYATLraqhlgarvpvewlesnepSYILYTSGTTGKPKGVQ---RDtggyAVALATSMD----------------TIF 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1688 DASIWELFW------W----PY-------AGAS--VY----LLPQGGekepeVIAKAIEEQKITAMHFVPSMLH------ 1738
Cdd:PRK10524   271 GGKAGETFFcasdigWvvghSYivyapllAGMAtiMYeglpTRPDAG-----IWWRIVEKYKVNRMFSAPTAIRvlkkqd 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1739 -AFLEhiKYrsvpiKTNRLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEaTVEAAFFDCPpheKLERIPI----- 1812
Cdd:PRK10524   346 pALLR--KH-----DLSSLRALFLAGEPLDEPTASWISEAL-GVPVIDNYWQTE-TGWPILAIAR---GVEDRPTrlgsp 413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1813 GKPVHHVRLYLLNQ--------NQR-------MLPVGCIGELYiagagvarGylnrpalTEERFLEDPFYP-GERMYKTG 1876
Cdd:PRK10524   414 GVPMYGYNVKLLNEvtgepcgpNEKgvlviegPLPPGCMQTVW--------G-------DDDRFVKTYWSLfGRQVYSTF 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1877 DVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV----------------TVRTDSG--EPELCAY 1938
Cdd:PRK10524   479 DWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVvgvkdalkgqvavafvVPKDSDSlaDREARLA 558

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1678550997 1939 VEGlqrnEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:PRK10524   559 LEK----EIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQA 601
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 2534-3019 3.13e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 59.66  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2534 TISQLFEQQAarTPKASALVSGDKTLTYQELDEWSNGIARALRSRGvKPDTP--VGIMMHRSFSMIASILGVWKAGGCYV 2611
Cdd:PRK13388     4 TIAQLLRDRA--GDDTIAVRYGDRTWTWREVLAEAAARAAALIALA-DPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2612 PIDPeypKERKRYILSD---SGTKLLMTiNEADLGVLA--DFEG-EILTIESVEEDDKSPLPQMSSAH------HLAYII 2679
Cdd:PRK13388    81 GLNT---TRRGAALAADirrADCQLLVT-DAEHRPLLDglDLPGvRVLDVDTPAYAELVAAAGALTPHrevdamDPFMLI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2680 YTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDT---ILQLFSfsfDGFITSMFTPLL-SGAKAVLLHEEEAKDILA 2755
Cdd:PRK13388   157 FTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVcyvSMPLFH---SNAVMAGWAPAVaSGAAVALPAKFSASGFLD 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2756 ikhQLSRQRITHMIIV--PVLYrALLDVVQPEDVKTLRVVTLAGEAA--DRELIARSLAIcphtELANEYGPTENSVATT 2831
Cdd:PRK13388   234 ---DVRRYGATYFNYVgkPLAY-ILATPERPDDADNPLRVAFGNEASprDIAEFSRRFGC----QVEDGYGSSEGAVIVV 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2832 VMRHMEKQayvSIGQPIDGtqVLILNSnHQLQPIGVA---------------GELC-IAGTGLARGYVNLPELT-ERAft 2894
Cdd:PRK13388   306 REPGTPPG---SIGRGAPG--VAIYNP-ETLTECAVArfdahgallnadeaiGELVnTAGAGFFEGYYNNPEATaERM-- 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2895 qnpfkpeaR--MYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV-------------VAH 2959
Cdd:PRK13388   378 --------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyavpdervgdqvmAAL 449

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2960 VTASGQT----ELSAYVVTKPGLSTNAVrselqnklpvfmhPAFIEKLDSLPLSPNGKLDRGAL 3019
Cdd:PRK13388   450 VLRDGATfdpdAFAAFLAAQPDLGTKAW-------------PRYVRIAADLPSTATNKVLKREL 500
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 1634-1919 3.20e-08

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 59.65  E-value: 3.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQSLAYVIYTSGSTGMPKGVEIEHRSAV-------NFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELF--------WWp 1698
Cdd:PLN02614   222 KSDICTIMYTSGTTGDPKGVMISNESIVtliagviRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFiqhgaaigFW- 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1699 yAGASVYLLPQGGEKEPEV---IAKAIE------EQKITAMHFVPSMLhaFLEHIKYRSVPIKT---------------- 1753
Cdd:PLN02614   301 -RGDVKLLIEDLGELKPTIfcaVPRVLDrvysglQKKLSDGGFLKKFV--FDSAFSYKFGNMKKgqshveasplcdklvf 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1754 NRLKR--------VFSGGEQLGTHLVSrFYELLPNVSITNSYGPTEATveAAFFDCPPHEKLERIPIGKPVHHVRLYLLN 1825
Cdd:PLN02614   378 NKVKQglggnvriILSGAAPLASHVES-FLRVVACCHVLQGYGLTESC--AGTFVSLPDELDMLGTVGPPVPNVDIRLES 454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1826 ---QNQRMLPVGCIGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRtddqvKIRGY 1902
Cdd:PLN02614   455 vpeMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLH-------TGDVGEWQPNGSMKIIDR-----KKNIF 522

                          330
                   ....*....|....*..
gi 1678550997 1903 RIEPGEIeAALRSIEGV 1919
Cdd:PLN02614   523 KLSQGEY-VAVENIENI 538
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 490-875 3.33e-08

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 59.62  E-value: 3.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIV----P---VD-PHYPAD---RIRYIlhd 558
Cdd:PRK07768    31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTmlhqPtprTDlAVWAEDtlrVIGMI--- 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  559 cGCSHVVSQA---HLPSSLEDNYIITHPedIESKVDGSNIKSVN-NADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFE 634
Cdd:PRK07768   108 -GAKAVVVGEpflAAAPVLEEKGIRVLT--VADLLAADPIDPVEtGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAM 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  635 YTHSGIDFEADVLQFATPSFD-------VCYQEIFSAllkgGTLHIVPEAIKRDvPQLFA-FINKHQTNIVFLPtAFIKM 706
Cdd:PRK07768   185 FVAAEFDVETDVMVSWLPLFHdmgmvgfLTVPMYFGA----ELVKVTPMDFLRD-PLLWAeLISKYRGTMTAAP-NFAYA 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  707 IFSEReLANSFPDG------VKHLIAAGEQLMISDL--FQDVLRKRGIH---LHNHYGPSETHVVSTY----------TI 765
Cdd:PRK07768   259 LLARR-LRRQAKPGafdlssLRFALNGAEPIDPADVedLLDAGARFGLRpeaILPAYGMAEATLAVSFspcgaglvvdEV 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  766 HP-------------GDPIPELPPIGKPIGCTDLYILNHQKQLQPCGVPGELYISGASVARGYvnhdkLTSDKF--SSDP 830
Cdd:PRK07768   338 DAdllaalrravpatKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFipAQDA 412

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1678550997  831 FKpdviMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIE 875
Cdd:PRK07768   413 DG----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
prpE PRK10524
propionyl-CoA synthetase; Provisional
 606-895 4.65e-08

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 59.19  E-value: 4.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  606 YMIYTSGTTGKPKGVQfehRN-------MANLLKFEYthsgiDFEADVLQFATPSFD--VCYQEIFSALLKGGTLHIVPE 676
Cdd:PRK10524   237 YILYTSGTTGKPKGVQ---RDtggyavaLATSMDTIF-----GGKAGETFFCASDIGwvVGHSYIVYAPLLAGMATIMYE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  677 A--IKRDVPQLFAFINKHQTNIVF-LPTAfIKMI--FSERELANSFPDGVKHLIAAGEQL--MISDLFQDVLRKRGIhlh 749
Cdd:PRK10524   309 GlpTRPDAGIWWRIVEKYKVNRMFsAPTA-IRVLkkQDPALLRKHDLSSLRALFLAGEPLdePTASWISEALGVPVI--- 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  750 NHYGPSETHVvSTYTIHPG-DPIP-ELPPIGKPIGCTDLYILNHQKQlQPCGvPGElyiSGASVARG----------YVN 817
Cdd:PRK10524   385 DNYWQTETGW-PILAIARGvEDRPtRLGSPGVPMYGYNVKLLNEVTG-EPCG-PNE---KGVLVIEGplppgcmqtvWGD 458

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678550997  818 HDKLTSDKFSSdpFKPDVimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQ 895
Cdd:PRK10524   459 DDRFVKTYWSL--FGRQV--YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDA 532
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 490-845 4.79e-08

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: 58.98  E-value: 4.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPA-----DRIRYI--------- 555
Cdd:cd05921     27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLfellkpglv 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 --------------LHDCGCSHVVSQAHLpsslEDNYIITHPEDIESKVDGSNIKSVNNA--DDLLYMIYTSGTTGKPKG 619
Cdd:cd05921    107 faqdaapfaralaaIFPLGTPLVVSRNAV----AGRGAISFAELAATPPTAAVDAAFAAVgpDTVAKFLFTSGSTGLPKA 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  620 VQFEHRNM-ANLLKFEYTHSGIDFEADVLQFATPsfdvcYQEIFSA-------LLKGGTLHIvpeAIKRDVPQLFAFINK 691
Cdd:cd05921    183 VINTQRMLcANQAMLEQTYPFFGEEPPVLVDWLP-----WNHTFGGnhnfnlvLYNGGTLYI---DDGKPMPGGFEETLR 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  692 HQTNIVflPTAFI------KMIFSERE----LANSFPDGVKHLIAAGEQLM--ISDLFQDVLRK---RGIHLHNHYGPSE 756
Cdd:cd05921    255 NLREIS--PTVYFnvpagwEMLVAALEkdeaLRRRFFKRLKLMFYAGAGLSqdVWDRLQALAVAtvgERIPMMAGLGATE 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  757 THVVSTYTIHPGDPIPElppIGKPIGCTDLyilnhqkQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFkpdvi 836
Cdd:cd05921    333 TAPTATFTHWPTERSGL---IGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF----- 397


                   ....*....
gi 1678550997  837 mYRTGDLAR 845
Cdd:cd05921    398 -YCLGDAAK 405
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 2940-3013 5.15e-08

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: 52.55  E-value: 5.15e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 2940 EIESVIRCIKGVKDAAVVA-HVTASGQTeLSAYVVTKPG--LSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGK 3013
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGvPDELKGEA-PVAFVVLKPGveLLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 473-952 5.83e-08

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 58.67  E-value: 5.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  473 AEKTPDAHAVIDQACSLTYRELNKAANRLARHLRMkgvVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRI 552
Cdd:PRK06334    30 SEMTTATVCWDEQLGKLSYNQVRKAVIALATKVSK---YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  553 RYILHDCGCSHVVSQAHLPSSLEDnyiiTHPEDIE---------------SKVDGSNIK----------------SVNNA 601
Cdd:PRK06334   107 TACANLVGVTHVLTSKQLMQHLAQ----THGEDAEypfsliymeevrkelSFWEKCRIGiymsipfewlmrwfgvSDKDP 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  602 DDLLYMIYTSGTTGKPKGVQFEHrnmANLLkfEYTHSGIDF----EADV-LQFATP----SFDVCyqEIFSaLLKGgtLH 672
Cdd:PRK06334   183 EDVAVILFTSGTEKLPKGVPLTH---ANLL--ANQRACLKFfspkEDDVmMSFLPPfhayGFNSC--TLFP-LLSG--VP 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  673 IVPEAIKRDVPQLFAFINKhqTNIVFLPTA--FIKMIFSERELANSFPDGVKHLIAAGeqlmisDLFQDVLRKRG----- 745
Cdd:PRK06334   253 VVFAYNPLYPKKIVEMIDE--AKVTFLGSTpvFFDYILKTAKKQESCLPSLRFVVIGG------DAFKDSLYQEAlktfp 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  746 -IHLHNHYGPSETHVVSTYTIHPGDPIPELppIGKPIGCTDLYILNHQKQLQ-PCGVPGELYISGASVARGYVNHD---- 819
Cdd:PRK06334   325 hIQLRQGYGTTECSPVITINTVNSPKHESC--VGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLGEDfgqg 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  820 --KLTSDKFssdpfkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNH---PDISEAAILIWQD 894
Cdd:PRK06334   403 fvELGGETW-----------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLVVCG 471

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678550997  895 QNGEHE-LCAYY---CSVQKLNTIdLRSYMASELpeyMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PRK06334   472 LPGEKVrLCLFTtfpTSISEVNDI-LKNSKTSSI---LKISYHHQVESIPMLGTGKPDYCSL 529
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 2532-2991 5.88e-08

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: 58.62  E-value: 5.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2532 VQTISQLFEQQAARTPKASALVSGDKT--LTYQELDEWSNGIARALRSRG------------VKPDTPVGIMMHRSFSMI 2597
Cdd:cd17632     28 IATVMTGYADRPALGQRATELVTDPATgrTTLRLLPRFETITYAELWERVgavaaahdpeqpVRPGDFVAVLGFTSPDYA 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2598 ASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEA-DLGVLADFEG-------------------------- 2650
Cdd:cd17632    108 TVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHlDLAVEAVLEGgtpprlvvfdhrpevdahraalesar 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2651 ----------EILTIESVEEDDKSPLPQM---SSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTLQWRRNAYAFNETDTI 2717
Cdd:cd17632    188 erlaavgipvTTLTLIAVRGRDLPPAPLFrpePDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASI 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2718 -LQLFSFSFDGFITSMFTPLLSGAKAVLLheeEAKDILAIKHQLSRQRITHMIIVPVL-------YRALLD--VVQPEDV 2787
Cdd:cd17632    268 tLNFMPMSHIAGRISLYGTLARGGTAYFA---AASDMSTLFDDLALVRPTELFLVPRVcdmlfqrYQAELDrrSVAGADA 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2788 KT--------LRVVTLAGEAADR---------ELIArSLAICPHTELANEYGPTEnsvATTVMRhmekQAYVSIGQPIDg 2850
Cdd:cd17632    345 ETlaervkaeLRERVLGGRLLAAvcgsaplsaEMKA-FMESLLDLDLHDGYGSTE---AGAVIL----DGVIVRPPVLD- 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2851 tqvlilnsnHQLqpIGVA-------------GELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADG 2917
Cdd:cd17632    416 ---------YKL--VDVPelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPD 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2918 TLEYLGRIDDQVKI-RGYRVETKEIESVIrcikgvKDAAVVAHVTASGQTE---LSAYVVTKP----GLSTNAVRSELQN 2989
Cdd:cd17632    479 RLVYVDRRNNVLKLsQGEFVTVARLEAVF------AASPLVRQIFVYGNSErayLLAVVVPTQdalaGEDTARLRAALAE 552


                   ..
gi 1678550997 2990 KL 2991
Cdd:cd17632    553 SL 554
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 490-952 6.75e-08

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 58.21  E-value: 6.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLR-MKGVVRQEPVAIMMERSAAFITGVLGILKAGGAivpvdphyPAdRIRYILHDCGCSHVVsqa 568
Cdd:cd05937      7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA-FINYNLSGDPLIHCL--- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  569 hlpsslednyiithpediesKVdgSNIKSV-NNADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVL 647
Cdd:cd05937     75 --------------------KL--SGSRFViVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTY 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  648 Q----FATPSFDVCyqeIFSALLKGGTLHIVPeaiKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSerelANSFPDGVKH 723
Cdd:cd05937    133 TcmplYHGTAAFLG---ACNCLMSGGTLALSR---KFSASQFWKDVRDSGATIIQYVGELCRYLLS----TPPSPYDRDH 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  724 -LIAAGEQLMISDLFQDvLRKR-GI-HLHNHYgpSETHVVSTYTIHPGDPIPelppigkpIGCTDLY------ILNHQKQ 794
Cdd:cd05937    203 kVRVAWGNGLRPDIWER-FRERfNVpEIGEFY--AATEGVFALTNHNVGDFG--------AGAIGHHglirrwKFENQVV 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  795 L---------------------QPCGVPGE----LYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRTGDLARRLED 849
Cdd:cd05937    272 LvkmdpetddpirdpktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDAD 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  850 GNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYCSVQK-------LNTIDLRSYMAS 922
Cdd:cd05937    352 GRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEEssavpteFTKSLLASLARK 431

                          490       500       510
                   ....*....|....*....|....*....|
gi 1678550997  923 ELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05937    432 NLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 3228-3384 7.41e-08

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: 58.04  E-value: 7.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3228 IQQKMDLKNGPLLQAGLFHTIDGDF-LFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYA----KK 3302
Cdd:cd19538     98 VRYPFDLSEEPPFRATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLPVQYADYAlwqqEL 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3303 LSDYAESQQLM-KQLKYWREAEEY---QTEaLPFD-QIDGTRAHEGQrsTISFTLNDKETAALLKDANSayNTDTQDMLL 3377
Cdd:cd19538    178 LGDESDPDSLIaRQLAYWKKQLAGlpdEIE-LPTDyPRPAESSYEGG--TLTFEIDSELHQQLLQLAKD--NNVTLFMVL 252


                   ....*..
gi 1678550997 3378 ASVILAL 3384
Cdd:cd19538    253 QAGFAAL 259
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 1634-1905 8.83e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 58.19  E-value: 8.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQSLAYVIYTSGSTGMPKGVEIEHRsavNFLNSLQSRYqlKHSdmIMHKtsYSFDAsiwELFWWP----YAGASVYL-LP 1708
Cdd:PTZ00342   303 PDFITSIVYTSGTSGKPKGVMLSNK---NLYNTVVPLC--KHS--IFKK--YNPKT---HLSYLPishiYERVIAYLsFM 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1709 QGGE-----KEPEVIAKAIEEQKITAMHFVP-----------------------------SM--------LHAFLEHIKY 1746
Cdd:PTZ00342   371 LGGTiniwsKDINYFSKDIYNSKGNILAGVPkvfnriytnimteinnlpplkrflvkkilSLrksnnnggFSKFLEGITH 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1747 RSVPIKTN---RLKRVFSGGEQLGTHLVSRFYELLpNVSITNSYGPTEATveAAFF-----DCPPHEkleripIGKPV-- 1816
Cdd:PTZ00342   451 ISSKIKDKvnpNLEVILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTETT--GPIFvqhadDNNTES------IGGPIsp 521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1817 ---HHVRLYLLNQNQRMLPVgciGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRT 1893
Cdd:PTZ00342   522 ntkYKVRTWETYKATDTLPK---GELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRS 592

                          330
                   ....*....|...
gi 1678550997 1894 DDQVKI-RGYRIE 1905
Cdd:PTZ00342   593 KGLVKLsQGEYIE 605
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 2533-3032 1.09e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 57.77  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTpkASALVSGDKTLTYQELDEWSNGIARALRSRgVKPDTP--VGIMMHRS--FSMIASILGVwkAGG 2608
Cdd:PRK07867     5 PTVAELLLPLAEDD--DRGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTpeFSLLLGAAAL--SGI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2609 CYVPIDPEYPKERKRYILSDSGTKLLMTiNEADLGVLADFEG--EILTIESVEEDDK-------SPLPQMSSAHHLAYII 2679
Cdd:PRK07867    80 VPVGLNPTRRGAALARDIAHADCQLVLT-ESAHAELLDGLDPgvRVINVDSPAWADElaahrdaEPPFRVADPDDLFMLI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2680 YTSGTTGRPKGVMVEHKGIA---NTLQWRRNAYAfnetDTILQLfsfsfdgfitSMftPLLSGAK-----AVLLHEEEAk 2751
Cdd:PRK07867   159 FTSGTSGDPKAVRCTHRKVAsagVMLAQRFGLGP----DDVCYV----------SM--PLFHSNAvmagwAVALAAGAS- 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2752 diLAIKHQLS---------RQRITHMIIV--PVLYrALLDVVQPEDV-KTLRVVtLAGEAADREL--IARSLAicphTEL 2817
Cdd:PRK07867   222 --IALRRKFSasgflpdvrRYGATYANYVgkPLSY-VLATPERPDDAdNPLRIV-YGNEGAPGDIarFARRFG----CVV 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2818 ANEYGPTENSVATTvmrHMEKQAYVSIGQPIDGTQVL-----------ILNSNHQLQPIGVAGELC-IAGTGLARGYVNL 2885
Cdd:PRK07867   294 VDGFGSTEGGVAIT---RTPDTPPGALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYND 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2886 PELTERaftqnpfKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAV--VAHVTAS 2963
Cdd:PRK07867   371 PEADAE-------RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVyaVPDPVVG 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2964 GQTElsAYVVTKPGLSTNAV--------RSELQNKlpvfMHPAFIEKLDSLPLSPNGKLDRGAL-------PKPVYNHEG 3028
Cdd:PRK07867   444 DQVM--AALVLAPGAKFDPDafaeflaaQPDLGPK----QWPSYVRVCAELPRTATFKVLKRQLsaegvdcADPVWWIRR 517


                   ....
gi 1678550997 3029 ERPF 3032
Cdd:PRK07867   518 LTPS 521
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 873-946 1.95e-07

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: 51.01  E-value: 1.95e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  873 EIEVTLMNHPDISEAA-ILIWQDQNGEhELCAYYCSVQKLNTI--DLRSYMASELPEYMIPAKWIWVDSIPLTPNGK 946
Cdd:pfam13193    1 EVESALVSHPAVAEAAvVGVPDELKGE-APVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 2510-2925 2.44e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 56.91  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2510 LTQEERHQLLNEFNTGQanqygvqTISQLFEQQAARTPKASAL---------------------------VSGDKTLTYQ 2562
Cdd:PTZ00216    53 VTDEEHERLRNEWYYGP-------NFLQRLERICKERGDRRALayrpvervekevvkdadgkertmevthFNETRYITYA 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2563 ELdeWSNGIA--RALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSD--------SGTK 2632
Cdd:PTZ00216   126 EL--WERIVNfgRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALREteckaivcNGKN 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2633 LLMTINEADLGVL--------------ADFEG-EILTIESVEEDDKS-----PLPQMSSAHHLAYIIYTSGTTGRPKGVM 2692
Cdd:PTZ00216   204 VPNLLRLMKSGGMpnttiiyldslpasVDTEGcRLVAWTDVVAKGHSagshhPLNIPENNDDLALIMYTSGTTGDPKGVM 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2693 VEHKGIA---NTLQWRRN------------------AYAFNETDTILQLFSFSFDGF-----ITSMFT-P---------- 2735
Cdd:PTZ00216   284 HTHGSLTagiLALEDRLNdligppeedetycsylplAHIMEFGVTNIFLARGALIGFgsprtLTDTFArPhgdltefrpv 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2736 LLSGA--------KAVllheeEAKdiLAIKHQLSRQRITHMIIVPVlyRALLD---------VV--QPEDV--KTLRVVT 2794
Cdd:PTZ00216   364 FLIGVprifdtikKAV-----EAK--LPPVGSLKRRVFDHAYQSRL--RALKEgkdtpywneKVfsAPRAVlgGRVRAML 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2795 LAG---EAADRELIARSLAIcphteLANEYGPTENSVATTVMR--HMEkqaYVSIGQPIDGTQVLILNSNH-----QLQP 2864
Cdd:PTZ00216   435 SGGgplSAATQEFVNVVFGM-----VIQGWGLTETVCCGGIQRtgDLE---PNAVGQLLKGVEMKLLDTEEykhtdTPEP 506

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678550997 2865 igvAGELCIAGTGLARGYVNLPELTERAFTqnpfkpEARMYRTGDAARWMADGTLEYLGRI 2925
Cdd:PTZ00216   507 ---RGEILLRGPFLFKGYYKQEELTREVLD------EDGWFHTGDVGSIAANGTLRIIGRV 558
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 1521-1983 2.52e-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: 2.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILllqsa 1600
Cdd:cd05939      5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL----- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1601 glhvpeftgeIVYLNQTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHrsavnflnslqSRY----QLKHS 1676
Cdd:cd05939     80 ----------IFNLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVH-----------SRYyriaAGAYY 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1677 DMIMHKTSYSFDAsiweLFWWPYAGASV---YLLPQGGEKepeVIAKaieeqKITAMHFvpsmlhaFLEHIKYRSVPI-- 1751
Cdd:cd05939    139 AFGMRPEDVVYDC----LPLYHSAGGIMgvgQALLHGSTV---VIRK-----KFSASNF-------WDDCVKYNCTIVqy 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1752 -----------------KTNRLKRVFSGG--EQLGTHLVSRFyellpNVS-ITNSYGPTEATVEAAFFD-----CpphEK 1806
Cdd:cd05939    200 igeicryllaqppseeeQKHNVRLAVGNGlrPQIWEQFVRRF-----GIPqIGEFYGATEGNSSLVNIDnhvgaC---GF 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1807 LERIPigKPVHHVRLYLLNQNQRML---PVG-CI----GElyiAGAGVAR-----------GYLNRPAlTEERFLEDPFY 1867
Cdd:cd05939    272 NSRIL--PSVYPIRLIKVDEDTGELirdSDGlCIpcqpGE---PGLLVGKiiqndplrrfdGYVNEGA-TNKKIARDVFK 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1868 PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA---VTVRTDSGEPELCAYV---EG 1941
Cdd:cd05939    346 KGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVvygVEVPGVEGRAGMAAIVdpeRK 425

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 1942 LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 1983
Cdd:cd05939    426 VDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 802-954 3.19e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 56.16  E-value: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  802 GELYISGASVARGYVNHdkltsdKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNH 881
Cdd:PRK07445   302 GNITIQAQSLALGYYPQ------ILDSQGI------FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678550997  882 PDISEAAILIWQDQN-GEHELCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPE 954
Cdd:PRK07445   370 GLVQDVCVLGLPDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 1521-1709 3.82e-07

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: 56.20  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1521 TYKELNEQANRIAWELIGR-GVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSG-------- 1591
Cdd:cd05905     16 TWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKvrvaltve 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1592 -TNILLLQSAGLHVPefTGEIVYLN-----------QTNSGLAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRS 1659
Cdd:cd05905     96 aCLKGLPKKLLKSKT--AAEIAKKKgwpkildfvkiPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 1660 AVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWelFWW---PYAGASVYLLPQ 1709
Cdd:cd05905    174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLW--HGCllsVYSGHHTILIPP 224
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 1519-1940 4.72e-07

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: 55.89  E-value: 4.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1519 VMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQ 1598
Cdd:cd17641     11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1599 -----------SAGLHVPEFtgeIVYLNQTN-----------------SGLAHRLSNPNV------DVLPQSLAYVIYTS 1644
Cdd:cd17641     91 deeqvdklleiADRIPSVRY---VIYCDPRGmrkyddprlisfedvvaLGRALDRRDPGLyerevaAGKGEDVAVLCTTS 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1645 GSTGMPKGVeiehrsavnflnslqsryQLKHSDMIMHKTSY-SFD--------ASIWELfwwPYAGASVYLLPQG---GE 1712
Cdd:cd17641    168 GTTGKPKLA------------------MLSHGNFLGHCAAYlAADplgpgdeyVSVLPL---PWIGEQMYSVGQAlvcGF 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1713 K-----EPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYR---SVPIKT------------------------------- 1753
Cdd:cd17641    227 IvnfpeEPETMMEDLREIGPTFVLLPPRVWEGIAADVRARmmdATPFKRfmfelgmklglraldrgkrgrpvslwlrlas 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1754 -----------------NRLKRVFSGGEQLGTHlVSRFYELLpNVSITNSYGPTEAtveAAFFDCPPHEKLERIPIGKPV 1816
Cdd:cd17641    307 wladallfrplrdrlgfSRLRSAATGGAALGPD-TFRFFHAI-GVPLKQLYGQTEL---AGAYTVHRDGDVDPDTVGVPF 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1817 HHVRLYLLNqnqrmlpvgcIGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQ 1896
Cdd:cd17641    382 PGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDV 445

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1678550997 1897 VKI-RGYRIEPGEIEAALRSIEGVREAAVTVRtdsGEPELCAYVE 1940
Cdd:cd17641    446 GTTsDGTRFSPQFIENKLKFSPYIAEAVVLGA---GRPYLTAFIC 487
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1908-1977 6.30e-07

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: 49.47  E-value: 6.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997 1908 EIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EGLQ--RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 1977
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDElkGE-APVAFVvlkPGVEllEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PLN02654 PLN02654
acetate-CoA ligase
 824-952 6.37e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 55.29  E-value: 6.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  824 DKFSSDPFKPDVIMYRTGDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILiwqdqNGEHEL-- 901
Cdd:PLN02654   501 ERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV-----GIEHEVkg 575

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997  902 CAYYCSVQKLNTI----DLRSYMA----SELPEYMIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:PLN02654   576 QGIYAFVTLVEGVpyseELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
489-952 7.85e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 55.17  E-value: 7.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMK-GVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYI------------ 555
Cdd:PRK05620    39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIinhaedevivad 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  556 ----------LHDCGC-SHVV---------SQAHLPSSLednyiitHPEDIESKVDGSNIK---SVNNADDLLYMIYTSG 612
Cdd:PRK05620   119 prlaeqlgeiLKECPCvRAVVfigpsdadsAAAHMPEGI-------KVYSYEALLDGRSTVydwPELDETTAAAICYSTG 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  613 TTGKPKGVQFEHRNManllkfeYTHSgidfeadvLQF-ATPSFDVCYQEIF----------------SALLKGGTL---- 671
Cdd:PRK05620   192 TTGAPKGVVYSHRSL-------YLQS--------LSLrTTDSLAVTHGESFlccvpiyhvlswgvplAAFMSGTPLvfpg 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  672 ---------HIVPEAIKR---DVP----QLFAFINKHQTNivflptafiKMIFSErelansfpdgvkhLIAAGEQlmISD 735
Cdd:PRK05620   257 pdlsaptlaKIIATAMPRvahGVPtlwiQLMVHYLKNPPE---------RMSLQE-------------IYVGGSA--VPP 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  736 LFQDVLRKR-GIHLHNHYGPSETHVVSTYTihpgdpipeLPPIGKPIGCTDLY--------------ILN---------- 790
Cdd:PRK05620   313 ILIKAWEERyGVDVVHVWGMTETSPVGTVA---------RPPSGVSGEARWAYrvsqgrfpasleyrIVNdgqvmestdr 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  791 HQKQLQPCG--VPGELYIS-------GASVARGYVNHDklTSDKFSSDPFkpdvimYRTGDLARRLEDGNIEYIGRADNQ 861
Cdd:PRK05620   384 NEGEIQVRGnwVTASYYHSpteegggAASTFRGEDVED--ANDRFTADGW------LRTGDVGSVTRDGFLTIHDRARDV 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  862 VKIRGYRIEPQEIEVTLMNHPDISEAAIL-IWQDQNGEHELCAYYCSVQKLNTI----DLRSYMASELPEYMIPAKWIWV 936
Cdd:PRK05620   456 IRSGGEWIYSAQLENYIMAAPEVVECAVIgYPDDKWGERPLAVTVLAPGIEPTRetaeRLRDQLRDRLPNWMLPEYWTFV 535

                          570
                   ....*....|....*.
gi 1678550997  937 DSIPLTPNGKVDRAAL 952
Cdd:PRK05620   536 DEIDKTSVGKFDKKDL 551
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 2551-2739 1.77e-06

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 53.96  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2551 ALVSGDKtLTYQELD--EWSNGIARAL-------RSRGV--------KPDTPVGIMMHRSFSMIASILGVWKAGGCYVPI 2613
Cdd:PRK07769    31 AKVRGDK-LAYRFLDfsTERDGVARDLtwsqfgaRNRAVgarlqqvtKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2614 -DPEYP--KERKRYILSDSGTKLLMTINEADLGVLADFEG-------EILTIESVEEDDKSPLPQMSSAHH-LAYIIYTS 2682
Cdd:PRK07769   110 fDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRArpakerpRVIAVDAVPDEVGATWVPPEANEDtIAYLQYTS 189

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2683 GTTGRPKGVMVEHKGIA-NTLQwRRNAYAFNETDTILQLFSFSFD-GFITSMFTPLLSG 2739
Cdd:PRK07769   190 GSTRIPAGVQITHLNLPtNVLQ-VIDALEGQEGDRGVSWLPFFHDmGLITVLLPALLGH 247
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 490-952 2.68e-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: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  490 TYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGC------SH 563
Cdd:cd05915     26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDkvllfdPN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  564 VVSQAHLPSSLEDNyiITHPEDIESKVD---------GSNIKSVNNAD--DLLYMIYTSGTTGKPKGVQFEHRNM-ANLL 631
Cdd:cd05915    106 LLPLVEAIRGELKT--VQHFVVMDEKAPegylayeeaLGEEADPVRVPerAACGMAYTTGTTGLPKGVVYSHRALvLHSL 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  632 KFEYTHSGIDFEADVLQFATPSFDV---CYqeIFSALLKGGTLHIVPEAIKRDVpqLFAFINKHQ-TNIVFLPTAfIKMI 707
Cdd:cd05915    184 AASLVDGTALSEKDVVLPVVPMFHVnawCL--PYAATLVGAKQVLPGPRLDPAS--LVELFDGEGvTFTAGVPTV-WLAL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  708 FSERE-LANSFPDGVKhLIAAGE---QLMISdlfqdvLRKRG-IHLHNHYGPSETHVVSTYTIHPgdPIPELPPIGKPIG 782
Cdd:cd05915    259 ADYLEsTGHRLKTLRR-LVVGGSaapRSLIA------RFERMgVEVRQGYGLTETSPVVVQNFVK--SHLESLSEEEKLT 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  783 CTDLYILNHQKQ----LQPC--GVPGE------LYISGASVARGYVNhdkltsDKFSSDPFKPDVIMYRTGDLARRLEDG 850
Cdd:cd05915    330 LKAKTGLPIPLVrlrvADEEgrPVPKDgkalgeVQLKGPWITGGYYG------NEEATRSALTPDGFFRTGDIAVWDEEG 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  851 NIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHELCAYYcsvqKLNTIDLRSymaSELPEY--- 927
Cdd:cd05915    404 YVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV----VPRGEKPTP---EELNEHllk 476

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1678550997  928 ------MIPAKWIWVDSIPLTPNGKVDRAAL 952
Cdd:cd05915    477 agfakwQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 2840-3018 5.40e-06

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 52.44  E-value: 5.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2840 AYVSIGQPIDGTQVLILNSNHQLQ-PIGVAGELCIAGTGLARGYVNLPELTERAFtQNPFK-------------PEARMY 2905
Cdd:PRK12476   400 AHVSCGQVARSQWAVIVDPDTGAElPDGEVGEIWLHGDNIGRGYWGRPEETERTF-GAKLQsrlaegshadgaaDDGTWL 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2906 RTGDAARWMaDGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTK---------P 2976
Cdd:PRK12476   479 RTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERLVIVAEraagtsradP 557

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1678550997 2977 GLSTNAVRSELQNKLPVFMHPAFIEKLDSLPLSPNGKLDRGA 3018
Cdd:PRK12476   558 APAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRA 599
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 2557-2933 8.38e-06

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: 51.59  E-value: 8.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2557 KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMT 2636
Cdd:cd05933      7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2637 INEADLGVLADFEGEILTIESV---------------------EEDDKSPLPQ----MSS--AHHLAYIIYTSGTTGRPK 2689
Cdd:cd05933     87 ENQKQLQKILQIQDKLPHLKAIiqykeplkekepnlyswdefmELGRSIPDEQldaiISSqkPNQCCTLIYTSGTTGMPK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2690 GVMVEHKGIANTLQWRRNAYAFNETD----TILQLFSFSFDGF-ITSMFTPLLSGAKAVLLHEEEAKDILAIkhQLSRQR 2764
Cdd:cd05933    167 GVMLSHDNITWTAKAASQHMDLRPATvgqeSVVSYLPLSHIAAqILDIWLPIKVGGQVYFAQPDALKGTLVK--TLREVR 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2765 ITHMIIVPVLYRALLDVVQP----------------------------------------------EDVKTL----RVVT 2794
Cdd:cd05933    245 PTAFMGVPRVWEKIQEKMKAvgaksgtlkrkiaswakgvgletnlklmggespsplfyrlakklvfKKVRKAlgldRCQK 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2795 LAGEAA--DRELIA--RSLAIcPHTELaneYGPTENSVATTVMRhmeKQAY--VSIGQPIDGTQVLILNSNHQLQpigva 2868
Cdd:cd05933    325 FFTGAApiSRETLEffLSLNI-PIMEL---YGMSETSGPHTISN---PQAYrlLSCGKALPGCKTKIHNPDADGI----- 392

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2869 GELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKIRG 2933
Cdd:cd05933    393 GEICFWGRHVFMGYLNMEDKTEEAIDEDGW------LHSGDLGKLDEDGFLYITGRIKELIITAG 451
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2019-2070 8.40e-06

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 46.47  E-value: 8.40e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1678550997  2019 VGIHDNFFDRGGHSLKATALVSRITKEFDVQVPLKDVFAHPTVEGLATVIRE 2070
Cdd:smart00823   33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 474-632 1.57e-05

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 50.90  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  474 EKTPDAHAVidqacSLTYREL----NKAANRLARHLRmkgvvRQEPVAIMMERSAAFITGVLGILKAGGAIVPV-DPHYP 548
Cdd:PRK12476    59 SHSAAGCAV-----ELTWTQLgvrlRAVGARLQQVAG-----PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELP 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  549 --ADRIRYILHDCGCSHVVSQAHLPSSLEDnYIITHPED-------IESKVD--GSNIKSVN-NADDLLYMIYTSGTTGK 616
Cdd:PRK12476   129 ghAERLDTALRDAEPTVVLTTTAAAEAVEG-FLRNLPRLrrprviaIDAIPDsaGESFVPVElDTDDVSHLQYTSGSTRP 207

                          170
                   ....*....|....*..
gi 1678550997  617 PKGVQFEHRN-MANLLK 632
Cdd:PRK12476   208 PVGVEITHRAvGTNLVQ 224
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 2533-2913 1.62e-05

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 50.65  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2533 QTISQLFEQQAARTPKASALV---SGD--KTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSF--SMIAsiLGVWK 2605
Cdd:PRK08180    39 RRLTDRLVHWAQEAPDRVFLAergADGgwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehALLA--LAAMY 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2606 AGGCYVPIDPEY-----PKERKRYILS---------DSGTKL---LMTINEADLGVLA----DFEGEILTIESVEEDdkS 2664
Cdd:PRK08180   117 AGVPYAPVSPAYslvsqDFGKLRHVLElltpglvfaDDGAAFaraLAAVVPADVEVVAvrgaVPGRAATPFAALLAT--P 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2665 PLPQMSSAH------HLAYIIYTSGTTGRPKGVMVEHKGI-ANTLQwrrnayafnetdtILQLFSFsfdgfitsmftplL 2737
Cdd:PRK08180   195 PTAAVDAAHaavgpdTIAKFLFTSGSTGLPKAVINTHRMLcANQQM-------------LAQTFPF-------------L 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2738 SGAKAVLLheeeakDILAIKHQLSRQRITHMII-----------------------------------VPVLYRALLDVV 2782
Cdd:PRK08180   249 AEEPPVLV------DWLPWNHTFGGNHNLGIVLynggtlyiddgkptpggfdetlrnlreisptvyfnVPKGWEMLVPAL 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2783 QPEDV------KTLRVVTLAGeAA------DReLIARSLAICPH-TELANEYGPTENS-VATTVMRHMEKQAYvsIGQPI 2848
Cdd:PRK08180   323 ERDAAlrrrffSRLKLLFYAG-AAlsqdvwDR-LDRVAEATCGErIRMMTGLGMTETApSATFTTGPLSRAGN--IGLPA 398

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 2849 DGTQVlilnsnhQLQPIGVAGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARW 2913
Cdd:PRK08180   399 PGCEV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 489-648 1.90e-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: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  489 LTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVV--- 565
Cdd:cd05933      9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVven 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  566 -SQAHLPSSLEDNY-----IITHPEDIESKVDG-------------------SNIKSVNNADDLLYMIYTSGTTGKPKGV 620
Cdd:cd05933     89 qKQLQKILQIQDKLphlkaIIQYKEPLKEKEPNlyswdefmelgrsipdeqlDAIISSQKPNQCCTLIYTSGTTGMPKGV 168

                          170       180
                   ....*....|....*....|....*...
gi 1678550997  621 QFEHRNMANLLKFEYTHSGIDfEADVLQ 648
Cdd:cd05933    169 MLSHDNITWTAKAASQHMDLR-PATVGQ 195
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 739-901 2.01e-05

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 50.15  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  739 DVLRKR-----GIHLHNHYGPSET-HVVST-------YTIHPGDPIPEL--PPIGKPIgctdlyilnhqkqlqPCGVPGE 803
Cdd:COG1541    217 EEMRKEieerwGIKAYDIYGLTEVgPGVAYeceaqdgLHIWEDHFLVEIidPETGEPV---------------PEGEEGE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  804 LYISGasvargyvnhdkLTSDKFssdpfkPdVIMYRTGDLARRLEDGN--------IEYI-GRADNQVKIRGYRIEPQEI 874
Cdd:COG1541    282 LVVTT------------LTKEAM------P-LIRYRTGDLTRLLPEPCpcgrthprIGRIlGRADDMLIIRGVNVFPSQI 342

                          170       180
                   ....*....|....*....|....*..
gi 1678550997  875 EVTLMNHPDISEAAILIWQDQNGEHEL 901
Cdd:COG1541    343 EEVLLRIPEVGPEYQIVVDREGGLDEL 369
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 2674-2938 2.02e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 50.49  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2674 HLAYIIYTSGTTGRPKGVMVEHKGIANTL----QW----------------------RRNAY-AFNETDTI------LQL 2720
Cdd:PTZ00342   305 FITSIVYTSGTSGKPKGVMLSNKNLYNTVvplcKHsifkkynpkthlsylpishiyeRVIAYlSFMLGGTIniwskdINY 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2721 FS---FSFDGFI--------TSMFTPLLSG-AKAVLLHEEEAKDILAIKHQ-----LSR--QRITHmiivpvLYRALLDV 2781
Cdd:PTZ00342   385 FSkdiYNSKGNIlagvpkvfNRIYTNIMTEiNNLPPLKRFLVKKILSLRKSnnnggFSKflEGITH------ISSKIKDK 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2782 VQPedvkTLRVVtLAGEAADRELIARSLAICPHTELANEYGPTENSVATTVmRHMEKQAYVSIGQPIDGTQVLILNSNHQ 2861
Cdd:PTZ00342   459 VNP----NLEVI-LNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFV-QHADDNNTESIGGPISPNTKYKVRTWET 532

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2862 LQPIGV--AGELCIAGTGLARGYVNLPELTERAFTQNPFkpearmYRTGDAARWMADGTLEYLGRIDDQVKI-RGYRVET 2938
Cdd:PTZ00342   533 YKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIET 606
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1634-1979 2.14e-05

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 50.73  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1634 PQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HktsySFDASiwelfwwpyAGAsvyLL 1707
Cdd:PRK06814   792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFnalpvfH----SFGLT---------GGL---VL 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1708 PqggekepeviakAIEEQKItamHFVPSMLHaflehikYRSVP---IKTN------------------------RLKRVF 1760
Cdd:PRK06814   856 P------------LLSGVKV---FLYPSPLH-------YRIIPeliYDTNatilfgtdtflngyaryahpydfrSLRYVF 913

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1761 SGGEQLGTHlVSRFYELLPNVSITNSYGPTEATVEAAFfDCPPHEKLE---RIPIGkpVHHvrlyllnqnqRMLPVGCI- 1836
Cdd:PRK06814   914 AGAEKVKEE-TRQTWMEKFGIRILEGYGVTETAPVIAL-NTPMHNKAGtvgRLLPG--IEY----------RLEPVPGId 979

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1837 --GELYIAGAGVARGYL--NRPALTEErfledpfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEA- 1911
Cdd:PRK06814   980 egGRLFVRGPNVMLGYLraENPGVLEP--------PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEl 1051

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1912 ----------ALRSIE----GVREAAVTVRTDSGEPELCAYVEGLQRNEVraqlerllpgyMVPAYMIEMEQWPVTPSGK 1977
Cdd:PRK06814  1052 aaelwpdalhAAVSIPdarkGERIILLTTASDATRAAFLAHAKAAGASEL-----------MVPAEIITIDEIPLLGTGK 1120


                   ..
gi 1678550997 1978 LD 1979
Cdd:PRK06814  1121 ID 1122
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 1631-1985 2.35e-05

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 50.20  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1631 DVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM------HktSYSFDASiwELFwwP-YAGAS 1703
Cdd:PRK06334   179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMsflppfH--AYGFNSC--TLF--PlLSGVP 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1704 VYLlpQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLkrVFSGGEQLGTHLVSRFYELLPNVSI 1783
Cdd:PRK06334   253 VVF--AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRF--VVIGGDAFKDSLYQEALKTFPHIQL 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1784 TNSYGPTEAT--VEAAFFDCPPHEKLeripIGKPVHHVRLYLLNQNQRM-LPVGCIGELYIAGAGVARGYL-NRPAlteE 1859
Cdd:PRK06334   329 RQGYGTTECSpvITINTVNSPKHESC----VGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLgEDFG---Q 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1860 RFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALrsIEGVREAA------VTVRTDSGEP 1933
Cdd:PRK06334   402 GFVE---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL--MEGFGQNAadhagpLVVCGLPGEK 476

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1678550997 1934 E-LCAYVE-GLQRNEVRAQLERL-LPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 1985
Cdd:PRK06334   477 VrLCLFTTfPTSISEVNDILKNSkTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 2681-2991 3.34e-05

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 49.38  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2681 TSGTTGRPKGVMVEHKGIANTL-QWRRNAYA--FNETDTILqlFSFSFDGFITSMFtpLLSGAKAVllheeeakDILAIK 2757
Cdd:COG1541     91 SSGTTGKPTVVGYTRKDLDRWAeLFARSLRAagVRPGDRVQ--NAFGYGLFTGGLG--LHYGAERL--------GATVIP 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2758 H---QLSRQ-------RITHMIIVP--VLYraLLDVVQPEDVK----TLRVVTLAGEA---ADRELIARSLAIcphtELA 2818
Cdd:COG1541    159 AgggNTERQlrlmqdfGPTVLVGTPsyLLY--LAEVAEEEGIDprdlSLKKGIFGGEPwseEMRKEIEERWGI----KAY 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2819 NEYGPTEnsVATTV---------MRHMEKQAYVSIGQPIDGTQVlilnsnhqlqPIGVAGELCIagTGLARgyvnlpelt 2889
Cdd:COG1541    233 DIYGLTE--VGPGVayeceaqdgLHIWEDHFLVEIIDPETGEPV----------PEGEEGELVV--TTLTK--------- 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2890 eraftqnpfkpEA----RmYRTGDAARWMAD----GT----LEY-LGRIDDQVKIRG---YRVetkEIESVIRCIKGVKD 2953
Cdd:COG1541    290 -----------EAmpliR-YRTGDLTRLLPEpcpcGRthprIGRiLGRADDMLIIRGvnvFPS---QIEEVLLRIPEVGP 354

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1678550997 2954 AAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKL 2991
Cdd:COG1541    355 EYQIVVDREGGLDELTVRVELAPGASLEALAEAIAAAL 392
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 2654-2702 4.58e-05

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


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 49.34  E-value: 4.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1678550997 2654 TIESVEEDDK----SPL-PQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIANTL 2702
Cdd:PLN02387   226 TVSSFSEVEKlgkeNPVdPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATV 279
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2676-3015 4.84e-05

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 49.58  E-value: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2676 AYIIYTSGTTGRPKGVMVEHKGI-ANTLQ------WRRNAYAFNetdtILQLF-SFsfdGFITSMFTPLLSGAKAVL--- 2744
Cdd:PRK06814   796 AVILFTSGSEGTPKGVVLSHRNLlANRAQvaaridFSPEDKVFN----ALPVFhSF---GLTGGLVLPLLSGVKVFLyps 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2745 -LH----EEEAKDILAikhqlsrqriTHMIIVPVLYRALLDVVQPEDVKTLRVVtLAG----EAADRELIARSLAIcpht 2815
Cdd:PRK06814   869 pLHyriiPELIYDTNA----------TILFGTDTFLNGYARYAHPYDFRSLRYV-FAGaekvKEETRQTWMEKFGI---- 933

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2816 ELANEYGPTENSVATTVMRHMEKQAYvSIGQPIDGTQvlilnsnHQLQPI-GV--AGELCIAGTGLARGYVnlpeLTERA 2892
Cdd:PRK06814   934 RILEGYGVTETAPVIALNTPMHNKAG-TVGRLLPGIE-------YRLEPVpGIdeGGRLFVRGPNVMLGYL----RAENP 1001

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2893 FTQNPfkPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKEIESVIRCIKGVKDAAVVAhVTASGQTELSAYV 2972
Cdd:PRK06814  1002 GVLEP--PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVS-IPDARKGERIILL 1078

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1678550997 2973 VTKPGLStnavRSELQ-----NKLPVFMHPAFIEKLDSLPLSPNGKLD 3015
Cdd:PRK06814  1079 TTASDAT----RAAFLahakaAGASELMVPAEIITIDEIPLLGTGKID 1122
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 449-628 7.67e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 48.82  E-value: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  449 RQLIGEITDQTPV-YETIHAMfEKQAEKTPDAHA------VIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMME 521
Cdd:PTZ00216    76 ERICKERGDRRALaYRPVERV-EKEVVKDADGKErtmevtHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEE 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997  522 RSAAFITGVLGILKAGGAIVPVDPHYPADRIRYILHDCGCSHVVSQAH------------------------LPSSLED- 576
Cdd:PTZ00216   155 TRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKnvpnllrlmksggmpnttiiyldsLPASVDTe 234

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997  577 NYIITHPEDI----ESKVDGSNIKSVNNADDLLYMIYTSGTTGKPKGVQFEHRNMA 628
Cdd:PTZ00216   235 GCRLVAWTDVvakgHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLT 290
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 1639-1913 9.81e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 48.20  E-value: 9.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1639 YVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVI 1718
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKHI 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1719 A----KAIEEQKITAMHFVPSMLHAFLE--------HIKYRSvpiktNRLKRVFSGGEQLgTHLVSRFYELLPNVSITNS 1786
Cdd:PTZ00237   338 EddlwNTIEKHKVTHTLTLPKTIRYLIKtdpeatiiRSKYDL-----SNLKEIWCGGEVI-EESIPEYIENKLKIKSSRG 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1787 YGPTEATVeaAFFDCPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIA---GAGVARGYLNRPALTEERFLE 1863
Cdd:PTZ00237   412 YGQTEIGI--TYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSK 489

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1864 DPFYpgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAAL 1913
Cdd:PTZ00237   490 FPGY-----YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSI 534
PLN03051 PLN03051
acyl-activating enzyme; Provisional
 1640-1983 1.51e-04

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 47.50  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1640 VIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIMHKTSYSFDASIWELFWWPYAGASVYLLpqGGEKEPEVIA 1719
Cdd:PLN03051   124 ILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALY--GGAPLGRGFG 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1720 KAIEEQKITAMHFVPSMLHAFLEHIKYRSVPIKTNRLKRVFSGGEqlgthlVSRFYELLPNVSITNSYGPTeatVEAaff 1799
Cdd:PLN03051   202 KFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGE------ASAVDDVLWLSSVRGYYKPV---IEY--- 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1800 dCPPHEKLERIPIGKPVH------------HVRLYLLNQNQRMLPVG--CIGELYIAGA--GVARGYLNrpALTEERFLE 1863
Cdd:PLN03051   270 -CGGTELASGYISSTLLQpqapgafstaslGTRFVLLNDNGVPYPDDqpCVGEVALAPPmlGASDRLLN--ADHDKVYYK 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1864 D-PFYP--GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIE-AALRSIEGVRE-AAVTVRTDSGEPELCAY 1938
Cdd:PLN03051   347 GmPMYGskGMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIErACDRAVAGIAEtAAVGVAPPDGGPELLVI 426

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1939 V---------------EGLQRNEVRAQLERLLPGYMVPAYMIEMEqWPVTPSGKLDRNAL 1983
Cdd:PLN03051   427 FlvlgeekkgfdqarpEALQKKFQEAIQTNLNPLFKVSRVKIVPE-LPRNASNKLLRRVL 485
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
2676-2746 1.78e-04

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 47.40  E-value: 1.78e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678550997 2676 AYIIYTSGTTGRPKGVMVEHKGI-ANTLQWRRNAyAFNETD---TILQLFSfSFdGFITSMFTPLLSGAKAVL----LH 2746
Cdd:PRK08043   368 ALILFTSGSEGHPKGVVHSHKSLlANVEQIKTIA-DFTPNDrfmSALPLFH-SF-GLTVGLFTPLLTGAEVFLypspLH 443
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 3233-3321 2.04e-04

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


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 46.93  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3233 DLKNGPLLQAGLFHTIDGD-FLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYAKKLSDYAESQQ 3311
Cdd:cd20484    104 VLENGPLMRVHLFSRSEQEhFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAWEQDMLAGAE 183

                           90
                   ....*....|
gi 1678550997 3312 LMKQLKYWRE 3321
Cdd:cd20484    184 GEEHRAYWKQ 193
PRK07868 PRK07868
acyl-CoA synthetase; Validated
 2525-2615 2.28e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 47.40  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2525 GQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGVKPDTPVGIMMHRSFSMIASILGVW 2604
Cdd:PRK07868   439 GQINDHTRISLGRIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALS 518

                           90
                   ....*....|.
gi 1678550997 2605 KAGGCYVPIDP 2615
Cdd:PRK07868   519 RLGAVAVLMPP 529
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 3227-3321 3.52e-04

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: 46.14  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 3227 DIQQKMDLkNGPLLQAGLF-HTIDGDFLFLSAHHLVVDGISWRVLLEDLALGYRqaagGEDIKLPPKTSSFKAYAKKLSD 3305
Cdd:cd19545     90 DRAAPMGL-GGPLVRLALVeDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ----GEPVPQPPPFSRFVKYLRQLDD 164

                           90
                   ....*....|....*.
gi 1678550997 3306 yAESQQlmkqlkYWRE 3321
Cdd:cd19545    165 -EAAAE------FWRS 173
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 988-1034 5.41e-04

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 41.47  E-value: 5.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1678550997   988 IGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVSLKDIFAHPTVEGLA 1034
Cdd:smart00823   33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 835-901 7.16e-04

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 45.31  E-value: 7.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678550997  835 VIMYRTGDLARrLEDGN---------IEYI-GRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHEL 901
Cdd:cd05913    290 LIRYRTRDITR-LLPGPcpcgrthrrIDRItGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDEL 365
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 2651-2700 7.24e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 45.48  E-value: 7.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1678550997 2651 EILTIESVEEDDK-SPLPQMSSA-HHLAYIIYTSGTTGRPKGVMVEHKG-IAN 2700
Cdd:PLN02736   197 EIVTYSKLLAQGRsSPQPFRPPKpEDVATICYTSGTTGTPKGVVLTHGNlIAN 249
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 1495-1977 1.31e-03

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: 44.57  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1495 TLHYALEQQAEKTPDQAAVIF--EDGV---MTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGILKAGG 1569
Cdd:cd05943     69 RLNYAENLLRHADADDPAAIYaaEDGErteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1570 AYLPIDPDYPE----ERIS-----FLLEDSG-----------TNILLLQsAGLhvPEFTgEIVYLNQTNSGLAHRLS-NP 1628
Cdd:cd05943    149 IWSSCSPDFGVpgvlDRFGqiepkVLFAVDAytyngkrhdvrEKVAELV-KGL--PSLL-AVVVVPYTVAAGQPDLSkIA 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1629 NVDVLPQSLA------------------YVIYTSGSTGMPK-------GVEIEHRSAVnflnSLQSryQLKHSDMIMHKT 1683
Cdd:cd05943    225 KALTLEDFLAtgaagelefeplpfdhplYILYSSGTTGLPKcivhgagGTLLQHLKEH----ILHC--DLRPGDRLFYYT 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1684 SYSfdasiWELFWWP----YAGASVYLL---PqgGEKEPEVIAKAIEEQKITAM-------------HFVP------SML 1737
Cdd:cd05943    299 TCG-----WMMWNWLvsglAVGATIVLYdgsP--FYPDTNALWDLADEEGITVFgtsakyldalekaGLKPaethdlSSL 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1738 HAFLE------HIKYRSVP--IKTNRLKRVFSGGeqlgTHLVSRFYELLPNVSITnsygPTE-------ATVEAafFDCP 1802
Cdd:cd05943    372 RTILStgsplkPESFDYVYdhIKPDVLLASISGG----TDIISCFVGGNPLLPVY----RGEiqcrglgMAVEA--FDEE 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1803 phekleripiGKPVhhvrlyllnqnqrmlpVGCIGELYIAgagvaRGYLNRPAlteeRFLEDP---------F--YPGer 1871
Cdd:cd05943    442 ----------GKPV----------------WGEKGELVCT-----KPFPSMPV----GFWNDPdgsryraayFakYPG-- 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1872 MYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA-AVTVRTDSGEPELCAYV---EGLQ---- 1943
Cdd:cd05943    485 VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSlVVGQEWKDGDERVILFVklrEGVEldde 564

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1678550997 1944 -RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 1977
Cdd:cd05943    565 lRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
PRK07868 PRK07868
acyl-CoA synthetase; Validated
 1500-1580 2.06e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 44.32  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1500 LEQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLGIYGI--LKAGGAYLPIDPD 1577
Cdd:PRK07868   453 IAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALsrLGAVAVLMPPDTD 532


                   ...
gi 1678550997 1578 YPE 1580
Cdd:PRK07868   533 LAA 535
PLN02654 PLN02654
acetate-CoA ligase
 1639-1924 2.63e-03

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 43.73  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1639 YVIYTSGSTGMPKGVEieHRSAvnflnslqsryqlkhSDMIMHKTS--YSFDASIWELFW------W----------PYA 1700
Cdd:PLN02654   279 FLLYTSGSTGKPKGVL--HTTG---------------GYMVYTATTfkYAFDYKPTDVYWctadcgWitghsyvtygPML 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1701 GASVYLLPQGGEKEPEV--IAKAIEEQKITAMHFVPSMLHAFL----EHIKYRSvpikTNRLKRVFSGGEQLGTHLVSRF 1774
Cdd:PLN02654   342 NGATVLVFEGAPNYPDSgrCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRHS----RKSLRVLGSVGEPINPSAWRWF 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 1775 YELLPN--VSITNSYGPTEAtveAAFFDCPPHEKLERIPIGK--PVHHVRLYLLNQNQRMLPVGCIGELYIAGA--GVAR 1848
Cdd:PLN02654   418 FNVVGDsrCPISDTWWQTET---GGFMITPLPGAWPQKPGSAtfPFFGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFR 494

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678550997 1849 GYLNrpalTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 1924
Cdd:PLN02654   495 TLYG----DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAV 566
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
2108-2233 5.22e-03

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 42.39  E-value: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678550997 2108 TGYNMpavlELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDEVPFTLQttVLGARTEQEAAAAfikPFD 2187
Cdd:PRK09294    24 TGYTA----HLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLHPGIV--VVDGDAARPLPEL---QLD 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1678550997 2188 LSQApLFRAQIVKVSDERHLLLVdMHHIISDGVSVNILIQEFGELY 2233
Cdd:PRK09294    95 QGVS-LLALDVVPDDGGARVTLY-IHHSIADAHHSASLLDELWSRY 138
 
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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