|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
6-657 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 1289.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 6 YSVKVGEPTPAGGGRPSAGPVYRSIYAKDGLMPLPKEIQSPWDFFSEAVKKYPKNRMLGQRQVSDGKAGDYVWQTYEEVY 85
Cdd:PLN02861 5 YTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTYKEVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 86 QKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIKSLL 165
Cdd:PLN02861 85 DAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 166 AILPKCTAHIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGVIITNRA 245
Cdd:PLN02861 165 SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 246 IIAGVMTTENLLELTDKVVSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQVMKPTIFCGVPRVYD 325
Cdd:PLN02861 245 IIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 326 RIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGFKQHEASPFFDKIVFSKIKEGLGGRIRLMLSGAAPLPRHIEEFMR 405
Cdd:PLN02861 325 RIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 406 VTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESIPEMGYDALSNVPRGEICLRGHTLFSGYYKRPD 485
Cdd:PLN02861 405 VTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYHKRQD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 486 LTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESFLVAVVVPEK 565
Cdd:PLN02861 485 LTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDR 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 566 QAIEDWAALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKDLITPTFKLKRPQLLKYY 645
Cdd:PLN02861 565 QALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYY 644
|
650
....*....|..
gi 357156424 646 KDRVDQLYKDAK 657
Cdd:PLN02861 645 KDCIDQLYSEAK 656
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
2-661 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 875.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 2 EEKMYSVKVGEPTPAGGGRPSAGPVYRSIYAKDGLmPLPKE-IQSPWDFFSEAVKKYPKNRMLGQRQVSDGKAGDYVWQT 80
Cdd:PLN02614 3 QQKKFIFQVEEGKEGSDGRPSVGPVYRSIFAKDGF-PNPIEgMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 81 YEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASK 160
Cdd:PLN02614 82 YQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 161 IKSLLAILPKCTAHIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTMGTETQ-DISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PLN02614 162 ISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQyDLPIKKKSDICTIMYTSGTTGDPKGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAI---IAGVMtteNLLELTDKVVSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQVMKPTI 316
Cdd:PLN02614 242 MISNESIvtlIAGVI---RLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 317 FCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGFKQHEASPFFDKIVFSKIKEGLGGRIRLMLSGAAPL 396
Cdd:PLN02614 319 FCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 397 PRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESIPEMGYDALSNVPRGEICLRGHTL 476
Cdd:PLN02614 399 ASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 477 FSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF 556
Cdd:PLN02614 479 FSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESF 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 557 LVAVVVPEKQAIEDWAALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKDLITPTFKL 636
Cdd:PLN02614 559 LVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKK 638
|
650 660
....*....|....*....|....*
gi 357156424 637 KRPQLLKYYKDRVDQLYKDAKMATA 661
Cdd:PLN02614 639 KRPQLLKYYQSVIDEMYKTTNEKLA 663
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
4-654 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 820.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 4 KMYSVKVGEPTPAGGGRPSAGPVYRSIYAKDGLMPLPKEIQSPWDFFSEAVKKYPKNRMLGQRQVSDGKAGDYVWQTYEE 83
Cdd:PLN02430 2 KSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 84 VYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIKS 163
Cdd:PLN02430 82 VYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 164 LLAILPKCTAHIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTMGTET-QDISRKQKDDICTIMYTSGTTGDPKGVIIT 242
Cdd:PLN02430 162 LLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENpSETNPPKPLDICTIMYTSGTSGDPKGVVLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 243 NRAIIAGVMTTENLLELTDKVVSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQVMKPTIFCGVPR 322
Cdd:PLN02430 242 HEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 323 VYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGFKQHEASPFFDKIVFSKIKEGLGGRIRLMLSGAAPLPRHIEE 402
Cdd:PLN02430 322 VFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 403 FMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESIPEMGYDALSNVPRGEICLRGHTLFSGYYK 482
Cdd:PLN02430 402 FLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 483 RPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESFLVAVVV 562
Cdd:PLN02430 482 NPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 563 PEKQAIEDWAALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKDLITPTFKLKRPQLL 642
Cdd:PLN02430 562 PNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLL 641
|
650
....*....|..
gi 357156424 643 KYYKDRVDQLYK 654
Cdd:PLN02430 642 KYYQVEIDEMYR 653
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
74-654 |
0e+00 |
|
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: 803.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVK--PGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEI 151
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 152 SIAFVQASkiksllailpkctahikaivsfgdvtnelkreveqlrVSCFSWEEFSTMGTETQ-DISRKQKDDICTIMYTS 230
Cdd:cd05927 81 SIVFCDAG-------------------------------------VKVYSLEEFEKLGKKNKvPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 231 GTTGDPKGVIITNRAIIAGVMTTENLLELTDKVvSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQ 310
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNKI-NPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 VMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGfkQHEASPFFDKIVFSKIKEGLGGRIRLML 390
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSG--VVRASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSmIGTVGPPVTAIQARLESIPEMGYDALSNVPRGEIC 470
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDVPEMNYDAKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVY 549
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 550 GNSFESFLVAVVVPEKQAIEDWAALNNK-TSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKD 628
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAASKGGgTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
570 580
....*....|....*....|....*.
gi 357156424 629 LITPTFKLKRPQLLKYYKDRVDQLYK 654
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2-654 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 620.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 2 EEKMYSVKVGEptpagggRPSAGP--VYRSIYAKDGLM---PLPKEIQSPWDFFSEAVKKYPKNRMLGQRQVSDGKAGDY 76
Cdd:PLN02736 4 HEQGYSVVLPE-------KLQTGKwnVYRSARSPLKLVsrfPDHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDGTVGEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 77 VWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFV 156
Cdd:PLN02736 77 KWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 157 QASKIKSLLAILPKCTAhIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTMGTETQDISRKQK-DDICTIMYTSGTTGD 235
Cdd:PLN02736 157 VPQTLNTLLSCLSEIPS-VRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKpEDVATICYTSGTTGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 236 PKGVIITNRAIIAGVMTTENLLELtdkvvSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQVMKPT 315
Cdd:PLN02736 236 PKGVVLTHGNLIANVAGSSLSTKF-----YPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 316 IFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGfkqHEASPFFDKIVFSKIKEGLGGRIRLMLSGAAP 395
Cdd:PLN02736 311 IFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENG---KNPSPMWDRLVFNKIKAKLGGRVRFMSSGASP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 396 LPRHIEEFMRVTGCCALAQGYGLTEScaGCFTSIANIF-SMIGTVGPPVTAIQARLESIPEMGY-DALSNVPRGEICLRG 473
Cdd:PLN02736 388 LSPDVMEFLRICFGGRVLEGYGMTET--SCVISGMDEGdNLSGHVGSPNPACEVKLVDVPEMNYtSEDQPYPRGEICVRG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 474 HTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGNS 552
Cdd:PLN02736 466 PIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 553 FESFLVAVVVPEKQAIEDWAALN-NKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKDLIT 631
Cdd:PLN02736 546 LNSSLVAVVVVDPEVLKAWAASEgIKYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLT 625
|
650 660
....*....|....*....|...
gi 357156424 632 PTFKLKRPQLLKYYKDRVDQLYK 654
Cdd:PLN02736 626 PTFKVKRPQAKAYFAKAISDMYA 648
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
74-638 |
0e+00 |
|
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: 537.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISi 153
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 afvqaskiksllailpkctahikAIVsfgdvTNelkreveqlrvscfsweefstmgtetqdisrKQKDDICTIMYTSGTT 233
Cdd:cd17639 80 -----------------------AIF-----TD-------------------------------GKPDDLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 234 GDPKGVIITNRAIIAGVMTtenLLELTDKVVSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFwqGDIRYLME------ 307
Cdd:cd17639 101 GNPKGVMLTHGNLVAGIAG---LGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgc 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 --DVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGFKqheaSPFFDKIVFSKIKEGLGGR 385
Cdd:cd17639 176 kgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG----TPLLDELVFKKVRAALGGR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPLPRHIEEFMRVTgCCALAQGYGLTESCA-GCFTSIANIFSmiGTVGPPVTAIQARLESIPEMGYDALSNV 464
Cdd:cd17639 252 LRYMLSGGAPLSADTQEFLNIV-LCPVIQGYGLTETCAgGTVQDPGDLET--GRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 465 PRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLV 543
Cdd:cd17639 329 PRGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 544 TSVWVYGNSFESFLVAVVVPEKQAIEDWA-ALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVP 622
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAeKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 357156424 623 FGIEKDLITPTFKLKR 638
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
48-656 |
2.17e-179 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 522.74 E-value: 2.17e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKNRMLGQRqvsdgKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG 127
Cdd:COG1022 15 DLLRRRAARFPDRVALREK-----EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 128 ICYVPLYDTLGPNAVEFILDHAEISIAFV----QASKIKSLLAILPkctaHIKAIVSFGDvtnelkrEVEQLRVSCFSWE 203
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVedqeQLDKLLEVRDELP----SLRHIVVLDP-------RGLRDDPRLLSLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 204 EFSTMGTETQD-------ISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPL 276
Cdd:COG1022 159 ELLALGREVADpaelearRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLG-----PGDRTLSFLPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 277 AHIFDQVIENYCIFKGASIGFWQgDIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYN----- 351
Cdd:COG1022 234 AHVFERTVSYYALAAGATVAFAE-SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAvgrry 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 352 --YKLANLRKGFKQHEASPFFDKIVFSKIKEGLGGRIRLMLSGAAPLPRHIEEFMR---VTgccaLAQGYGLTESCAGCF 426
Cdd:COG1022 313 arARLAGKSPSLLLRLKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRalgIP----VLEGYGLTETSPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 427 TSIANIFsMIGTVGPPVTAIQARLEsipemgydalsnvPRGEICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQ 505
Cdd:COG1022 389 VNRPGDN-RIGTVGPPLPGVEVKIA-------------EDGEILVRGPNVMKGYYKNPEATAEAFDaDGWLHTGDIGELD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 506 PDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSfESFLVAVVVPEKQAIEDWAALNNKT-SDFAEL 584
Cdd:COG1022 455 EDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAEL 533
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 585 CNDPKARRYIQDELNKTGKklGLRGFEMLRAVHLEPVPFGIEKDLITPTFKLKRPQLLKYYKDRVDQLYKDA 656
Cdd:COG1022 534 AQDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
40-653 |
3.87e-139 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 422.60 E-value: 3.87e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 40 PKEIQSPWD-------FFSEAVKKYPKNRMLGQRQV--------SDGKA------GDYVWQTYEEVYQKVIKIGAAIRSF 98
Cdd:PLN02387 47 PELVETPWEgattlaaLFEQSCKKYSDKRLLGTRKLisrefetsSDGRKfeklhlGEYEWITYGQVFERVCNFASGLVAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 99 GVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIKSLLAILPKCTAhIKAI 178
Cdd:PLN02387 127 GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLET-VKRV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 179 VSF---GDVTNELKREVEQLRVSCFSweEFSTMGTETQ-DISRKQKDDICTIMYTSGTTGDPKGVIITNR---AIIAGVM 251
Cdd:PLN02387 206 IYMddeGVDSDSSLSGSSNWTVSSFS--EVEKLGKENPvDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGnivATVAGVM 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 252 TTENLLeltdkvvSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFwqGDIRYLME-----------DVQVMKPTIFCGV 320
Cdd:PLN02387 284 TVVPKL-------GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 321 PRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLrkgfkqhEASPF---------FDKIVFSKIKEGLGGRIRLMLS 391
Cdd:PLN02387 355 PAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAI-------EGSWFgawglekllWDALVFKKIRAVLGGRIRFMLS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 392 GAAPLPRHIEEFMRVTGCCALAQGYGLTESCAG-CFTSIANifSMIGTVGPPVTAIQARLESIPEMGYDAL-SNVPRGEI 469
Cdd:PLN02387 428 GGAPLSGDTQRFINICLGAPIGQGYGLTETCAGaTFSEWDD--TSVGRVGPPLPCCYVKLVSWEEGGYLISdKPMPRGEI 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 470 CLRGHTLFSGYYKRPDLTEEVFSDG-----WFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVT 544
Cdd:PLN02387 506 VIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVD 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 545 SVWVYGNSFESFLVAVVVPEKQAIEDWA-ALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPF 623
Cdd:PLN02387 586 NIMVHADPFHSYCVALVVPSQQALEKWAkKAGIDYSNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPW 665
|
650 660 670
....*....|....*....|....*....|
gi 357156424 624 GIEKDLITPTFKLKRPQLLKYYKDRVDQLY 653
Cdd:PLN02387 666 TPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
74-641 |
1.44e-128 |
|
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: 386.95 E-value: 1.44e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI 153
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQAskiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqKDDICTIMYTSGTT 233
Cdd:cd05907 81 LFVED-------------------------------------------------------------PDDLATIIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 234 GDPKGVIITNRAIIAgvmTTENLLELTDKvvSEDDSYFSYLPLAHIFDQV-IENYCIFKGASIGFWQgDIRYLMEDVQVM 312
Cdd:cd05907 100 GRPKGVMLSHRNILS---NALALAERLPA--TEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDDLSEV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 KPTIFCGVPRVYDRIYTGINLKIQSGGLigKQIFQYAYnyklanlrkgfkqheaspffdkivfskikeglGGRIRLMLSG 392
Cdd:cd05907 174 RPTVFLAVPRVWEKVYAAIKVKAVPGLK--RKLFDLAV--------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 393 AAPLPRHIEEFMRVTGCCALaQGYGLTESCAGCFTSIANIFSmIGTVGPPVTAIQARLesipemgydalsnVPRGEICLR 472
Cdd:cd05907 220 GAPLPAELLHFFRALGIPVY-EGYGLTETSAVVTLNPPGDNR-IGTVGKPLPGVEVRI-------------ADDGEILVR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 473 GHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGN 551
Cdd:cd05907 285 GPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGD 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 552 SfESFLVAVVVPEKQAIEDWAALNNKT-SDFAELCNDPKARRYIQDELNKTGKKLGLrgFEMLRAVHLEPVPFGIEKDLI 630
Cdd:cd05907 365 G-RPFLVALIVPDPEALEAWAEEHGIAyTDVAELAANPAVRAEIEAAVEAANARLSR--YEQIKKFLLLPEPFTIENGEL 441
|
570
....*....|.
gi 357156424 631 TPTFKLKRPQL 641
Cdd:cd05907 442 TPTLKLKRPVI 452
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
80-655 |
2.42e-123 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 382.02 E-value: 2.42e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTAHIKAIVSFGdvtnELKREVEQLRVSCFSWEEFSTMGTETQDI----SRKQKDDICTIMYTSGTTGD 235
Cdd:PTZ00216 203 NVPNLLRLMKSGGMPNTTIIYLD----SLPASVDTEGCRLVAWTDVVAKGHSAGSHhplnIPENNDDLALIMYTSGTTGD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 236 PKGVIITNRAIIAGVMTTEN-LLELTDKVvSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFwqGDIRYLME------- 307
Cdd:PTZ00216 279 PKGVMHTHGSLTAGILALEDrLNDLIGPP-EEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfarphg 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 DVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGfkqhEASPFFDKIVFSKIKEGLGGRIR 387
Cdd:PTZ00216 356 DLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEG----KDTPYWNEKVFSAPRAVLGGRVR 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 LMLSGAAPLPRHIEEFMRVT-GCcaLAQGYGLTESCagCFTSIANIFSM-IGTVGPPVTAIQARLESIPEMGY-DALSnv 464
Cdd:PTZ00216 432 AMLSGGGPLSAATQEFVNVVfGM--VIQGWGLTETV--CCGGIQRTGDLePNAVGQLLKGVEMKLLDTEEYKHtDTPE-- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 465 PRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLV 543
Cdd:PTZ00216 506 PRGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELV 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 544 T--SVWVYGNSFESFLVAVVVPEKQAIEDWAALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHL--- 618
Cdd:PTZ00216 586 VpnGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVlsd 665
|
570 580 590
....*....|....*....|....*....|....*..
gi 357156424 619 EPVPfgiEKDLITPTFKLKRPQLLKYYKDRVDQLYKD 655
Cdd:PTZ00216 666 EWTP---ENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
74-523 |
2.89e-111 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 341.21 E-value: 2.89e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI 153
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQAS-KIKSLLAILPKCTAHIKAIVSfgDVTNELKREVEQLRVSCFSWEEFstmgtetqDISRKQKDDICTIMYTSGT 232
Cdd:pfam00501 97 LITDDAlKLEELLEALGKLEVVKLVLVL--DRDPVLKEEPLPEEAKPADVPPP--------PPPPPDPDDLAYIIYTSGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 233 TGDPKGVIITNRAIIAGVMTTENLLELTDKVVsEDDSYFSYLPLAHIFDQVIENYC-IFKGASIGFWQGDIRY----LME 307
Cdd:pfam00501 167 TGKPKGVMLTHRNLVANVLSIKRVRPRGFGLG-PDDRVLSTLPLFHDFGLSLGLLGpLLAGATVVLPPGFPALdpaaLLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 DVQVMKPTIFCGVPRVYDRIytginlkiqsggligkqifqyaynyklanLRKGFkqheaspffdkivfskIKEGLGGRIR 387
Cdd:pfam00501 246 LIERYKVTVLYGVPTLLNML-----------------------------LEAGA----------------PKRALLSSLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 LMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANI--FSMIGTVGPPVTAIQARLESIPEMGYDALSNVp 465
Cdd:pfam00501 281 LVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDedLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEP- 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 466 rGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLS 523
Cdd:pfam00501 360 -GELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
74-639 |
1.59e-80 |
|
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: 263.07 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI 153
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQASKiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTT 233
Cdd:cd17640 81 LVVENDS------------------------------------------------------------DDLATIIYTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 234 GDPKGVIITNRAIIAGVmttENLLELTDKVVSedDSYFSYLPLAHIFDQVIENYCIFKGASIGFwqGDIRYLMEDVQVMK 313
Cdd:cd17640 101 GNPKGVMLTHANLLHQI---RSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 314 PTIFCGVPRVYDRIYTGInlkiqsggligkqifqyaynyklanlrkgFKQHEASPFFDKIVFSKIKegLGGRIRLMLSGA 393
Cdd:cd17640 174 PHYIVSVPRLWESLYSGI-----------------------------QKQVSKSSPIKQFLFLFFL--SGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 394 APLPRHIEEFMRVTGCcALAQGYGLTESCAG--CFTSIANIfsmIGTVGPPVTAIQARLesipemgYDALSNVP-----R 466
Cdd:cd17640 223 GALPPHVDTFFEAIGI-EVLNGYGLTETSPVvsARRLKCNV---RGSVGRPLPGTEIKI-------VDPEGNVVlppgeK 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 467 GEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTS 545
Cdd:cd17640 292 GIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQ 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 546 VWVYGNSfESFLVAVVVPEKQAIEDWAALNNK--TSDFAELCNDPKARRYIQDELNKT-GKKLGLRGFEMLRAVHLEPVP 622
Cdd:cd17640 372 IMVVGQD-QKRLGALIVPNFEELEKWAKESGVklANDRSQLLASKKVLKLYKNEIKDEiSNRPGFKSFEQIAPFALLEEP 450
|
570
....*....|....*..
gi 357156424 623 FgIEKDLITPTFKLKRP 639
Cdd:cd17640 451 F-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
74-645 |
7.56e-80 |
|
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: 262.40 E-value: 7.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI 153
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFV-QASKIKSLLAILPKctAHIKAIVSFGDVTNELkreveqlrvscFSWEEFSTMGTETQDISRKQKDDICTIMYTSGT 232
Cdd:cd05932 82 LFVgKLDDWKAMAPGVPE--GLISISLPPPSAANCQ-----------YQWDDLIAQHPPLEERPTRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 233 TGDPKGVIITNRAIiagVMTTENLLELTDkvVSEDDSYFSYLPLAHIFDQV-IENYCIFKGASIGFWQgDIRYLMEDVQV 311
Cdd:cd05932 149 TGQPKGVMLTFGSF---AWAAQAGIEHIG--TEENDRMLSYLPLAHVTERVfVEGGSLYGGVLVAFAE-SLDTFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 312 MKPTIFCGVPRVYDRIYTGINLKIqsggliGKQifqyaynyKLANLRKgfkqheaSPFFDKIVFSKIKEGLG-GRIRLML 390
Cdd:cd05932 223 ARPTLFFSVPRLWTKFQQGVQDKI------PQQ--------KLNLLLK-------IPVVNSLVKRKVLKGLGlDQCRLAG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAAPLPRHIEEFMRVTGCcALAQGYGLTESCAgcfTSIANI--FSMIGTVGPPVTAIQARLEsipemgydalsnvPRGE 468
Cdd:cd05932 282 CGSAPVPPALLEWYRSLGL-NILEAYGMTENFA---YSHLNYpgRDKIGTVGNAGPGVEVRIS-------------EDGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 469 ICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVW 547
Cdd:cd05932 345 ILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVC 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 548 VYGNSFeSFLVAVVVPekqaiedwaalnnktSDFAELCNDPKARRYIQDELNKTGKKLG--LRGFEMLRAVHLEPVPFGI 625
Cdd:cd05932 425 VIGSGL-PAPLALVVL---------------SEEARLRADAFARAELEASLRAHLARVNstLDSHEQLAGIVVVKDPWSI 488
|
570 580
....*....|....*....|
gi 357156424 626 EKDLITPTFKLKRPQLLKYY 645
Cdd:cd05932 489 DNGILTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
72-653 |
7.18e-79 |
|
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: 262.29 E-value: 7.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 72 KAGDYvWQ--TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMA-MQACSSQGICyVPLYDTLGPNAVEFILDH 148
Cdd:cd05933 1 KRGDK-WHtlTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAaVGAIFAGGIA-VGIYTTNSPEACQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 149 AEISIAFV----QASKIKSLLAILPkctaHIKAIVSFGDvtnelkrEVEQLRVSCFSWEEFSTMGTETQD------ISRK 218
Cdd:cd05933 79 SEANILVVenqkQLQKILQIQDKLP----HLKAIIQYKE-------PLKEKEPNLYSWDEFMELGRSIPDeqldaiISSQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAII---AGVMTTENLLELTDKvvseDDSYFSYLPLAHIFDQVIENY-CIFKGAS 294
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITwtaKAASQHMDLRPATVG----QESVVSYLPLSHIAAQILDIWlPIKVGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 295 IGFWQGDIR--YLMEDVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKL-ANLRKGFKQHEASPFF- 370
Cdd:cd05933 224 VYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLeTNLKLMGGESPSPLFYr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 371 --DKIVFSKIKEGLG-GRIRLMLSGAAPLPRHIEEFMrVTGCCALAQGYGLTEsCAGCFT-SIANIFSmIGTVGPPVTAI 446
Cdd:cd05933 304 laKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSE-TSGPHTiSNPQAYR-LLSCGKALPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 447 QARLESIPEMGYdalsnvprGEICLRGHTLFSGYYKRPDLTEE-VFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQG 525
Cdd:cd05933 381 KTKIHNPDADGI--------GEICFWGRHVFMGYLNMEDKTEEaIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 526 EYVA-VEVLESAYVQSPLVTSVWVYGNS--FESFLVAV---VVPEK---------QAIEDWAALNNKTSDFAELCN--DP 588
Cdd:cd05933 453 ENVPpVPIEDAVKKELPIISNAMLIGDKrkFLSMLLTLkceVNPETgepldelteEAIEFCRKLGSQATRVSEIAGgkDP 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357156424 589 KARRYIQDELNKTGKKLGLRGFEMLRAVHLePVPFGIEKDLITPTFKLKRPQLLKYYKDRVDQLY 653
Cdd:cd05933 533 KVYEAIEEGIKRVNKKAISNAQKIQKWVIL-EKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
47-648 |
2.16e-69 |
|
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: 232.78 E-value: 2.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 47 WDFFSEAVKKYPKNRMLgqrqVSDGKAgdyvwQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQ 126
Cdd:COG0318 2 ADLLRRAAARHPDRPAL----VFGGRR-----LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 127 GICYVPLYDTLGPNAVEFILDHAEISIAFVqaskiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefs 206
Cdd:COG0318 73 GAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 207 tmgtetqdisrkqkddiCTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIE- 285
Cdd:COG0318 103 -----------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT-----PGDVVLVALPLFHVFGLTVGl 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 286 NYCIFKGASI----GFWQGDIRYLMEDVQVmkpTIFCGVPRVYDRiytginlkiqsggligkqifqyaynykLANLrkgf 361
Cdd:COG0318 161 LAPLLAGATLvllpRFDPERVLELIERERV---TVLFGVPTMLAR---------------------------LLRH---- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 362 kqheasPFFDKIVFSkikeglggRIRLMLSGAAPLPRH-IEEFMRVTGCcALAQGYGLTE-SCAGCFTSIANIFSMIGTV 439
Cdd:COG0318 207 ------PEFARYDLS--------SLRLVVSGGAPLPPElLERFEERFGV-RIVEGYGLTEtSPVVTVNPEDPGERRPGSV 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 440 GPPVTAIQARLesIPEMGYDalsnVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:COG0318 272 GRPLPGVEVRI--VDEDGRE----LPPgevGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRK 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 517 KNIFKLSqGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAiedwaalnnkTSDFAELcndpkaRRY 593
Cdd:COG0318 346 KDMIISG-GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWgerVVAFVVLRPGA----------ELDAEEL------RAF 408
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 357156424 594 IQDElnktgkklgLRGFEMLRAVH-LEPVPfgiekdlITPTFKLKRPQLLKYYKDR 648
Cdd:COG0318 409 LRER---------LARYKVPRRVEfVDELP-------RTASGKIDRRALRERYAAG 448
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
186-655 |
4.71e-63 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 222.67 E-value: 4.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 186 NELKREVEQLRVSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTtenlleLTDKVVS 265
Cdd:PTZ00342 269 KDLKEKAKKLGISIILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVP------LCKHSIF 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 266 ED---DSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIG 342
Cdd:PTZ00342 343 KKynpKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 343 KQIFQyaynyKLANLRKGFKQHEASPFFDKI--VFSKIKEGLGGRIRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTE 420
Cdd:PTZ00342 423 RFLVK-----KILSLRKSNNNGGFSKFLEGIthISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 421 SCAGCFTSIANIFSMIGTVGP--PVTAIQARLESIpemgYDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVFS-DGWFH 497
Cdd:PTZ00342 498 TTGPIFVQHADDNNTESIGGPisPNTKYKVRTWET----YKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFK 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 498 TGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGN----------SFESFLVAVVVPEKQA 567
Cdd:PTZ00342 574 TGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDdsmdgplaiiSVDKYLLFKCLKDDNM 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 568 IEDW----AALNNKTSDfaELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIeKDLITPTFKLKRPQLLK 643
Cdd:PTZ00342 654 LESTgineKNYLEKLTD--ETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDT-NNYLTPTFKVKRFYVFK 730
|
490
....*....|....*
gi 357156424 644 YYK---DRVDQLYKD 655
Cdd:PTZ00342 731 DYAffiDQVKKIYKN 745
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
47-519 |
1.10e-59 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 207.42 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 47 WDFFSEAVKKYPknrmlgqrqvsDGKA--GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACS 124
Cdd:cd05936 2 ADLLEEAARRFP-----------DKTAliFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 125 SQGICYVPLYDTLGPNAVEFILDHAEISIAFVqaskiksllailpkctahikaIVSFGDVTNELKREVEQLRVScfswee 204
Cdd:cd05936 71 KAGAVVVPLNPLYTPRELEHILNDSGAKALIV---------------------AVSFTDLLAAGAPLGERVALT------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 205 fstmgtetqdisrkqKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLEltdKVVSEDDSYFSYLPLAHIFDQ-V 283
Cdd:cd05936 124 ---------------PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLE---DLLEGDDVVLAALPLFHVFGLtV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 284 IENYCIFKGASIGFWQG-DIRYLMEDVQVMKPTIFCGVPRvydrIYTGINlkiqsggligkqifqyaynyklanlrkgfk 362
Cdd:cd05936 186 ALLLPLALGATIVLIPRfRPIGVLKEIRKHRVTIFPGVPT----MYIALL------------------------------ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 363 QHEAspfFDKIVFSkikeglggRIRLMLSGAAPLPR-HIEEFMRVTGCcALAQGYGLTESC-AGCFTSIaNIFSMIGTVG 440
Cdd:cd05936 232 NAPE---FKKRDFS--------SLRLCISGGAPLPVeVAERFEELTGV-PIVEGYGLTETSpVVAVNPL-DGPRKPGSIG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 441 PPVTAIQARLesipemgYDALSN-VPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:cd05936 299 IPLPGTEVKI-------VDDDGEeLPPgevGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRK 371
|
...
gi 357156424 517 KNI 519
Cdd:cd05936 372 KDM 374
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
37-631 |
7.59e-59 |
|
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: 208.08 E-value: 7.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 37 MPLPKEIQSpwdffseAVKKYPKNRMLGQRQ---VSDGKAGDYVWQ--------TYEEVYQKVIKIGAAIRS-FGVKPGG 104
Cdd:cd17632 22 LRLAQIIAT-------VMTGYADRPALGQRAtelVTDPATGRTTLRllprfetiTYAELWERVGAVAAAHDPeQPVRPGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 105 HCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIKSLLAILPKCTAHIKAIV----- 179
Cdd:cd17632 95 FVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVVfdhrp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 180 SFGDVTNELKREVEQLRvscfswEEFSTMGTETQDISRKQK-------------DDICTIMYTSGTTGDPKGVIITNR-- 244
Cdd:cd17632 175 EVDAHRAALESARERLA------AVGIPVTTLTLIAVRGRDlppaplfrpepddDPLALLIYTSGSTGTPKGAMYTERlv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 245 --------AIIAGVMTTENLLeltdkvvseddsyfSYLPLAHIFDQVIENYCIFKGASIGFW-QGDIRYLMEDVQVMKPT 315
Cdd:cd17632 249 atfwlkvsSIQDIRPPASITL--------------NFMPMSHIAGRISLYGTLARGGTAYFAaASDMSTLFDDLALVRPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 316 IFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYKlANLRKgfkqheaspffdkivfskikEGLGGRIRLMLSGAAP 395
Cdd:cd17632 315 ELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVK-AELRE--------------------RVLGGRLLAAVCGSAP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 396 LPRHIEEFMRVTGCCALAQGYGLTEscagcftsiANIFSMIGTVG-PPVtaIQARLESIPEMGYDAL-SNVPRGEICLRG 473
Cdd:cd17632 374 LSAEMKAFMESLLDLDLHDGYGSTE---------AGAVILDGVIVrPPV--LDYKLVDVPELGYFRTdRPHPRGELLVKT 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 474 HTLFSGYYKRPDLTEEVF-SDGWFHTGDI-GEWQPDgTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGN 551
Cdd:cd17632 443 DTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPD-RLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGN 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 552 SFESFLVAVVVPEKQAIEDwaalnnktSDFAELcndpKARryIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKDLIT 631
Cdd:cd17632 522 SERAYLLAVVVPTQDALAG--------EDTARL----RAA--LAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
80-600 |
1.98e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 202.72 E-value: 1.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTaHIKAIVsfgdVTNELKREVEQLRVSCFswEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK06187 113 FVPLLAAILPQLP-TVRTVI----VEGDGPAAPLAPEVGEY--EELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTDkvvseDDSYFSYLPLAHIF-------------DQVIenycifkgasIG-FwqgDIRYL 305
Cdd:PRK06187 186 VLSHRNLFLHSLAVCAWLKLSR-----DDVYLVIVPMFHVHawglpylalmagaKQVI----------PRrF---DPENL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 306 MEDVQVMKPTIFCGVPRvydrIYTGInlkiqsggligkqifqyaynyklanLRkgfkqHEASPFFDkivFSkikeglggR 385
Cdd:PRK06187 248 LDLIETERVTFFFAVPT----IWQML-------------------------LK-----APRAYFVD---FS--------S 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPLPRH-IEEFMRVTGCcALAQGYGLTESC-AGCFT----SIANIFSMIGTVGPPVTAIQARL-----ESIP 454
Cdd:PRK06187 283 LRLVIYGGAALPPAlLREFKEKFGI-DLVQGYGMTETSpVVSVLppedQLPGQWTKRRSAGRPLPGVEARIvdddgDELP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 455 EMGYDAlsnvprGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYV-AVEvL 533
Cdd:PRK06187 362 PDGGEV------GEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIyPRE-L 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 534 ESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKqaiedwaalnNKTSDFAELcndpkaRRYIQDELNK 600
Cdd:PRK06187 434 EDALYGHPAVAEVAVIGVPDEKWgerPVAVVVLKP----------GATLDAKEL------RAFLRGRLAK 487
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-575 |
2.69e-56 |
|
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: 194.43 E-value: 2.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENYCIFKGASI----GF 297
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-----EGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 298 wqgDIRYLMEDVQVMKPTIFCGVPRVYDRIytginlkiqsggligkqifqyaynyklanlrkgfKQHEASPFFDkivFSk 377
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARL----------------------------------LKAPESAGYD---LS- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 378 ikeglggRIRLMLSGAAPLPRH-IEEFMRVTGCcALAQGYGLTESC-AGCFTSIANIFSMIGTVGPPVTAIQARLesIPE 455
Cdd:cd04433 115 -------SLRALVSGGAPLPPElLERFEEAPGI-KLVNGYGLTETGgTVATGPPDDDARKPGSVGRPVPGVEVRI--VDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 456 MGYDALSNVPrGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYVAVEVLES 535
Cdd:cd04433 185 DGGELPPGEI-GELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEA 262
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 357156424 536 AYVQSPLVTSVWVYG---NSFESFLVAVVVPEKQAIEDWAALN 575
Cdd:cd04433 263 VLLGHPGVAEAAVVGvpdPEWGERVVAVVVLRPGADLDAEELR 305
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
80-575 |
4.66e-56 |
|
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: 198.21 E-value: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTAHIKAIVSfgDVTNELKREVEQLrvscfsWEEFSTMGTETQDISRKQ-KDDICTIMYTSGTTGDPKG 238
Cdd:cd05911 92 GLEKVKEAAKELGPKDKIIVL--DDKPDGVLSIEDL------LSPTLGEEDEDLPPPLKDgKDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAGVMTTENLLELTDKVvseDDSYFSYLPLAHIFDQVIENYCIFKGAS-IGFWQGDIRYLMEDVQVMKPTIF 317
Cdd:cd05911 164 VCLSHRNLIANLSQVQTFLYGNDGS---NDVILGFLPLYHIYGLFTTLASLLNGATvIIMPKFDSELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 318 CGVPRVYdriytginlkiqsggligkqifqyaynYKLANlrkgfkqheaSPFFDKIVFSKIKEglggrirlMLSGAAPLP 397
Cdd:cd05911 241 YLVPPIA---------------------------AALAK----------SPLLDKYDLSSLRV--------ILSGGAPLS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 398 RHIEEFM-RVTGCCALAQGYGLTESCAGCFTSIANIFSMiGTVGPPVTAIQARLesIPEMGYDALSNVPRGEICLRGHTL 476
Cdd:cd05911 276 KELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKP-GSVGRLLPNVEAKI--VDDDGKDSLGPNEPGEICVRGPQV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 477 FSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSPLVTSVWVYG----N 551
Cdd:cd05911 353 MKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIGipdeV 431
|
490 500 510
....*....|....*....|....*....|
gi 357156424 552 SFESfLVAVVVPEK------QAIEDWAALN 575
Cdd:cd05911 432 SGEL-PRAYVVRKPgeklteKEVKDYVAKK 460
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
77-605 |
2.32e-55 |
|
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: 198.03 E-value: 2.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 77 VWQ--TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIA 154
Cdd:cd17641 8 IWQefTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 155 FV----QASKIKSLLAILPkctaHIKAIVSFgdvtnELK--REVEQLRVSCFswEEFSTMGTET---------QDISRKQ 219
Cdd:cd17641 88 IAedeeQVDKLLEIADRIP----SVRYVIYC-----DPRgmRKYDDPRLISF--EDVVALGRALdrrdpglyeREVAAGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 220 KDDICTIMYTSGTTGDPKGVIITNRAIIAgvmTTENLLELTDKvvSEDDSYFSYLPLAHIFDQVienYCIFKGASIGF-- 297
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLG---HCAAYLAADPL--GPGDEYVSVLPLPWIGEQM---YSVGQALVCGFiv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 298 -WQGDIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQY-------AYNYKLANLRKGFKQHEASPF 369
Cdd:cd17641 229 nFPEEPETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELgmklglrALDRGKRGRPVSLWLRLASWL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 370 FDKIVFSKIKEGLG-GRIRLMLSGAAPLPRHIEEFMRVTGCcALAQGYGLTESCaGCFTSIANIFSMIGTVGPPVTAIQA 448
Cdd:cd17641 309 ADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAIGV-PLKQLYGQTELA-GAYTVHRDGDVDPDTVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 449 RLesipemgydalSNVprGEICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEY 527
Cdd:cd17641 387 RI-----------DEV--GEILVRSPGVFVGYYKNPEATAEDFDeDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTR 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 528 VAVEVLESAYVQSPLVTSVWVYGNSFEsFLVAVVVPEKQAIEDWAALNNKT-SDFAELCNDPKARRYIQDELNKTGKKL 605
Cdd:cd17641 454 FSPQFIENKLKFSPYIAEAVVLGAGRP-YLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNASL 531
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
80-584 |
1.02e-53 |
|
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: 191.12 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQas 159
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd05914 87 -----------------------------------------------------------DEDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAI---IAGVMTTEnLLELTDKVVSeddsyfsYLPLAHIFDQVIEN-YCIFKGASIGFWQ---GDIRYLMEDVQVm 312
Cdd:cd05914 108 MLTYRNIvsnVDGVKEVV-LLGKGDKILS-------ILPLHHIYPLTFTLlLPLLNGAHVVFLDkipSAKIIALAFAQV- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 KPTIfcGVPRVYDRIYTGINLKIQSgglIGKQIFQYAYNYKLANLRkgfkqheaspfFDKIVFSKIKEGLGGRIRLMLSG 392
Cdd:cd05914 179 TPTL--GVPVPLVIEKIFKMDIIPK---LTLKKFKFKLAKKINNRK-----------IRKLAFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 393 AAPLPRHIEEFMRVTGCCAlAQGYGLTEsCAG--CFTSIANIfsMIGTVGPPVTAIQARLESIPEMGYDalsnvprGEIC 470
Cdd:cd05914 243 GAKINPDVEEFLRTIGFPY-TIGYGMTE-TAPiiSYSPPNRI--RLGSAGKVIDGVEVRIDSPDPATGE-------GEII 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVY 549
Cdd:cd05914 312 VRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 357156424 550 GNSFESFLVAVVVPE--------KQAIED---WAA---LNNKTSDFAEL 584
Cdd:cd05914 392 VQEKKLVALAYIDPDfldvkalkQRNIIDaikWEVrdkVNQKVPNYKKI 440
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
80-520 |
1.07e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 183.95 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAIlPKCTAHIKAIVSFGDvtnelkREVEQLRVSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK07656 112 FLGVDYSA-TTRLPALEHVVICET------EEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFD-QVIENYCIFKGASI----GFwqgDIRYLMEDVQVMKP 314
Cdd:PRK07656 185 MLTHRQLLSNAADWAEYLGLT-----EGDRYLAANPFFHVFGyKAGVNAPLMRGATIlplpVF---DPDEVFRLIETERI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 315 TIFCGVPRVYdriytginlkiqsggligkqifQYAYnyklanlrkgfkQHEASPFFDkivFSKikeglggrIRLMLSGAA 394
Cdd:PRK07656 257 TVLPGPPTMY----------------------NSLL------------QHPDRSAED---LSS--------LRLAVTGAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 395 PLP-RHIEEFMRVTGCCALAQGYGLTESC-AGCFTSIANIFSMI-GTVGPPVTAIQARLesIPEMGYDALSNVPrGEICL 471
Cdd:PRK07656 292 SMPvALLERFESELGVDIVLTGYGLSEASgVTTFNRLDDDRKTVaGTIGTAIAGVENKI--VNELGEEVPVGEV-GELLV 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 357156424 472 RGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIF 520
Cdd:PRK07656 369 RGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
80-563 |
7.45e-48 |
|
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: 174.34 E-value: 7.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFvqas 159
Cdd:cd17631 22 TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd17631 98 -------------------------------------------------------------DDLALLMYTSGTTGRPKGA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTenlleLTDKVVSEDDSYFSYLPLAHIF-DQVIENYCIFKGASI----GFwqgDIRYLMEDVQVMKP 314
Cdd:cd17631 117 MLTHRNLLWNAVNA-----LAALDLGPDDVLLVVAPLFHIGgLGVFTLPTLLRGGTVvilrKF---DPETVLDLIERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 315 TIFCGVPRVYDRIYtginlkiqsggligkqifqyaynyklanlrkgfkQHEASPFFDkivFSkikeglggRIRLMLSGAA 394
Cdd:cd17631 189 TSFFLVPTMIQALL----------------------------------QHPRFATTD---LS--------SLRAVIYGGA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 395 PLPRHIEEFMRVTGCcALAQGYGLTESCAG-CFTSIANIFSMIGTVGPPVTAIQARLESipemgyDALSNVP---RGEIC 470
Cdd:cd17631 224 PMPERLLRALQARGV-KFVQGYGMTETSPGvTFLSPEDHRRKLGSAGRPVFFVEVRIVD------PDGREVPpgeVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYVA-VEVlESAYVQSPLVTSVWVY 549
Cdd:cd17631 297 VRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYpAEV-EDVLYEHPAVAEVAVI 374
|
490
....*....|....*..
gi 357156424 550 GNSFESF---LVAVVVP 563
Cdd:cd17631 375 GVPDEKWgeaVVAVVVP 391
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
222-567 |
1.33e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 153.98 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENYC-IFKGASIGFWQG 300
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT-----EDDVLLHVLPLHHVHGLVNALLCpLFAGASVEFLPK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 301 DIRYLMEDVQVMKP-TIFCGVPRVYDRiytginlkiqsggligkqifqyaynyklanLRKGFKQHEASPFFdkivfsKIK 379
Cdd:cd05941 165 FDPKEVAISRLMPSiTVFMGVPTIYTR------------------------------LLQYYEAHFTDPQF------ARA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 380 EGLGgRIRLMLSGAAPLPRHI-EEFMRVTGCcALAQGYGLTEscagcftsianiFSMI-----------GTVGPPVTAIQ 447
Cdd:cd05941 209 AAAE-RLRLMVSGSAALPVPTlEEWEAITGH-TLLERYGMTE------------IGMAlsnpldgerrpGTVGMPLPGVQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 448 ARLesIPEMGYDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKK-NIFKlSQG 525
Cdd:cd05941 275 ARI--VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFtDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGG 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 357156424 526 EYV-AVEVlESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQA 567
Cdd:cd05941 352 YKVsALEI-ERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLRAGA 396
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
48-574 |
1.70e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 156.31 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKNRML---GQRQvsdgkagdyvwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACS 124
Cdd:PRK05605 36 DLYDNAVARFGDRPALdffGATT------------TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 125 SQGICYV---PLYDT---LGPNAvefilDH-AEISIAFvqaSKIKSLLAILPKCTAhIKAIVSFgDVTNE--------LK 189
Cdd:PRK05605 104 RLGAVVVehnPLYTAhelEHPFE-----DHgARVAIVW---DKVAPTVERLRRTTP-LETIVSV-NMIAAmpllqrlaLR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 190 REVEQLRVS----------CFSWEEF--STMGTETQDIS--RKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTEN 255
Cdd:PRK05605 174 LPIPALRKAraaltgpapgTVPWETLvdAAIGGDGSDVShpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 256 LL-ELTDKvvseDDSYFSYLPLAHIFDQVIenyCIFKGASIG-----FWQGDIRYLMedvQVMK---PTIFCGVPRVYDR 326
Cdd:PRK05605 254 WVpGLGDG----PERVLAALPMFHAYGLTL---CLTLAVSIGgelvlLPAPDIDLIL---DAMKkhpPTWLPGVPPLYEK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 327 IytginlkiqsggligkqifqyaynyklanlRKGFKQHEASpffdkivfskikegLGGrIRLMLSGAAPLPRHI-EEFMR 405
Cdd:PRK05605 324 I------------------------------AEAAEERGVD--------------LSG-VRNAFSGAMALPVSTvELWEK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 406 VTGCcALAQGYGLTEscagcfTS---IANIFS---MIGTVGPPVTAIQARLESiPEmgyDALSNVP---RGEICLRGHTL 476
Cdd:PRK05605 359 LTGG-LLVEGYGLTE------TSpiiVGNPMSddrRPGYVGVPFPDTEVRIVD-PE---DPDETMPdgeEGELLVRGPQV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 477 FSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNI-----FKLSQGEyvavevLESAYVQSPLVTSVWVYG- 550
Cdd:PRK05605 428 FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELiitggFNVYPAE------VEEVLREHPGVEDAAVVGl 501
|
570 580
....*....|....*....|....*..
gi 357156424 551 ---NSFESfLVAVVVPEKQAIEDWAAL 574
Cdd:PRK05605 502 preDGSEE-VVAAVVLEPGAALDPEGL 527
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
68-550 |
2.25e-38 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 149.32 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 68 VSDGKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG-ICYvPLYDTLGPNAVEFIL 146
Cdd:cd12119 15 VSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGaVLH-TINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 147 DHAEISIAFVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREVEQLrvscfSWEEFSTMGTETQDISRKQKDDICTI 226
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVL-----AYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 227 MYTSGTTGDPKGVIITNRAIIAGVMTtenlLELTDKV-VSEDDSYFSYLPLAHI------FdqvienycifkgasIGFWQ 299
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHAMA----ALLTDGLgLSESDVVLPVVPMFHVnawglpY--------------AAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 300 G-------------DIRYLMEDvqvMKPTIFCGVPRVYdriytginlkiqsggligKQIFQY--AYNYKLANLRkgfkqh 364
Cdd:cd12119 231 GaklvlpgpyldpaSLAELIER---EGVTFAAGVPTVW------------------QGLLDHleANGRDLSSLR------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 365 easpffdkivfskikeglggriRLMLSGAAPLPRHIEEF----MRVTgccalaQGYGLTESCA-GCF---------TSIA 430
Cdd:cd12119 284 ----------------------RVVIGGSAVPRSLIEAFeergVRVI------HAWGMTETSPlGTVarppsehsnLSED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 431 NIFSMIGTVGPPVTAIQARLESiPEMGYDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTM 510
Cdd:cd12119 336 EQLALRAKQGRPVPGVELRIVD-DDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYL 414
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357156424 511 KIIDRKKNIFKlSQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd12119 415 TITDRSKDVIK-SGGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
74-605 |
1.10e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 147.39 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI 153
Cdd:PRK08316 33 GDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQAskiksllAILPkctaHIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTM---GTETQDISRKQKDDICTIMYTS 230
Cdd:PRK08316 112 FLVDP-------ALAP----TAEAALALLPVDTLILSLVLGGREAPGGWLDFADWaeaGSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 231 GTTGDPKGVIITNRAIIAGVMTTenlleLTDKVVSEDDSYFSYLPLAHI--FDqVIENYCIFKGASIGFWQG-DIRYLME 307
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAEYVSC-----IVAGDMSADDIPLHALPLYHCaqLD-VFLGPYLYVGATNVILDApDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 DVQVMKPTIFCGVPRVYdriytginlkIqsgGLIGKQIFQyayNYKLANLRKGFkqheaspffdkivfskikeglggrir 387
Cdd:PRK08316 255 TIEAERITSFFAPPTVW----------I---SLLRHPDFD---TRDLSSLRKGY-------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 lmlSGAAPLPRHI-EEFMRVTGCCALAQGYGLTEscagcftsIANIFSMI---------GTVGPPVTAIQARLESipemg 457
Cdd:PRK08316 293 ---YGASIMPVEVlKELRERLPGLRFYNCYGQTE--------IAPLATVLgpeehlrrpGSAGRPVLNVETRVVD----- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 458 yDALSNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYVAV-EVL 533
Cdd:PRK08316 357 -DDGNDVAPgevGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASrEVE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 534 ESAYvQSPLVTSVWVYGNSFESFL---VAVVVPEKQAIEDWAALnnktsdfAELCND-------PKaRRYIQDEL--NKT 601
Cdd:PRK08316 435 EALY-THPAVAEVAVIGLPDPKWIeavTAVVVPKAGATVTEDEL-------IAHCRArlagfkvPK-RVIFVDELprNPS 505
|
....
gi 357156424 602 GKKL 605
Cdd:PRK08316 506 GKIL 509
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-601 |
1.20e-37 |
|
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: 145.13 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVqas 159
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkdDICTIMYTSGTTGDPKGV 239
Cdd:cd05934 82 --------------------------------------------------------------DPASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNR-AIIAGVMTTENLleltdkVVSEDDSYFSYLPLAHIFDQVIENY-CIFKGASI---------GFWQgDIR----Y 304
Cdd:cd05934 100 VITHAnLTFAGYYSARRF------GLGEDDVYLTVLPLFHINAQAVSVLaALSVGATLvllprfsasRFWS-DVRrygaT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 305 LMEDVQVMKPTIFCGVPRVYDRiytginlkiqsggligkqifqyaynyklanlrkgfkQHeaspffdkivfskikeglgg 384
Cdd:cd05934 173 VTNYLGAMLSYLLAQPPSPDDR------------------------------------AH-------------------- 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 385 RIRLMLsGAAPLPRHIEEFMRVTGCcALAQGYGLTESCAGCFTSI--ANIFSMIGTVGPpvtAIQARLesIPEMGYDALS 462
Cdd:cd05934 197 RLRAAY-GAPNPPELHEEFEERFGV-RLLEGYGMTETIVGVIGPRdePRRPGSIGRPAP---GYEVRI--VDDDGQELPA 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 463 NVPrGEICLR---GHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYV-AVEVlESAYV 538
Cdd:cd05934 270 GEP-GELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENIsSAEV-ERAIL 346
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 539 QSPLVTSVWVYG----NSFESFLVAVVVPEKQA---IEDWAALNNKTSDFaelcndpKARRYIQ--DELNKT 601
Cdd:cd05934 347 RHPAVREAAVVAvpdeVGEDEVKAVVVLRPGETldpEELFAFCEGQLAYF-------KVPRYIRfvDDLPKT 411
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
80-543 |
1.74e-37 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 147.18 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 -----KIKSLLAILPKCTA---HIKAIVSFGDVTNELKREveqlrvSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSG 231
Cdd:COG0365 121 glrggKVIDLKEKVDEALEelpSLEHVIVVGRTGADVPME------GDLDWDELLAAASAEFEPEPTDADDPLFILYTSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 232 TTGDPKGVIITNRAIIAGVMTT-ENLLELTdkvvsEDDSYFS--------------YLPLAH-----IFDQVIenycIFK 291
Cdd:COG0365 195 TTGKPKGVVHTHGGYLVHAATTaKYVLDLK-----PGDVFWCtadigwatghsyivYGPLLNgatvvLYEGRP----DFP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 292 GASIgFWQgdiryLMEDvqvMKPTIFCGVPRVYDRIytginlkIQSGGLIGKQifqyaynYKLANLrkgfkqheaspffd 371
Cdd:COG0365 266 DPGR-LWE-----LIEK---YGVTVFFTAPTAIRAL-------MKAGDEPLKK-------YDLSSL-------------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 372 kivfskikeglggriRLMLSGAAPLPRH-IEEFMRVTGCCaLAQGYGLTESCaGCFtsIANIFSM---IGTVGPPVTAIQ 447
Cdd:COG0365 309 ---------------RLLGSAGEPLNPEvWEWWYEAVGVP-IVDGWGQTETG-GIF--ISNLPGLpvkPGSMGKPVPGYD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 448 ARLesipemgYDALSN-VPR---GEICLRGH--TLFSGYYKRPDLTEEVFSD---GWFHTGDIGEWQPDGTMKIIDRKKN 518
Cdd:COG0365 370 VAV-------VDEDGNpVPPgeeGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDD 442
|
490 500
....*....|....*....|....*.
gi 357156424 519 IFKLSqGEYVA-VEVlESAYVQSPLV 543
Cdd:COG0365 443 VINVS-GHRIGtAEI-ESALVSHPAV 466
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
80-550 |
7.63e-37 |
|
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: 143.36 E-value: 7.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILdhAEISIAFVQAS 159
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQL--EDLDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kikSLLailpkcTAHIKAIVSFGDVTNELKREVEQLrvscfsweefstmgtetqdiSRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:TIGR01923 79 ---SLL------EEKDFQADSLDRIEAAGRYETSLS--------------------ASFNMDQIATLMFTSGTTGKPKAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRyLMEDVQVMKPTIFCG 319
Cdd:TIGR01923 130 PHTFRNHYASAVGSKENLGFT-----EDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ-LLEMIANERVTHISL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 VPRVYDRIytginlkiqsggligkqifqyaynyklanLRKGfkqheaspffdkivfskikeGLGGRIRLMLSGAAPLPRH 399
Cdd:TIGR01923 204 VPTQLNRL-----------------------------LDEG--------------------GHNENLRKILLGGSAIPAP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 400 IEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESIPEMGYdalsnvprGEICLRGHTLFSG 479
Cdd:TIGR01923 235 LIEEAQQYGL-PIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH--------GEIMVKGANLMKG 305
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357156424 480 YYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:TIGR01923 306 YLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVVP 375
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
77-550 |
1.01e-34 |
|
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: 138.20 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 77 VWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFV 156
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 157 QASkiksllailpkctahikaivsfgdvtnelkreveqlrvscFSWEEFSTMGTETQDISRKQ-KDDICTIMYTSGTTGD 235
Cdd:cd12118 108 DRE----------------------------------------FEYEDLLAEGDPDFEWIPPAdEWDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 236 PKGVIITNRAiiAGVMTTENLL--ELTDKVVseddsYFSYLPLAH---------IFDQVIENYCIFKGASIGFWQgdiry 304
Cdd:cd12118 148 PKGVVYHHRG--AYLNALANILewEMKQHPV-----YLWTLPMFHcngwcfpwtVAAVGGTNVCLRKVDAKAIYD----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 305 LMEDVQVmkpTIFCGVPRVYDRIytginlkiqsggligkqifqyaynyklANLRKGFKQHeaspffdkivfskikegLGG 384
Cdd:cd12118 216 LIEKHKV---THFCGAPTVLNML---------------------------ANAPPSDARP-----------------LPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 385 RIRLMLSGAAPlPRHIEEFMRVTGCCaLAQGYGLTEscagcftsianifsmigTVGPPV------------TAIQARLES 452
Cdd:cd12118 249 RVHVMTAGAPP-PAAVLAKMEELGFD-VTHVYGLTE-----------------TYGPATvcawkpewdelpTEERARLKA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 453 ---IPEMGYDALS--------NVPR-----GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:cd12118 310 rqgVRYVGLEEVDvldpetmkPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRS 389
|
490 500 510
....*....|....*....|....*....|....*
gi 357156424 517 KNIFkLSQGEYVA-VEVlESAYVQSPLVTSVWVYG 550
Cdd:cd12118 390 KDII-ISGGENISsVEV-EGVLYKHPAVLEAAVVA 422
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
80-550 |
1.03e-33 |
|
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: 133.63 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEIsiafvqas 159
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd05912 75 -----------------------------------------------------------KLDDIATIMYTSGTTGKPKGV 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTDkvvseDDSYFSYLPLAHIfdqvienycifKGASIgfwqgdirylmedvqVMKPTIFcG 319
Cdd:cd05912 96 QQTFGNHWWSAIGSALNLGLTE-----DDNWLCALPLFHI-----------SGLSI---------------LMRSVIY-G 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 VP-RVYDRI-YTGINLKIQSGGLIGKQIFQYAYNYKLANLRKGFKQHeaspffdkivfskikeglggrIRLMLSGAAPLP 397
Cdd:cd05912 144 MTvYLVDKFdAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNN---------------------LRCILLGGGPAP 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 398 RHIEEFMRVTGCcALAQGYGLTESCAGCFT-SIANIFSMIGTVGPPVTAIQARLESipemgyDALSNVPRGEICLRGHTL 476
Cdd:cd05912 203 KPLLEQCKEKGI-PVYQSYGMTETCSQIVTlSPEDALNKIGSAGKPLFPVELKIED------DGQPPYEVGEILLKGPNV 275
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357156424 477 FSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd05912 276 TKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVG 348
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
80-603 |
3.05e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 130.75 E-value: 3.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIR-SFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQA 158
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 SKIKSLLAIlpKCTAHIKAIVSFGDVTNELKREVEqlrvscfsweefstmgtetqDISRKQKDDICTIMYTSGTTGDPKG 238
Cdd:PRK06839 109 TFQNMALSM--QKVSYVQRVISITSLKEIEDRKID--------------------NFVEKNESASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENY-CIFKGASI---GFWQGDIRYLMedVQVMKP 314
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLT-----MHDRSIVLLPLFHIGGIGLFAFpTLFAGGVIivpRKFEPTKALSM--IEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 315 TIFCGVPRVYDRIYTginlkiqsggligkqifqyaynyklanlrkgfkqheaSPFFDKIVFSKIkeglggriRLMLSGAA 394
Cdd:PRK06839 240 TVVMGVPTIHQALIN-------------------------------------CSKFETTNLQSV--------RWFYNGGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 395 PLPrhiEEFMR--VTGCCALAQGYGLTESCAGCFTSIANIFS-MIGTVGPPVTAIQARLESipemgyDALSNVPRG---E 468
Cdd:PRK06839 275 PCP---EELMRefIDRGFLFGQGFGMTETSPTVFMLSEEDARrKVGSIGKPVLFCDYELID------ENKNKVEVGevgE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 469 ICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWV 548
Cdd:PRK06839 346 LLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 549 YGNSFESF---LVAVVVPEKQAIEDWAALNNKTSDFAELCNDPKaRRYIQDEL--NKTGK 603
Cdd:PRK06839 425 VGRQHVKWgeiPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK-EIVFLKELpkNATGK 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
70-521 |
1.09e-31 |
|
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: 129.28 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 70 DGKAGDYVwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHA 149
Cdd:cd05904 26 DAATGRAL--TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 150 EISIAFVQAskiksllAILPKCTAHIKAIVSFGDVtnelkrEVEQLRVSCFSWEEFSTMGTETQDisrKQkDDICTIMYT 229
Cdd:cd05904 104 GAKLAFTTA-------ELAEKLASLALPVVLLDSA------EFDSLSFSDLLFEADEAEPPVVVI---KQ-DDVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 230 SGTTGDPKGVIITNRAIIAGVmttENLLELTDKVVSEDDSYFSYLPLAHIFDQVIENYCIFK-GASI----GFwqgDIRY 304
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMV---AQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVvvmpRF---DLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 305 LMEDVQVMKPTIFCGVPRVydriytginlkiqsggligkqifqyaynykLANLRKgfkqheaSPFFDKIVFSKIkeglgg 384
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPI------------------------------VLALVK-------SPIVDKYDLSSL------ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 385 riRLMLSGAAPLPR-HIEEFMRVTGCCALAQGYGLTESCAG---CFTSIANIfSMIGTVGPPVTAIQARLESiPEMGyDA 460
Cdd:cd05904 278 --RQIMSGAAPLGKeLIEAFRAKFPNVDLGQGYGMTESTGVvamCFAPEKDR-AKYGSVGRLVPNVEAKIVD-PETG-ES 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 461 LSNVPRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFK 521
Cdd:cd05904 353 LPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
74-574 |
2.71e-31 |
|
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: 128.20 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAeisi 153
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 afvqaskiKSLLAILPKCTA--HIKAIVSFGDVTNELKREVEQLRVScFSWEEFSTM---GTETQDISRKQKDDICTIMY 228
Cdd:cd05926 86 --------GSKLVLTPKGELgpASRAASKLGLAILELALDVGVLIRA-PSAESLSNLladKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 229 TSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVienyC-----IFKGASI-------- 295
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLT-----PDDRTLVVMPLFHVHGLV----AsllstLAAGGSVvlpprfsa 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 296 -GFWQgdirylmeDVQVMKPTIFCGVPrvydriytginlkiqsggligkQIFQYaynykLANLRKGFKQHEASPffdkiv 374
Cdd:cd05926 228 sTFWP--------DVRDYNATWYTAVP----------------------TIHQI-----LLNRPEPNPESPPPK------ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 375 fskikeglggrIRLMLSGAAPL-PRHIEEFMRVTGCCALaQGYGLTESCAGCFTS-IANIFSMIGTVGPPVtAIQARLes 452
Cdd:cd05926 267 -----------LRFIRSCSASLpPAVLEALEATFGAPVL-EAYGMTEAAHQMTSNpLPPGPRKPGSVGKPV-GVEVRI-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 453 IPEMGyDALSNVPRGEICLRGHTLFSGYYKRPDLTEEV-FSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVE 531
Cdd:cd05926 332 LDEDG-EILPPGVVGEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPL 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 357156424 532 VLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAIEDWAAL 574
Cdd:cd05926 410 EVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLREGASVTEEEL 455
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
80-570 |
5.19e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 127.00 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPkctahikaiVSFGDVTNELKREVEQLrvscfswEEFSTmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:PRK03640 109 FEAKLIPGIS---------VKFAELMNGPKEEAEIQ-------EEFDL-------------DEVATIMYTSGTTGKPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IIT--NRAIIAgVMTTENLlELTdkvvsEDDSYFSYLPLAHIfdqvienycifKGASIgfwqgdirylmedvqVMKPTIF 317
Cdd:PRK03640 160 IQTygNHWWSA-VGSALNL-GLT-----EDDCWLAAVPIFHI-----------SGLSI---------------LMRSVIY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 318 cGVP-RVYDRI-YTGINLKIQSGGLIGKQIFQYAynykLANLRKGFKQHEASPFFdkivfskikeglggriRLMLSGAAP 395
Cdd:PRK03640 207 -GMRvVLVEKFdAEKINKLLQTGGVTIISVVSTM----LQRLLERLGEGTYPSSF----------------RCMLLGGGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 396 LPRHIEEFMRVTGCcALAQGYGLTESCAGCFT-SIANIFSMIGTVGPPVTAIQARLESipemgyDALSNVPR--GEICLR 472
Cdd:PRK03640 266 APKPLLEQCKEKGI-PVYQSYGMTETASQIVTlSPEDALTKLGSAGKPLFPCELKIEK------DGVVVPPFeeGEIVVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 473 GHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGNS 552
Cdd:PRK03640 339 GPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGVP 417
|
490 500
....*....|....*....|.
gi 357156424 553 FE---SFLVAVVVPEKQAIED 570
Cdd:PRK03640 418 DDkwgQVPVAFVVKSGEVTEE 438
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
29-602 |
6.00e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.97 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 29 SIYAKDGLMPLPKeiQSPWDFFSEAVKKYPKNRMLgqrqVSDGKAGDYVWQtyeEVYQKVIKIGAAIRSFGVKPGGHCGI 108
Cdd:PRK12583 5 SYYQGGGDKPLLT--QTIGDAFDATVARFPDREAL----VVRHQALRYTWR---QLADAVDRLARGLLALGVQPGDRVGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 109 YGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI-----AFVQASKIKSLLAILP-----KCTA----- 173
Cdd:PRK12583 76 WAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWvicadAFKTSDYHAMLQELLPglaegQPGAlacer 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 174 --HIKAIVSFGdvtnelKREVEQLRVscfsWEEFSTMG--TETQDISRKQ----KDDICTIMYTSGTTGDPKGVIITNRA 245
Cdd:PRK12583 156 lpELRGVVSLA------PAPPPGFLA----WHELQARGetVSREALAERQasldRDDPINIQYTSGTTGFPKGATLSHHN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 246 IIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENY-CIFKGASIGFWQGDIRYL--MEDVQVMKPTIFCGVPR 322
Cdd:PRK12583 226 ILNNGYFVAESLGLT-----EHDRLCVPVPLYHCFGMVLANLgCMTVGACLVYPNEAFDPLatLQAVEEERCTALYGVPT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 323 VYdriytginlkiqsggligkqifqyaynykLANLrkgfkQHeasPFFDKIVFSKIKEGlggrirLMlsGAAPLPrhIEE 402
Cdd:PRK12583 301 MF-----------------------------IAEL-----DH---PQRGNFDLSSLRTG------IM--AGAPCP--IEV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 403 FMRVTG---CCALAQGYGLTESCAGCFTSIAN--IFSMIGTVGppvtAIQARLESipeMGYDALSN-VPRGEI---CLRG 473
Cdd:PRK12583 334 MRRVMDemhMAEVQIAYGMTETSPVSLQTTAAddLERRVETVG----RTQPHLEV---KVVDPDGAtVPRGEIgelCTRG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 474 HTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGNS 552
Cdd:PRK12583 407 YSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFGVP 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357156424 553 FESF---LVAVVV--PEKQAIEDwaalnnktsDFAELCNDP----KARRYIQ--DELNKTG 602
Cdd:PRK12583 486 DEKYgeeIVAWVRlhPGHAASEE---------ELREFCKARiahfKVPRYFRfvDEFPMTV 537
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
74-592 |
6.75e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 124.33 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI 153
Cdd:PRK06188 34 GDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGIST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQASK-IKSLLAILPKCTAhIKAIVSFGDVtnELKREVeqlrvscfsWEEFSTMGTETQdISRKQKDDICTIMYTSGT 232
Cdd:PRK06188 113 LIVDPAPfVERALALLARVPS-LKHVLTLGPV--PDGVDL---------LAAAAKFGPAPL-VAAALPPDIAGLAYTGGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 233 TGDPKGVIITNRAiiagvMTTENLLELTDKVVSEDDSYFSYLPLAH----IFDQVIenyciFKGASIGFWQGdirylmed 308
Cdd:PRK06188 180 TGKPKGVMGTHRS-----IATMAQIQLAEWEWPADPRFLMCTPLSHaggaFFLPTL-----LRGGTVIVLAK-------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 309 vqvMKPTIFCGVPRVYdriytginlKIQSGGLIGKQIfqyaynYKLANlrkgfkqHEASPFFDkivFSKIKeglggrirL 388
Cdd:PRK06188 242 ---FDPAEVLRAIEEQ---------RITATFLVPTMI------YALLD-------HPDLRTRD---LSSLE--------T 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 389 MLSGAAPL-PRHIEEFMRVTGCcALAQGYGLTEsCAGCFTSIANIFSM------IGTVGPPVTAIQARLESipemgyDAL 461
Cdd:PRK06188 286 VYYGASPMsPVRLAEAIERFGP-IFAQYYGQTE-APMVITYLRKRDHDpddpkrLTSCGRPTPGLRVALLD------EDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 462 SNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKK--------NIFklsqgeyvAV 530
Cdd:PRK06188 358 REVAQgevGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKdmivtggfNVF--------PR 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357156424 531 EVlESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAiedwaalnnkTSDFAELCNDPKARR 592
Cdd:PRK06188 430 EV-EDVLAEHPAVAQVAVIGVPDEKWgeaVTAVVVLRPGA----------AVDAAELQAHVKERK 483
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
218-536 |
1.01e-29 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 123.21 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 218 KQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIenyCIF----KGA 293
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPN-----PEDVVFGALPFFHSFGLTG---CLWlpllSGI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 294 SIGFWQG--DIRYLMEDVQVMKPTIFCGVPrVYDRIYTginlkiqsggligkqifQYAYNYKLANLRkgfkqheaspffd 371
Cdd:cd05909 216 KVVFHPNplDYKKIPELIYDKKATILLGTP-TFLRGYA-----------------RAAHPEDFSSLR------------- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 372 kivfskikeglggrirLMLSGAAPLPRHI-EEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARL 450
Cdd:cd05909 265 ----------------LVVAGAEKLKDTLrQEFQEKFGI-RILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 451 ESIPemGYDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAV 530
Cdd:cd05909 328 VSVE--THEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSL 404
|
....*.
gi 357156424 531 EVLESA 536
Cdd:cd05909 405 EAIEDI 410
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
77-562 |
1.39e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 123.52 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 77 VWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFV 156
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 157 Q---ASKIKSLLAILPkctaHIKAIVSfgDVTNELKREVEqlRVSCFSWEEFSTMGTETQDISRKQKD-DICTIMYTSGT 232
Cdd:PRK08162 122 DtefAEVAREALALLP----GPKPLVI--DVDDPEYPGGR--FIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 233 TGDPKGVIITNRAiiAGVMTTENLLE--LTDKVVseddsYFSYLPLAH---------IFDQVIENYCIFKgasigFWQGD 301
Cdd:PRK08162 194 TGNPKGVVYHHRG--AYLNALSNILAwgMPKHPV-----YLWTLPMFHcngwcfpwtVAARAGTNVCLRK-----VDPKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 302 IRYLMEDVQVmkpTIFCGVPRVYDriytginlkiqsggligkqifqyaynyKLANLRKGFKqheaspffdkivfskikEG 381
Cdd:PRK08162 262 IFDLIREHGV---THYCGAPIVLS---------------------------ALINAPAEWR-----------------AG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 382 LGGRIRLMLSGAAPLPRHIEEfMRVTGCCaLAQGYGLTEscagcftsianifsmigTVGP-------------PVT---A 445
Cdd:PRK08162 295 IDHPVHAMVAGAAPPAAVIAK-MEEIGFD-LTHVYGLTE-----------------TYGPatvcawqpewdalPLDeraQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 446 IQAR-------LESIPEMGYDALSNVPR-----GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKII 513
Cdd:PRK08162 356 LKARqgvryplQEGVTVLDPDTMQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIK 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 357156424 514 DRKKNIFkLSQGEYVA-VEVlESAYVQSPLVtsvwvygnsfesfLVAVVV 562
Cdd:PRK08162 436 DRSKDII-ISGGENISsIEV-EDVLYRHPAV-------------LVAAVV 470
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
80-574 |
1.65e-29 |
|
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: 121.72 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQas 159
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfswEEFSTMGTEtqdisrKQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd05903 81 -------------------------------------------ERFRQFDPA------AMPDAVALLLFTSGTTGEPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIfdqvienycifkgasIGFWQGdirylmedvqVMKPTIFcG 319
Cdd:cd05903 112 MHSHNTLSASIRQYAERLGLG-----PGDVFLVASPMAHQ---------------TGFVYG----------FTLPLLL-G 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 VPRVYDRIYT---GINLKIQSGGLIGKQifqyaynyklanlrkgfkqheASPFFDKIVfsKIKEGLG---GRIRLMLSGA 393
Cdd:cd05903 161 APVVLQDIWDpdkALALMREHGVTFMMG---------------------ATPFLTDLL--NAVEEAGeplSRLRTFVCGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 394 APLPRHIEEFMRVTGCCALAQGYGLTESCaGCFTSI--ANIFSMIGTVGPPVTAIQARLesIPEMGyDALSNVPRGEICL 471
Cdd:cd05903 218 ATVPRSLARRAAELLGAKVCSAYGSTECP-GAVTSItpAPEDRRLYTDGRPLPGVEIKV--VDDTG-ATLAPGVEGELLS 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 472 RGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGN 551
Cdd:cd05903 294 RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAL 372
|
490 500
....*....|....*....|....*.
gi 357156424 552 SFESF---LVAVVVPEKQAIEDWAAL 574
Cdd:cd05903 373 PDERLgerACAVVVTKSGALLTFDEL 398
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
40-541 |
6.50e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 121.67 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 40 PKEI-----QSPWDFFSEAVKKYPKNRMLgqrqVSDGKAgdyvwQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCP 114
Cdd:PRK07059 14 PAEIdasqyPSLADLLEESFRQYADRPAF----ICMGKA-----ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 115 EWVMAMQACSSQGICYV---PLYDtlgPNAVEFILDHAEISIAFVQASKIKSLLAILPKcTAhIKAIV--SFGD------ 183
Cdd:PRK07059 85 QYPVAIAAVLRAGYVVVnvnPLYT---PRELEHQLKDSGAEAIVVLENFATTVQQVLAK-TA-VKHVVvaSMGDllgfkg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 184 -VTNELKREVEQLrVSCFS---WEEFSTMGTETQDISRK----QKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTEN 255
Cdd:PRK07059 160 hIVNFVVRRVKKM-VPAWSlpgHVRFNDALAEGARQTFKpvklGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 256 LLE--LTDKVVSEDDSYFSYLPLAHIFDQVIenyCIFKGASIGfwqG---------DIRYLMEDVQVMKPTIFCGVPRVY 324
Cdd:PRK07059 239 WLQpaFEKKPRPDQLNFVCALPLYHIFALTV---CGLLGMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 325 DriytginlkiqsggligkqifqyaynyKLANlrkgfkqheaSPFFDKIVFSKIKEGLGGrirlmlsGAAPLPRHIEEFM 404
Cdd:PRK07059 313 N---------------------------ALLN----------NPDFDKLDFSKLIVANGG-------GMAVQRPVAERWL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 405 RVTGCcALAQGYGLTES--CAGCFTSIANIFSmiGTVGPPV--TAIQARLESIPEMgydALSNVprGEICLRGHTLFSGY 480
Cdd:PRK07059 349 EMTGC-PITEGYGLSETspVATCNPVDATEFS--GTIGLPLpsTEVSIRDDDGNDL---PLGEP--GEICIRGPQVMAGY 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 481 YKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLS-------QGEYVAVE---VLESAYVQSP 541
Cdd:PRK07059 421 WNRPDETAKVMTaDGFFRTGDVGVMDERGYTKIVDRKKDMILVSgfnvypnEIEEVVAShpgVLEVAAVGVP 492
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-509 |
1.05e-28 |
|
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: 118.91 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRS-FGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDHAEISIAFVQ 157
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 158 aSKIKSLLAILPKCTAHIkAIVSFGDVTNELkreveqlrvscfsweefstmgTETQDISRKQKDDICTIMYTSGTTGDPK 237
Cdd:TIGR01733 80 -SALASRLAGLVLPVILL-DPLELAALDDAP---------------------APPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 238 GVIITNRAIIAGVMTTENLLELtdkvvSEDDSYFSYLPLAhiFD-QVIENY---------CIFKGASIGFWQGDIRYLME 307
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARRYGL-----DPDDRVLQFASLS--FDaSVEEIFgallagatlVVPPEDEERDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 DVQVmkpTIFCGVPRVYDRIytginlkiqsggligkqifQYAYNYKLANLRkgfkqheaspffdkivfskikeglggriR 387
Cdd:TIGR01733 210 EHPV---TVLNLTPSLLALL-------------------AAALPPALASLR----------------------------L 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 LMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTEscaGCFTSIANIFSMIGT-------VGPPVTAIQARLESipemgyDA 460
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPGARLINLYGPTE---TTVWSTATLVDPDDAprespvpIGRPLANTRLYVLD------DD 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357156424 461 LSNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWF---------HTGDIGEWQPDGT 509
Cdd:TIGR01733 311 LRPVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRTGDLVRYLPDGN 371
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
177-569 |
2.38e-28 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 119.98 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 177 AIVSFgdVTNELKREVEQLRVS-CFSWEEFSTMGTE----TQDIsrkQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVM 251
Cdd:PRK08751 164 ALVNF--VVKYVKKLVPEYRINgAIRFREALALGRKhsmpTLQI---EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 252 TTENLLELTDKVVSEDDSYFSYLPLAHIFdQVIENYCIFKGAsigfwqGDIRYLMEDVQVMkPTIFCGVPRVYDRIYTGI 331
Cdd:PRK08751 239 QAHQWLAGTGKLEEGCEVVITALPLYHIF-ALTANGLVFMKI------GGCNHLISNPRDM-PGFVKELKKTRFTAFTGV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 332 NlkiqsggligkQIFQyaynyKLANlrkgfkqheaSPFFDKIVFSKIKEGLGGRIRLMLSGAaplprhiEEFMRVTGCcA 411
Cdd:PRK08751 311 N-----------TLFN-----GLLN----------TPGFDQIDFSSLKMTLGGGMAVQRSVA-------ERWKQVTGL-T 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 412 LAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQArleSIPEMGYDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVF 491
Cdd:PRK08751 357 LVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDA---CIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVM 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 492 -SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSVwvygnsfesflVAVVVPEKQAIE 569
Cdd:PRK08751 434 dADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPDEKSGE 500
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
222-570 |
6.58e-28 |
|
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: 114.74 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTDKvvsedDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGD 301
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGG-----DSWLLSLPLYHVGGLAILVRSLLAGAELVLLERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 302 iRYLMEDVQVMKPTIFCGVPrvydriytginlkiqsggligkqifqyaynyklANLRKGFKQHEASPFFDkivfskikeg 381
Cdd:cd17630 76 -QALAEDLAPPGVTHVSLVP---------------------------------TQLQRLLDSGQGPAALK---------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 382 lggRIRLMLSGAAPLPRHIEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMiGTVGPPVTAIQARLesipemgydal 461
Cdd:cd17630 112 ---SLRAVLLGGAPIPPELLERAADRGI-PLYTTYGMTETASQVATKRPDGFGR-GGVGVLLPGRELRI----------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 462 snVPRGEICLRGHTLFSGYYkRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSP 541
Cdd:cd17630 176 --VEDGEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHP 251
|
330 340 350
....*....|....*....|....*....|..
gi 357156424 542 LVTSVWVYGNSFESF---LVAVVVPEKQAIED 570
Cdd:cd17630 252 AVRDAFVVGVPDEELgqrPVAVIVGRGPADPA 283
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
59-602 |
9.69e-28 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 117.47 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 59 KNRMLGQRQVSDGKAGDYvwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLG 138
Cdd:cd05959 13 LNEGRGDKTAFIDDAGSL---TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 139 PNAVEFILDHAEISIAFVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREVeqlrvscfsWEEFSTMGTETQDISRK 218
Cdd:cd05959 90 PDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALL---------LAELVAAEAEQLKPAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMT-TENLLELTdkvvsEDDSYFSYLPLAHIFDqvIENYCIFKgasigF 297
Cdd:cd05959 161 HADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIR-----EDDVCFSAAKLFFAYG--LGNSLTFP-----L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 298 WQGDIRYLM----------EDVQVMKPTIFCGVPRVYdriytginlkiqsggligkqifqyaynyklANLRkgfkqheAS 367
Cdd:cd05959 229 SVGATTVLMperptpaavfKRIRRYRPTVFFGVPTLY------------------------------AAML-------AA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 368 PFFDKIVFSkikeglggRIRLMLSGAAPLPRHI-EEFMRVTGCCALaQGYGLTEscagcftsIANIF-------SMIGTV 439
Cdd:cd05959 272 PNLPSRDLS--------SLRLCVSAGEALPAEVgERWKARFGLDIL-DGIGSTE--------MLHIFlsnrpgrVRYGTT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 440 GPPVTAIQARLesIPEMGYDALSNVPrGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:cd05959 335 GKPVPGYEVEL--RDEDGGDVADGEP-GELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDM 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 520 FKLSqGEYVA-VEVlESAYVQSPLVTSVWVYGNSFESFL---VAVVVPeKQAIEDWAALnnkTSDFAELCNDP----KAR 591
Cdd:cd05959 412 LKVS-GIWVSpFEV-ESALVQHPAVLEAAVVGVEDEDGLtkpKAFVVL-RPGYEDSEAL---EEELKEFVKDRlapyKYP 485
|
570
....*....|...
gi 357156424 592 RYIQ--DELNKTG 602
Cdd:cd05959 486 RWIVfvDELPKTA 498
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
80-537 |
1.53e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 117.44 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYV---PLYD------TLGPNAVEFILDhae 150
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTereleyQLHDSGAKVILC--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 151 ISIAFVQASKIKSLLAILPKCTAHIKAIVSFGD--VTNELKREVEQLRVSCFS------WEEFSTMGTETQDISRKQKDD 222
Cdd:PRK06710 128 LDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKnlLYPFVQKKQSNLVVKVSEsetihlWNSVEKEVNTGVEVPCDPEND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 223 ICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLEltdKVVSEDDSYFSYLPLAHIFDQV-IENYCIFKGASIGFW-QG 300
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY---NCKEGEEVVLGVLPFFHVYGMTaVMNLSIMQGYKMVLIpKF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 301 DIRYLMEDVQVMKPTIFCGVPRVYdriytginlkiqsggligkqifqyaynYKLANlrkgfkqheaSPFfdkivfskIKE 380
Cdd:PRK06710 285 DMKMVFEAIKKHKVTLFPGAPTIY---------------------------IALLN----------SPL--------LKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 381 GLGGRIRLMLSGAAPLPRHIEE-FMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESIpEMGyD 459
Cdd:PRK06710 320 YDISSIRACISGSAPLPVEVQEkFETVTGG-KLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL-ETG-E 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357156424 460 ALSNVPRGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVLESAY 537
Cdd:PRK06710 397 ALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
70-565 |
1.60e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 117.00 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 70 DGKAGDYVwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYV---PLYDTlgpnavefil 146
Cdd:PLN02246 44 DGATGRVY--TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTtanPFYTP---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 147 dhAEIsiaFVQASKIKSLLAILPKCtaHIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTMGTETQDISRKQKDDICTI 226
Cdd:PLN02246 112 --AEI---AKQAKASGAKLIITQSC--YVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 227 MYTSGTTGDPKGVIITNRAIIAGV---MTTENL-LELTdkvvsEDDSYFSYLPLAHIF--DQVIenYCIFK-GASIGFWQ 299
Cdd:PLN02246 185 PYSSGTTGLPKGVMLTHKGLVTSVaqqVDGENPnLYFH-----SDDVILCVLPMFHIYslNSVL--LCGLRvGAAILIMP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 300 G-DIRYLMEDVQVMKPTIFCGVPRVYdriytginlkiqsggligkqifqyaynykLAnLRKgfkqheaSPFFDKIVFSKI 378
Cdd:PLN02246 258 KfEIGALLELIQRHKVTIAPFVPPIV-----------------------------LA-IAK-------SPVVEKYDLSSI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 379 keglggriRLMLSGAAPLPRHIEEFMRVTGCCA-LAQGYGLTEscAGCFTSIANIFS---------MIGTVgppvtAIQA 448
Cdd:PLN02246 301 --------RMVLSGAAPLGKELEDAFRAKLPNAvLGQGYGMTE--AGPVLAMCLAFAkepfpvksgSCGTV-----VRNA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 449 RLESI-PEMGYDALSNVPrGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGE 526
Cdd:PLN02246 366 ELKIVdPETGASLPRNQP-GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGF 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 357156424 527 YVAVEVLESAYVQSPLVTSvwvygnsfesflvAVVVPEK 565
Cdd:PLN02246 444 QVAPAELEALLISHPSIAD-------------AAVVPMK 469
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
80-550 |
1.86e-27 |
|
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: 116.86 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTaHIKAIVSFGDVTN-----ELKREVEQLRVSCFSWEEFSTmgtetqdISRKQKDDICTIMYTSGTTG 234
Cdd:cd17642 126 GLQKVLNVQKKLK-IIKTIIILDSKEDykgyqCLYTFITQNLPPGFNEYDFKP-------PSFDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 235 DPKGVIITNRAIIAGVMTTENllELTDKVVSEDDSYFSYLPLAHIFDQVienycifkgASIGFWQGDIRYLMedvqvmkp 314
Cdd:cd17642 198 LPKGVQLTHKNIVARFSHARD--PIFGNQIIPDTAILTVIPFHHGFGMF---------TTLGYLICGFRVVL-------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 315 tifcgVPRVYDRIY--TGINLKIQSGGLIGKQIFQYAynyklanlrkgfkqheASPFFDKIVFSKIKEglggrirlMLSG 392
Cdd:cd17642 259 -----MYKFEEELFlrSLQDYKVQSALLVPTLFAFFA----------------KSTLVDKYDLSNLHE--------IASG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 393 AAPLPRHIEEFM-RVTGCCALAQGYGLTESCAGCFTSiANIFSMIGTVGPPVTAIQARLESiPEMGyDALSNVPRGEICL 471
Cdd:cd17642 310 GAPLSKEVGEAVaKRFKLPGIRQGYGLTETTSAILIT-PEGDDKPGAVGKVVPFFYAKVVD-LDTG-KTLGPNERGELCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 472 RGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd17642 387 KGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG 465
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-519 |
2.43e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 113.53 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENY-CIFKGASI---- 295
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLT-----EQDRLCIPVPLFHCFGSVLGVLaCLTHGATMvfps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 296 -GFwqgDIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKiqsggligkqifqyayNYKLANLRKGFkqheaspffdkiv 374
Cdd:cd05917 77 pSF---DPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFD----------------KFDLSSLRTGI------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 375 fskikegLGGrirlmlsgaAPLP----RHIEEFMRVTgccALAQGYGLTESCAGCFTSIAN--IFSMIGTVGPPVTAIQA 448
Cdd:cd05917 125 -------MAG---------APCPpelmKRVIEVMNMK---DVTIAYGMTETSPVSTQTRTDdsIEKRVNTVGRIMPHTEA 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 449 RLESiPEMGYDALSNVPrGEICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:cd05917 186 KIVD-PEGGIVPPVGVP-GELCIRGYSVMKGYWNDPEKTAEAIDgDGWLHTGDLAVMDEDGYCRIVGRIKDM 255
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
226-570 |
9.49e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.93 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 226 IMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIfdqvienycifKGASIGFWqGDIRYL 305
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT-----ADDVLVHGLPLFHV-----------HGLVLGVL-GPLRIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 306 MEDVQVMKP-------------TIFCGVPRVYDRIytginlkiqsggligkqifqyAYNYKLAnlrkgfkqheaspffdk 372
Cdd:PRK07787 196 NRFVHTGRPtpeayaqalseggTLYFGVPTVWSRI---------------------AADPEAA----------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 373 ivfskikEGLGGrIRLMLSGAAPLPRHI-EEFMRVTGCcALAQGYGLTESCAGCFTSiANIFSMIGTVGPPVTAIQARL- 450
Cdd:PRK07787 238 -------RALRG-ARLLVSGSAALPVPVfDRLAALTGH-RPVERYGMTETLITLSTR-ADGERRPGWVGLPLAGVETRLv 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 451 -ESIPEMGYDALSnvpRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDR------KKNIFKL 522
Cdd:PRK07787 308 dEDGGPVPHDGET---VGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRI 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 357156424 523 SQGEyvavevLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAIED 570
Cdd:PRK07787 385 GAGE------IETALLGHPGVREAAVVGVPDDDLgqrIVAYVVGADDVAAD 429
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
219-523 |
2.97e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 113.70 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLelTDKVVSEDDSYFSYLPLAHIFDQVIenYCIFkgasigfw 298
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALM--GSNLNEGCEILIAPLPLYHIYAFTF--HCMA-------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 299 qgdiryLMEdvqVMKPTIFCGVPRVYDRIYTGINlKIQSGGLIGkqifqyaynykLANLRKGFKQHEAspfFDKIVFSKI 378
Cdd:PRK05677 273 ------MML---IGNHNILISNPRDLPAMVKELG-KWKFSGFVG-----------LNTLFVALCNNEA---FRKLDFSAL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 379 KEGLGGRIRLMLSGAaplprhiEEFMRVTGCcALAQGYGLTE-SCAGCFTSIANIfsMIGTVGPPVTAIQARLesIPEMG 457
Cdd:PRK05677 329 KLTLSGGMALQLATA-------ERWKEVTGC-AICEGYGMTEtSPVVSVNPSQAI--QVGTIGIPVPSTLCKV--IDDDG 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 458 YDalsnVPRGEI---CLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLS 523
Cdd:PRK05677 397 NE----LPLGEVgelCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS 462
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
73-608 |
6.37e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 109.46 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 73 AGDYVWqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPL-YDTLGPNaVEFILDHAEI 151
Cdd:PRK06155 42 FGGTRW-TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPInTALRGPQ-LEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 152 SIAFVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREveqlrvscFSWEEFSTmGTETQDISRKQKDDICTIMYTSG 231
Cdd:PRK06155 120 RLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAG--------WSTAPLPP-LDAPAPAAAVQPGDTAAILYTSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 232 TTGDPKGVIITN-RAIIAGVMTTEnLLELTdkvvsEDDSYFSYLPLAHI-----FDQVIENYCIF----KGASIGFW--- 298
Cdd:PRK06155 191 TTGPSKGVCCPHaQFYWWGRNSAE-DLEIG-----ADDVLYTTLPLFHTnalnaFFQALLAGATYvlepRFSASGFWpav 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 299 ---QGDIRYLMedvQVMKPTIFCGVPRVYDRiytginlkiqsggligkqifqyaynyklanlrkgfkqheaspffdkivf 375
Cdd:PRK06155 265 rrhGATVTYLL---GAMVSILLSQPARESDR------------------------------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 376 skikeglGGRIRLMLSGAAPlPRHIEEFMRVTGCcALAQGYGLTESCAGCFTSIANifSMIGTVGPPVTAIQARLesIPE 455
Cdd:PRK06155 293 -------AHRVRVALGPGVP-AALHAAFRERFGV-DLLDGYGSTETNFVIAVTHGS--QRPGSMGRLAPGFEARV--VDE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 456 MGYDALSNVPrGEICLRG---HTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYV-AVE 531
Cdd:PRK06155 360 HDQELPDGEP-GELLLRAdepFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENIsSFE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 532 VlESAYVQSPLVTSVWVYGNSFE----SFLVAVVVPEKQAIedwaalnnktsDFAELCNDPKAR-------RYI--QDEL 598
Cdd:PRK06155 438 V-EQVLLSHPAVAAAAVFPVPSElgedEVMAAVVLRDGTAL-----------EPVALVRHCEPRlayfavpRYVefVAAL 505
|
570
....*....|....
gi 357156424 599 NKT--GK--KLGLR 608
Cdd:PRK06155 506 PKTenGKvqKFVLR 519
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
80-574 |
3.14e-24 |
|
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: 106.79 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:TIGR03098 27 TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTAhIKAIVSFGDVTnelKREVEQLRVSCFSWEEFSTMGTeTQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:TIGR03098 107 RLDLLHPALPGCHD-LRTLIIVGDPA---HASEGHPGEEPASWPKLLALGD-ADPPHPVIDSDMAAILYTSGSTGRPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQgdirYLM-EDV--QVMKPTI 316
Cdd:TIGR03098 182 VLSHRNLVAGAQSVATYLENR-----PDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD----YLLpRDVlkALEKHGI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 317 --FCGVPRVYdriytginlkiqsggligkqifqyaynYKLANLrkgfkqheaspffdkivfsKIKEGLGGRIRLMLSGAA 394
Cdd:TIGR03098 253 tgLAAVPPLW---------------------------AQLAQL-------------------DWPESAAPSLRYLTNSGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 395 PLPR----HIEEFMRVTgccALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTaiQARLESIPEMGYDALSNVPrGEIC 470
Cdd:TIGR03098 287 AMPRatlsRLRSFLPNA---RLFLMYGLTEAFRSTYLPPEEVDRRPDSIGKAIP--NAEVLVLREDGSECAPGEE-GELV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTLFSGYYKRPDLTEEVF------SDG--------WfhTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESA 536
Cdd:TIGR03098 361 HRGALVAMGYWNDPEKTAERFrplppfPGElhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEV 437
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 357156424 537 YVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAIEDWAAL 574
Cdd:TIGR03098 438 AYATGLVAEAVAFGVPDPTLgqaIVLVVTPPGGEELDRAAL 478
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-574 |
4.70e-24 |
|
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: 105.69 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAs 159
Cdd:cd05930 14 TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTDP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd05930 93 -------------------------------------------------------------DDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELT--DKV-----VSEDDSYFS-YLPLAHifdqvienycifkGASI----GFWQGDIRYL-- 305
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAYPLTpgDRVlqftsFSFDVSVWEiFGALLA-------------GATLvvlpEEVRKDPEALad 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 306 -MEDVQVmkpTIFCGVPRVYdriytginlkiqsggligKQIFQYAYNYKLANLRkgfkqheaspffdkivfskikeglgg 384
Cdd:cd05930 179 lLAEEGI---TVLHLTPSLL------------------RLLLQELELAALPSLR-------------------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 385 riRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGC-FTSIANIFSMIGTV--GPPVTAIQARLesipeMGyDAL 461
Cdd:cd05930 212 --LVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDAtYYRVPPDDEEDGRVpiGRPIPNTRVYV-----LD-ENL 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 462 SNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFH-------TGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVE 531
Cdd:cd05930 284 RPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELG 362
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 357156424 532 VLESAYVQSPLVTS---VWVYGNSFESFLVAVVVPEKQAIEDWAAL 574
Cdd:cd05930 363 EIEAALLAHPGVREaavVAREDGDGEKRLVAYVVPDEGGELDEEEL 408
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
74-647 |
6.38e-24 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 106.21 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLydtlGPNAVEFILDHAEisi 153
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL----TVPPTYDEPNARL--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 afvqaSKIKSLLAIL--PKCTAHIKAIVSFGDVTNELKREVEQLRVScfswEEFSTMGTETqDISRKQKDDICTIMYTSG 231
Cdd:cd05906 108 -----RKLRHIWQLLgsPVVLTDAELVAEFAGLETLSGLPGIRVLSI----EELLDTAADH-DLPQSRPDDLALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 232 TTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIfdqvienycifkgASIGFWQ-GDIRYLMEDVQ 310
Cdd:cd05906 178 STGFPKAVPLTHRNILARSAGKIQHNGLT-----PQDVFLNWVPLDHV-------------GGLVELHlRAVYLGCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 VMKPTIFCGVPRVYDriytginlkiqsggLIGK-QI-FQYAYNYKLANLRkgfkQHEASPffdkivfsKIKEGLGGRIRL 388
Cdd:cd05906 240 VPTEEILADPLRWLD--------------LIDRyRVtITWAPNFAFALLN----DLLEEI--------EDGTWDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 389 MLSGAAPLPRH-IEEFMRVTGCC-----ALAQGYGLTESCAGCF---------TSIANIFSmigTVGPPVTAIQARlesI 453
Cdd:cd05906 294 LVNAGEAVVAKtIRRLLRLLEPYglppdAIRPAFGMTETCSGVIysrsfptydHSQALEFV---SLGRPIPGVSMR---I 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 454 PEMGYDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGeWQPDGTMKIIDRKKNIFKLSQGEYVAVEv 532
Cdd:cd05906 368 VDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHE- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 533 LESAYVQSPLVTSvwvygnsfeSFLVAVVV-PEKQAIEDWAALNNKTSDfaelcndpkarryIQDELNKTGKKlgLRGfE 611
Cdd:cd05906 446 IEAAVEEVPGVEP---------SFTAAFAVrDPGAETEELAIFFVPEYD-------------LQDALSETLRA--IRS-V 500
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 357156424 612 MLRAVHLEP---VPfgIEKDLITPTF--KLKRPQLLKYYKD 647
Cdd:cd05906 501 VSREVGVSPaylIP--LPKEEIPKTSlgKIQRSKLKAAFEA 539
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
78-550 |
7.13e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 105.66 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 78 WqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIafvq 157
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 158 askiksLLAilpkcTAHIKAIVSFGDVTNELKREVEQLrvscfsweefstmgtETQDISRKQKDDICTIMYTSGTTGDPK 237
Cdd:PRK09088 98 ------LLG-----DDAVAAGRTDVEDLAAFIASADAL---------------EPADTPSIPPERVSLILFTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 238 GVIITNRAIIAgvmTTENLLELTDkvVSEDDSYFSYLPLAHIFDqVIENY--CIFKGASI----GF-------WQGDiry 304
Cdd:PRK09088 152 GVMLSERNLQQ---TAHNFGVLGR--VDAHSSFLCDAPMFHIIG-LITSVrpVLAVGGSIlvsnGFepkrtlgRLGD--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 305 lmedvQVMKPTIFCGVPRVYDRIytginlkiqsggligkqifqyaynyklanlrkgfkqhEASPFFDKIVFskikeglgG 384
Cdd:PRK09088 223 -----PALGITHYFCVPQMAQAF-------------------------------------RAQPGFDAAAL--------R 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 385 RIRLMLSGAAPlprHIEEFMR--VTGCCALAQGYGLTE--SCAGCFTSIANIFSMIGTVGPPVTAIQARLesIPEMGYDA 460
Cdd:PRK09088 253 HLTALFTGGAP---HAAEDILgwLDDGIPMVDGFGMSEagTVFGMSVDCDVIRAKAGAAGIPTPTVQTRV--VDDQGNDC 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 461 LSNVPrGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQ 539
Cdd:PRK09088 328 PAGVP-GELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLAD 405
|
490
....*....|.
gi 357156424 540 SPLVTSVWVYG 550
Cdd:PRK09088 406 HPGIRECAVVG 416
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
58-656 |
3.57e-23 |
|
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: 104.05 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 58 PKNRMLGQRQvsdgkaGDYVWQ--TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPL-- 133
Cdd:cd05921 9 PDRTWLAERE------GNGGWRrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVsp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 134 -YDTLGPNAVEF--ILDHAEISIAFVQASKI--KSLLAILPkctAHIKAIVSFGDVTNElkreveqlRVSCFSwEEFSTM 208
Cdd:cd05921 83 aYSLMSQDLAKLkhLFELLKPGLVFAQDAAPfaRALAAIFP---LGTPLVVSRNAVAGR--------GAISFA-ELAATP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 209 GTETQD--ISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAG-VMTTENLLELTDkvvsEDDSYFSYLPLAHIFdqvie 285
Cdd:cd05921 151 PTAAVDaaFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANqAMLEQTYPFFGE----EPPVLVDWLPWNHTF----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 286 nycifkGASIGF----WQGDIRYL-------------MEDVQVMKPTIFCGVPRVYDRIytginlkiqsggligkqifqy 348
Cdd:cd05921 222 ------GGNHNFnlvlYNGGTLYIddgkpmpggfeetLRNLREISPTVYFNVPAGWEML--------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 349 aynykLANLRKgfKQHEASPFFDkivfskikeglggRIRLMLSGAAPLPRHIEEFM----------RVTgccaLAQGYGL 418
Cdd:cd05921 275 -----VAALEK--DEALRRRFFK-------------RLKLMFYAGAGLSQDVWDRLqalavatvgeRIP----MMAGLGA 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 419 TEScAGCFTSIANIFSMIGTVGPPVTAIQARLesipemgydalsnVPRG---EICLRGHTLFSGYYKRPDLTEEVF-SDG 494
Cdd:cd05921 331 TET-APTATFTHWPTERSGLIGLPAPGTELKL-------------VPSGgkyEVRVKGPNVTPGYWRQPELTAQAFdEEG 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 495 WFHTGDIGEW-QPDGTMKIID---RKKNIFKLSQGEYVAVEVLESAYVQ--SPLVTSVWVYGNSFEsFLVAVVVPEKQAI 568
Cdd:cd05921 397 FYCLGDAAKLaDPDDPAKGLVfdgRVAEDFKLASGTWVSVGPLRARAVAacAPLVHDAVVAGEDRA-EVGALVFPDLLAC 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 569 EdwAALNNKTSDFAELCNDPKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPvPFGIEKDLITPTFKLKRPQLLKYYKDR 648
Cdd:cd05921 476 R--RLVGLQEASDAEVLRHAKVRAAFRDRLAALNGEATGSSSRIARALLLDE-PPSIDKGEITDKGYINQRAVLERRAAL 552
|
....*...
gi 357156424 649 VDQLYKDA 656
Cdd:cd05921 553 VERLYADT 560
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
80-574 |
8.30e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 102.26 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTAhikaivsfgdvtnelkREVEQL---RVSCFSwEEFSTMGTETQDISRkQKDDICTIMYTSGTTGDP 236
Cdd:PRK07514 110 NFAWLSKIAAAAGA----------------PHVETLdadGTGSLL-EAAAAAPDDFETVPR-GADDLAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 237 KGVIITNRAIIAgvmtteNLLELTDK-VVSEDDSYFSYLPLAH---IFdqVIENYCIFKGASIGFWQGdirylMEDVQVM 312
Cdd:PRK07514 172 KGAMLSHGNLLS------NALTLVDYwRFTPDDVLIHALPIFHthgLF--VATNVALLAGASMIFLPK-----FDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 K----PTIFCGVPRVYDRIYtginlkiqsggligkqifqyaynyklanlrkgfkqheASPFFDKivfskikeGLGGRIRL 388
Cdd:PRK07514 239 AlmprATVMMGVPTFYTRLL-------------------------------------QEPRLTR--------EAAAHMRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 389 MLSGAAP-LPRHIEEFMRVTGCcALAQGYGLTEscAGCFTS-------IAnifsmiGTVGPPVTAIQARLESiPEMGYDa 460
Cdd:PRK07514 274 FISGSAPlLAETHREFQERTGH-AILERYGMTE--TNMNTSnpydgerRA------GTVGFPLPGVSLRVTD-PETGAE- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 461 lsnVPRGEIC---LRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKK--------NIF-KLSQGEY 527
Cdd:PRK07514 343 ---LPPGEIGmieVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGKdliisggyNVYpKEVEGEI 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357156424 528 VAVE-VLESAYVQSPLVtsvwvygnSFESFLVAVVVPEKQAIEDWAAL 574
Cdd:PRK07514 420 DELPgVVESAVIGVPHP--------DFGEGVTAVVVPKPGAALDEAAI 459
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
80-603 |
1.06e-22 |
|
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: 101.38 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAs 159
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd05919 91 -------------------------------------------------------------DDIAYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRA--IIAGVMTTENL-LELTDKVVSEDDSYFSYlPLAH--IFDqvienycIFKGASIGFWQG--DIRYLMEDVQVM 312
Cdd:cd05919 110 MHAHRDplLFADAMAREALgLTPGDRVFSSAKMFFGY-GLGNslWFP-------LAVGASAVLNPGwpTAERVLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 KPTIFCGVPRVYdriytginlkiqsggligkqifqyaynyklANLRkgfkqheASPFFDKIVFSKIkeglggriRLMLSG 392
Cdd:cd05919 182 RPTVLYGVPTFY------------------------------ANLL-------DSCAGSPDALRSL--------RLCVSA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 393 AAPLPRHIEEFMRVTGCCALAQGYGLTESCagcFTSIANIFSMI--GTVGPPVTAIQARLesIPEMGYDALSNVPrGEIC 470
Cdd:cd05919 217 GEALPRGLGERWMEHFGGPILDGIGATEVG---HIFLSNRPGAWrlGSTGRPVPGYEIRL--VDEEGHTIPPGEE-GDLL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVA-VEVlESAYVQSPLVTSVWVY 549
Cdd:cd05919 291 VRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSpVEV-ESLIIQHPAVAEAAVV 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357156424 550 GNSFESFLV---AVVVPEKQAIEDWAALNNKTSDFAELCNDPKARRYIQ--DELNKT--GK 603
Cdd:cd05919 369 AVPESTGLSrltAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAfvDELPRTatGK 429
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
80-563 |
1.08e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 102.55 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kIKSLLAILPKCTAHIKAIVSFGDVTNElkreveqlrvSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK07786 124 -LAPVATAVRDIVPLLSTVVVAGGSSDD----------SVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTtenlLELTDKVVSEDDSYFSYLPLAHIfdqvienycifkgASIGfwqgdirylmedvqVMKPTIFCG 319
Cdd:PRK07786 193 VLTHANLTGQAMT----CLRTNGADINSDVGFVGVPLFHI-------------AGIG--------------SMLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 VPRVydrIYTginlkiqSGGLIGKQIFQYAYNYKLANLRKGFKQHEAspffdkIVFSKIKEGLGGRIRLMLSGAAPLPRH 399
Cdd:PRK07786 242 APTV---IYP-------LGAFDPGQLLDVLEAEKVTGIFLVPAQWQA------VCAEQQARPRDLALRVLSWGAAPASDT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 400 IEEFMRVT--GCCALAqGYGLTE-SCAGCFTSIANIFSMIGTVGPPVTAIQARLESipemgyDALSNVPRG---EICLRG 473
Cdd:PRK07786 306 LLRQMAATfpEAQILA-AFGQTEmSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVD------ENMNDVPVGevgEIVYRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 474 HTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSF 553
Cdd:PRK07786 379 PTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRAD 457
|
490
....*....|...
gi 357156424 554 ESF---LVAVVVP 563
Cdd:PRK07786 458 EKWgevPVAVAAV 470
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
48-517 |
1.17e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 102.20 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKNRMLGQRqvsdgkAGDYVWqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG 127
Cdd:PRK08315 20 QLLDRTAARYPDREALVYR------DQGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 128 ICYV---PLYDTlgpNAVEFILDHAEIS-IAFVQASKIKSLLAIL----PKCTA------------HIKAIVSFGDvtne 187
Cdd:PRK08315 93 AILVtinPAYRL---SELEYALNQSGCKaLIAADGFKDSDYVAMLyelaPELATcepgqlqsarlpELRRVIFLGD---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 188 lkrevEQLRvSCFSWEEFSTMGTETQDI------SRKQKDDICTIMYTSGTTGDPKGVIITNRAII-AGVMTTENlLELT 260
Cdd:PRK08315 166 -----EKHP-GMLNFDELLALGRAVDDAelaarqATLDPDDPINIQYTSGTTGFPKGATLTHRNILnNGYFIGEA-MKLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 261 dkvvsEDDSYFSYLPLAHIFDQVIENY-CIFKGASI-----GFwqgDIRYLMEDVQVMKPTIFCGVPRVYdriytginlk 334
Cdd:PRK08315 239 -----EEDRLCIPVPLYHCFGMVLGNLaCVTHGATMvypgeGF---DPLATLAAVEEERCTALYGVPTMF---------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 335 iqsggligkqifqyaynykLANLrkgfkQHeasPFFDKIVFSKIKEGlggrirLMlsGAAPLPrhiEEFMR--------- 405
Cdd:PRK08315 301 -------------------IAEL-----DH---PDFARFDLSSLRTG------IM--AGSPCP---IEVMKrvidkmhms 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 406 -VTGCcalaqgYGLTESCAGCFTSIAN--IFSMIGTVGppvtAIQARLES-I--PEMGYDalsnVPR---GEICLRGHTL 476
Cdd:PRK08315 343 eVTIA------YGMTETSPVSTQTRTDdpLEKRVTTVG----RALPHLEVkIvdPETGET----VPRgeqGELCTRGYSV 408
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 357156424 477 FSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKK 517
Cdd:PRK08315 409 MKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIK 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
222-550 |
3.10e-22 |
|
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: 98.34 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFdqvieNY------CIFKGASI 295
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT-----EDDRYLIINPFFHTF-----GYkagivaCLLTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 296 GFWQG-DIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKiqsggligkqifqyayNYKLANLRKGfkqheaspffdkiv 374
Cdd:cd17638 71 VPVAVfDVDAILEAIERERITVLPGPPTLFQSLLDHPGRK----------------KFDLSSLRAA-------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 375 fskikeglggrirlmLSGAAPLPRHIEEFMRVT-GCCALAQGYGLTEscAGC---------FTSIANifsmigTVGPPVT 444
Cdd:cd17638 121 ---------------VTGAATVPVELVRRMRSElGFETVLTAYGLTE--AGVatmcrpgddAETVAT------TCGRACP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 445 AIQARLESipemgydalsnvpRGEICLRGHTLFSGYYKRPDLTEE-VFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLS 523
Cdd:cd17638 178 GFEVRIAD-------------DGEVLVRGYNVMQGYLDDPEATAEaIDADGWLHTGDVGELDERGYLRITDRLKDMY-IV 243
|
330 340
....*....|....*....|....*..
gi 357156424 524 QGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd17638 244 GGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
222-519 |
4.05e-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: 98.10 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAgvmTTENLLELTDKVVSEDDSYfSYLPLAHIFDQVIENYCIFKGASIGFWQGD 301
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFA---VPDILQKEGLNWVVGDVTY-LPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 302 IRY--LMEDVQVMKPTIFCGVPRVYDriytginlkiqsggligkqifqyaynyKLANLRKgfkqheaspffDKIVFSKik 379
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLS---------------------------KLVSELK-----------SANATVP-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 380 eglggRIRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESIPEMgyd 459
Cdd:cd17635 118 -----SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGI--- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 460 ALSNVPRGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:cd17635 190 AGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSES 249
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
80-550 |
6.19e-22 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 99.09 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd05935 83 L------------------------------------------------------------DDLALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQV-IENYCIFKGASI---GFWQGDIryLMEDVQVMKPT 315
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLT-----PSDVILACLPLFHVTGFVgSLNTAVYVGGTYvlmARWDRET--ALELIEKYKVT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 316 IFCGVPrvydriyTGINLKIqsggligkqifqyaynyklanlrkgfkqheASPFFDKIVFSKIKEgLGGrirlmlsGAAP 395
Cdd:cd05935 176 FWTNIP-------TMLVDLL------------------------------ATPEFKTRDLSSLKV-LTG-------GGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 396 LPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSiANIFSMIGTVGPPVTAIQARLESiPEMGYDALSNVpRGEICLRGHT 475
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTN-PPLRPKLQCLGIP*FGVDARVID-IETGRELPPNE-VGEIVVRGPQ 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 476 LFSGYYKRPDLTEEVFS--DG--WFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd05935 288 IFKGYWNRPEETEESFIeiKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
26-618 |
6.76e-22 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 100.05 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 26 VYRSIYAKdglMPLPKEIQSPwDFFSEAVKKYPKNrmLGQRQVSDGKAgdyvwQTYEEVYQKVIKIGAAIRSFGVKPGGH 105
Cdd:PLN02330 14 IFRSRYPS---VPVPDKLTLP-DFVLQDAELYADK--VAFVEAVTGKA-----VTYGEVVRDTRRFAKALRSLGLRKGQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 106 CGIYGSNCPEW-VMAMQACSSQGIcyvplYDTLGPNAVEF-ILDHAEISIAF------VQASKIKSLLaiLPkctahika 177
Cdd:PLN02330 83 VVVVLPNVAEYgIVALGIMAAGGV-----FSGANPTALESeIKKQAEAAGAKlivtndTNYGKVKGLG--LP-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 178 IVSFGDVTNElkreveqlrvSCFSWEEFSTMGTETQDISRKQ---KDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTe 254
Cdd:PLN02330 148 VIVLGEEKIE----------GAVNWKELLEAADRAGDTSDNEeilQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 255 nLLELTDKVVSEDDSyFSYLPLAHIFDqvIENYCIF----KGASIGFWQGDIRYLMEDVQVMKPTIFCGVPRVydriytg 330
Cdd:PLN02330 217 -LFSVGPEMIGQVVT-LGLIPFFHIYG--ITGICCAtlrnKGKVVVMSRFELRTFLNALITQEVSFAPIVPPI------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 331 inlkiqsggligkqifqyaynykLANLRKgfkqheaSPFFDKIVFSKIKeglggrIRLMLSGAAPL-PRHIEEFMRVTGC 409
Cdd:PLN02330 286 -----------------------ILNLVK-------NPIVEEFDLSKLK------LQAIMTAAAPLaPELLTAFEAKFPG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 410 CALAQGYGLTEScaGCFT------SIANIFSMIGTVGPPVTAIQARLESiPEMGYDALSNVPrGEICLRGHTLFSGYYKR 483
Cdd:PLN02330 330 VQVQEAYGLTEH--SCITlthgdpEKGHGIAKKNSVGFILPNLEVKFID-PDTGRSLPKNTP-GELCVRSQCVMQGYYNN 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 484 PDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSPLVTSVWVygnsfesflvaVVV 562
Cdd:PLN02330 406 KEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV-----------VPL 473
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 357156424 563 PEKQAIEDWAALnnktsdfaeLCNDPKARRYIQDELNKTGKKLGlrGFEMLRAVHL 618
Cdd:PLN02330 474 PDEEAGEIPAAC---------VVINPKAKESEEDILNFVAANVA--HYKKVRVVQF 518
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
80-550 |
1.48e-21 |
|
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: 97.79 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEIsiafvqas 159
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahiKAIVSfgdvtnelkreveqlrvscfsweefstmgtetqdisrkQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd05972 74 ----------------KAIVT--------------------------------------DAEDPALIYFTSGTTGLPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELtdkvvSEDDSYFS--------------YLPLAHIFDQVIENYCIFkgasigfwqgDIRYL 305
Cdd:cd05972 100 LHTHSYPLGHIPTAAYWLGL-----RPDDIHWNiadpgwakgawssfFGPWLLGATVFVYEGPRF----------DAERI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 306 MEDVQVMKPTIFCGVPRVYDRIytginlkIQSGGLIGKqifqyaynyklanlrkgfkqheaspffdkivFSkikeglggR 385
Cdd:cd05972 165 LELLERYGVTSFCGPPTAYRML-------IKQDLSSYK-------------------------------FS--------H 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPL-PRHIEEFMRVTGCcALAQGYGLTESCAgcftSIANI-FSMI--GTVGPPVTAIQARLesIPEMGYDAL 461
Cdd:cd05972 199 LRLVVSAGEPLnPEVIEWWRAATGL-PIRDGYGQTETGL----TVGNFpDMPVkpGSMGRPTPGYDVAI--IDDDGRELP 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 462 SNVPrGEICLR--GHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEVlESAYVQ 539
Cdd:cd05972 272 PGEE-GDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV-ESALLE 349
|
490
....*....|.
gi 357156424 540 SPLVTSVWVYG 550
Cdd:cd05972 350 HPAVAEAAVVG 360
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
76-548 |
1.58e-21 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 98.76 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 76 YVWQtyeEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAF 155
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 156 VQA---SKIKSLLAILP-KCTAHIKA--IVSFGDVTNELKREVEQLRVSCFSWEEFSTMGtETQDISRKQKDDICTIM-- 227
Cdd:PLN02479 123 VDQeffTLAEEALKILAeKKKSSFKPplLIVIGDPTCDPKSLQYALGKGAIEYEKFLETG-DPEFAWKPPADEWQSIAlg 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 228 YTSGTTGDPKGVIITNRAiiAGVMTTENLL--ELTDKVVseddsYFSYLPLAHI----FDQVIENYCifkGASIGFWQGD 301
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRG--AYLMALSNALiwGMNEGAV-----YLWTLPMFHCngwcFTWTLAALC---GTNICLRQVT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 302 IRYLMEDVQVMKPTIFCGVPRVYDRIytgINlkiqsggligkqifqyaynyklanlrkgfkqheaSPFFDKIVfskikeG 381
Cdd:PLN02479 272 AKAIYSAIANYGVTHFCAAPVVLNTI---VN----------------------------------APKSETIL------P 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 382 LGGRIRLMLSGAAPLPRHI----EEFMRVTGCCALAQGYGLTESCAGC--FTSIanifsmigtvgPPVTaiQARLESIPE 455
Cdd:PLN02479 309 LPRVVHVMTAGAAPPPSVLfamsEKGFRVTHTYGLSETYGPSTVCAWKpeWDSL-----------PPEE--QARLNARQG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 456 MGYDALSN-----------VPR-----GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:PLN02479 376 VRYIGLEGldvvdtktmkpVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
490 500
....*....|....*....|....*....
gi 357156424 520 FkLSQGEYVAVEVLESAYVQSPLVTSVWV 548
Cdd:PLN02479 456 I-ISGGENISSLEVENVVYTHPAVLEASV 483
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
80-574 |
1.92e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 98.57 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLydtlGPNAVEFILDH----AEISIAF 155
Cdd:PRK06178 60 TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV----SPLFREHELSYelndAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 156 VQASKIKSLLAILPKCTAHIKAIVSFGDV-----TNELKREVEQLRVSCFSWEE-FSTMGTETQDIS--RKQKDDICTIM 227
Cdd:PRK06178 136 ALDQLAPVVEQVRAETSLRHVIVTSLADVlpaepTLPLPDSLRAPRLAAAGAIDlLPALRACTAPVPlpPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 228 YTSGTTGDPKGVIITNRAIIaGVMTTENLLELtdkVVSEDDSYFSYLPlahIFDQVIENYC----IFKGASIGF---Wqg 300
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAV---VGGEDSVFLSFLP---EFWIAGENFGllfpLFSGATLVLlarW-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 301 DIRYLMEDVQVMKPTIFCGV----------PRVYDriytginlkiqsggligkqifqyaynYKLANLRkgfkQHEASPFF 370
Cdd:PRK06178 287 DAVAFMAAVERYRVTRTVMLvdnavelmdhPRFAE--------------------------YDLSSLR----QVRVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 371 DKIVfskikeglggrirlmlsgaaplPRHIEEFMRVTGCCALAQGYGLTES-CAGCFTS--IANIFSMIGT---VGPPVT 444
Cdd:PRK06178 337 KKLN----------------------PDYRQRWRALTGSVLAEAAWGMTEThTCDTFTAgfQDDDFDLLSQpvfVGLPVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 445 AIQARLESipemgYDALSNVP---RGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFK 521
Cdd:PRK06178 395 GTEFKICD-----FETGELLPlgaEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 357156424 522 LSqGEYVAVEVLESAYVQSPLVTSVWVYGNSFE---SFLVAVVVPEKQAIEDWAAL 574
Cdd:PRK06178 470 VN-GMSVFPSEVEALLGQHPAVLGSAVVGRPDPdkgQVPVAFVQLKPGADLTAAAL 524
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
220-541 |
2.00e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 98.59 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 220 KDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTEN-----LLELTDKVVSEddsyfsyLPLAHIFDQVIeNYCIF--KG 292
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAaygplLHPGKELVVTA-------LPLYHIFALTV-NCLLFieLG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 293 ASiGFWQGDIRYLMEDVQVMKPTIFCGVprvydriyTGINlkiqsggligkQIFQYAYNyklanlrkgfkqheaSPFFDK 372
Cdd:PRK08974 277 GQ-NLLITNPRDIPGFVKELKKYPFTAI--------TGVN-----------TLFNALLN---------------NEEFQE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 373 IVFSkikeglggRIRLMLSGAAPLPRHI-EEFMRVTGCcALAQGYGLTEsCAGCFTSIA-NIFSMIGTVGPPVTAIQARL 450
Cdd:PRK08974 322 LDFS--------SLKLSVGGGMAVQQAVaERWVKLTGQ-YLLEGYGLTE-CSPLVSVNPyDLDYYSGSIGLPVPSTEIKL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 451 esIPEMGYDaLSNVPRGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKK--------NIFKL 522
Cdd:PRK08974 392 --VDDDGNE-VPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKdmilvsgfNVYPN 468
|
330 340
....*....|....*....|.
gi 357156424 523 SQGEYVAV--EVLESAYVQSP 541
Cdd:PRK08974 469 EIEDVVMLhpKVLEVAAVGVP 489
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
221-523 |
2.68e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.97 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTD----KVVSE-DDSYFSYLPLAHIFDQVIENYCIFKgasi 295
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGpdgqPLMKEgQEVMIAPLPLYHIYAFTANCMCMMV---- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 296 gfwQGDIRYLMEDvqvmkptifcgvPRvydriytginlkiQSGGLIgKQIFQYAYNyKLANLRKGFKQHEASPFFDKIVF 375
Cdd:PRK12492 283 ---SGNHNVLITN------------PR-------------DIPGFI-KELGKWRFS-ALLGLNTLFVALMDHPGFKDLDF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 376 SKIKEGLGGrirlmlsGAAPLPRHIEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAiqARLESIPE 455
Cdd:PRK12492 333 SALKLTNSG-------GTALVKATAERWEQLTGC-TIVEGYGLTETSPVASTNPYGELARLGTVGIPVPG--TALKVIDD 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 456 MGyDALSNVPRGEICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLS 523
Cdd:PRK12492 403 DG-NELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
48-615 |
3.37e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 97.82 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKNRMLGQRQVSDGKAGDYvwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG 127
Cdd:PRK13295 28 DDLDACVASCPDKTAVTAVRLGTGAPRRF---TYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 128 ICYVPLYDTLGPNAVEFILDHAEisiafvqaskikSLLAILPKctaHIKAIvSFGDVTNELKREVEQLRVSCF------- 200
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAE------------SKVLVVPK---TFRGF-DHAAMARRLRPELPALRHVVVvggdgad 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 201 SWEE-FSTMGTETQ-------DISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFS 272
Cdd:PRK13295 169 SFEAlLITPAWEQEpdapailARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG-----ADDVILM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 273 YLPLAHIfdqvienycifkgasIGFWQGdirylmedvqVMKPTIFcGVPRVYDRIYT---GINLkIQSGGLigkqifqya 349
Cdd:PRK13295 244 ASPMAHQ---------------TGFMYG----------LMMPVML-GATAVLQDIWDparAAEL-IRTEGV--------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 350 yNYKLAnlrkgfkqheASPFFDKIVfSKIKEGlgGR----IRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGC 425
Cdd:PRK13295 288 -TFTMA----------STPFLTDLT-RAVKES--GRpvssLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 426 FTSIANIFS-MIGTVGPPVTAIQARLESipemgyDALSNVPRGEI---CLRGHTLFSGYYKRPDLTEEVFsDGWFHTGDI 501
Cdd:PRK13295 354 LTKLDDPDErASTTDGCPLPGVEVRVVD------ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTDA-DGWFDTGDL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 502 GEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKqaiedwaalnNKT 578
Cdd:PRK13295 427 ARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLgerACAFVVPRP----------GQS 495
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 357156424 579 SDFAELCNDPK----ARRYI------QDELNKT--GK--KLGLRgfEMLRA 615
Cdd:PRK13295 496 LDFEEMVEFLKaqkvAKQYIperlvvRDALPRTpsGKiqKFRLR--EMLRG 544
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
71-603 |
3.41e-21 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 98.03 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 71 GKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPL---Y------------- 134
Cdd:PRK08180 62 GADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYslvsqdfgklrhv 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 135 -DTLGPNAVeFILDHAeisiAFVQAskiksLLAILPkctAHIKAIVSFGDVTNElkreveqlrvSCFSWEEF-STMGTET 212
Cdd:PRK08180 142 lELLTPGLV-FADDGA----AFARA-----LAAVVP---ADVEVVAVRGAVPGR----------AATPFAALlATPPTAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 213 QD--ISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAG-VMTTENLLELTDkvvsEDDSYFSYLPLAH------IFDQV 283
Cdd:PRK08180 199 VDaaHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANqQMLAQTFPFLAE----EPPVLVDWLPWNHtfggnhNLGIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 284 IENycifkGASI----------GFWQgDIRYLMEdvqvMKPTIFCGVPRVYDRIYTGinLKiqsggligkqifqyaynyK 353
Cdd:PRK08180 275 LYN-----GGTLyiddgkptpgGFDE-TLRNLRE----ISPTVYFNVPKGWEMLVPA--LE------------------R 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 354 LANLRKGFkqheaspffdkivFSkikeglggRIRLMLSGAAPLPRHI----EEF-MRVTG-CCALAQGYGLTEScAGCFT 427
Cdd:PRK08180 325 DAALRRRF-------------FS--------RLKLLFYAGAALSQDVwdrlDRVaEATCGeRIRMMTGLGMTET-APSAT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 428 SIANIFSMIGTVGPPVTAIQARLesipemgydalsnVPRG---EICLRGHTLFSGYYKRPDLTEEVFSD-GWFHTGDIGE 503
Cdd:PRK08180 383 FTTGPLSRAGNIGLPAPGCEVKL-------------VPVGgklEVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGDAVR 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 504 W----QP------DGtmkiidRKKNIFKLSQGEYVAVEVLESAYVQ--SPLVTSVWVYGNSFEsFLVAVVVPEKQAIEDW 571
Cdd:PRK08180 450 FvdpaDPerglmfDG------RIAEDFKLSSGTWVSVGPLRARAVSagAPLVQDVVITGHDRD-EIGLLVFPNLDACRRL 522
|
570 580 590
....*....|....*....|....*....|....*
gi 357156424 572 AALNNKTSDfAELCNDPKARRYIQD---ELNKTGK 603
Cdd:PRK08180 523 AGLLADASL-AEVLAHPAVRAAFRErlaRLNAQAT 556
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
80-562 |
3.99e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 97.26 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kikslLAILPkctahikAIVSFGDVTNELKREveqlrvscfSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK06145 109 -----FDAIV-------ALETPKIVIDAAAQA---------DSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IIT---------NRAIIAGVMTTENLLeltdkVVSeddsyfsylPLAHIfdqvieNYCIFKGASIgFWQGDIRYLMEDVQ 310
Cdd:PRK06145 168 MHSygnlhwksiDHVIALGLTASERLL-----VVG---------PLYHV------GAFDLPGIAV-LWVGGTLRIHREFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 vmKPTIFCGVPRvyDRIYTGINLKIQSGGLIGkqiFQYAYNYKLANLRKGFKQHEASPffdkivfskikeglGGRIRlml 390
Cdd:PRK06145 227 --PEAVLAAIER--HRLTCAWMAPVMLSRVLT---VPDRDRFDLDSLAWCIGGGEKTP--------------ESRIR--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 sgaaplprhieEFMRVTGCCALAQGYGLTESCAG-CFTSIANIFSMIGTVGPPVTAIQARLESipEMGYDALSNVpRGEI 469
Cdd:PRK06145 283 -----------DFTRVFTRARYIDAYGLTETCSGdTLMEAGREIEKIGSTGRALAHVEIRIAD--GAGRWLPPNM-KGEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 470 CLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVY 549
Cdd:PRK06145 349 CMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVI 427
|
490
....*....|....*.
gi 357156424 550 G---NSFESFLVAVVV 562
Cdd:PRK06145 428 GvhdDRWGERITAVVV 443
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
220-550 |
8.98e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 96.45 E-value: 8.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 220 KDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTDKVVSEDDSYFSYLPLAHIFdqvienycifkGASIgFWQ 299
Cdd:PLN02574 197 QDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIY-----------GLSL-FVV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 300 GDIRyLMEDVQVMKptifcgvprvydriytginlKIQSGGLIgKQIFQYAYNY------KLANLRKGFKQHEASPFfdki 373
Cdd:PLN02574 265 GLLS-LGSTIVVMR--------------------RFDASDMV-KVIDRFKVTHfpvvppILMALTKKAKGVCGEVL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 374 vfskikeglgGRIRLMLSGAAPLPRH-IEEFMRVTGCCALAQGYGLTESCA----GCFTSIANIFSMIGTVGPPVTAIQA 448
Cdd:PLN02574 319 ----------KSLKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSSVGLLAPNMQAKVV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 449 RLES---IPEMGydalsnvpRGEICLRGHTLFSGYYKRPDLTE-EVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLsQ 524
Cdd:PLN02574 389 DWSTgclLPPGN--------CGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-K 459
|
330 340
....*....|....*....|....*.
gi 357156424 525 GEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:PLN02574 460 GFQIAPADLEAVLISHPEIIDAAVTA 485
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-602 |
2.49e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 95.11 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFiLDHAEISI 153
Cdd:PRK07470 29 GDRSW-TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAY-LAEASGAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELkrEVEQLRVScfsweefsTMGTETQDiSRKQKDDICTIMYTSGTT 233
Cdd:PRK07470 107 AMICHADFPEHAAAVRAASPDLTHVVAIGGARAGL--DYEALVAR--------HLGARVAN-AAVDHDDPCWFFFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 234 GDPKGVIITNraiiaGVMT---TENLLELTDKVvSEDDSYFSYLPLAHifdqvienycifkGASIgfwqgdiRYLMedvQ 310
Cdd:PRK07470 176 GRPKAAVLTH-----GQMAfviTNHLADLMPGT-TEQDASLVVAPLSH-------------GAGI-------HQLC---Q 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 VMK--PTIFCGVPRvydriytginlkiqsggLIGKQIFQYAYNYKLANL------RKGFKQHEASPFFDKivfskikegl 382
Cdd:PRK07470 227 VARgaATVLLPSER-----------------FDPAEVWALVERHRVTNLftvptiLKMLVEHPAVDRYDH---------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 383 gGRIRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTEsCAGCFTSIANIF--------SMIGTVGPPVTAIQARLESip 454
Cdd:PRK07470 280 -SSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE-VTGNITVLPPALhdaedgpdARIGTCGFERTGMEVQIQD-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 455 emgyDALSNVP---RGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVE 531
Cdd:PRK07470 356 ----DEGRELPpgeTGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 532 VLESAYVQSPLVTSVWVYG---NSFESFLVAVVVPEKQAIEDWAALNnktsdfAELcnDPKARRY-------IQDELNKT 601
Cdd:PRK07470 431 EIEEKLLTHPAVSEVAVLGvpdPVWGEVGVAVCVARDGAPVDEAELL------AWL--DGKVARYklpkrffFWDALPKS 502
|
.
gi 357156424 602 G 602
Cdd:PRK07470 503 G 503
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
75-574 |
8.29e-20 |
|
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: 92.74 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 75 DYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDHAEISI 153
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQASKIKSLLAILPKCTAHIKAIVSFGDVtnelkreveqlrvscfsweefstMGTETQDisrkqkDDICTIMYTSGTT 233
Cdd:cd12116 88 VLTDDALPDRLPAGLPVLLLALAAAAAAPAA-----------------------PRTPVSP------DDLAYVIYTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 234 GDPKGVIITNRAIIA---------GVMTTENLLELTdkVVSEDDSYFS-YLPLAHifdqvienycifkGASIGFWQGDIR 303
Cdd:cd12116 139 GRPKGVVVSHRNLVNflhsmrerlGLGPGDRLLAVT--TYAFDISLLElLLPLLA-------------GARVVIAPRETQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 304 YlmeDVQVMKPTIfcgvprvyDRIytGINLkiqsggligkqiFQyaynyklanlrkgfkqheASPFFDKIVFSkikEGLG 383
Cdd:cd12116 204 R---DPEALARLI--------EAH--SITV------------MQ------------------ATPATWRMLLD---AGWQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 GRIRL-MLSGAAPLPRHIEEFMRVTGCCaLAQGYGLTEscagcftsiANIFSMIGTVGPPVTAIQARlESIPemGY---- 458
Cdd:cd12116 238 GRAGLtALCGGEALPPDLAARLLSRVGS-LWNLYGPTE---------TTIWSTAARVTAAAGPIPIG-RPLA--NTqvyv 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 459 --DALSNVPRG---EICLRGHTLFSGYYKRPDLTEEVFSDG--------WFHTGDIGEWQPDGTMKIIDRKKNIFKLsQG 525
Cdd:cd12116 305 ldAALRPVPPGvpgELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI-RG 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 357156424 526 EYVAVEVLESAYVQSPLVT--SVWVYGNSFESFLVAVVVPEKQAIEDWAAL 574
Cdd:cd12116 384 HRIELGEIEAALAAHPGVAqaAVVVREDGGDRRLVAYVVLKAGAAPDAAAL 434
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
221-641 |
8.75e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 93.32 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIagvmtTENLLELTDKVVSEDDSYFSYLPLAHIfdqvienycifkgasigfwqG 300
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALI-----VQSLAKIAIVGYGEDDVYLHTAPLCHI--------------------G 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 301 DIRYLMEDVQVMkptifcgvprvydriytginlkiqsggliGKQIFQYAYNYKLAnlRKGFKQHEASPFF-------DKI 373
Cdd:PLN02860 227 GLSSALAMLMVG-----------------------------ACHVLLPKFDAKAA--LQAIKQHNVTSMItvpammaDLI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 374 VFSKIKEGLGGR--IRLMLSGAAPLP-RHIEEFMRVTGCCALAQGYGLTESCAG----------CFTSIANIFSMIGT-- 438
Cdd:PLN02860 276 SLTRKSMTWKVFpsVRKILNGGGSLSsRLLPDAKKLFPNAKLFSAYGMTEACSSltfmtlhdptLESPKQTLQTVNQTks 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 439 ----------VGPPVTAIQARLesipemGYDALSNVprGEICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPD 507
Cdd:PLN02860 356 ssvhqpqgvcVGKPAPHVELKI------GLDESSRV--GRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 508 GTMKIIDRKKNIFKlSQGEYVAVEVLESAYVQSPLVTSVWVYGNSfESFLVAVVVPEKQAIEDWAALNNktsdfaELCND 587
Cdd:PLN02860 428 GNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGVP-DSRLTEMVVACVRLRDGWIWSDN------EKENA 499
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 357156424 588 PKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGiekdlITPTFKLKRPQL 641
Cdd:PLN02860 500 KKNLTLSSETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
48-519 |
1.12e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.89 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKnrmlgQRQVSDGKAGDYvwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG 127
Cdd:PRK06087 27 DYWQQTARAMPD-----KIAVVDNHGASY---TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 128 ICYVPLydtlGPNavefiLDHAEISIAFvqaSKIKSLLAILP---KCTAHIKAIVSfgdvtneLKREVEQLRVSCFswee 204
Cdd:PRK06087 99 AVSVPL----LPS-----WREAELVWVL---NKCQAKMFFAPtlfKQTRPVDLILP-------LQNQLPQLQQIVG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 205 FSTMGTETQDISRKQ---------------KDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDS 269
Cdd:PRK06087 156 VDKLAPATSSLSLSQiiadyeplttaitthGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-----WQDV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 270 YFSYLPLAHifdqvienycifkgaSIGFWQGdirylmedvqVMKPTIFcgvprvydriytginlkiqSGGLIGKQIFQYA 349
Cdd:PRK06087 231 FMMPAPLGH---------------ATGFLHG----------VTAPFLI-------------------GARSVLLDIFTPD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 350 YNYKLANLRKGFKQHEASPF-FDKIVFSKIKEGLGGRIRLMLSGAAPLPRhieefmRVTGCC-----ALAQGYGLTESCA 423
Cdd:PRK06087 267 ACLALLEQQRCTCMLGATPFiYDLLNLLEKQPADLSALRFFLCGGTTIPK------KVARECqqrgiKLLSVYGSTESSP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 424 GCFTSIANIFS-MIGTVGPPVTAIQARLESipemgyDALSNVPRG---EICLRGHTLFSGYYKRPDLTEEVF-SDGWFHT 498
Cdd:PRK06087 341 HAVVNLDDPLSrFMHTDGYAAAGVEIKVVD------EARKTLPPGcegEEASRGPNVFMGYLDEPELTARALdEEGWYYS 414
|
490 500
....*....|....*....|.
gi 357156424 499 GDIGEWQPDGTMKIIDRKKNI 519
Cdd:PRK06087 415 GDLCRMDEAGYIKITGRKKDI 435
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
80-567 |
6.35e-19 |
|
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: 90.00 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDhaeisiafvqa 158
Cdd:cd05945 18 TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILD----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 skiksllailpkcTAHIKAIVSFGDvtnelkreveqlrvscfsweefstmgtetqdisrkqkdDICTIMYTSGTTGDPKG 238
Cdd:cd05945 86 -------------AAKPALLIADGD--------------------------------------DNAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAgvmTTENLLELTDkvVSEDDSYFSYLPLAhiFDqvIENYCIFKGASIG--FW------QGDIRYLMEDVQ 310
Cdd:cd05945 115 VQISHDNLVS---FTNWMLSDFP--LGPGDVFLNQAPFS--FD--LSVMDLYPALASGatLVpvprdaTADPKQLFRFLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 VMKPTIFCGVPRVydriytgINLKIQSGGLIGKqifqyaynyKLANLRkgfkqheaSPFFDKIVFSKikeglgGRIRlML 390
Cdd:cd05945 186 EHGITVWVSTPSF-------AAMCLLSPTFTPE---------SLPSLR--------HFLFCGEVLPH------KTAR-AL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAAPLprhieefmrvtgcCALAQGYGLTESCAGCfTSIANIFSMIGT-----VGPPVTAiqARLESIPEMGyDALSNVP 465
Cdd:cd05945 235 QQRFPD-------------ARIYNTYGPTEATVAV-TYIEVTPEVLDGydrlpIGYAKPG--AKLVILDEDG-RPVPPGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 466 RGEICLRGHTLFSGYYKRPDLTEEVF--SDG--WFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSP 541
Cdd:cd05945 298 KGELVISGPSVSKGYLNNPEKTAAAFfpDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVP 376
|
490 500
....*....|....*....|....*....
gi 357156424 542 LVTS---VWVYGNSFESFLVAVVVPEKQA 567
Cdd:cd05945 377 GVKEavvVPKYKGEKVTELIAFVVPKPGA 405
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
45-602 |
1.06e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 90.08 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 45 SPWDFFSEAVKKYPkNR---MLGQRQVsdgkagdyvwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQ 121
Cdd:PLN03102 15 TPITFLKRASECYP-NRtsiIYGKTRF-----------TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 122 ACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQ---ASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREV-EQLRV 197
Cdd:PLN03102 83 AVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDrsfEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSsEELDY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 198 SCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGVIITNR--------AIIAGVMTTENLleltdkvvsedds 269
Cdd:PLN03102 163 ECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRgaylstlsAIIGWEMGTCPV------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 270 YFSYLPLAHIFDQVIE-NYCIFKGASIGFWQGDIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKIQsggligkqifqy 348
Cdd:PLN03102 230 YLWTLPMFHCNGWTFTwGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 349 aynyklanlrkgfkqHEASPffdkivfskikeglggrIRLMLSGAAPLPRHIEEFMRVTgcCALAQGYGLTESCAGC-FT 427
Cdd:PLN03102 298 ---------------PRSGP-----------------VHVLTGGSPPPAALVKKVQRLG--FQVMHAYGLTEATGPVlFC 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 428 SIANIFSMIgtvgPPVTAI--QAR-------LESIPEMGYDALSNVPR-----GEICLRGHTLFSGYYKRPDLTEEVFSD 493
Cdd:PLN03102 344 EWQDEWNRL----PENQQMelKARqgvsilgLADVDVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFKH 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 494 GWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGE-----------YVAVEVLESAYVQSPLVTsvwvYGNSFESFLVaVVV 562
Cdd:PLN03102 420 GWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGEnissvevenvlYKYPKVLETAVVAMPHPT----WGETPCAFVV-LEK 493
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 357156424 563 PEKQAIEDWAALNNKTSDFAELCND-------PKARRYIQdELNKTG 602
Cdd:PLN03102 494 GETTKEDRVDKLVTRERDLIEYCREnlphfmcPRKVVFLQ-ELPKNG 539
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
41-550 |
1.10e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 89.74 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 41 KEIQSPWDffsEAVKKYPKNRMLgqrqVSDGKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAM 120
Cdd:PRK08008 7 QHLRQMWD---DLADVYGHKTAL----IFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 121 QACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIKSLLAILPKCTAHIKAIVsfgdVTNELKREVEQlrVSCF 200
Cdd:PRK08008 80 FGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHIC----LTRVALPADDG--VSSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 201 SwEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGVIITNRAII-AGVMTT-ENLLeltdkvvSEDDSYFSYLPLAH 278
Cdd:PRK08008 154 T-QLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAwQCAL-------RDDDVYLTVMPAFH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 279 IFDQ---------------VIENYCIFKgasigFWQGDIRY---LMEDVQVMKPTIFCGVPRVYDR------IYTGINLK 334
Cdd:PRK08008 226 IDCQctaamaafsagatfvLLEKYSARA-----FWGQVCKYratITECIPMMIRTLMVQPPSANDRqhclreVMFYLNLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 335 IQSggligKQIFQYAYNyklanlrkgfkqheaspffdkivfskikeglggrIRLMLSgaaplprhieefmrvtgccalaq 414
Cdd:PRK08008 301 DQE-----KDAFEERFG----------------------------------VRLLTS----------------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 415 gYGLTESCAGcftsianifsMIGTvgPPVTAiqARLESI--PEMGYDA---------LSNVPRGEICLRG---HTLFSGY 480
Cdd:PRK08008 319 -YGMTETIVG----------IIGD--RPGDK--RRWPSIgrPGFCYEAeirddhnrpLPAGEIGEICIKGvpgKTIFKEY 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357156424 481 YKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:PRK08008 384 YLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
20-655 |
1.34e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 89.72 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 20 RPSAGPVYRSIYAkdgLMPLPKEIQspwDFFSEAVKKYPKNRMLGQRqvsDGKAGDYVWQTYEEVYQKVIKIGAAIRSFG 99
Cdd:PRK12582 31 RADGSIVIKSRHP---LGPYPRSIP---HLLAKWAAEAPDRPWLAQR---EPGHGQWRKVTYGEAKRAVDALAQALLDLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 100 VKPGGHCGIYGSNCPEWVMAMQACSSQGICYVP-----------------LYDTLGPNAVeFILDHAEIS--IAFVQASK 160
Cdd:PRK12582 102 LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPvspayslmshdhaklkhLFDLVKPRVV-FAQSGAPFAraLAALDLLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 161 IkSLLAILPKCTAhiKAIVSFGD-VTNELKREVEQlrvscfsweEFSTMGTETqdisrkqkddICTIMYTSGTTGDPKGV 239
Cdd:PRK12582 181 V-TVVHVTGPGEG--IASIAFADlAATPPTAAVAA---------AIAAITPDT----------VAKYLFTSGSTGMPKAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNR---AIIAGVMTTENLLELTDKVVSEDdsyfsYLPLAHIFdqvienycifkGASIGF----WQGDIRYLMEDvqvm 312
Cdd:PRK12582 239 INTQRmmcANIAMQEQLRPREPDPPPPVSLD-----WMPWNHTM-----------GGNANFngllWGGGTLYIDDG---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 KPtifcgVPrvydriytginlkiqsgGLIGKQIfqyaynyklANLRkgfkqhEASPffdkIVFSKIKEGLG--------- 383
Cdd:PRK12582 299 KP-----LP-----------------GMFEETI---------RNLR------EISP----TVYGNVPAGYAmlaeamekd 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 --------GRIRLMLSGAAPLPRHIEEFM-----RVTGC-CALAQGYGLTEScAGCFTSIANIFSMIGTVGPPVTAIQAR 449
Cdd:PRK12582 338 dalrrsffKNLRLMAYGGATLSDDLYERMqalavRTTGHrIPFYTGYGATET-APTTTGTHWDTERVGLIGLPLPGVELK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 450 LesipemgydalsnVPRG---EICLRGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEW-QPDGTMK--IID-RKKNIFK 521
Cdd:PRK12582 417 L-------------APVGdkyEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARFvDPDDPEKglIFDgRVAEDFK 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 522 LSQGEYVAVEVLESAYVQ--SPLVTSVWVYGNSfESFLVAVVVPEKQAIEDWAAlnNKTSDFAELCNDPKARRYIQDEL- 598
Cdd:PRK12582 484 LSTGTWVSVGTLRPDAVAacSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAG--DPDAAPEDVVKHPAVLAILREGLs 560
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 599 --NKTGKKLGLRgfemLRAVHLEPVPFGIEKDLITPTFKLKRPQLLKYYKDRVDQLYKD 655
Cdd:PRK12582 561 ahNAEAGGSSSR----IARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
80-517 |
3.34e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 88.48 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAI-RSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFV-- 156
Cdd:PRK08314 37 SYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVgs 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 157 -QASKIKSLLAILPkcTAHikAIV-SFGD---VTNELK--------REVEQLRVS-CFSWEEFSTMGtETQDISRKQKDD 222
Cdd:PRK08314 117 eLAPKVAPAVGNLR--LRH--VIVaQYSDylpAEPEIAvpawlraePPLQALAPGgVVAWKEALAAG-LAPPPHTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 223 ICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIfdqvienycifkgasIGFwqgdi 302
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST-----PESVVLAVLPLFHV---------------TGM----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 303 rylmedVQVMKPTIFCG-----VPRvYDRIytginlkiQSGGLIGKqifqyaynYKL---ANLRKGFKQHEASPFFDKIV 374
Cdd:PRK08314 247 ------VHSMNAPIYAGatvvlMPR-WDRE--------AAARLIER--------YRVthwTNIPTMVVDFLASPGLAERD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 375 FSKIKeGLGGrirlmlsGAAPLPRHIEEFMR-VTGCCALaQGYGLTESCAGcftSIANifsmigtvgPPVtaiQARLE-- 451
Cdd:PRK08314 304 LSSLR-YIGG-------GGAAMPEAVAERLKeLTGLDYV-EGYGLTETMAQ---THSN---------PPD---RPKLQcl 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 452 SIPEMGYDA-------LSNVPR---GEICLRGHTLFSGYYKRPDLTEEVFS--DG--WFHTGDIGEWQPDGTMKIIDRKK 517
Cdd:PRK08314 360 GIPTFGVDArvidpetLEELPPgevGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLK 439
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
80-517 |
7.06e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 87.70 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICyVPLYDTLGPNAVEFILDHAEISI-----A 154
Cdd:PRK07529 60 TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVlvtlgP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 155 FVQ---ASKIKSLLAILPkctaHIKAIVSFG---------DVTNELKREVEQLRVSCFSWEEFSTMGTETQDISRKQKDD 222
Cdd:PRK07529 139 FPGtdiWQKVAEVLAALP----ELRTVVEVDlarylpgpkRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 223 ICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQ-VIENYCIFKGASIGF---- 297
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLG-----PGDTVFCGLPLFHVNALlVTGLAPLARGAHVVLatpq 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 298 -WQGD--IRYLMEDVQVMKPTIFCGVPRVYdriytGINLKIQSGGligkqifqyaynYKLANLRKGFkqheaspffdkiv 374
Cdd:PRK07529 290 gYRGPgvIANFWKIVERYRINFLSGVPTVY-----AALLQVPVDG------------HDISSLRYAL------------- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 375 fskikeglggrirlmlSGAAPLPRH-IEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESI 453
Cdd:PRK07529 340 ----------------CGAAPLPVEvFRRFEAATGV-RIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVIL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 454 PEMGyDALSNVPR---GEICLRGHTLFSGYykrpdLTEE-----VFSDGWFHTGDIGEWQPDGTMKIIDRKK 517
Cdd:PRK07529 403 DDAG-RYLRDCAVdevGVLCIAGPNVFSGY-----LEAAhnkglWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
80-550 |
8.92e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 86.40 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILdhaeisiafvQAS 159
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRL----------ENS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLailpkctahikaivsfgdVTNELKReveqlrvscfsweefstmgtetqdisRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd05969 72 EAKVLI------------------TTEELYE--------------------------RTDPEDPTLLHYTSGTTGTPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTDkvvseDDSYFSYLPLAHIFDQVienYCIF----KGASIGFWQG--DIRYLMEDVQVMK 313
Cdd:cd05969 108 LHVHDAMIFYYFTGKYVLDLHP-----DDIYWCTADPGWVTGTV---YGIWapwlNGVTNVVYEGrfDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 314 PTIFCGVPrvydriyTGINLKIQSGGLIGKQifqyaynYKLANLRkgfkqheaspffdkivfskikeglggrirLMLSGA 393
Cdd:cd05969 180 VTVWYTAP-------TAIRMLMKEGDELARK-------YDLSSLR-----------------------------FIHSVG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 394 APL-PRHIEEFMRVTGCcALAQGYGLTESCAgcfTSIANIFSM---IGTVGPPVTAIQARLesIPEMGyDALSNVPRGEI 469
Cdd:cd05969 217 EPLnPEAIRWGMEVFGV-PIHDTWWQTETGS---IMIANYPCMpikPGSMGKPLPGVKAAV--VDENG-NELPPGTKGIL 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 470 CLRGH--TLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVA-VEVlESAYVQSPLVTSV 546
Cdd:cd05969 290 ALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGpFEV-ESALMEHPAVAEA 367
|
....
gi 357156424 547 WVYG 550
Cdd:cd05969 368 GVIG 371
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
53-662 |
1.06e-17 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 87.99 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 53 AVKKYPKNRMLGQRQvsdgKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVP 132
Cdd:PTZ00297 436 SVTRHSTFRCLGQTS----ESGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLP 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 133 LYDTlgPNAVEFILDHAEISIAFVQASKIKSLLAilpkC-TAHIKAIV---SFGDVTNELKreVEQLRVSCFSWEEFSTM 208
Cdd:PTZ00297 512 LVGK--GSTMRTLIDEHKIKVVFADRNSVAAILT----CrSRKLETVVythSFYDEDDHAV--ARDLNITLIPYEFVEQK 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 209 GTETQDISRKQKDDICTIMYTSGTT----GDPKGVIitnRAIIAGVMTTENLLELTDKVVS--EDDSYFSYLPLAHIFDQ 282
Cdd:PTZ00297 584 GRLCPVPLKEHVTTDTVFTYVVDNTtsasGDGLAVV---RVTHADVLRDISTLVMTGVLPSsfKKHLMVHFTPFAMLFNR 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 283 VIENYCIFKGASIGfwQGDIRYLMEDVQVMKPTIFCGVPRVYDRIYTGINLKIQSGGLIGKQIFQYAYNYK--LANLRKg 360
Cdd:PTZ00297 661 VFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRsrLINIHR- 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 361 fkqhEASPFFDKIVFSKIKEGLGGRIR-LMLSGAaplprhiEEfmrvtgccalAQGYGLTESCAGCFT------SIANIF 433
Cdd:PTZ00297 738 ----RDSSLLRFIFFRATQELLGGCVEkIVLCVS-------EE----------STSFSLLEHISVCYVpclrevFFLPSE 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 434 SMIGTVGPPVTAIQARLESIpemgyDALSN-VPRGEICL--RGhtlfsgyykRPDLTEEVFSdgwfhtgdigEWQPDGTM 510
Cdd:PTZ00297 797 GVFCVDGTPAPSLQVDLEPF-----DEPSDgAGIGQLVLakKG---------EPRRTLPIAA----------QWKRDRTL 852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 511 KIIDRKKNIFKLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESfLVAVVVPEKQAIE-DW--------AALNNKTSDF 581
Cdd:PTZ00297 853 RLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWrqshcmgeGGGPARQLGW 931
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 582 AELCNdpKARRYIQDELNKTGKKLGLRGFEMLRAVHLEPVPFGIEKDLITPTFKLKRPQLLKYYKDRVDQLYKDAKMATA 661
Cdd:PTZ00297 932 TELVA--YASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDVETTPL 1009
|
.
gi 357156424 662 P 662
Cdd:PTZ00297 1010 P 1010
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
73-567 |
1.76e-17 |
|
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: 85.79 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 73 AGDYVWqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPnavefildhaeis 152
Cdd:cd12114 8 CGDGTL-TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV-DIDQP------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 153 iafvqASKIKSLLAilpkcTAHIKAIVSFGdvtnelkrEVEQLRVSCF--SWEEFSTMGTETQDISRK-QKDDICTIMYT 229
Cdd:cd12114 73 -----AARREAILA-----DAGARLVLTDG--------PDAQLDVAVFdvLILDLDALAAPAPPPPVDvAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 230 SGTTGDPKGVIITNRAiiagVMTTenLLELTDK-VVSEDDSYFSYLPLAH---IFDqvienycIF----KGASIGFWQGD 301
Cdd:cd12114 135 SGSTGTPKGVMISHRA----ALNT--ILDINRRfAVGPDDRVLALSSLSFdlsVYD-------IFgalsAGATLVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 302 IR----YLMEDVQVMKPTIFCGVPrvydriytginlkiqsggligkQIFQYAYNYKLANlrkgfkqheaspffdkivfsk 377
Cdd:cd12114 202 RRrdpaHWAELIERHGVTLWNSVP----------------------ALLEMLLDVLEAA--------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 378 ikEGLGGRIRL-MLSG---AAPLPRHIEEfmRVTGCCALAQGyGLTEscagcfTSIANIFSmigtvgpPVTAIQARLESI 453
Cdd:cd12114 239 --QALLPSLRLvLLSGdwiPLDLPARLRA--LAPDARLISLG-GATE------ASIWSIYH-------PIDEVPPDWRSI 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 454 P--------------EMGYDALSNVPrGEICLRGHTLFSGYYKRPDLTEEVF---SDG--WFHTGDIGEWQPDGTMKIID 514
Cdd:cd12114 301 PygrplanqryrvldPRGRDCPDWVP-GELWIGGRGVALGYLGDPELTAARFvthPDGerLYRTGDLGRYRPDGTLEFLG 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 357156424 515 RKKNIFKLsQGEYVAVEVLESAYVQSPLVTS--VWVYGNSFESFLVAVVVPEKQA 567
Cdd:cd12114 380 RRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
80-515 |
1.82e-17 |
|
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: 85.84 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGP-NAVEFILDHAEISIAFVQA 158
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPeERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 SkiksllaiLPKCTAHIKAIVSFGDVTNElKREVEQLRVSCfsweefstmgtetqdisrkQKDDICTIMYTSGTTGDPKG 238
Cdd:cd17655 103 H--------LQPPIAFIGLIDLLDEDTIY-HEESENLEPVS-------------------KSDDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIagvmtteNLLELTDKVV--SEDDSYFSYLPLAhiFDqvienycifkgASigfwqgdirylmedVQVMKPTI 316
Cdd:cd17655 155 VMIEHRGVV-------NLVEWANKVIyqGEHLRVALFASIS--FD-----------AS--------------VTEIFASL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 317 FCGvprvyDRIYTGINLKIQSGGLIGKQIFQYAynyklANLRKGFKQHeaspfFDKIVFSKIKEGLggRIRLMLSGAAPL 396
Cdd:cd17655 201 LSG-----NTLYIVRKETVLDGQALTQYIRQNR-----ITIIDLTPAH-----LKLLDAADDSEGL--SLKHLIVGGEAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 397 P-RHIEEFMRVTGC-CALAQGYGLTESCAGCftsianifsMIGtvgpPVTAIQARLESIPeMGyDALSN----------- 463
Cdd:cd17655 264 StELAKKIIELFGTnPTITNAYGPTETTVDA---------SIY----QYEPETDQQVSVP-IG-KPLGNtriyildqygr 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357156424 464 -VP---RGEICLRGHTLFSGYYKRPDLTEEVFSDGWF-------HTGDIGEWQPDGTMKIIDR 515
Cdd:cd17655 329 pQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermyRTGDLARWLPDGNIEFLGR 391
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
80-564 |
2.63e-17 |
|
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: 85.33 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:cd12117 24 TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPkctahikaivsFGDVTNELKREVEQLRVSCFSweefstmgtetqdisrkqKDDICTIMYTSGTTGDPKGV 239
Cdd:cd12117 104 LAGRAGGLEV-----------AVVIDEALDAGPAGNPAVPVS------------------PDDLAYVMYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTeNLLELTdkvvsEDDSYFSYLPLAhiFDqvienycifkGASIGFWqgdirylmedvqvmkptifcg 319
Cdd:cd12117 155 AVTHRGVVRLVKNT-NYVTLG-----PDDRVLQTSPLA--FD----------ASTFEIW--------------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 VPRVydriyTGINLKIQSGGLIgkqifqyaynYKLANLRKGFKQHEA------SPFFDKIVfSKIKEGLGGRIRLMLSGA 393
Cdd:cd12117 196 GALL-----NGARLVLAPKGTL----------LDPDALGALIAEEGVtvlwltAALFNQLA-DEDPECFAGLRELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 394 APLPRHIEEFMRVTGCCALAQGYGLTES--CAGCFtSIANIFSMIGTV--GPPVTAIQARLesIPEMGYDALSNVPrGEI 469
Cdd:cd12117 260 VVSPPHVRRVLAACPGLRLVNGYGPTENttFTTSH-VVTELDEVAGSIpiGRPIANTRVYV--LDEDGRPVPPGVP-GEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 470 CLRGHTLFSGYYKRPDLTEEVFS-----DG--WFHTGDIGEWQPDGTMKIIDR-----KKNIFKLSQGEyvavevLESAY 537
Cdd:cd12117 336 YVGGDGLALGYLNRPALTAERFVadpfgPGerLYRTGDLARWLPDGRLEFLGRiddqvKIRGFRIELGE------IEAAL 409
|
490 500 510
....*....|....*....|....*....|
gi 357156424 538 VQSPLVTSVWVY---GNSFESFLVAVVVPE 564
Cdd:cd12117 410 RAHPGVREAVVVvreDAGGDKRLVAYVVAE 439
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
61-550 |
9.68e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 83.65 E-value: 9.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 61 RMLGQRQ-VSDGKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPE----W--VMAMQAcssqgICYVpL 133
Cdd:PRK06018 21 RIHGNREvVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRhleaWygIMGIGA-----ICHT-V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 134 YDTLGPNAVEFILDHAEISIAFVQASKIKSLLAILPKcTAHIKAIVSFGDVT----NELKREV--EQLRVSC---FSWEE 204
Cdd:PRK06018 95 NPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADK-LPSVERYVVLTDAAhmpqTTLKNAVayEEWIAEAdgdFAWKT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 205 FStmgtetqdisrkqKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTEN--LLELTDKvvsedDSYFSYLPLAH---- 278
Cdd:PRK06018 174 FD-------------ENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNgdALGTSAA-----DTMLPVVPLFHansw 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 279 --------IFDQVIENYCIFKGASIgfwqgdirYLMEDVQvmKPTIFCGVPRVYdriytginlkiqsggligKQIFQY-- 348
Cdd:PRK06018 236 giafsapsMGTKLVMPGAKLDGASV--------YELLDTE--KVTFTAGVPTVW------------------LMLLQYme 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 349 AYNYKLANLRKgfkqheaspffdkivfskikeglggrirlMLSGAAPLPRHIEEFMRVTGcCALAQGYGLTEScagcfts 428
Cdd:PRK06018 288 KEGLKLPHLKM-----------------------------VVCGGSAMPRSMIKAFEDMG-VEVRHAWGMTEM------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 429 ianifSMIGTVG---PPVTAIQ--ARLESIPEMGY-----------DALSNVPR-----GEICLRGHTLFSGYYKRPDlt 487
Cdd:PRK06018 331 -----SPLGTLAalkPPFSKLPgdARLDVLQKQGYppfgvemkitdDAGKELPWdgktfGRLKVRGPAVAAAYYRVDG-- 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357156424 488 EEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:PRK06018 404 EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
226-550 |
1.29e-16 |
|
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: 81.55 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 226 IMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDqVIENYCIFK--GASIGFWQGDIR 303
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLT-----EADVYLNMLPLFHIAG-LNLALATFHagGANVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 304 YLMEDVQVMKPTIFCGVPRVYDRIYTGINlkiqsggligkqifqyAYNYKLANLRkgfkqheaspffdkIVFskikeGLG 383
Cdd:cd17637 79 EALELIEEEKVTLMGSFPPILSNLLDAAE----------------KSGVDLSSLR--------------HVL-----GLD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 GrirlmlsgaaplPRHIEEFMRVTGCCALAqGYGLTEscAGCFTSIANIFSMIGTVGPPVTAIQARLesipemgYDALSN 463
Cdd:cd17637 124 A------------PETIQRFEETTGATFWS-LYGQTE--TSGLVTLSPYRERPGSAGRPGPLVRVRI-------VDDNDR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 464 -VPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRK--KNIFKlSQGEYVAVEVLESAY 537
Cdd:cd17637 182 pVPAgetGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVI 260
|
330
....*....|...
gi 357156424 538 VQSPLVTSVWVYG 550
Cdd:cd17637 261 LEHPAIAEVCVIG 273
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
80-509 |
2.57e-16 |
|
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: 83.37 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDHAEISIAFVQA 158
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPL-DPAYPAErLAYMLEDAGARLVLTQS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 SkiksLLAILPKctahikaivsfgdvtnelkrevEQLRVSCFSWEEFSTMGTETQDISRkQKDDICTIMYTSGTTGDPKG 238
Cdd:COG1020 582 A----LAARLPE----------------------LGVPVLALDALALAAEPATNPPVPV-TPDDLAYVIYTSGSTGRPKG 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAGVMTTENLLELT--DKV-----VSEDDSYFS-YLPLAHifdqvienycifkGASI----GFWQGDIRYLM 306
Cdd:COG1020 635 VMVEHRALVNLLAWMQRRYGLGpgDRVlqfasLSFDASVWEiFGALLS-------------GATLvlapPEARRDPAALA 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 307 EDVQVMKPTIFCGVPRVYdriytginlkiqsggligkQIFQYAYNYKLANLRkgfkqheaspffdkivfskikeglggri 386
Cdd:COG1020 702 ELLARHRVTVLNLTPSLL-------------------RALLDAAPEALPSLR---------------------------- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 387 RLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTEscagcfTSI-ANIFsmigtvgpPVTAIQARLESIPeMGYdALSN-- 463
Cdd:COG1020 735 LVLVGGEALPPELVRRWRARLPGARLVNLYGPTE------TTVdSTYY--------EVTPPDADGGSVP-IGR-PIANtr 798
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357156424 464 ----------VP---RGEICLRGHTLFSGYYKRPDLTEEVF------SDG--WFHTGDIGEWQPDGT 509
Cdd:COG1020 799 vyvldahlqpVPvgvPGELYIGGAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGN 865
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
80-600 |
8.97e-16 |
|
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: 80.63 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQas 159
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahIKAIVSFGDVTNELKREVEQLRVSCFSWEEFstmGTETQDISRKQKDDiCTIMYTSGTTGDPKGV 239
Cdd:cd05923 108 ---------------VDAQVMDAIFQSGVRVLALSDLVGLGEPESA---GPLIEDPPREPEQP-AFVFYTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGV--MTTENLLELTDKVVSeddsyFSYLPLAHifdqVIENYCIFKGASI--GFW-------QGDIRYLMED 308
Cdd:cd05923 169 VIPQRAAESRVlfMSTQAGLRHGRHNVV-----LGLMPLYH----VIGFFAVLVAALAldGTYvvveefdPADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 309 VQVmkpTIFCGVPRVYDriytginlkiqsgGLIGKQIFQYAynyKLANLRK-GFkqheASPFFDKIVFSKIKEGLGGRIr 387
Cdd:cd05923 240 ERV---TSLFATPTHLD-------------ALAAAAEFAGL---KLSSLRHvTF----AGATMPDAVLERVNQHLPGEK- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 lmlsgaaplprhieefmrvtgccalAQGYGLTEScagcFTSIANIFSMIGTVGPPVTAIQARLESIPEMGYDALSNVPRG 467
Cdd:cd05923 296 -------------------------VNIYGTTEA----MNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 468 EIC--LRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTS 545
Cdd:cd05923 347 ELIvaAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTE 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 357156424 546 VWVYGNSFESF---LVAVVVPEKQAIEdwAALNNKTSDFAELCNDPKARRY-IQDELNK 600
Cdd:cd05923 426 VVVIGVADERWgqsVTACVVPREGTLS--ADELDQFCRASELADFKRPRRYfFLDELPK 482
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
74-577 |
1.35e-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: 79.84 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 74 GDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPlydtlgpnavefildhaeISI 153
Cdd:cd05908 11 KKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVP------------------VSI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 154 AFVQASKIKSLlailpkctahikaivsfgDVTNELKREVeqlrvscfsweefstMGTEtQDISRKQKDDICTIMYTSGTT 233
Cdd:cd05908 73 GSNEEHKLKLN------------------KVWNTLKNPY---------------LITE-EEVLCELADELAFIQFSSGST 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 234 GDPKGVIITNRAIIAGVMTTENLLELTDKvvsedDSYFSYLPLAHIFDQVIENY-CIFKGASigfwqgdiRYLMedvqvm 312
Cdd:cd05908 119 GDPKGVMLTHENLVHNMFAILNSTEWKTK-----DRILSWMPLTHDMGLIAFHLaPLIAGMN--------QYLM------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 kPTifcgvprvydriytgiNLKIQSGGLIGKQIFQYAYNyKLANLRKGFKQheaspFFDKIVFSKIKEGLGGRIRLMLSG 392
Cdd:cd05908 180 -PT----------------RLFIRRPILWLKKASEHKAT-IVSSPNFGYKY-----FLKTLKPEKANDWDLSSIRMILNG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 393 AAP-LPRHIEEFMRVTGCCALAQG-----YGLTE-SCAGCFTSIANIFSMIG------TVGPPVTAI---QARLESIPEM 456
Cdd:cd05908 237 AEPiDYELCHEFLDHMSKYGLKRNailpvYGLAEaSVGASLPKAQSPFKTITlgrrhvTHGEPEPEVdkkDSECLTFVEV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 457 GYdALSN------------VPR---GEICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGeWQPDGTMKIIDRKKN-I 519
Cdd:cd05908 317 GK-PIDEtdiricdednkiLPDgyiGHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLG-FIRNGRLVITGREKDiI 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357156424 520 FKLSQGEY------VAVEVLEsayVQSPLVTSVWVYGNSFESFLVAVVVPEKQAIEDWAALNNK 577
Cdd:cd05908 395 FVNGQNVYphdierIAEELEG---VELGRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKK 455
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-550 |
1.96e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 79.02 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 93 AAIRSFGVKPGGHCGIYGSNCPEWVMAM----QACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIKSLLAIL 168
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTYIELSfavaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 169 PKCtaHIKAIVSFGDVTNELKREVEQLRVScfsweefstmgtetqdisrkqKDDICTIMYTSGTTGDPKGVIITNRAIIA 248
Cdd:cd05922 88 PAS--PDPGTVLDADGIRAARASAPAHEVS---------------------HEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 249 GVMTTENLLELTdkvvsEDDSYFSYLPLAHIFDQVIENYCIFKGASI----------GFWqgdirylmEDVQVMKPTIFC 318
Cdd:cd05922 145 NARSIAEYLGIT-----ADDRALTVLPLSYDYGLSVLNTHLLRGATLvltndgvlddAFW--------EDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 319 GVPRVYdriytginlkiqsgGLIGKQIFQYAynyKLANLRkgfkqheaspFFDKIvfskikeglGGRIRlmlsgaaplPR 398
Cdd:cd05922 212 GVPSTY--------------AMLTRLGFDPA---KLPSLR----------YLTQA---------GGRLP---------QE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 399 HIEEFmrvtgcCALAQG------YGLTEscagCFTSIA-----NIFSMIGTVGPPVTaiQARLESIPEMGYDALSNVPrG 467
Cdd:cd05922 247 TIARL------RELLPGaqvyvmYGQTE----ATRRMTylppeRILEKPGSIGLAIP--GGEFEILDDDGTPTPPGEP-G 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 468 EICLRGHTLFSGYYKRP-DLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSV 546
Cdd:cd05922 314 EIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGLIIEA 392
|
....
gi 357156424 547 WVYG 550
Cdd:cd05922 393 AAVG 396
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
79-550 |
3.91e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.67 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 79 QTYEEVYQKVIKIGAAIR-SFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQ 157
Cdd:PRK05620 39 TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 158 ASKIKSLLAILPKCTAhIKAIVSFGDVTNELKREVEQLRVSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPK 237
Cdd:PRK05620 119 PRLAEQLGEILKECPC-VRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 238 GVIITNRAIIAGVMTtenlLELTDKV-VSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIR--YLMEDVQVMKP 314
Cdd:PRK05620 198 GVVYSHRSLYLQSLS----LRTTDSLaVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSapTLAKIIATAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 315 TIFCGVPRVYdriytgINLkiqsggligkqIFQYAYNyklanlrkgfkqheaSPffDKIVFSKIKEGlggrirlmlsGAA 394
Cdd:PRK05620 274 RVAHGVPTLW------IQL-----------MVHYLKN---------------PP--ERMSLQEIYVG----------GSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 395 PLPRHI---EEFMRVTgccaLAQGYGLTEScagcftsianifSMIGTVGPPVTAI--QARL---ES---IP-EMGY---- 458
Cdd:PRK05620 310 VPPILIkawEERYGVD----VVHVWGMTET------------SPVGTVARPPSGVsgEARWayrVSqgrFPaSLEYrivn 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 459 --DALSNVPR--GEICLRGHTLFSGYYKRP-----------------DLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKK 517
Cdd:PRK05620 374 dgQVMESTDRneGEIQVRGNWVTASYYHSPteegggaastfrgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRAR 453
|
490 500 510
....*....|....*....|....*....|...
gi 357156424 518 NIFKlSQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:PRK05620 454 DVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
70-520 |
2.68e-14 |
|
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: 76.12 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 70 DGKAGDYVWQTYEEVYQKVIKIGAAIRSFGvKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVE---FIL 146
Cdd:cd05931 16 DDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAErlaAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 147 DHAEISIAFVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREveqlrvscfSWEEFStmgtetqdisrKQKDDICTI 226
Cdd:cd05931 95 ADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAA---------DWPPPS-----------PDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 227 MYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAH---IFDQVIENycIFKGASIgfwqgdir 303
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLD-----PGDVVVSWLPLYHdmgLIGGLLTP--LYSGGPS-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 304 YLMEdvqvmkPTIFCGVPRVYdriytginLKiqsggLIGKqifqyaynyklanlRKGfkQHEASP-F-FDKIVfSKIK-E 380
Cdd:cd05931 220 VLMS------PAAFLRRPLRW--------LR-----LISR--------------YRA--TISAAPnFaYDLCV-RRVRdE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 381 GLGG----RIRLMLSGAAPL-PRHIEEFMRVTGCC-----ALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARL 450
Cdd:cd05931 264 DLEGldlsSWRVALNGAEPVrPATLRRFAEAFAPFgfrpeAFRPSYGLAEATLFVSGGPPGTGPVVLRVDRDALAGRAVA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 451 ESIPEMGY------------------DALSNVPR-----GEICLRGHTLFSGYYKRPDLTEEVF-------SDGWFHTGD 500
Cdd:cd05931 344 VAADDPAArelvscgrplpdqevrivDPETGRELpdgevGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGD 423
|
490 500
....*....|....*....|....*..
gi 357156424 501 IG-----EWQPDGTMK--IIDRKKNIF 520
Cdd:cd05931 424 LGflhdgELYITGRLKdlIIVRGRNHY 450
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
218-609 |
3.01e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 76.50 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 218 KQKDDICTIMYTSGTTGDPKGVIITNRAIIAgvmtteNLLELTDKV-VSEDDSYFSYLPLAHIFdqvienycifkGASIG 296
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNILS------NIEQISDVFnLRNDDVILSSLPFFHSF-----------GLTVT 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 297 FWQgdirylmedvqvmkPTIfCGVPRVY-----DriytginlkiqsGGLIGKQIFQYAYNYKLANlrkgfkqheaSPFF- 370
Cdd:PRK08633 842 LWL--------------PLL-EGIKVVYhpdptD------------ALGIAKLVAKHRATILLGT----------PTFLr 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 371 --------DKIVFSKIkeglggriRLMLSGAAPLPRHI-EEFMRVTGCCALaQGYGLTESCAGCFTSIANI--------- 432
Cdd:PRK08633 885 lylrnkklHPLMFASL--------RLVVAGAEKLKPEVaDAFEEKFGIRIL-EGYGATETSPVASVNLPDVlaadfkrqt 955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 433 FSMIGTVGPPVTAIQARLESiPEmgydALSNVPRGE---ICLRGHTLFSGYYKRPDLTEEVFSD----GWFHTGDIGEWQ 505
Cdd:PRK08633 956 GSKEGSVGMPLPGVAVRIVD-PE----TFEELPPGEdglILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLD 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 506 PDGTMKIIDRKKNIFKLSqGEYVAVEVLESAyVQSPLVTSVWVygnsfesfLVAVVVPEKQAIEDWAAL-NNKTSDFAEL 584
Cdd:PRK08633 1031 EDGFLTITDRYSRFAKIG-GEMVPLGAVEEE-LAKALGGEEVV--------FAVTAVPDEKKGEKLVVLhTCGAEDVEEL 1100
|
410 420 430
....*....|....*....|....*....|....*.
gi 357156424 585 ------CNDP---KARRYIQ-DELNKTGK-KLGLRG 609
Cdd:PRK08633 1101 kraikeSGLPnlwKPSRYFKvEALPLLGSgKLDLKG 1136
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
81-515 |
4.38e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.43 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 81 YEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEF---ILDHAEISIA--- 154
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERfcqITDPAAALVApgs 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 155 FVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREVEQLrvscfsweefsTMGTetqdisrkqkDDICTIMYTSGTTG 234
Cdd:PRK05857 124 KMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA-----------DQGS----------EDPLAMIFTSGTTG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 235 DPKGVIITNRAIIA--GVMTTENlLELTDKVVSEddSYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDIRYLMEDVQVM 312
Cdd:PRK05857 183 EPKAVLLANRTFFAvpDILQKEG-LNWVTWVVGE--TTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 313 KPTIFCGVPRVYDRIytginlkiqsggligkqifqyAYNYKLAnlrkgfkqheaspffDKIVFSkikeglggrIRLMLSG 392
Cdd:PRK05857 260 AVATTCLVPTLLSKL---------------------VSELKSA---------------NATVPS---------LRLVGYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 393 AAPLPRHIEEFMRVTGcCALAQGYGLTEScaGCFT--------SIANIFSmiGTVGPPVTAIQARLEsiPEMG-----YD 459
Cdd:PRK05857 295 GSRAIAADVRFIEATG-VRTAQVYGLSET--GCTAlclptddgSIVKIEA--GAVGRPYPGVDVYLA--ATDGigptaPG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 357156424 460 ALSNVPRGEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDR 515
Cdd:PRK05857 368 AGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGR 423
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
80-240 |
6.35e-14 |
|
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: 74.83 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQ-- 157
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 158 ---ASKIKSLLAILPKCTAH---IKAIVsfgdVTNELKREVEQLRVSCFSWEEFstMGTETQDISRKQKDDICTIMYTSG 231
Cdd:cd05968 173 ftrRGREVNLKEEADKACAQcptVEKVV----VVRHLGNDFTPAKGRDLSYDEE--KETAGDGAERTESEDPLMIIYTSG 246
|
....*....
gi 357156424 232 TTGDPKGVI 240
Cdd:cd05968 247 TTGKPKGTV 255
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
173-550 |
6.41e-14 |
|
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: 74.84 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 173 AHIKAIVSFGDvtNELKREVEQLRVSCFS--------------WEEF-------STMGTETQDISRKQKDDICTIMYTSG 231
Cdd:cd05970 118 ADIKMIVAIAE--DNIPEEIEKAAPECPSkpklvwvgdpvpegWIDFrkliknaSPDFERPTANSYPCGEDILLVYFSSG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 232 TTGDPKgviitnraiiagvmttenlleltdkVVSEDDSYfsylPLAHIfdqvienycifkgASIGFWQ----GDIRYLME 307
Cdd:cd05970 196 TTGMPK-------------------------MVEHDFTY----PLGHI-------------VTAKYWQnvreGGLHLTVA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 DVQVMKPtifcgvprVYDRIYtginlkiqSGGLIGKQIFQYAYN-YKLANLRKGFKQHEASPFF--DKIVFSKIKEGLG- 383
Cdd:cd05970 234 DTGWGKA--------VWGKIY--------GQWIAGAAVFVYDYDkFDPKALLEKLSKYGVTTFCapPTIYRFLIREDLSr 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 ---GRIRLMLSGAAPL-PRHIEEFMRVTGCcALAQGYGLTEscagCFTSIANIFSM---IGTVGPPvtAIQARLESIPEM 456
Cdd:cd05970 298 ydlSSLRYCTTAGEALnPEVFNTFKEKTGI-KLMEGFGQTE----TTLTIATFPWMepkPGSMGKP--APGYEIDLIDRE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 457 GyDALSNVPRGEICLRGHT-----LFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVE 531
Cdd:cd05970 371 G-RSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFE 449
|
410
....*....|....*....
gi 357156424 532 VlESAYVQSPLVTSVWVYG 550
Cdd:cd05970 450 V-ESALIQHPAVLECAVTG 467
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-564 |
1.88e-13 |
|
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: 72.73 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAfvqas 159
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd17653 99 -------------------------------------------------------LTTDSPDDLAYIIFTSGSTGIPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELT--DKVvseddsyfsyLPLAHI-FDQVIENY--CIFKGASIGF------WQGDIRYLmeD 308
Cdd:cd17653 124 MVPHRGVLNYVSQPPARLDVGpgSRV----------AQVLSIaFDACIGEIfsTLCNGGTLVLadpsdpFAHVARTV--D 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 309 VQVMKPTIFCGV-PRVYDRIYTginlkIQSGGligkqifqyaynyklanlrkgfkqhEASPFfdkivfSKIKEGLGGRir 387
Cdd:cd17653 192 ALMSTPSILSTLsPQDFPNLKT-----IFLGG-------------------------EAVPP------SLLDRWSPGR-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 lmlsgaaplprhieefmrvtgccALAQGYGLTE-SCAGCFTSIANI-FSMIGTVGP--PVTAIQARLESIPEMgydalsn 463
Cdd:cd17653 234 -----------------------RLYNAYGPTEcTISSTMTELLPGqPVTIGKPIPnsTCYILDADLQPVPEG------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 464 vPRGEICLRGHTLFSGYYKRPDLT-----EEVFSDGW--FHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESA 536
Cdd:cd17653 284 -VVGEICISGVQVARGYLGNPALTaskfvPDPFWPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEV 361
|
490 500
....*....|....*....|....*....
gi 357156424 537 YVQS-PLVTSVWVYgnSFESFLVAVVVPE 564
Cdd:cd17653 362 VLQSqPEVTQAAAI--VVNGRLVAFVTPE 388
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
415-564 |
2.03e-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: 71.95 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 415 GYGLTEsCAGCFTSIANIFSMIGTVGPPVTAIQARLesIPEMGYDalsnVPRG---EICLRGHTLFSGYYKRPDLTEEVF 491
Cdd:cd17636 142 GYGQTE-VMGLATFAALGGGAIGGAGRPSPLVQVRI--LDEDGRE----VPDGevgEIVARGPTVMAGYWNRPEVNARRT 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357156424 492 SDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYV-AVEVlESAYVQSPLVTSVWVYG---NSFESFLVAVVVPE 564
Cdd:cd17636 215 RGGWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIyPAEV-ERCLRQHPAVADAAVIGvpdPRWAQSVKAIVVLK 289
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-550 |
3.27e-13 |
|
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: 72.08 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISiafvqas 159
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikAIVSfgdvtnelkreveqlrvscfsweefstmgtetqDISrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd05971 81 -----------------ALVT---------------------------------DGS----DDPALIIYTSGTTGPPKGA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIA---GVMTTENLLELTDkvvseddsyfsylplahifdqvienYCIFKGASIGfWQGDIrylmedVQVMKPTI 316
Cdd:cd05971 107 LHAHRVLLGhlpGVQFPFNLFPRDG-------------------------DLYWTPADWA-WIGGL------LDVLLPSL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 317 FCGVPRVYDRiytginlkiqSGGLIGKQIFQYAYNYKLANL------RKGFKQHEaSPFFDKIVfskikeglggRIRLML 390
Cdd:cd05971 155 YFGVPVLAHR----------MTKFDPKAALDLMSRYGVTTAflpptaLKMMRQQG-EQLKHAQV----------KLRAIA 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAAPLPRHIEEFMRVTGCCALAQGYGLTEsCAGCFTSIANIFSMI-GTVGPPVTAiqarleSIPEMGYDALSNVP---R 466
Cdd:cd05971 214 TGGESLGEELLGWAREQFGVEVNEFYGQTE-CNLVIGNCSALFPIKpGSMGKPIPG------HRVAIVDDNGTPLPpgeV 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 467 GEICLR--GHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYVAVEVLESAYVQSPLVT 544
Cdd:cd05971 287 GEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVL 365
|
....*.
gi 357156424 545 SVWVYG 550
Cdd:cd05971 366 MAAVVG 371
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-550 |
3.58e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 71.36 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTeNLLELTDkvvsEDDSYFSYLPLAHIFDQVIENYC-IFKGASIGF-- 297
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWML-ALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 298 ---WQGD--IRYLMEDVQVMKPTIFCGVPRVYdriytginlkiqsggligKQIFQYAYNYKLANLRkgfkqheaspffdk 372
Cdd:cd05944 77 pagYRNPglFDNFWKLVERYRITSLSTVPTVY------------------AALLQVPVNADISSLR-------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 373 ivfskikeglggrirLMLSGAAPLP----RHIEEFMRVTgccaLAQGYGLTEscAGCFTSIA--NIFSMIGTVGPPVTAI 446
Cdd:cd05944 125 ---------------FAMSGAAPLPvelrARFEDATGLP----VVEGYGLTE--ATCLVAVNppDGPKRPGSVGLRLPYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 447 QARLESIpemgyDALSNVPR-------GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:cd05944 184 RVRIKVL-----DGVGRLLRdcapdevGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
330 340 350
....*....|....*....|....*....|.
gi 357156424 520 FkLSQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd05944 259 I-IRGGHNIDPALIEEALLRHPAVAFAGAVG 288
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
80-574 |
5.46e-13 |
|
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: 71.34 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAs 159
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd17650 93 -------------------------------------------------------------EDLAYVIYTSGTTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTDKVVSeddsyfsYLPLAHI-FDQVIENYCIfkgasiGFWQGDIRYLMEDVQVMKPTifc 318
Cdd:cd17650 112 MVEHRNVAHAAHAWRREYELDSFPVR-------LLQMASFsFDVFAGDFAR------SLLNGGTLVICPDEVKLDPA--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 319 gvpRVYDRIYT-GINLKIQSGGLIgKQIFQYAYnyklanlRKGFKqheaspfFDKIvfskikeglggRIRLMLSGAAPLP 397
Cdd:cd17650 176 ---ALYDLILKsRITLMESTPALI-RPVMAYVY-------RNGLD-------LSAM-----------RLLIVGSDGCKAQ 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 398 RHIEEFMRVTGCCALAQGYGLTESC--AGCFTSIANIFSMIGTV--GPPV--TAI---QARLESIPEMGYdalsnvprGE 468
Cdd:cd17650 227 DFKTLAARFGQGMRIINSYGVTEATidSTYYEEGRDPLGDSANVpiGRPLpnTAMyvlDERLQPQPVGVA--------GE 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 469 ICLRGHTLFSGYYKRPDLTEEVFSDGWF-------HTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSP 541
Cdd:cd17650 299 LYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHP 377
|
490 500 510
....*....|....*....|....*....|....*.
gi 357156424 542 LVTSVWV---YGNSFESFLVAVVVPEkqAIEDWAAL 574
Cdd:cd17650 378 AIDEAVVavrEDKGGEARLCAYVVAA--ATLNTAEL 411
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
48-239 |
5.94e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.84 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKNRML--GQRQVsdgkagdyvwqTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSS 125
Cdd:PRK07798 7 DLFEAVADAVPDRVALvcGDRRL-----------TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 126 QGIC-------YVplydtlgPNAVEFILDHAEISIAFVQASKIKSLLAILPKcTAHIKAIVSFGDVT-NELKREVEqlrv 197
Cdd:PRK07798 76 ARAVpvnvnyrYV-------EDELRYLLDDSDAVALVYEREFAPRVAEVLPR-LPKLRTLVVVEDGSgNDLLPGAV---- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 357156424 198 scfSWEEFSTMGTETQDISRKQKDDIcTIMYTSGTTGDPKGV 239
Cdd:PRK07798 144 ---DYEDALAAGSPERDFGERSPDDL-YLLYTGGTTGMPKGV 181
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
215-537 |
7.04e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.31 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 215 ISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAgvmtteNLLELTDKV-VSEDDSYFSYLPLAHIFdqvienycifkga 293
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLA------NRAQVAARIdFSPEDKVFNALPVFHSF------------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 294 siGFWQGDIRYLMEDVqvmkPTIFCGVPRVY----DRIYtGINLKIqsggLIGKQIFQYAYnyklANLrkgfkqheASPF 369
Cdd:PRK06814 848 --GLTGGLVLPLLSGV----KVFLYPSPLHYriipELIY-DTNATI----LFGTDTFLNGY----ARY--------AHPY 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 370 -FdkivFSkikeglggrIRLMLSGAAPL---PRHIeeFMRVTGCCALaQGYGLTESCAG--CFTSIANIFsmiGTVGPPV 443
Cdd:PRK06814 905 dF----RS---------LRYVFAGAEKVkeeTRQT--WMEKFGIRIL-EGYGVTETAPViaLNTPMHNKA---GTVGRLL 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 444 TAIQARLESIP--EMGydalsnvprGEICLRGHTLFSGYYK--RPDLTEEVfSDGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:PRK06814 966 PGIEYRLEPVPgiDEG---------GRLFVRGPNVMLGYLRaeNPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRF 1035
|
330 340
....*....|....*....|.
gi 357156424 520 FKLSqGEYV---AVEVLESAY 537
Cdd:PRK06814 1036 AKIA-GEMIslaAVEELAAEL 1055
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
80-603 |
7.54e-13 |
|
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: 70.97 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRS-FGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVqa 158
Cdd:cd05958 12 TYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 skiksllailpkctahikaivsfgdvtnelkreVEQLRVScfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKG 238
Cdd:cd05958 90 ---------------------------------AHALTAS----------------------DDICILAFTSGTTGAPKA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAGVMT-TENLLELTdkvvsEDDSYFSYLPLAHIF--DQVIenycIFK---GAS-IGFWQGDIRYLMEDVQV 311
Cdd:cd05958 115 TMHFHRDPLASADRyAVNVLRLR-----EDDRFVGSPPLAFTFglGGVL----LFPfgvGASgVLLEEATPDLLLSAIAR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 312 MKPTIFCGVPRVYDRIytgINLKIQSGGLIGkqifqyaynyklaNLRKGFKQHEASPffdKIVFSKIKEGLGgrIRLMls 391
Cdd:cd05958 186 YKPTVLFTAPTAYRAM---LAHPDAAGPDLS-------------SLRKCVSAGEALP---AALHRAWKEATG--IPII-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 392 gaaplprhieefmrvtgccalaQGYGLTESCAgCFTSIANIFSMIGTVGPPVTAIQARLesipemgYDALSN-VPRGEI- 469
Cdd:cd05958 243 ----------------------DGIGSTEMFH-IFISARPGDARPGATGKPVPGYEAKV-------VDDEGNpVPDGTIg 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 470 --CLRGHTlfsGYYKRPDLTEE-VFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKlSQGEYVAVEVLESAYVQSPLVTSV 546
Cdd:cd05958 293 rlAVRGPT---GCRYLADKRQRtYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAEC 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357156424 547 WVYGNSFESFLV---AVVVPEKQAIEDwAALNNKTSDFAELCNDP-KARRYIQ--DELNKT--GK 603
Cdd:cd05958 369 AVVGHPDESRGVvvkAFVVLRPGVIPG-PVLARELQDHAKAHIAPyKYPRAIEfvTELPRTatGK 432
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
219-574 |
9.42e-13 |
|
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: 70.93 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAIIagvmtteNLLELTDKVVSEDDSyfsylplahifDQVIENycifkgASIGFw 298
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLV-------NLSHGLIKEYGITSS-----------DRVLQF------ASIAF- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 299 qgdirylmeDVqvmkptifcGVPRVYDRIYTGINLKIQSGGLI--GKQIFQYAYNYKLA--NLRKGFKQHEASpffdkiV 374
Cdd:cd17644 159 ---------DV---------AAEEIYVTLLSGATLVLRPEEMRssLEDFVQYIQQWQLTvlSLPPAYWHLLVL------E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 375 FSKIKEGLGGRIRLMLSGA-APLPRHIEEFMRVTG-CCALAQGYGLTESC--AGCF--TSIANIFSMIGTVGPPVTAIQA 448
Cdd:cd17644 215 LLLSTIDLPSSLRLVIVGGeAVQPELVRQWQKNVGnFIQLINVYGPTEATiaATVCrlTQLTERNITSVPIGRPIANTQV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 449 RLesipemgYDA-LSNVP---RGEICLRGHTLFSGYYKRPDLTEEVFSDGWFH---------TGDIGEWQPDGTMKIIDR 515
Cdd:cd17644 295 YI-------LDEnLQPVPvgvPGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGR 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357156424 516 -----KKNIFKLSQGEyvavevLESAYVQSPLVTSVWVYGNSFES---FLVAVVVPEKQAIEDWAAL 574
Cdd:cd17644 368 idnqvKIRGFRIELGE------IEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVPHYEESPSTVEL 428
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
366-567 |
1.49e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 70.30 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 366 ASPFFDKIVFSKIKEGLGGR----IRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSiaNIFSMIGTVGP 441
Cdd:PRK05852 273 AVPTIHQILLERAATEPSGRkpaaLRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTT--QIEGIGQTENP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 442 PVTAIQARLESIPEM---GYDALSNVPR--GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:PRK05852 351 VVSTGLVGRSTGAQIrivGSDGLPLPAGavGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRI 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 357156424 517 KNIFKLSqGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQA 567
Cdd:PRK05852 431 KELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESA 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-574 |
2.51e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDHAEISIAFVQa 158
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAALLLTQ- 2107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 skiKSLLAILPkCTAHIKAIvsfgdvtnELKREVEqlrvscfsWEEFSTMGTETQdisrKQKDDICTIMYTSGTTGDPKG 238
Cdd:PRK12316 2108 ---RHLLERLP-LPAGVARL--------PLDRDAE--------WADYPDTAPAVQ----LAGENLAYVIYTSGSTGLPKG 2163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAGVMTTENLLELTDKvvsedDSYFSYLPLAhiFDQVIENYC--IFKGAsigfwqgdiRYLMEDVQVMKPTi 316
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPA-----DCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDPE- 2226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 317 fcgvpRVYDRIYtginlkiQSGGLIGkqIFQYAYNYKLAnlrkgfkQHEAspffdkivfskiKEGLGGRIRLMLSGAAPL 396
Cdd:PRK12316 2227 -----QLYDEME-------RHGVTIL--DFPPVYLQQLA-------EHAE------------RDGRPPAVRVYCFGGEAV 2273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 397 PRH-IEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPV-TAIQARLESIPEMGYDALSNVPRGEICLRGH 474
Cdd:PRK12316 2274 PAAsLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIgRALGNRRAYILDADLNLLAPGMAGELYLGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 475 TLFSGYYKRPDLTEEVF------SDG--WFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSPLVTSV 546
Cdd:PRK12316 2354 GLARGYLNRPGLTAERFvpdpfsASGerLYRTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREA 2432
|
490 500 510
....*....|....*....|....*....|
gi 357156424 547 WVYGNSFES--FLVAVVVPEKQAIEDWAAL 574
Cdd:PRK12316 2433 VVVAQDGASgkQLVAYVVPDDAAEDLLAEL 2462
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
221-596 |
3.10e-12 |
|
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: 69.11 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvSEDDSY-FSylplAHIFDqvienycifkgASIgfwq 299
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SESRVLqFA----SYTFD-----------VSI---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 300 gdirylMEdvqVMKPTIFCG---VPRVYDRIytginlkiqsGGLIGkqifqYAYNYK---------LANLrkgfkqheas 367
Cdd:cd05918 163 ------LE---IFTTLAAGGclcIPSEEDRL----------NDLAG-----FINRLRvtwafltpsVARL---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 368 pfFDKIVFSKIKeglggriRLMLSGAAPLPRHIEEFmrvTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQ 447
Cdd:cd05918 209 --LDPEDVPSLR-------TLVLGGEALTQSDVDTW---ADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATC 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 448 ARLEsipEMGYDALsnVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDG--W------------FHTGDIGEWQPDGTM 510
Cdd:cd05918 277 WVVD---PDNHDRL--VPIgavGELLIEGPILARGYLNDPEKTAAAFIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGSL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 511 KIIDRKKNIFKLsQGEyvAVEVLE-SAYVQSPLVTSVWVY-------GNSFESFLVAVVVPEKqaiedwAALNNKTSDFA 582
Cdd:cd05918 352 EYVGRKDTQVKI-RGQ--RVELGEiEHHLRQSLPGAKEVVvevvkpkDGSSSPQLVAFVVLDG------SSSGSGDGDSL 422
|
410
....*....|....
gi 357156424 583 ELCNDPKARRYIQD 596
Cdd:cd05918 423 FLEPSDEFRALVAE 436
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
68-543 |
3.52e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 69.35 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 68 VSDGKAGDYVWQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG-ICYVpLYDTLGPNAVEFIL 146
Cdd:PRK07008 29 VSRRVEGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGaVCHT-INPRLFPEQIAYIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 147 DHAEISIAFVQASKIKSLLAILPKCTaHIKAIVSfgdVTNELKREVEQLRVSCF-SWEEFSTMGTETQDISRKQKDDICt 225
Cdd:PRK07008 108 NHAEDRYVLFDLTFLPLVDALAPQCP-NVKGWVA---MTDAAHLPAGSTPLLCYeTLVGAQDGDYDWPRFDENQASSLC- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 226 imYTSGTTGDPKGVIITNRAIIAGVMTTEnlleLTDKV-VSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGF----WQG 300
Cdd:PRK07008 183 --YTSGTTGNPKGALYSHRSTVLHAYGAA----LPDAMgLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLpgpdLDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 301 DIRY-LMEDVQVmkpTIFCGVPRVYdriytginlkiqsggligKQIFQYAynyKLANLRkgfkqheaspffdkivFSKIK 379
Cdd:PRK07008 257 KSLYeLIEAERV---TFSAGVPTVW------------------LGLLNHM---REAGLR----------------FSTLR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 380 eglggriRLMLSGAAPLPRHIEEFMRVTGCCALaQGYGLTEscagcftsianiFSMIGTV--------GPPVTAIQARLE 451
Cdd:PRK07008 297 -------RTVIGGSACPPAMIRTFEDEYGVEVI-HAWGMTE------------MSPLGTLcklkwkhsQLPLDEQRKLLE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 452 SIPEMGY--------DALSNVP-----RGEICLRGHTLFSGYYKRpdlTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKN 518
Cdd:PRK07008 357 KQGRVIYgvdmkivgDDGRELPwdgkaFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKD 433
|
490 500
....*....|....*....|....*
gi 357156424 519 IFKlSQGEYVAVEVLESAYVQSPLV 543
Cdd:PRK07008 434 VIK-SGGEWISSIDIENVAVAHPAV 457
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
217-534 |
4.22e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 69.35 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 217 RKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVmttENLLELTDkvVSEDDSYFSYLPLAHIFdqvienycifkGASIG 296
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANV---EQIKTIAD--FTPNDRFMSALPLFHSF-----------GLTVG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 297 FWQGdiryLMEDVQVM---KPTIFCGVPR-VYDRiytgiNLKIqsggLIGKQIFqyaynykLANLRKgFkqheASPF-Fd 371
Cdd:PRK08043 425 LFTP----LLTGAEVFlypSPLHYRIVPElVYDR-----NCTV----LFGTSTF-------LGNYAR-F----ANPYdF- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 372 kivfskikeglgGRIRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTEsCAGCFTSIANIFSMIGTVGPPVTAIQARLE 451
Cdd:PRK08043 479 ------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGRILPGMDARLL 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 452 SIP--EMGydalsnvprGEICLRGHTLFSGYYK--RPDLTEEVFSD--------GWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:PRK08043 546 SVPgiEQG---------GRLQLKGPNIMNGYLRveKPGVLEVPTAEnargemerGWYDTGDIVRFDEQGFVQIQGRAKRF 616
|
330
....*....|....*
gi 357156424 520 FKLSqGEYVAVEVLE 534
Cdd:PRK08043 617 AKIA-GEMVSLEMVE 630
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-550 |
6.22e-12 |
|
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: 67.93 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEisiafvqas 159
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctAHIKaivsfgdVTNELKREveqlrvscfsweefstmgtetqdisrKQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd05973 73 -------------ARLV-------VTDAANRH--------------------------KLDSDPFVMMFTSGTTGLPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTDkvvseDDSYfsylplahifdqvienYCIfkgASIGfWQGDIRYlmedvQVMKPtifcg 319
Cdd:cd05973 107 PVPLRALAAFGAYLRDAVDLRP-----EDSF----------------WNA---ADPG-WAYGLYY-----AITGP----- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 vprvydrIYTGINLKIQSGGLIGKQIFQYAYNYKLANLrkgfkqhEASPFFDKIVFS---KIKEGLGGRIRLMLSGAAPL 396
Cdd:cd05973 152 -------LALGHPTILLEGGFSVESTWRVIERLGVTNL-------AGSPTAYRLLMAagaEVPARPKGRLRRVSSAGEPL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 397 PRHIEEFMRVTGCCALAQGYGLTEscAGCFtsIANIFSM-----IGTVGPPVTAiqARLESIPEMGYDALSNVP-RGEIC 470
Cdd:cd05973 218 TPEVIRWFDAALGVPIHDHYGQTE--LGMV--LANHHALehpvhAGSAGRAMPG--WRVAVLDDDGDELGPGEPgRLAID 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTL--FSGYYKRPDLTeevFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSVWV 548
Cdd:cd05973 292 IANSPLmwFRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAV 367
|
..
gi 357156424 549 YG 550
Cdd:cd05973 368 IG 369
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
415-548 |
1.17e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 67.20 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 415 GYGLTEscagcftsianifsMIGTVgppvTAIQArlesipemgyDALSNVPR-----------GEICLRGHTLFSGYYKR 483
Cdd:PRK09029 270 GYGLTE--------------MASTV----CAKRA----------DGLAGVGSplpgrevklvdGEIWLRGASLALGYWRQ 321
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357156424 484 PDLTEEVFSDGWFHTGDIGEWQpDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWV 548
Cdd:PRK09029 322 GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
80-243 |
1.82e-11 |
|
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: 67.22 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISI-----A 154
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLlitadG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 155 FVQASKIKSLLAILPKCtahikAIVSFGDVTNELKREVEQLRVSC-----FSWEEFSTMGTETQDISRKQKDDICTIMYT 229
Cdd:cd17634 166 GVRAGRSVPLKKNVDDA-----LNPNVTSVEHVIVLKRTGSDIDWqegrdLWWRDLIAKASPEHQPEAMNAEDPLFILYT 240
|
170
....*....|....
gi 357156424 230 SGTTGDPKGVIITN 243
Cdd:cd17634 241 SGTTGKPKGVLHTT 254
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
105-550 |
1.38e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 64.32 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 105 HCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASKIksllailpkctahikaivsfgDV 184
Cdd:PRK07867 56 HVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHA---------------------EL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 185 TNELKREVEQLRVSCFSW-EEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGVIITNRAI-IAGVMttenlleLTDK 262
Cdd:PRK07867 115 LDGLDPGVRVINVDSPAWaDELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-------LAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 263 V-VSEDDSYFSYLPLAHIfDQVIENYC--IFKGASI---------GFwqgdirylMEDVqvmkptifcgvpRVYDRIYTG 330
Cdd:PRK07867 188 FgLGPDDVCYVSMPLFHS-NAVMAGWAvaLAAGASIalrrkfsasGF--------LPDV------------RRYGATYAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 331 inlkiqsggLIGKqifqyAYNYKLAN----------LRKGFKqHEASPffdkivfskikeglggrirlmlsgaaplpRHI 400
Cdd:PRK07867 247 ---------YVGK-----PLSYVLATperpddadnpLRIVYG-NEGAP-----------------------------GDI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 401 EEFMRVTGCcALAQGYGLTESCAgcftSIAnifsmiGTVGPPVTAIQARLESIPEMGYDALSNVPRGEICLRGHT----- 475
Cdd:PRK07867 283 ARFARRFGC-VVVDGFGSTEGGV----AIT------RTPDTPPGALGPLPPGVAIVDPDTGTECPPAEDADGRLLnadea 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 476 -----------LFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVT 544
Cdd:PRK07867 352 igelvntagpgGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD-GENLGTAPIERILLRYPDAT 430
|
....*.
gi 357156424 545 SVWVYG 550
Cdd:PRK07867 431 EVAVYA 436
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
80-574 |
2.11e-10 |
|
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: 63.52 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAs 159
Cdd:cd17651 22 TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgDVTNELkrEVEQLRVSCFSWEEFSTmGTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd17651 101 -----------------------ALAGEL--AVELVAVTLLDQPGAAA-GADAEPDPALDADDLAYVIYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIagvmtteNLLELTDKV--VSEDDSYFSYLPLAhiFD-QVIEnycIFK----GASIGF----WQGDIRYLMEd 308
Cdd:cd17651 155 VMPHRSLA-------NLVAWQARAssLGPGARTLQFAGLG--FDvSVQE---IFStlcaGATLVLppeeVRTDPPALAA- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 309 vqvmkptiFCGVPRVyDRIYtginlkiqsggligkqiFQYAYNYKLANLrkgfkqheaspffdkivfSKIKEGLGGRIRL 388
Cdd:cd17651 222 --------WLDEQRI-SRVF-----------------LPTVALRALAEH------------------GRPLGVRLAALRY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 389 MLSGAAPLPRH--IEEFMRVTGCCALAQGYGLTEscagcfTSIANIFSMIG---------TVGPPVTAIQARLESipemg 457
Cdd:cd17651 258 LLTGGEQLVLTedLREFCAGLPGLRLHNHYGPTE------THVVTALSLPGdpaawpappPIGRPIDNTRVYVLD----- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 458 yDALSNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWF-------HTGDIGEWQPDGTMKIIDR-----KKNIFKL 522
Cdd:cd17651 327 -AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRaddqvKIRGFRI 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 357156424 523 SQGEyVAVEVLESAYVQSPLVTSVWVYGNsfESFLVAVVVPEKQAIEDWAAL 574
Cdd:cd17651 406 ELGE-IEAALARHPGVREAVVLAREDRPG--EKRLVAYVVGDPEAPVDAAEL 454
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
80-564 |
8.43e-10 |
|
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: 61.52 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDHAEISIAFVQA 158
Cdd:cd17646 25 TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL-DPGYPADrLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 SkiksLLAILPKCTAHikaivsfgdvtnelkreveqlrVSCFSWEEFSTMGTETQDISRKqkDDICTIMYTSGTTGDPKG 238
Cdd:cd17646 104 D----LAARLPAGGDV----------------------ALLGDEALAAPPATPPLVPPRP--DNLAYVIYTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAI---IAGvMTTENLLELTDKV-----VSEDDSYFSYL-PLAHifdqvienycifkGASI------GfwQGDIR 303
Cdd:cd17646 156 VMVTHAGIvnrLLW-MQDEYPLGPGDRVlqktpLSFDVSVWELFwPLVA-------------GARLvvarpgG--HRDPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 304 YLMEDVQVMKPTIFCGVPRVYDriytginLKIQSGGLIGkqifqyaynykLANLRkgfkqheaspffdkivfskikeglg 383
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSMLR-------VFLAEPAAGS-----------CASLR------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 griRLMLSGAAPLPRHIEEFMRVTGCcALAQGYGLTEscagcfTSIAnifsmigtvgppVTAIQARLE----SIPeMGY- 458
Cdd:cd17646 257 ---RVFCSGEALPPELAARFLALPGA-ELHNLYGPTE------AAID------------VTHWPVRGPaetpSVP-IGRp 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 459 ----------DALSNVPRG---EICLRGHTLFSGYYKRPDLTEEVFSDGWF-------HTGDIGEWQPDGTMKIIDRKKN 518
Cdd:cd17646 314 vpntrlyvldDALRPVPVGvpgELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDD 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 357156424 519 IFKLsQGEYVAVEVLESAYVQSPLVTSVWVY---GNSFESFLVAVVVPE 564
Cdd:cd17646 394 QVKI-RGFRVEPGEIEAALAAHPAVTHAVVVaraAPAGAARLVGYVVPA 441
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
80-240 |
2.01e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 60.75 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVefiLD-----HAEISIA 154
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGV---LDrfgqiEPKVLFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 155 ----------FVQASKIKSLLAILPKCTAHIKAIVSFGDVTNELKREVEqlrvsCFSWEEFSTMGTETQ-DISRKQKDDI 223
Cdd:cd05943 177 vdaytyngkrHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAK-----ALTLEDFLATGAAGElEFEPLPFDHP 251
|
170
....*....|....*..
gi 357156424 224 CTIMYTSGTTGDPKGVI 240
Cdd:cd05943 252 LYILYSSGTTGLPKCIV 268
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
48-653 |
2.39e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 60.27 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 48 DFFSEAVKKYPKNRMLgqrqVSDGKAgdyvwQTYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG 127
Cdd:PRK08279 41 DVFEEAAARHPDRPAL----LFEDQS-----ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 128 ICyVPLYDT-------------LGPNAVefILDHaEISIAFvqaSKIKSLLAILPKCTAHIKAIVSFGDVTNELKREVEQ 194
Cdd:PRK08279 112 AV-VALLNTqqrgavlahslnlVDAKHL--IVGE-ELVEAF---EEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 195 LRVSCFSWEEFSTMgtetqdisrkqkDDICTIMYTSGTTGDPKGVIITNRAIIA--GVMTteNLLELTdkvvsEDDSYFS 272
Cdd:PRK08279 185 APTTNPASRSGVTA------------KDTAFYIYTSGTTGLPKAAVMSHMRWLKamGGFG--GLLRLT-----PDDVLYC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 273 YLPLAH------IFDQVIENycifkGASI---------GFWqgdirylmEDVQVMKPTIFCgvprvydriYTGinlkiqs 337
Cdd:PRK08279 246 CLPLYHntggtvAWSSVLAA-----GATLalrrkfsasRFW--------DDVRRYRATAFQ---------YIG------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 338 ggligkQIFQYaynykLANlrkgfkqHEASPfFDKivfskikeglGGRIRLMLsGAAPLPRHIEEFMRVTGCCALAQGYG 417
Cdd:PRK08279 297 ------ELCRY-----LLN-------QPPKP-TDR----------DHRLRLMI-GNGLRPDIWDEFQQRFGIPRILEFYA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 418 LTEscagCFTSIANIFSMIGTVG--PPVTAIQARLesipeMGYDALSN------------VPRGEICL-------RGHtl 476
Cdd:PRK08279 347 ASE----GNVGFINVFNFDGTVGrvPLWLAHPYAI-----VKYDVDTGepvrdadgrcikVKPGEVGLligritdRGP-- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 477 FSGyYKRPDLTE-----EVFSDG--WFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAV-EVlESAYVQSPLVTSVWV 548
Cdd:PRK08279 416 FDG-YTDPEASEkkilrDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRW-KGENVATtEV-ENALSGFPGVEEAVV 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 549 YGnsfesflvaVVVPEKQAIEDWAALnnKTSDFAELcnDPKA-RRYIQDELNKTGKKLGLRgfemLRAvHLEpvpfgiek 627
Cdd:PRK08279 493 YG---------VEVPGTDGRAGMAAI--VLADGAEF--DLAAlAAHLYERLPAYAVPLFVR----LVP-ELE-------- 546
|
650 660
....*....|....*....|....*....
gi 357156424 628 dlITPTFKLKRPQLLK--YYKDRV-DQLY 653
Cdd:PRK08279 547 --TTGTFKYRKVDLRKegFDPSKVdDPLY 573
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
221-574 |
5.32e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 58.52 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLeltdkvvSEDDSYFSYLPLAHIFD-QVI--------ENYCIfk 291
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRL-------GGPGQWLLALPAHHIAGlQVLvrsviagsEPVEL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 292 GASIGFwqgDIRYLMEDVQVMKPtifcgvprvyDRIYTGinlkiqsggLIGKQifqyaynyklanLRKGFKQHEASP--- 368
Cdd:PRK07824 106 DVSAGF---DPTALPRAVAELGG----------GRRYTS---------LVPMQ------------LAKALDDPAATAala 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 369 FFDKIvfskikeglggrirlmLSGAAPLPRHIEEFMRVTGCcALAQGYGLTESCAGCFTSianifsmigtvGPPVTAIQA 448
Cdd:PRK07824 152 ELDAV----------------LVGGGPAPAPVLDAAAAAGI-NVVRTYGMSETSGGCVYD-----------GVPLDGVRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 449 RLESipemgydalsnvprGEICLRGHTLFSGYYKRPDltEEVFSD-GWFHTGDIGEWQpDGTMKIIDRKKNIFKlSQGEY 527
Cdd:PRK07824 204 RVED--------------GRIALGGPTLAKGYRNPVD--PDPFAEpGWFRTDDLGALD-DGVLTVLGRADDAIS-TGGLT 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 357156424 528 VAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAIEDWAAL 574
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGLPDDRLgqrVVAAVVGDGGPAPTLEAL 315
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
219-574 |
7.26e-09 |
|
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: 58.47 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAIIAgvmttenLLELTDKV--VSEDD------SY---FS----YLPLAHIFDQV 283
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLA-------LFAATQRWfgFNEDDvwtlfhSYafdFSvweiWGALLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 284 IENYCIFKGASigfwqgDIRYLMEDVQVmkpTIFCGVPRvydriytginlkiqsggligkqifqyAYNYKLANLRKGFKQ 363
Cdd:cd17643 164 VVPYEVARSPE------DFARLLRDEGV---TVLNQTPS--------------------------AFYQLVEAADRDGRD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 364 HEASPFfdkIVFskikeglGGRiRLMLSGAAPLPRHIEEfmrvtGCCALAQGYGLTESCAgcFTSI---------ANIFS 434
Cdd:cd17643 209 PLALRY---VIF-------GGE-ALEAAMLRPWAGRFGL-----DRPQLVNMYGITETTV--HVTFrpldaadlpAAAAS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 435 MIGTvgpPVTAIQARLesipemgYDA-LSNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWF--------HTGDIG 502
Cdd:cd17643 271 PIGR---PLPGLRVYV-------LDAdGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmyRTGDLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 503 EWQPDGTMKIIDR-----KKNIFKLSQGEyvavevLESAYVQSPLV--TSVWVY-GNSFESFLVAVVVPEKQAIEDWAAL 574
Cdd:cd17643 341 RRLPDGELEYLGRadeqvKIRGFRIELGE------IEAALATHPSVrdAAVIVReDEPGDTRLVAYVVADDGAAADIAEL 414
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
215-535 |
7.74e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 58.67 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 215 ISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAgvmTTENLLELTDKVvsEDDSYFSYLPLAHIFDQvieNYC----IF 290
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLA---NQRACLKFFSPK--EDDVMMSFLPPFHAYGF---NSCtlfpLL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 291 KGASIGFWQGDI--RYLMEDVQVMKPTIFCGVPRVYDRIytginlkiqsggligkqifqyaynyklanLRKGFKQHEASP 368
Cdd:PRK06334 249 SGVPVVFAYNPLypKKIVEMIDEAKVTFLGSTPVFFDYI-----------------------------LKTAKKQESCLP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 369 ffdkivfskikeglggRIRLMLSGAAPLPRHI-EEFMRVTGCCALAQGYGLTEsCAGCFTsIANIFS--MIGTVGPPVTA 445
Cdd:PRK06334 300 ----------------SLRFVVIGGDAFKDSLyQEALKTFPHIQLRQGYGTTE-CSPVIT-INTVNSpkHESCVGMPIRG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 446 IQARLESipEMGYDALSNVPRGEICLRGHTLFSGYYKRpDLTE---EVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKL 522
Cdd:PRK06334 362 MDVLIVS--EETKVPVSSGETGLVLTRGTSLFSGYLGE-DFGQgfvELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
330
....*....|...
gi 357156424 523 SqGEYVAVEVLES 535
Cdd:PRK06334 439 G-AEMVSLEALES 450
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
226-574 |
8.44e-09 |
|
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: 58.15 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 226 IMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTdkvvSEDdsyfSYLPLAHI-FDQVIEnyCIF----KGASIgfwqg 300
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGD----RELQFASFnFDGAHE--QLLppliCGACV----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 301 dirylmedvqVMKPTIFCGVPRVYDRIytginlkIQSGGlIGKQIFQYAYNYKLANlrkgfkqheaspffdkiVFSKIKE 380
Cdd:cd17649 164 ----------VLRPDELWASADELAEM-------VRELG-VTVLDLPPAYLQQLAE-----------------EADRTGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 381 GLGGRIRLMLSGAAPLPrhIEEFMRVTGC-CALAQGYGLTES--------CAGCFTSIANifSM-IGTVGPPVTA--IQA 448
Cdd:cd17649 209 GRPPSLRLYIFGGEALS--PELLRRWLKApVRLFNAYGPTEAtvtplvwkCEAGAARAGA--SMpIGRPLGGRSAyiLDA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 449 RLESIPemgydalsNVPRGEICLRGHTLFSGYYKRPDLTEEVF------SDG--WFHTGDIGEWQPDGTMKIIDR----- 515
Cdd:cd17649 285 DLNPVP--------VGVTGELYIGGEGLARGYLGRPELTAERFvpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRvdhqv 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357156424 516 KKNIFKLSQGEyVAVEVLESAYVQSPLVTSVWVYGnsfESFLVAVVVPEKQAI--EDWAAL 574
Cdd:cd17649 357 KIRGFRIELGE-IEAALLEHPGVREAAVVALDGAG---GKQLVAYVVLRAAAAqpELRAQL 413
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
81-519 |
1.06e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.09 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 81 YEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLydtlgpnavefildhaEISIAFVQ-AS 159
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL----------------PLPMGFGGrES 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTAhikAIVSFGDVTNELKREV---EQLRVScFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDP 236
Cdd:PRK09192 116 YIAQLRGMLASAQP---AAIITPDELLPWVNEAthgNPLLHV-LSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 237 KGVIITNRAIIAgvmtteNLLELTDK--VVSEDDSYFSYLPLAHifDQVIenycifkgasIGFW------QGDIRYLMED 308
Cdd:PRK09192 192 RGVIITHRALMA------NLRAISHDglKVRPGDRCVSWLPFYH--DMGL----------VGFLltpvatQLSVDYLPTR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 309 VQVMKPTIFcgvprvydriytginLKiqsggLIGKQIFQYAYN----YKLANLRKGFKQHEAspfFDkivFSKIK-EGLG 383
Cdd:PRK09192 254 DFARRPLQW---------------LD-----LISRNRGTISYSppfgYELCARRVNSKDLAE---LD---LSCWRvAGIG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 GR-IRlmlsgAAPLPRHIEEFMRVtGCCALA--QGYGLTEScagcftSIANIFSMIGT------------------VGPP 442
Cdd:PRK09192 308 ADmIR-----PDVLHQFAEAFAPA-GFDDKAfmPSYGLAEA------TLAVSFSPLGSgivveevdrdrleyqgkaVAPG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 443 VTAIQARL-----ESIPEMGY----DALSNVPR---GEICLRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGeWQPDGTM 510
Cdd:PRK09192 376 AETRRVRTfvncgKALPGHEIeirnEAGMPLPErvvGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLG-YLLDGYL 454
|
....*....
gi 357156424 511 KIIDRKKNI 519
Cdd:PRK09192 455 YITGRAKDL 463
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
222-550 |
1.55e-08 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 57.36 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTDKvvsedDSYFSYLPLAHIFDQVIE-NYCIFKGASI----- 295
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS-----DVLYTCLPLYHSTALIVGwSACLASGATLvirkk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 296 ----GFWqgdirylmEDVQVMKPTIFcgvprVYdriytginlkiqsgglIGkQIFQYAYNYKLANLRKGfkqHeaspffd 371
Cdd:cd05940 157 fsasNFW--------DDIRKYQATIF-----QY----------------IG-ELCRYLLNQPPKPTERK---H------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 372 kivfsKIKEGLGGRIRlmlsgaaplPRHIEEFMRVTGCCALAQGYGLTEscagCFTSIANIFSMIGTVG--PPVTAIQAR 449
Cdd:cd05940 197 -----KVRMIFGNGLR---------PDIWEEFKERFGVPRIAEFYAATE----GNSGFINFFGKPGAIGrnPSLLRKVAP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 450 LESI-----------PEMGYdaLSNVPRGE----IC-LRGHTLFSGYYKrPDLTEE-----VFSDG--WFHTGDIGEWQP 506
Cdd:cd05940 259 LALVkydlesgepirDAEGR--CIKVPRGEpgllISrINPLEPFDGYTD-PAATEKkilrdVFKKGdaWFNTGDLMRLDG 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 357156424 507 DGTMKIIDRKKNIFKLsQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd05940 336 EGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
80-550 |
1.71e-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: 57.44 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRS-FGVKPGGHCGIYGSNCPEWVMAMQACSSQGicyvplydtlgpnAVEFILDHAEISIAFVQA 158
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIG-------------AAPAFINYNLSGDPLIHC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 SKIksllailpkctAHIKAIVSfgdvtnelkreveqlrvscfsweefstmgtetqDIsrkqkDDICTIMYTSGTTGDPKG 238
Cdd:cd05937 74 LKL-----------SGSRFVIV---------------------------------DP-----DDPAILIYTSGTTGLPKA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 239 VIITNRAIIAGVMTTENLLELTDkvvseDDSYFSYLPLAHIFDQVIEN-YCIFKGASIG---------FWqgdirylmed 308
Cdd:cd05937 105 AAISWRRTLVTSNLLSHDLNLKN-----GDRTYTCMPLYHGTAAFLGAcNCLMSGGTLAlsrkfsasqFW---------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 309 vqvmkptifcgvPRVYDRiytginlkiqsggliGKQIFQY---AYNYKLANlrkgfkqhEASPfFDKIVFSKIKEGLGGR 385
Cdd:cd05937 170 ------------KDVRDS---------------GATIIQYvgeLCRYLLST--------PPSP-YDRDHKVRVAWGNGLR 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 irlmlsgaaplPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSmIGTVGPPVTAIQARLESI-------PEMGY 458
Cdd:cd05937 214 -----------PDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFG-AGAIGHHGLIRRWKFENQvvlvkmdPETDD 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 459 DALSN-------VPRGE-------ICLRGHTLFSGYYKRPDLTE-----EVFSDG--WFHTGDIGEWQPDGTMKIIDRKK 517
Cdd:cd05937 282 PIRDPktgfcvrAPVGEpgemlgrVPFKNREAFQGYLHNEDATEsklvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLG 361
|
490 500 510
....*....|....*....|....*....|...
gi 357156424 518 NIFKLsQGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:cd05937 362 DTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
221-519 |
2.16e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 57.31 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDICTIMYTSGTTGDPKGVIITNRAIIAGV--MTTENLLELtdkvvsEDDSYFSYLPLAHifDQvienycifkgASIGFW 298
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAeaMFVAAEFDV------ETDVMVSWLPLFH--DM----------GMVGFL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 299 QGDIRYLMEDVQVmKPTIFCGVPRVYDRiytginlkiqsggLIGKqifqyaynYKLANLrkgfkqheASPFFDKIVFSK- 377
Cdd:PRK07768 214 TVPMYFGAELVKV-TPMDFLRDPLLWAE-------------LISK--------YRGTMT--------AAPNFAYALLARr 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 378 ----IKEG---LGGrIRLMLSGAAPL-PRHIEEFmrvtgcCALAQGYGLTESCAGCF-----TSIANIFSMIG------- 437
Cdd:PRK07768 264 lrrqAKPGafdLSS-LRFALNGAEPIdPADVEDL------LDAGARFGLRPEAILPAygmaeATLAVSFSPCGaglvvde 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 438 ------------------------TVGPPVTAIQARLesipemgYDALSNV--PR--GEICLRGHTLFSGYykrpdLTEE 489
Cdd:PRK07768 337 vdadllaalrravpatkgntrrlaTLGPPLPGLEVRV-------VDEDGQVlpPRgvGVIELRGESVTPGY-----LTMD 404
|
330 340 350
....*....|....*....|....*....|....*
gi 357156424 490 VF-----SDGWFHTGDIGEWQPDGTMKIIDRKKNI 519
Cdd:PRK07768 405 GFipaqdADGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
99-567 |
2.20e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.86 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 99 GVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQASkiksLLAILPKCTAhIKAI 178
Cdd:PRK12467 558 GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH----LLAQLPVPAG-LRSL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 179 VsfgdvTNELKREveqlrvscfsWEEFSTMGTETqdisRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLE 258
Cdd:PRK12467 633 C-----LDEPADL----------LCGYSGHNPEV----ALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQ 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 259 LTdkvvsEDDSYFSYLPLAhiFDqvienycifkgasIGFWQgdirylmedvqvmkptifcgvprVYDRIYTGINLKiqsg 338
Cdd:PRK12467 694 LA-----ADDSMLMVSTFA--FD-------------LGVTE-----------------------LFGALASGATLH---- 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 339 gLIGKQIFQYAYNYKLANLRKGFKQHEASP-FFDKIVFSKIKEGLGGRIRLMLSGAAPLPRHIEEFMRVTGCCALAQGYG 417
Cdd:PRK12467 727 -LLPPDCARDAEAFAALMADQGVTVLKIVPsHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 418 LTESCAGCFT---SIANIFSMIGTVGPPVTAIQARLesipemgYDA-LSNVP---RGEICLRGHTLFSGYYKRPDLTEEV 490
Cdd:PRK12467 806 PTETTVGVSTyelSDEERDFGNVPIGQPLANLGLYI-------LDHyLNPVPvgvVGELYIGGAGLARGYHRRPALTAER 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 491 F------SDG--WFHTGDIGEWQPDGTMKIIDR-----KKNIFKLSQGEyVAVEVLESAYVQSPLVTSVwvyGNSFESFL 557
Cdd:PRK12467 879 FvpdpfgADGgrLYRTGDLARYRADGVIEYLGRmdhqvKIRGFRIELGE-IEARLLAQPGVREAVVLAQ---PGDAGLQL 954
|
490
....*....|
gi 357156424 558 VAVVVPEKQA 567
Cdd:PRK12467 955 VAYLVPAAVA 964
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-570 |
4.56e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK12316 4578 TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSH 4657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksLLAILPkctahikaiVSFGDVTNELKREVEqlrvscfsWEEFStmgtETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK12316 4658 ----LLQRLP---------IPDGLASLALDRDED--------WEGFP----AHDPAVRLHPDNLAYVIYTSGSTGRPKGV 4712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAhiFDQVIENYC--IFKGASIgfwqgdiryLMEDVQVMKPtif 317
Cdd:PRK12316 4713 AVSHGSLVNHLHATGERYELT-----PDDRVLQFMSFS--FDGSHEGLYhpLINGASV---------VIRDDSLWDP--- 4773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 318 cgvprvyDRIYTginlkiqsggLIGKQ-----IFQYAYNYKLANlrkGFKQHEASPFFDKIVFSkiKEGLG-GRIRLMLS 391
Cdd:PRK12316 4774 -------ERLYA----------EIHEHrvtvlVFPPVYLQQLAE---HAERDGEPPSLRVYCFG--GEAVAqASYDLAWR 4831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 392 GAAPLprhieefmrvtgccALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLEsipemGY---DALSNVP--- 465
Cdd:PRK12316 4832 ALKPV--------------YLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRS-----GYvldGQLNPLPvgv 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 466 RGEICLRGHTLFSGYYKRPDLTEEVFSDGWF--------HTGDIGEWQPDGTMKIIDR-----KKNIFKLSQGEyvavev 532
Cdd:PRK12316 4893 AGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlyRTGDLARYRADGVIDYLGRvdhqvKIRGFRIELGE------ 4966
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357156424 533 LESAYVQSPLV--TSVWVYGNSFESFLVAVVVPEKQAIED 570
Cdd:PRK12316 4967 IEARLREHPAVreAVVIAQEGAVGKQLVGYVVPQDPALAD 5006
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
61-550 |
4.57e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.19 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 61 RMLGQRQVSDG---KAGDYVWqTYEEVYQKVIKIGAAIRSFGvKPGG--HCGIYGSNCPEWVMAMQACSSQGICYVPLYD 135
Cdd:PRK13388 7 QLLRDRAGDDTiavRYGDRTW-TWREVLAEAAARAAALIALA-DPDRplHVGVLLGNTPEMLFWLAAAALGGYVLVGLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 136 TLGPNAVEFILDHAEISIAFVQASKiKSLLAILpkctahikaivsfgDVTnelkrEVEQLRVSCFSWEEFSTMGTETQDI 215
Cdd:PRK13388 85 TRRGAALAADIRRADCQLLVTDAEH-RPLLDGL--------------DLP-----GVRVLDVDTPAYAELVAAAGALTPH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 216 SRKQKDDICTIMYTSGTTGDPKGVIITN-RAIIAGVMTTENLleltdKVVSEDDSYFSyLPLAHiFDQVIENY--CIFKG 292
Cdd:PRK13388 145 REVDAMDPFMLIFTSGTTGAPKAVRCSHgRLAFAGRALTERF-----GLTRDDVCYVS-MPLFH-SNAVMAGWapAVASG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 293 ASI---------GFwqgdirylMEDVQVMKPTIFCGVprvydriytginlkiqsggliGKqifqyAYNYKLAN------- 356
Cdd:PRK13388 218 AAValpakfsasGF--------LDDVRRYGATYFNYV---------------------GK-----PLAYILATperpdda 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 357 ---LRKGFKQhEASpffdkivfskikeglggrirlmlsgaaplPRHIEEFMRVTGcCALAQGYGLTEScAGCFT------ 427
Cdd:PRK13388 264 dnpLRVAFGN-EAS-----------------------------PRDIAEFSRRFG-CQVEDGYGSSEG-AVIVVrepgtp 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 428 --SIANIFSMIGTVGPPVTAIQARLEsIPEMGydALSNVPR--GEIC-LRGHTLFSGYYKRPDLTEEVFSDGWFHTGDIG 502
Cdd:PRK13388 312 pgSIGRGAPGVAIYNPETLTECAVAR-FDAHG--ALLNADEaiGELVnTAGAGFFEGYYNNPEATAERMRHGMYWSGDLA 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357156424 503 EWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSVWVYG 550
Cdd:PRK13388 389 YRDADGWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRVAVYA 435
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
386-569 |
4.71e-08 |
|
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: 55.80 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPL-PRHIEEFMRVTGCcALAQGYGLTESCAgCFTSIANIFSMI-GTVGPPVTAI-QARLesIPEMGYDals 462
Cdd:cd05920 257 LRLLQVGGARLsPALARRVPPVLGC-TLQQVFGMAEGLL-NYTRLDDPDEVIiHTQGRPMSPDdEIRV--VDEEGNP--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 463 nVPRGEI---CLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYV 538
Cdd:cd05920 330 -VPPGEEgelLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLL 407
|
170 180 190
....*....|....*....|....*....|....*
gi 357156424 539 QSPLVTSVWVYGNSfESFL----VAVVVPEKQAIE 569
Cdd:cd05920 408 RHPAVHDAAVVAMP-DELLgersCAFVVLRDPPPS 441
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
386-574 |
5.18e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 55.86 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAiqARLESIPEMGydalSNVP 465
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPG--AELRFVDEDG----RPLP 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 466 RGEIC-----LRGHTLFSgYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQS 540
Cdd:PRK12406 347 QGEIGeiysrIAGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAV 424
|
170 180 190
....*....|....*....|....*....|....*..
gi 357156424 541 PLVTSVWVYGNSFESF---LVAVVVPEKQAIEDWAAL 574
Cdd:PRK12406 425 PGVHDCAVFGIPDAEFgeaLMAVVEPQPGATLDEADI 461
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
80-573 |
9.08e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 55.94 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH 3201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksLLAILPKcTAHIKAIVsfgdvtnelkreVEQLrvscfSWEEFStmgtETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK12467 3202 ----LLEQLPA-PAGDTALT------------LDRL-----DLNGYS----ENNPSTRVMGENLAYVIYTSGSTGKPKGV 3255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELtdkvvSEDDSYFSYLPLAhiFDQVIENY--CIFKGASIGFWQGDIRYLMEDVQVM---KP 314
Cdd:PRK12467 3256 GVRHGALANHLCWIAEAYEL-----DANDRVLLFMSFS--FDGAQERFlwTLICGGCLVVRDNDLWDPEELWQAIhahRI 3328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 315 TIFCGVPrvydriytginlkiqsggligkqifqyAYNYKLANLRKGfkqhEASPFFDKIVFSkikeglggrirlmlsGAA 394
Cdd:PRK12467 3329 SIACFPP---------------------------AYLQQFAEDAGG----ADCASLDIYVFG---------------GEA 3362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 395 PLPRHIEEFMRVTGCCALAQGYGLTESCAgcfTSIANIFSMIGTVGPPVTAIQARLESIPEMGYD-ALSNVPRG---EIC 470
Cdd:PRK12467 3363 VPPAAFEQVKRKLKPRGLTNGYGPTEAVV---TVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDgQLNPVPVGvagELY 3439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 471 LRGHTLFSGYYKRPDLTEEVFSDGWFH--------TGDIGEWQPDGTMKIIDR-----KKNIFKLSQGEyVAVEVLESAY 537
Cdd:PRK12467 3440 IGGVGLARGYHQRPSLTAERFVADPFSgsggrlyrTGDLARYRADGVIEYLGRidhqvKIRGFRIELGE-IEARLLQHPS 3518
|
490 500 510
....*....|....*....|....*....|....*.
gi 357156424 538 VQSPLVTSVWVYGNsfeSFLVAVVVPEKQAiEDWAA 573
Cdd:PRK12467 3519 VREAVVLARDGAGG---KQLVAYVVPADPQ-GDWRE 3550
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
218-567 |
1.05e-07 |
|
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: 54.87 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 218 KQKDDICTIMYTSGTTGDPKGVIITNRAIIagvmtteNLLELTDkvvseddSYFSYLPlahifdqvIENYCIFkgASIGF 297
Cdd:cd17645 101 TNPDDLAYVIYTSGSTGLPKGVMIEHHNLV-------NLCEWHR-------PYFGVTP--------ADKSLVY--ASFSF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 298 ----WQgdirylmedvqvMKPTIFCGVPRvydriytginlkiqsggligkQIFQYAYNYKLANLRKGFKQHEAS-PFFDK 372
Cdd:cd17645 157 dasaWE------------IFPHLTAGAAL---------------------HVVPSERRLDLDALNDYFNQEGITiSFLPT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 373 IVFSKIKEGLGGRIRLMLSGAAPLPRHIEEFMRvtgccaLAQGYGLTEsCAGCFTSI------ANIfsmigTVGPPVTAI 446
Cdd:cd17645 204 GAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGPTE-NTVVATSFeidkpyANI-----PIGKPIDNT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 447 QARLESipemgyDALSNVP---RGEICLRGHTLFSGYYKRPDLTEEVF-------SDGWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:cd17645 272 RVYILD------EALQLQPigvAGELCIAGEGLARGYLNRPELTAEKFivhpfvpGERMYRTGDLAKFLPDGNIEFLGRL 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 357156424 517 KNIFKLsQGEYVAVEVLESAYVQSPLVTSVWVYG---NSFESFLVAVVVPEKQA 567
Cdd:cd17645 346 DQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVLAkedADGRKYLVAYVTAPEEI 398
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
99-541 |
1.20e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 54.78 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 99 GVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILdhaeisiafvQASKIKSLLA----------IL 168
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRL----------QASKAKCIVTsdelapevdsVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 169 PKCTA-HIKAIVS------FGDVtNELKREVEqlrvscfswEEFSTMGTETQDISrkqkddicTIMYTSGTTGDPKGVII 241
Cdd:cd05928 133 SECPSlKTKLLVSeksrdgWLNF-KELLNEAS---------TEHHCVETGSQEPM--------AIYFTSGTTGSPKMAEH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 242 TNRAIIAG-VMTTENLLELT--DKVVSEDDSYFSYLPLAHIFDQVIENYCIFKGASIGFwqgDIRYLMEDVQVMKPTIFC 318
Cdd:cd05928 195 SHSSLGLGlKVNGRYWLDLTasDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRF---DPLVILKTLSSYPITTFC 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 319 GVPRVYdRIYTGINLKiqsggligkqifqyayNYKLANLRKgfkqheaspffdkivfskikeglggrirlMLSGAAPL-P 397
Cdd:cd05928 272 GAPTVY-RMLVQQDLS----------------SYKFPSLQH-----------------------------CVTGGEPLnP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 398 RHIEEFMRVTGCcALAQGYGLTESCAGCftsiANIFSM---IGTVGPPVTAIQARLesIPEMGyDALSNVPRGEICL--- 471
Cdd:cd05928 306 EVLEKWKAQTGL-DIYEGYGQTETGLIC----ANFKGMkikPGSMGKASPPYDVQI--IDDNG-NVLPPGTEGDIGIrvk 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 472 --RGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQG--------EYVAVE---VLESAYV 538
Cdd:cd05928 378 piRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI-NSSGyrigpfevESALIEhpaVVESAVV 456
|
...
gi 357156424 539 QSP 541
Cdd:cd05928 457 SSP 459
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
80-564 |
2.11e-07 |
|
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: 53.86 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAs 159
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelkreveqlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd12115 105 -------------------------------------------------------------DDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIA------GVMTTENL---LELTDkvVSEDDSYFS-YLPLAHifdqvienycifkGASIgfwqgdirYLMEDV 309
Cdd:cd12115 124 AIEHRNAAAflqwaaAAFSAEELagvLASTS--ICFDLSVFElFGPLAT-------------GGKV--------VLADNV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 310 QVM-------KPTIFCGVPRVYDRIYtginlkiqsggligkqifqyaynyklanlrkgfkQHEASPFFDKIVfskikeGL 382
Cdd:cd12115 181 LALpdlpaaaEVTLINTVPSAAAELL----------------------------------RHDALPASVRVV------NL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 383 GGRirlmlsgaaPLPRHIEEFMRvtgccALAQG------YGLTEscagcfTSIANIFSMIG-------TVGPPVTAIQAR 449
Cdd:cd12115 221 AGE---------PLPRDLVQRLY-----ARLQVervvnlYGPSE------DTTYSTVAPVPpgasgevSIGRPLANTQAY 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 450 LESipemgyDALSNVP---RGEICLRGHTLFSGYYKRPDLTEEVFSDGWFH-------TGDIGEWQPDGTMKIIDRKKNI 519
Cdd:cd12115 281 VLD------RALQPVPlgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQ 354
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357156424 520 FKLsQGEYVAVEVLESAYVQSPLVTS--VWVYGNSF-ESFLVAVVVPE 564
Cdd:cd12115 355 VKV-RGFRIELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
386-548 |
2.18e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 53.73 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPL-PRHIEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSmIGTVGPPVTAIQARLesipemgYDALSN- 463
Cdd:cd05974 202 LREVVGAGEPLnPEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGQPVK-AGSMGRPLPGYRVAL-------LDPDGAp 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 464 VPRGEICL-----RGHTLFSGYYKRPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSQGEYVAVEvLESAYV 538
Cdd:cd05974 273 ATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE-LESVLI 351
|
170
....*....|
gi 357156424 539 QSPLVTSVWV 548
Cdd:cd05974 352 EHPAVAEAAV 361
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
469-556 |
2.96e-07 |
|
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: 53.59 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 469 ICLRGHTLFSGYYKRPDLTE-EVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTSVW 547
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKEAA 441
|
....*....
gi 357156424 548 VYGNSFESF 556
Cdd:cd05915 442 VVAIPHPKW 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-567 |
4.29e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAs 159
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS- 3162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctaHIKAIVSFGDVTNELKREVEQLrvscfsweefstmgTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK12316 3163 --------------HLRLPLAQGVQVLDLDRGDENY--------------AEANPAIRTMPENLAYVIYTSGSTGKPKGV 3214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvseddsyfsylplahifdqviENYCIFKGASIGFwqgdirylmeDVQVMKptifcg 319
Cdd:PRK12316 3215 GIRHSALSNHLCWMQQAYGLG------------------------VGDRVLQFTTFSF----------DVFVEE------ 3254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 320 vprVYDRIYTGINLKiqsggLIGKQIFQYAYNYKLANLRKGFKQHEASPFFDKIVFSKIKEGLGGRIRLMLSGAAPLPRh 399
Cdd:PRK12316 3255 ---LFWPLMSGARVV-----LAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPA- 3325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 400 iEEFMRVTGCCALAQGYGLTESCAGCFT-SIANIFSMIGTVGPPVTAIQARLESipemgyDALSNVPRG---EICLRGHT 475
Cdd:PRK12316 3326 -DLQQQVFAGLPLYNLYGPTEATITVTHwQCVEEGKDAVPIGRPIANRACYILD------GSLEPVPVGalgELYLGGEG 3398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 476 LFSGYYKRPDLTEEVFSDGWF-------HTGDIGEWQPDGTMKIIDR-----KKNIFKLSQGEYVAvEVLESAYVQSPLV 543
Cdd:PRK12316 3399 LARGYHNRPGLTAERFVPDPFvpgerlyRTGDLARYRADGVIEYIGRvdhqvKIRGFRIELGEIEA-RLLEHPWVREAVV 3477
|
490 500
....*....|....*....|....
gi 357156424 544 TSVWvygnsfESFLVAVVVPEKQA 567
Cdd:PRK12316 3478 LAVD------GRQLVAYVVPEDEA 3495
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
80-243 |
7.64e-07 |
|
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: 52.32 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAE----ISIAF 155
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKpkliVTASC 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 156 -VQASKIKSLLAILPKCTA------HIKAIVSFGDVTNELKREVEQLrvscfSWEEFSTMGTETQDISRKQKDDICtIMY 228
Cdd:cd05967 164 gIEPGKVVPYKPLLDKALElsghkpHHVLVLNRPQVPADLTKPGRDL-----DWSELLAKAEPVDCVPVAATDPLY-ILY 237
|
170
....*....|....*
gi 357156424 229 TSGTTGDPKGVIITN 243
Cdd:cd05967 238 TSGTTGKPKGVVRDN 252
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-567 |
9.44e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQas 159
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiKSLLAILPkctahikaivsfgdvtneLKREVEQL---RVScfSWeeFSTMGTETQDIsRKQKDDICTIMYTSGTTGDP 236
Cdd:PRK12316 616 --SHLGRKLP------------------LAAGVQVLdldRPA--AW--LEGYSEENPGT-ELNPENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 237 KGVIITNRAIIAGV--MTTENLLELTDKVVSEDDSYFS------YLPLAhifdqvienycifKGASIGF-WQGDIRYLME 307
Cdd:PRK12316 671 KGAGNRHRALSNRLcwMQQAYGLGVGDTVLQKTPFSFDvsvwefFWPLM-------------SGARLVVaAPGDHRDPAK 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 308 DVQVMKPtifcgvprvyDRIYTgINLkiqsggligkqifqyaynykLANLRKGFKQHEASPFFDKIVfskikeglggriR 387
Cdd:PRK12316 738 LVELINR----------EGVDT-LHF--------------------VPSMLQAFLQDEDVASCTSLR------------R 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 388 LMLSGAApLPRHIEEfmRVTG---CCALAQGYGLTESCAG--CFTSIANIFSMIgTVGPPVTAIQARLesipemgYDA-L 461
Cdd:PRK12316 775 IVCSGEA-LPADAQE--QVFAklpQAGLYNLYGPTEAAIDvtHWTCVEEGGDSV-PIGRPIANLACYI-------LDAnL 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 462 SNVP---RGEICLRGHTLFSGYYKRPDLTEEVF-----SDG--WFHTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYVAVE 531
Cdd:PRK12316 844 EPVPvgvLGELYLAGRGLARGYHGRPGLTAERFvpspfVAGerMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELG 922
|
490 500 510
....*....|....*....|....*....|....*.
gi 357156424 532 VLESAYVQSPLVTSVWVYGNSFESfLVAVVVPEKQA 567
Cdd:PRK12316 923 EIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLESEG 957
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
464-546 |
9.96e-07 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 51.68 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 464 VPRGEI---CLRG-HTlFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNifklsQ----GEYVAVEVLE 534
Cdd:COG1021 375 VPPGEVgelLTRGpYT-IRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEKIAAEEVE 448
|
90
....*....|..
gi 357156424 535 SAYVQSPLVTSV 546
Cdd:COG1021 449 NLLLAHPAVHDA 460
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
80-570 |
1.07e-06 |
|
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: 51.71 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVQAS 159
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kIKSLLAILPKCTAHIKAIVSFGDvTNELKREVEQlrvscfsweefstmgtetqdisrkqkDDICTIMYTSGTTGDPKGV 239
Cdd:cd17656 95 -LKSKLSFNKSTILLEDPSISQED-TSNIDYINNS--------------------------DDLLYIIYTSGTTGKPKGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIagvmtteNLLELTdkvvseddsyFSYLpLAHIFDQVIE------NYC---IFKGASIGfwqGDIRYLMEDVQ 310
Cdd:cd17656 147 QLEHKNMV-------NLLHFE----------REKT-NINFSDKVLQfatcsfDVCyqeIFSTLLSG---GTLYIIREETK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 VMKPTIFCGVPRvydriytginlkiqsgGLIGKQIFQYAYNYKLANLRKGFkqheaSPFFDKIvfskiKEGLGGRIRLML 390
Cdd:cd17656 206 RDVEQLFDLVKR----------------HNIEVVFLPVAFLKFIFSEREFI-----NRFPTCV-----KHIITAGEQLVI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAaplprhIEEFMRVTGCcALAQGYGLTEscagcftsiANIFSMIgTVGPpvtaiQARLESIPEMGyDALSNV------ 464
Cdd:cd17656 260 TNE------FKEMLHEHNV-HLHNHYGPSE---------THVVTTY-TINP-----EAEIPELPPIG-KPISNTwiyild 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 465 ------PRG---EICLRGHTLFSGYYKRPDLTEEVFSDGWF-------HTGDIGEWQPDGTMKIIDRKKNIFKLsQGEYV 528
Cdd:cd17656 317 qeqqlqPQGivgELYISGASVARGYLNRQELTAEKFFPDPFdpnermyRTGDLARYLPDGNIEFLGRADHQVKI-RGYRI 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 357156424 529 AVEVLESAYVQSPLVTS--VWVYGNSF-ESFLVAVVVPEkQAIED 570
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVME-QELNI 439
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
415-574 |
1.16e-06 |
|
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: 51.48 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 415 GYGLTES--CA---GCFTSIANIfsmigTVGPPVTAIQAR-LEsipemgyDALSNVP---RGEICLRGHTLFSGYYKRPD 485
Cdd:cd17652 233 AYGPTETtvCAtmaGPLPGGGVP-----PIGRPVPGTRVYvLD-------ARLRPVPpgvPGELYIAGAGLARGYLNRPG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 486 LTEEVF--------SDGWFHTGDIGEWQPDGTMKIIDR-----KKNIFKLSQGEYVAVeVLESAYVQSPLVTsVWVYGNS 552
Cdd:cd17652 301 LTAERFvadpfgapGSRMYRTGDLARWRADGQLEFLGRaddqvKIRGFRIELGEVEAA-LTEHPGVAEAVVV-VRDDRPG 378
|
170 180
....*....|....*....|..
gi 357156424 553 fESFLVAVVVPEKQAIEDWAAL 574
Cdd:cd17652 379 -DKRLVAYVVPAPGAAPTAAEL 399
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-561 |
1.29e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 50.84 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 221 DDIcTIMYTSGTTGDPKGVI----------ITNRAIIAGVMTTENLLELTdKVVSEDDSYFSYLPLAHifdqvienycif 290
Cdd:cd05924 4 DDL-YILYTGGTTGMPKGVMwrqedifrmlMGGADFGTGEFTPSEDAHKA-AAAAAGTVMFPAPPLMH------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 291 kGASIGFWQGDirylmedvqvmkptiFCGVPRVYdriytginlkIQSGGLIGKQIFQYAYNYKlANLRKGFKQHEASPFF 370
Cdd:cd05924 70 -GTGSWTAFGG---------------LLGGQTVV----------LPDDRFDPEEVWRTIEKHK-VTSMTIVGDAMARPLI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 371 DKIvfskikEGLGGR----IRLMLSGAAPLPRHI-EEFMRVTGCCALAQGYGLTESCAGCFTSIANifsmigtvGPPVTA 445
Cdd:cd05924 123 DAL------RDAGPYdlssLFAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSGHSAG--------SGPETG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 446 IQARLESIPEMGYDALSNVP-----RGEICLRGHTLFsGYYKRPDLTEEVFS--DG--WFHTGDIGEWQPDGTMKIIDRK 516
Cdd:cd05924 189 PFTRANPDTVVLDDDGRVVPpgsggVGWIARRGHIPL-GYYGDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRG 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 357156424 517 KNIFKlSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVV 561
Cdd:cd05924 268 SVCIN-TGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWgqeVVAVV 314
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
80-261 |
2.34e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDHAEISIAFVqas 159
Cdd:PRK04813 29 TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIA--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvTNELKREVEQLRVscFSWEEFSTMGTETQDISRK---QKDDICTIMYTSGTTGDP 236
Cdd:PRK04813 106 -------------------------TEELPLEILGIPV--ITLDELKDIFATGNPYDFDhavKGDDNYYIIFTSGTTGKP 158
|
170 180
....*....|....*....|....*
gi 357156424 237 KGVIITNraiiagvmttENLLELTD 261
Cdd:PRK04813 159 KGVQISH----------DNLVSFTN 173
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
467-574 |
2.65e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 50.51 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 467 GEICLRGHTLFSGYYKRPDLTEEVFS-DGWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVLESAYVQSPLVTS 545
Cdd:PRK06164 378 GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAA 456
|
90 100 110
....*....|....*....|....*....|.
gi 357156424 546 VWVYGNSFESFLVAV--VVPEKQAIEDWAAL 574
Cdd:PRK06164 457 AQVVGATRDGKTVPVafVIPTDGASPDEAGL 487
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
80-247 |
2.89e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.81 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLyDTLGPNA-VEFILDHAEISIAFVQA 158
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-DTGYPDDrLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 159 SkiksLLAILPKctahikaivsfGDVTNELKREVEQLRvscfsweefstmgTETQDISRKQKDDICTIMYTSGTTGDPKG 238
Cdd:PRK10252 564 D----QLPRFAD-----------VPDLTSLCYNAPLAP-------------QGAAPLQLSQPHHTAYIIFTSGSTGRPKG 615
|
....*....
gi 357156424 239 VIITNRAII 247
Cdd:PRK10252 616 VMVGQTAIV 624
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
461-568 |
4.14e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.61 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 461 LSNVPRGEICLRGHTLFSGYYkrPDLTEevfSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQS 540
Cdd:PRK07445 296 IPANQTGNITIQAQSLALGYY--PQILD---SQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILAT 369
|
90 100 110
....*....|....*....|....*....|.
gi 357156424 541 PLVTSVWVYG---NSFESFLVAVVVPEKQAI 568
Cdd:PRK07445 370 GLVQDVCVLGlpdPHWGEVVTAIYVPKDPSI 400
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
464-544 |
4.96e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.60 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 464 VPRGEICL---RGHTLFSGYYKRPDLTEEVF-SDGWFHTGDIGEWQPDGTMKIIDRKKNifklsQ----GEYVAVEVLES 535
Cdd:PRK10946 375 LPQGEVGRlmtRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIEN 449
|
....*....
gi 357156424 536 AYVQSPLVT 544
Cdd:PRK10946 450 LLLRHPAVI 458
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
80-563 |
7.26e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 49.77 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFIldhaeisiafVQAS 159
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYM----------IEDS 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAilpkcTAHIKAIVSFGDVTNELKREVEQLRVSCFSweefstmgtETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:PRK12467 1671 GIELLLT-----QSHLQARLPLPDGLRSLVLDQEDDWLEGYS---------DSNPAVNLAPQNLAYVIYTSGSTGRPKGA 1736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIAGVMTTENLLELTdkvvsEDDSYFSYLPLAhiFDQVIENY--CIFKGASI-----GFWQ--GDIRYLMEDVQ 310
Cdd:PRK12467 1737 GNRHGALVNRLCATQEAYQLS-----AADVVLQFTSFA--FDVSVWELfwPLINGARLviappGAHRdpEQLIQLIERQQ 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 311 VmkpTIFCGVPRVYdriytginlkiqsggligKQIFQYAynyklanlrkgfkQHEASPffdkivfSKIKeglggriRLML 390
Cdd:PRK12467 1810 V---TTLHFVPSML------------------QQLLQMD-------------EQVEHP-------LSLR-------RVVC 1841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTaiqarlESIPEMGYDALSN----VPR 466
Cdd:PRK12467 1842 GGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIG------QPIANLSTYILDAslnpVPI 1915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 467 ---GEICLRGHTLFSGYYKRPDLTEEVFSDGWF--------HTGDIGEWQPDGTMKI---IDRKKNI--FKLSQGEYVAv 530
Cdd:PRK12467 1916 gvaGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlyRTGDLARYRADGVIEYlgrIDHQVKIrgFRIELGEIEA- 1994
|
490 500 510
....*....|....*....|....*....|...
gi 357156424 531 EVLESAYVQSplvTSVWVYGNSFESFLVAVVVP 563
Cdd:PRK12467 1995 RLREQGGVRE---AVVIAQDGANGKQLVAYVVP 2024
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
80-270 |
8.13e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 49.12 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVefiLDHAEISiafvQAS 159
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAV---RDRLEDS----EAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KIKSLLAILPKCTA----HIKAIVsfgdVTNELKREVEQlrvsCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGD 235
Cdd:PRK04319 148 VLITTPALLERKPAddlpSLKHVL----LVGEDVEEGPG----TLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGK 219
|
170 180 190
....*....|....*....|....*....|....*
gi 357156424 236 PKGVIITNRAIIAGVMTTENLLELtdkvvSEDDSY 270
Cdd:PRK04319 220 PKGVLHVHNAMLQHYQTGKYVLDL-----HEDDVY 249
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
384-532 |
8.98e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 384 GRIRLMLSGAAPLprHIEEFMRVTGCC--------ALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARL----E 451
Cdd:PRK05851 272 GALRVALNGGEPV--DCDGFERFATAMapfgfdagAAAPSYGLAESTCAVTVPVPGIGLRVDEVTTDDGSGARRHavlgN 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 452 SIPEM------GYDALSNVPR--GEICLRGHTLFSGYYKRPDLTeevfSDGWFHTGDIGeWQPDGTMKIIDRKK------ 517
Cdd:PRK05851 350 PIPGMevrispGDGAAGVAGReiGEIEIRGASMMSGYLGQAPID----PDDWFPTGDLG-YLVDGGLVVCGRAKelitva 424
|
170
....*....|....*..
gi 357156424 518 --NIFKlSQGEYVAVEV 532
Cdd:PRK05851 425 grNIFP-TEIERVAAQV 440
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
135-570 |
1.04e-05 |
|
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: 48.53 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 135 DTLGPNAVEFILDHAEISIAFVQASKIKSLLAILPKCTAHIKA-------IVSFGDVTNELKREVEQLRVSCFSWEefst 207
Cdd:cd05929 43 DGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIeikaaalVCGLFTGGGALDGLEDYEAAEGGSPE---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 208 mgTETQDISRKQKddictIMYTSGTTGDPKGViitNRAIIAGVMTTENLLELTDKV-VSEDDSYFSYLPLAHIFDQVIEN 286
Cdd:cd05929 119 --TPIEDEAAGWK-----MLYSGGTTGRPKGI---KRGLPGGPPDNDTLMAAALGFgPGADSVYLSPAPLYHAAPFRWSM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 287 YCIFKGASI---------GFWQGDIRYLMEDVQVMkPTIFCGVPRVYDRIytginlkiqsggligkqifQYAYNykLANL 357
Cdd:cd05929 189 TALFMGGTLvlmekfdpeEFLRLIERYRVTFAQFV-PTMFVRLLKLPEAV-------------------RNAYD--LSSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 358 RKGFkqHeaspffdkivfskikeglggrirlmlsGAAPLPRHIEEFMRVTGCCALAQGYGLTESCAGCFTSIANIFSMIG 437
Cdd:cd05929 247 KRVI--H---------------------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 438 TVGPPVtaiQARLESIPEMGydalSNVPRGEIclrGHTLFSG-----YYKRPDLT-EEVFSDGWFHTGDIGEWQPDGTMK 511
Cdd:cd05929 298 SVGRAV---LGKVHILDEDG----NEVPPGEI---GEVYFANgpgfeYTNDPEKTaAARNEGGWSTLGDVGYLDEDGYLY 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 512 IIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEKQAIED 570
Cdd:cd05929 368 LTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELgqrVHAVVQPAPGADAG 428
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
80-278 |
1.67e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 47.94 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGicyvplydtlgpnAVefildHaeiSIAFVQAS 159
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG-------------AV-----H---SVVFAGFS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 KiKSLLAILPKCTAhiKAIVSF-----GDVTNELKREVEQLRVSCFSWEE---FSTMGTET----------QDISRKQKD 221
Cdd:cd05966 145 A-ESLADRINDAQC--KLVITAdggyrGGKVIPLKEIVDEALEKCPSVEKvlvVKRTGGEVpmtegrdlwwHDLMAKQSP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DiCT-----------IMYTSGTTGDPKGVIITnraiIAGVM-----TTENLLELTDkvvseDDSYF-----------SYL 274
Cdd:cd05966 222 E-CEpewmdsedplfILYTSGSTGKPKGVVHT----TGGYLlyaatTFKYVFDYHP-----DDIYWctadigwitghSYI 291
|
....*..
gi 357156424 275 ---PLAH 278
Cdd:cd05966 292 vygPLAN 298
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
391-603 |
4.35e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.68 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 391 SGAAPLPRHIEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESipemgyDALSNVPRGE-- 468
Cdd:PRK13382 320 SGSRMRPDVVIAFMDQFGD-VIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILD------QDFREVPTGEvg 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 469 -ICLRGHTLFSGYykRPDLTEEvFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPLVTSVW 547
Cdd:PRK13382 393 tIFVRNDTQFDGY--TSGSTKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDVAEAA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 548 VYGNSFESF---LVAVVVPEKQAIEDWAALNNKTSDfaELCNDPKARRY-IQDEL--NKTGK 603
Cdd:PRK13382 469 VIGVDDEQYgqrLAAFVVLKPGASATPETLKQHVRD--NLANYKVPRDIvVLDELprGATGK 528
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
386-641 |
5.62e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.14 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPL-PRHIEEFMRVTGCcALAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLesipeMGYDALSNV 464
Cdd:PRK13383 294 LRVVMSSGDRLdPTLGQRFMDTYGD-ILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRI-----LDRNNRPVG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 465 PR--GEICLRGHTLFSGYykrPDLTEEVFSDGWFHTGDIGEWQPDGTMKIIDRKKNIFkLSQGEYVAVEVLESAYVQSPL 542
Cdd:PRK13383 368 PRvtGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 543 VTSVWVYGNSFESF---LVAVVVPEKQAIEDWAALnnktsdfaelcndpkaRRYIQDELNKtgkklglrgFEMLRAVHL- 618
Cdd:PRK13383 444 VADNAVIGVPDERFghrLAAFVVLHPGSGVDAAQL----------------RDYLKDRVSR---------FEQPRDINIv 498
|
250 260
....*....|....*....|...
gi 357156424 619 EPVPFgiekdliTPTFKLKRPQL 641
Cdd:PRK13383 499 SSIPR-------NPTGKVLRKEL 514
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
219-278 |
8.40e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.88 E-value: 8.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELtdkvvSEDDSYFSYLPLAH 278
Cdd:PRK07769 178 NEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG-----QEGDRGVSWLPFFH 232
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
214-517 |
1.23e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 214 DISRKQKDDICTIMYTSGTTGDPKGVIITNRAIIAGV---MTteNLLELTDKVVSEDDSYFSYLPLAHifdqvienycif 290
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlMS--DYFGDTGGVPPPDTTVVSWLPFYH------------ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 291 kgaSIGFWQGdirylmedvqVMKPtIFCGVPRVydriytginlkiqsggLIGKQIF--------QyaynyKLANLRKGFk 362
Cdd:PRK05850 219 ---DMGLVLG----------VCAP-ILGGCPAV----------------LTSPVAFlqrparwmQ-----LLASNPHAF- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 363 qhEASP-F-FDKIVfSKIKE----GLG-GRIRLMLSGA-----APLPRHIEEF----MRVTgccALAQGYGLTEscagcf 426
Cdd:PRK05850 263 --SAAPnFaFELAV-RKTSDddmaGLDlGGVLGIISGServhpATLKRFADRFapfnLRET---AIRPSYGLAE------ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 427 tsiANIFSMIGTVG-PPVT---------AIQARLeSIPEMGYDALS-NVPR--------------------GEICLRGHT 475
Cdd:PRK05850 331 ---ATVYVATREPGqPPESvrfdyeklsAGHAKR-CETGGGTPLVSyGSPRsptvrivdpdtciecpagtvGEIWVHGDN 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 357156424 476 LFSGYYKRPDLTEEVF-------SDG-----WFHTGDIGeWQPDGTMKIIDRKK 517
Cdd:PRK05850 407 VAAGYWQKPEETERTFgatlvdpSPGtpegpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
437-565 |
1.55e-04 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 44.32 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 437 GTVGPPVTAIQARLEsipemgydALSNVPRGEICLRGHTLFSGYYKRPDLTEevfsDGWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:cd17633 163 NSVGRPFPNVEIEIR--------NADGGEIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRE 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 357156424 517 KNIFkLSQGEYVAVEVLESAYVQSPLVTSVWVYGNSFESF---LVAVVVPEK 565
Cdd:cd17633 231 SDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFgeiAVALYSGDK 281
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
80-239 |
2.32e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 44.36 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAV-EFILD-HAEISI---A 154
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALaDRIIDaGAKLVItadE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 155 FVQASKIKSLLAI----LPKCTAHIKAIV---SFGDVTNELKREVeqlrvscfSWEEfstmgtetqdISRKQKDDiCT-- 225
Cdd:PRK00174 180 GVRGGKPIPLKANvdeaLANCPSVEKVIVvrrTGGDVDWVEGRDL--------WWHE----------LVAGASDE-CEpe 240
|
170 180
....*....|....*....|...
gi 357156424 226 ---------IMYTSGTTGDPKGV 239
Cdd:PRK00174 241 pmdaedplfILYTSGSTGKPKGV 263
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
80-240 |
3.33e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.02 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQG----ICyVPLYdtlGPNAVefiLDH-AEIS-- 152
Cdd:PRK03584 116 SWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiwsSC-SPDF---GVQGV---LDRfGQIEpk 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 153 --IA----------FVQASKIKSLLAILPKctahIKAIVSfgdVTNELKREVEQLRVSCFSWEEFSTMGTETQ-DISRKQ 219
Cdd:PRK03584 189 vlIAvdgyryggkaFDRRAKVAELRAALPS----LEHVVV---VPYLGPAAAAAALPGALLWEDFLAPAEAAElEFEPVP 261
|
170 180
....*....|....*....|.
gi 357156424 220 KDDICTIMYTSGTTGDPKGVI 240
Cdd:PRK03584 262 FDHPLWILYSSGTTGLPKCIV 282
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
226-562 |
9.13e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.42 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 226 IMYTSGTTGDPKGVIITNRAIIAGVMTTENLLELTDKVVSeddsYFSYLPLAHIFDQVIENYCIFKGASIGFWQGDI--- 302
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTV----VFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIikn 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 303 ----RYLMEDVQVMKPTIFCGVPRVYDRIytginLKIQSGGLIGKQifqyayNYKLANLRKGFKQHEAspffdkivfskI 378
Cdd:PTZ00237 335 khieDDLWNTIEKHKVTHTLTLPKTIRYL-----IKTDPEATIIRS------KYDLSNLKEIWCGGEV-----------I 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 379 KEglggrirlmlsgaaPLPRHIEEFMRVtgCCAlaQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLESipEMGY 458
Cdd:PTZ00237 393 EE--------------SIPEYIENKLKI--KSS--RGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILS--EDGK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 459 DALSNvPRGEICLR---GHTLFSGYYKRPDLTEEVFSD--GWFHTGDIGEWQPDGTMKIIDRKKNIFKLSqGEYVAVEVL 533
Cdd:PTZ00237 453 ELNVN-EIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKIS-GNKVQLNTI 530
|
330 340 350
....*....|....*....|....*....|..
gi 357156424 534 ESAYVQSPLV---TSVWVYGNSFESFLVAVVV 562
Cdd:PTZ00237 531 ETSILKHPLVlecCSIGIYDPDCYNVPIGLLV 562
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
386-516 |
1.31e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 41.81 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 386 IRLMLSGAAPLPRHIEEFM-RVTGCCaLAQGYGLTESCAGCFTSIANIFSMIGTVGPPVTAIQARLEsipemgyDALSNV 464
Cdd:PRK08276 264 LRVAIHAAAPCPVEVKRAMiDWWGPI-IHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLGEVRILD-------EDGNEL 335
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 357156424 465 PRGEICL----RGHTLFSgYYKRPDLTEEVFSD-GWFHTGDIGEWQPDGTMKIIDRK 516
Cdd:PRK08276 336 PPGEIGTvyfeMDGYPFE-YHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRK 391
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
222-550 |
1.44e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.51 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 222 DICTIMYTSGTTGDPKGVIITNRAIIAGvmttENLLELTDkvVSEDDSYFSYLPLAHIFDQVIE-NYCIFKGASI----- 295
Cdd:cd05938 145 SPALYIYTSGTTGLPKAARISHLRVLQC----SGFLSLCG--VTADDVIYITLPLYHSSGFLLGiGGCIELGATCvlkpk 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 296 ----GFWqgdirylmEDVQVMKPTIFcgvprvydrIYTGinlkiqsggligkQIFQYaynykLANL--RKGFKQHeaspf 369
Cdd:cd05938 219 fsasQFW--------DDCRKHNVTVI---------QYIG-------------ELLRY-----LCNQpqSPNDRDH----- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 370 fdkivfsKIKEGLGGRIRlmlsgaaplPRHIEEFMRVTGCCALAQGYGLTESCAGCFtsiaNIFSMIGTVGpPVTAIQAR 449
Cdd:cd05938 259 -------KVRLAIGNGLR---------ADVWREFLRRFGPIRIREFYGSTEGNIGFF----NYTGKIGAVG-RVSYLYKL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 450 LESIPEMGYDALSN------------VPRGEICL-----RGHTLFSGYYKRPDLTE-----EVFSDG--WFHTGDIGEWQ 505
Cdd:cd05938 318 LFPFELIKFDVEKEepvrdaqgfcipVAKGEPGLlvakiTQQSPFLGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQD 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 357156424 506 PDGTMKIIDRKKNIFKLsQGEYVAV----EVLESAyvqsPLVTSVWVYG 550
Cdd:cd05938 398 QQNFLYFHDRVGDTFRW-KGENVATtevaDVLGLL----DFLQEVNVYG 441
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
80-521 |
1.96e-03 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 41.30 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 80 TYEEVYQKVIKIGAAIRSFGVKPGGHCGIYGSNCPEWVMAMQACSSQGICYVPLYDTLGPNAVEFILDhaeisiafvqas 159
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMK------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 160 kiksllailpkctahikaivsfgdvtnelKREVEQLRVSCFSWEEFSTMGTETQDISRKQKDDICTIMYTSGTTGDPKGV 239
Cdd:cd17654 86 -----------------------------KCHVSYLLQNKELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 240 IITNRAIIagvmttENLLELTDKV-VSEDDSYFSYLPLahIFD-QVIEnycIFKGASIGfwqgdirylmeDVQVMKPTIF 317
Cdd:cd17654 137 AVPHKCIL------PNIQHFRSLFnITSEDILFLTSPL--TFDpSVVE---IFLSLSSG-----------ATLLIVPTSV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 318 CGVPRVYDRIYTGINlKIQSGGLIGKQIFQYaynykLANLRKGFkqheaspffdkiVFSKIKEglggrIRLMLSGAAPLP 397
Cdd:cd17654 195 KVLPSKLADILFKRH-RITVLQATPTLFRRF-----GSQSIKST------------VLSATSS-----LRVLALGGEPFP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357156424 398 RHIE------EFMRVTGCcalaQGYGLTESCagCFTSIANIFSMIGTV--GPPV--TAIQARlesipemgyDALSNVPRG 467
Cdd:cd17654 252 SLVIlsswrgKGNRTRIF----NIYGITEVS--CWALAYKVPEEDSPVqlGSPLlgTVIEVR---------DQNGSEGTG 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 357156424 468 EICLRGhtlFSGYYKRPDLTEEVFSDgWFHTGDIGEWQpDGTMKIIDRKKNIFK 521
Cdd:cd17654 317 QVFLGG---LNRVCILDDEVTVPKGT-MRATGDFVTVK-DGELFFLGRKDSQIK 365
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
219-278 |
3.25e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.49 E-value: 3.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357156424 219 QKDDICTIMYTSGTTGDPKGVIITNRAiiagVMTteNLLE--LTDKVVSEDDSYFSYLPLAH 278
Cdd:PRK12476 191 DTDDVSHLQYTSGSTRPPVGVEITHRA----VGT--NLVQmiLSIDLLDRNTHGVSWLPLYH 246
|
|
| |
