|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1-666 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 1429.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 1 MSQQKKYIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPDPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQ 80
Cdd:PLN02614 1 MSQQKKFIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPNPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFC 320
Cdd:PLN02614 241 VMISNESIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 321 AVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGGNVRIILSGAAPLAS 400
Cdd:PLN02614 321 AVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLAS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 401 HVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVPEMEYDALASTARGEICIRGKTLFS 480
Cdd:PLN02614 401 HVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTLFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 481 GYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLI 560
Cdd:PLN02614 481 GYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 561 AIANPNQHILERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKR 640
Cdd:PLN02614 561 AIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKR 640
|
650 660
....*....|....*....|....*.
gi 15236634 641 PQLLKYYQSVIDEMYKTINAKFASRG 666
Cdd:PLN02614 641 PQLLKYYQSVIDEMYKTTNEKLASRG 666
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
7-656 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 948.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 7 YIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPDPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVY 86
Cdd:PLN02861 5 YTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTYKEVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 87 DIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELF 166
Cdd:PLN02861 85 DAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 167 KTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEgKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNE 246
Cdd:PLN02861 165 SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGS-LDCELPPKQKTDICTIMYTSGTTGEPKGVILTNR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 247 SIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPRVL 326
Cdd:PLN02861 244 AIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 327 DRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGGNVRIILSGAAPLASHVESFL 406
Cdd:PLN02861 324 DRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 407 RVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVPEMEYDALASTARGEICIRGKTLFSGYYKRE 486
Cdd:PLN02861 404 RVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYHKRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 487 DLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLIAIANPN 566
Cdd:PLN02861 484 DLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 567 QHILERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKY 646
Cdd:PLN02861 564 RQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKY 643
|
650
....*....|
gi 15236634 647 YQSVIDEMYK 656
Cdd:PLN02861 644 YKDCIDQLYS 653
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
75-656 |
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: 861.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 75 GKYVWQTYQEVYDIVMKLGNSLRSVGVK--DEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEV 152
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 153 SIVFVEEkkiselfktcpnsteymktvvsfggvsreqkeeaetfGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTS 232
Cdd:cd05927 81 SIVFCDA-------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 233 GTTGDPKGVMISNESIVTLIAGVIRLLKSANeALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLA 312
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILN-KINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 313 ELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGqsHVEASPLFDKLVFSKVKQGLGGNVRIIL 392
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSG--VVRASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 393 SGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGmLGTVGPPVPNVDIRLESVPEMEYDALASTARGEIC 472
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDVPEMNYDAKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 473 IRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVY 551
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 552 GNSFESFLIAIANPNQHILERWAAEN-GVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERD 630
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
570 580
....*....|....*....|....*.
gi 15236634 631 LLTPTFKKKRPQLLKYYQSVIDEMYK 656
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
5-661 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 857.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 5 KKYIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPDPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQE 84
Cdd:PLN02430 2 KSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 85 VYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISE 164
Cdd:PLN02430 82 VYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 165 LFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMIS 244
Cdd:PLN02430 162 LLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 245 NESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPR 324
Cdd:PLN02430 242 HEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 325 VLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGGNVRIILSGAAPLASHVES 404
Cdd:PLN02430 322 VFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 405 FLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVPEMEYDALASTARGEICIRGKTLFSGYYK 484
Cdd:PLN02430 402 FLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 485 REDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLIAIAN 564
Cdd:PLN02430 482 NPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 565 PNQHILERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLL 644
Cdd:PLN02430 562 PNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLL 641
|
650
....*....|....*..
gi 15236634 645 KYYQSVIDEMYKTINAK 661
Cdd:PLN02430 642 KYYQVEIDEMYRKLAEK 658
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
27-659 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 623.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 27 VYRSIFA----KDGFPDPIEgMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVYDIVMKLGNSLRSVGVK 102
Cdd:PLN02736 23 VYRSARSplklVSRFPDHPE-IGTLHDNFVYAVETFRDYKYLGTRIRVDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 103 DEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFkTCPNSTEYMKTVVSF 182
Cdd:PLN02736 102 KGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLL-SCLSEIPSVRLIVVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 183 GGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsa 262
Cdd:PLN02736 181 GGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK-- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 263 neaLTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGF 342
Cdd:PLN02736 259 ---FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 343 LKKFIFDSAFSYKFGYMKKGQShveASPLFDKLVFSKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTE 422
Cdd:PLN02736 336 LKERLFNAAYNAKKQALENGKN---PSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 423 -SCAGTFVSLPDELgmLGTVGPPVPNVDIRLESVPEMEY-DALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLH 499
Cdd:PLN02736 413 tSCVISGMDEGDNL--SGHVGSPNPACEVKLVDVPEMNYtSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLH 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 500 TGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLIAIANPNQHILERWAAENGV 579
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 580 -SGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTI 658
Cdd:PLN02736 571 kYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
.
gi 15236634 659 N 659
Cdd:PLN02736 651 A 651
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
49-656 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 527.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 49 DVFRMSVEKYPNNPMLGRREivdgkPGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
Cdd:COG1022 15 DLLRRRAARFPDRVALREKE-----DGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 129 LYCVPLYDTLGADAVEFIISHSEVSIVFVEE----KKISELFKTCPNsteyMKTVVSFggvsreqKEEAETFGLVIYAWD 204
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqeqlDKLLEVRDELPS----LRHIVVL-------DPRGLRDDPRLLSLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 205 EFLKLGEGKQYDLPIK------KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPL 278
Cdd:COG1022 159 ELLALGREVADPAELEarraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-----LGPGDRTLSFLPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 279 AHIFDRVIEECFIQHGAAIGFWRgDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFsyKFG- 357
Cdd:COG1022 234 AHVFERTVSYYALAAGATVAFAE-SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWAL--AVGr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 358 -YMKKGQSHVEASP-------LFDKLVFSKVKQGLGGNVRIILSGAAPLASHVESFLR---VvaccHVLQGYGLTESCAG 426
Cdd:COG1022 311 rYARARLAGKSPSLllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRalgI----PVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 427 TFVSLPDELgMLGTVGPPVPNVDIRLesvpemeydalasTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGE 505
Cdd:COG1022 387 ITVNRPGDN-RIGTVGPPLPGVEVKI-------------AEDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 506 WQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSfESFLIAIANPNQHILERWAAENGVS-GDYD 584
Cdd:COG1022 453 LDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYA 531
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236634 585 ALCQNEKAKEFILGElVKMAKeKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
Cdd:COG1022 532 ELAQDPEVRALIQEE-VDRAN-AGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
75-640 |
9.76e-178 |
|
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: 515.23 E-value: 9.76e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 75 GKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSI 154
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 155 VFVEekkiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpiKKKSDICTIMYTSGT 234
Cdd:cd17639 81 IFTD-------------------------------------------------------------GKPDDLACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 235 TGDPKGVMISNESIVTLIAGVIRLLksaNEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwrGDVKLLIE----- 309
Cdd:cd17639 100 TGNPKGVMLTHGNLVAGIAGLGDRV---PELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 310 ---DLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQShveaSPLFDKLVFSKVKQGLGG 386
Cdd:cd17639 175 ckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG----TPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 387 NVRIILSGAAPLASHVESFLRVVaCCHVLQGYGLTESCAGTFVSLPDELgMLGTVGPPVPNVDIRLESVPEMEYDALAST 466
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIV-LCPVIQGYGLTETCAGGTVQDPGDL-ETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 467 ARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAV 545
Cdd:cd17639 329 PRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 546 DSVWVYGNSFESFLIAIANPNQHILERWAAENGVS-GDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVP 624
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVInSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 15236634 625 FDMERDLLTPTFKKKR 640
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
37-655 |
6.10e-137 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 417.21 E-value: 6.10e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 37 FPDPI----EGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYVWQTYQEVYDIVMKLGNSLRS 98
Cdd:PLN02387 46 FPELVetpwEGATTLAALFEQSCKKYSDKRLLGTRKLIsrefetssDGRKfeklhlGEYEWITYGQVFERVCNFASGLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 99 VGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTcPNSTEYMKT 178
Cdd:PLN02387 126 LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDI-SSQLETVKR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 179 VVSF--GGVSREQKEEAETfGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVI 256
Cdd:PLN02387 205 VIYMddEGVDSDSSLSGSS-NWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVM 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 257 RLLKsaneALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwrGDVKLLIE-----------DLAELKPTIFCAVPRV 325
Cdd:PLN02387 284 TVVP----KLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 326 LDRVYSGLQKKLSDGGFLKKFIFDSAFsykfgymKKGQSHVEAS---------PLFDKLVFSKVKQGLGGNVRIILSGAA 396
Cdd:PLN02387 358 LDRVRDGVRKKVDAKGGLAKKLFDIAY-------KRRLAAIEGSwfgawglekLLWDALVFKKIRAVLGGRIRFMLSGGA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 397 PLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGmLGTVGPPVPNVDIRLESVPEMEYdaLASTA---RGEICI 473
Cdd:PLN02387 431 PLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTS-VGRVGPPLPCCYVKLVSWEEGGY--LISDKpmpRGEIVI 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 474 RGKTLFSGYYKREDLTKEVL-IDG----WLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSV 548
Cdd:PLN02387 508 GGPSVTLGYFKNQEKTDEVYkVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNI 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 549 WVYGNSFESFLIAIANPNQHILERWAAENGVS-GDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDM 627
Cdd:PLN02387 588 MVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTP 667
|
650 660
....*....|....*....|....*...
gi 15236634 628 ERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
Cdd:PLN02387 668 ESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
75-643 |
7.08e-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: 385.41 E-value: 7.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 75 GKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSI 154
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 155 VFVEekkiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikKKSDICTIMYTSGT 234
Cdd:cd05907 81 LFVE--------------------------------------------------------------DPDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 235 TGDPKGVMISNESIVTLIAGVIRLLKSANEaltvkDVYLSYLPLAHIFDRVIEECF-IQHGAAIGFWRgDVKLLIEDLAE 313
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLPATEG-----DRHLSFLPLAHVFERRAGLYVpLLAGARIYFAS-SAETLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 314 LKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFIFDSAfsykfgymkkgqshveasplfdklvfskvkqgLGGNVRIILS 393
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAIKVKAVPG--LKRKLFDLA--------------------------------VGGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 394 GAAPLASHVESFLRVvACCHVLQGYGLTESCAGTFVSLPDELgMLGTVGPPVPNVDIRLesvpemeydalasTARGEICI 473
Cdd:cd05907 219 GGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDN-RIGTVGKPLPGVEVRI-------------ADDGEILV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 474 RGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd05907 284 RGPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIG 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 553 NSfESFLIAIANPNQHILERWAAENGVSG-DYDALCQNEKAKEFILGELVKMakEKKMKGFEIIKAIHLDPVPFDMERDL 631
Cdd:cd05907 364 DG-RPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAA--NARLSRYEQIKKFLLLPEPFTIENGE 440
|
570
....*....|..
gi 15236634 632 LTPTFKKKRPQL 643
Cdd:cd05907 441 LTPTLKLKRPVI 452
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
51-525 |
2.92e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 343.91 E-value: 2.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 51 FRMSVEKYPNNPMLGrreivdgkPGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLY 130
Cdd:pfam00501 1 LERQAARTPDKTALE--------VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 131 CVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEflklg 210
Cdd:pfam00501 73 YVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 211 egkqyDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRlLKSANEALTVKDVYLSYLPLAHIFDRVIEE-C 289
Cdd:pfam00501 148 -----PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKR-VRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 290 FIQHGAAIGFWRG----DVKLLIEDLAELKPTIFCAVPRVLDRvysglqkkLSDGGFLKKFIFDSafsykfgymkkgqsh 365
Cdd:pfam00501 222 PLLAGATVVLPPGfpalDPAALLELIERYKVTVLYGVPTLLNM--------LLEAGAPKRALLSS--------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 366 veasplfdklvfskvkqglggnVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDE--LGMLGTVGP 443
Cdd:pfam00501 279 ----------------------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDedLRSLGSVGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 444 PVPNVDIRLESVPEMEYdaLASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIF 522
Cdd:pfam00501 337 PLPGTEVKIVDDETGEP--VPPGEPGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
...
gi 15236634 523 KLS 525
Cdd:pfam00501 415 KLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
81-656 |
9.75e-109 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 343.88 E-value: 9.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFKTCPNSTEYMKTVVSFGgvsrEQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIK---KKSDICTIMYTSGTTGD 237
Cdd:PTZ00216 203 NVPNLLRLMKSGGMPNTTIIYLD----SLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNipeNNDDLALIMYTSGTTGD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 238 PKGVMisnESIVTLIAGVIRLLKSANEAL---TVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwrGDVKLLIE----- 309
Cdd:PTZ00216 279 PKGVM---HTHGSLTAGILALEDRLNDLIgppEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfarp 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 310 --DLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQShveaSPLFDKLVFSKVKQGLGGN 387
Cdd:PTZ00216 354 hgDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKD----TPYWNEKVFSAPRAVLGGR 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 388 VRIILSGAAPLASHVESFLRVVACChVLQGYGLTESCAGTFVSLPDELGMlGTVGPPVPNVDIRLESVPEMEY-DAlaST 466
Cdd:PTZ00216 430 VRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEP-NAVGQLLKGVEMKLLDTEEYKHtDT--PE 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 467 ARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAV 545
Cdd:PTZ00216 506 PRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELV 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 546 --DSVWVYGNSFESFLIAIANPNQHILERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPV 623
Cdd:PTZ00216 586 vpNGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSD 665
|
570 580 590
....*....|....*....|....*....|...
gi 15236634 624 PFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
Cdd:PTZ00216 666 EWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
77-641 |
4.31e-77 |
|
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: 254.21 E-value: 4.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 77 YVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVF 156
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 157 VEekkiselfktcpNSTEymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksDICTIMYTSGTTG 236
Cdd:cd17640 83 VE------------NDSD-------------------------------------------------DLATIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 237 DPKGVMISNESivtLIAGVIRLlkSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwrGDVKLLIEDLAELKP 316
Cdd:cd17640 102 NPKGVMLTHAN---LLHQIRSL--SDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVKP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 317 TIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSykfgymkkgqshveasplfdklvfskvkqglGGNVRIILSGAA 396
Cdd:cd17640 175 HYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLS-------------------------------GGIFKFGISGGG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 397 PLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPDElGMLGTVGPPVPNVDIRLesVPEMEYDALASTARGEICIRGK 476
Cdd:cd17640 224 ALPPHVDTFFEAIG-IEVLNGYGLTETSPVVSARRLKC-NVRGSVGRPLPGTEIKI--VDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 477 TLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSf 555
Cdd:cd17640 300 QVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD- 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 556 ESFLIAIANPNQHILERWAAENGVS--GDYDALCQNEKAKEFILGEL-VKMAKEKKMKGFEIIKAIHLDPVPFdMERDLL 632
Cdd:cd17640 379 QKRLGALIVPNFEELEKWAKESGVKlaNDRSQLLASKKVLKLYKNEIkDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*....
gi 15236634 633 TPTFKKKRP 641
Cdd:cd17640 458 TQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
75-647 |
3.34e-76 |
|
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: 252.77 E-value: 3.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 75 GKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSI 154
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 155 VFVeeKKIselfktcpNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLGEGKQyDLPIKKKSDICTIMYTSGT 234
Cdd:cd05932 82 LFV--GKL--------DDWKAMAPGVPEGLISISLPPPSA--ANCQYQWDDLIAQHPPLE-ERPTRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 235 TGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFDRVieecFIQHGAAIG----FWRGDVKLLIED 310
Cdd:cd05932 149 TGQPKGVMLTFGSFAWAAQAGIEHIG-----TEENDRMLSYLPLAHVTERV----FVEGGSLYGgvlvAFAESLDTFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 311 LAELKPTIFCAVPRVLDRVYSGLQKKLSdggflkkfifdsafsykfgymKKGQSHVEASPLFDKLVFSKVKQGLGGN-VR 389
Cdd:cd05932 220 VQRARPTLFFSVPRLWTKFQQGVQDKIP---------------------QQKLNLLLKIPVVNSLVKRKVLKGLGLDqCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 390 IILSGAAPLASHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDElGMLGTVGPPVPNVDIRLESvpemeydalastaRG 469
Cdd:cd05932 279 LAGCGSAPVPPALLEWYRSLGL-NILEAYGMTENFAYSHLNYPGR-DKIGTVGNAGPGVEVRISE-------------DG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 470 EICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSV 548
Cdd:cd05932 344 EILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 549 WVYGNSFeSFLIAIANPNQHIleRWAAENGVSGDYDAlcqneKAKEFILGELVKMAKEKKMKGFEIIKAihldpvPFDME 628
Cdd:cd05932 424 CVIGSGL-PAPLALVVLSEEA--RLRADAFARAELEA-----SLRAHLARVNSTLDSHEQLAGIVVVKD------PWSID 489
|
570
....*....|....*....
gi 15236634 629 RDLLTPTFKKKRPQLLKYY 647
Cdd:cd05932 490 NGILTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
75-655 |
3.95e-75 |
|
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: 252.28 E-value: 3.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 75 GKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIIS-MEACNAHGLyCVPLYDTLGADAVEFIISHSEVS 153
Cdd:cd05933 4 DKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAaVGAIFAGGI-AVGIYTTNSPEACQYVAETSEAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 154 IVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEaetfglvIYAWDEFLKLGEG---KQYDLPIK--KKSDICTI 228
Cdd:cd05933 83 ILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPN-------LYSWDEFMELGRSipdEQLDAIISsqKPNQCCTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 229 MYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsANEALTVKDVYLSYLPLAHIFDRVIEECF-IQHGAAIGFWRGDV--K 305
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMD-LRPATVGQESVVSYLPLSHIAAQILDIWLpIKVGGQVYFAQPDAlkG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 306 LLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQSHVEASPLF----DKLVFSKVK 381
Cdd:cd05933 235 TLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFyrlaKKLVFKKVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 382 QGLG-GNVRIILSGAAPLASHVESF-----LRVVACchvlqgYGLTESCAGTFVSLPDELGmLGTVGPPVPNVDIRLEsv 455
Cdd:cd05933 315 KALGlDRCQKFFTGAAPISRETLEFflslnIPIMEL------YGMSETSGPHTISNPQAYR-LLSCGKALPGCKTKIH-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 456 pemEYDALAStarGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVEN 534
Cdd:cd05933 386 ---NPDADGI---GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 535 IEN-IYGEVQAVDSVWVYGNS--FESFLIAI---ANPnqhilERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKK 608
Cdd:cd05933 460 IEDaVKKELPIISNAMLIGDKrkFLSMLLTLkceVNP-----ETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKV 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15236634 609 MKGFE----------------IIKAIHLDpVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
Cdd:cd05933 535 YEAIEegikrvnkkaisnaqkIQKWVILE-KDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
50-661 |
3.82e-70 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 242.32 E-value: 3.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 50 VFRMSVEKYP-NNPMLGRREIVDGKPGKYVwqTYQEVYDIVMKLGNSLRSVGVK-------DEAK-------CGIYGANS 114
Cdd:PTZ00342 63 IMKLLLEKYKlNNNKIAIVEHSCGEPQNYI--TYGNFFKKVLSFSHSLNTYEGKgipekkyNEEQnngkfklLGLYGSNS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 115 PEWIISMEACNAHGLYCVPLYDT-------------------LGADAVEFIISH-------------------SEVSIVF 156
Cdd:PTZ00342 141 INWLVADLACMLSGVTTLVMHSKfsidvivdilnetklewlcLDLDLVEGLLERknelphlkkliildtliksKEININK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 157 VEEKKISEL-FKTCPNSTEYMKT--------VVSFGGVSREQ---------KEEAETFGLVIYAWDEFLKlGEGKQYDLP 218
Cdd:PTZ00342 221 EEKNNGSNVnNNGNKNNKEEQKGndlsneleDISLGPLEYDKeklekikdlKEKAKKLGISIILFDDMTK-NKTTNYKIQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTliaGVIRLLK-SANEALTVKDvYLSYLPLAHIFDRVIEECFIQHGAAI 297
Cdd:PTZ00342 300 NEDPDFITSIVYTSGTSGKPKGVMLSNKNLYN---TVVPLCKhSIFKKYNPKT-HLSYLPISHIYERVIAYLSFMLGGTI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 298 GFWRGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSykfgyMKKGQSHVEASPLFDKL-- 375
Cdd:PTZ00342 376 NIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILS-----LRKSNNNGGFSKFLEGIth 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 376 VFSKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESV 455
Cdd:PTZ00342 451 ISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPISPNTKYKVRTW 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 456 PemEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVEN 534
Cdd:PTZ00342 531 E--TYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDM 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 535 IENIYGEVQAVDSVWVYGNSFESFLIAIANPNQHILERWAAENGV-------SGDY-----DALCQNEKAKEFILGELVK 602
Cdd:PTZ00342 609 LNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginEKNYlekltDETINNNIYVDYVKGKMLE 688
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 15236634 603 MAKEKKMKGFEIIKAIHLDPVPFDMErDLLTPTFKKKRPQLLKYYQSVIDEMYKTINAK 661
Cdd:PTZ00342 689 VYKKTNLNRYNIINDIYLTSKVWDTN-NYLTPTFKVKRFYVFKDYAFFIDQVKKIYKNK 746
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
48-552 |
2.96e-66 |
|
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: 224.69 E-value: 2.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 48 WDVFRMSVEKYPNNPML--GRREIvdgkpgkyvwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACN 125
Cdd:COG0318 2 ADLLRRAAARHPDRPALvfGGRRL-----------TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 126 AHGLYCVPLYDTLGADAVEFIISHSEVSIVFVeekkiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawde 205
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 206 flklgegkqydlpikkksdiCTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAHIFdrv 285
Cdd:COG0318 103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAL-----GLTPGDVVLVALPLFHVF--- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 286 ieecfiqhGAAIGFWRG-------------DVKLLIEDLAELKPTIFCAVPRVLDRVYsglqkklsdggflkkfifdsaf 352
Cdd:COG0318 155 --------GLTVGLLAPllagatlvllprfDPERVLELIERERVTVLFGVPTMLARLL---------------------- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 353 sykfgymkkgqshveASPLFDKLVFSkvkqglggNVRIILSGAAPL-ASHVESFLRVvACCHVLQGYGLTESCAGTFVSL 431
Cdd:COG0318 205 ---------------RHPEFARYDLS--------SLRLVVSGGAPLpPELLERFEER-FGVRIVEGYGLTETSPVVTVNP 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 432 PDELG-MLGTVGPPVPNVDIRLESvPEMEydALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDG 510
Cdd:COG0318 261 EDPGErRPGSVGRPLPGVEVRIVD-EDGR--ELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDG 337
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15236634 511 SMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:COG0318 338 YLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVVG 378
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
49-545 |
4.77e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 212.74 E-value: 4.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 49 DVFRMSVEKYPNnpmlgrREIVDgkPGKYVWqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
Cdd:PRK06187 10 RILRHGARKHPD------KEAVY--FDGRRT-TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 129 LYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSfggvsrEQKEEAETFGLViYAWDEFLK 208
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVE------GDGPAAPLAPEV-GEYEELLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 209 lGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFDRVIee 288
Cdd:PRK06187 154 -AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK-----LSRDDVYLVIVPMFHVHAWGL-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 289 CF--IQHGAAI---GfwRGDVKLLIEDLAELKPTIFCAVPRVLDRVysgLQKKLSDGgflkkfiFDsafsykfgymkkgq 363
Cdd:PRK06187 226 PYlaLMAGAKQvipR--RFDPENLLDLIETERVTFFFAVPTIWQML---LKAPRAYF-------VD-------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 364 shveasplfdklvFSKvkqglggnVRIILSGAAPLASH-VESFLRVVaCCHVLQGYGLTESC-AGTFVSLPDELG----M 437
Cdd:PRK06187 280 -------------FSS--------LRLVIYGGAALPPAlLREFKEKF-GIDLVQGYGMTETSpVVSVLPPEDQLPgqwtK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 438 LGTVGPPVPNVDIRLesV-PEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIID 516
Cdd:PRK06187 338 RRSAGRPLPGVEARI--VdDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITD 415
|
490 500 510
....*....|....*....|....*....|....
gi 15236634 517 RKKNIFKlSQGEYV---AVENIenIYG--EVQAV 545
Cdd:PRK06187 416 RIKDVII-SGGENIyprELEDA--LYGhpAVAEV 446
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
78-655 |
1.55e-60 |
|
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: 212.28 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 78 VWQ--TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIV 155
Cdd:cd17641 8 IWQefTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 156 FVEEK----KISELFKTCPnSTEYMkTVVSFGGVSREQKEEAETFGLViYAWDEFLKLGEGKQYD--LPIKKKSDICTIM 229
Cdd:cd17641 88 IAEDEeqvdKLLEIADRIP-SVRYV-IYCDPRGMRKYDDPRLISFEDV-VALGRALDRRDPGLYEreVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 230 YTSGTTGDPKGVMISNESIVTLIAGVIRLlksanEALTVKDVYLSYLPLAHIFDRVIEecfiqhgAAIGFWRG------- 302
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLGHCAAYLAA-----DPLGPGDEYVSVLPLPWIGEQMYS-------VGQALVCGfivnfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 DVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFD-------SAFSYKFGYMKKGQSHVEASPLFDKL 375
Cdd:cd17641 233 EPETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFElgmklglRALDRGKRGRPVSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 376 VFSKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSlPDELGMLGTVGPPVPNVDIRLES 454
Cdd:cd17641 313 LFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAIG-VPLKQLYGQTELAGAYTVH-RDGDVDPDTVGVPFPGTEVRIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 455 VpemeydalastarGEICIRGKTLFSGYYKREDLTKE-VLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVE 533
Cdd:cd17641 391 V-------------GEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 534 NIENIYGEVQAVDSVWVYGNSFEsFLIAIANPNQHILERWAAENGVS-GDYDALCQNEKAKEFILGELVK----MAKEKK 608
Cdd:cd17641 458 FIENKLKFSPYIAEAVVLGAGRP-YLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKvnasLPEAQR 536
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15236634 609 MKGFEII-KAIHLDpvpfDMErdlLTPTFKKKRpqllkyyqSVIDEMY 655
Cdd:cd17641 537 IRRFLLLyKELDAD----DGE---LTRTRKVRR--------GVIAEKY 569
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
81-538 |
2.39e-57 |
|
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: 201.13 E-value: 2.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksDICTIMYTSGTTGDPKG 240
Cdd:cd05914 89 D--------------------------------------------------------------DVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFdrviEECF-----IQHGAAIGFWrGDV---KLLIEDLA 312
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEVVL-----LGKGDKILSILPLHHIY----PLTFtlllpLLNGAHVVFL-DKIpsaKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 313 ELKPTIFCAVPRVLDRVY-SGLQKKLSDGGF---LKKFIFDSAFSykfgymkkgqshveasplfdKLVFSKVKQGLGGNV 388
Cdd:cd05914 177 QVTPTLGVPVPLVIEKIFkMDIIPKLTLKKFkfkLAKKINNRKIR--------------------KLAFKKVHEAFGGNI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 389 RIILSGAAPLASHVESFLRVVACChVLQGYGLTEsCAGTFVSLPDELGMLGTVGPPVPNVDIRLesvpemeYDALASTAR 468
Cdd:cd05914 237 KEFVIGGAKINPDVEEFLRTIGFP-YTIGYGMTE-TAPIISYSPPNRIRLGSAGKVIDGVEVRI-------DSPDPATGE 307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236634 469 GEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENI 538
Cdd:cd05914 308 GEIIVRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAK 378
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
69-552 |
1.00e-55 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 197.05 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 69 IVDGKPGKYVwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIIS 148
Cdd:cd05911 2 QIDADTGKEL--TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 149 HSEVSIVFVEEK---KISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGlvIYAWDEFLKLGEGKQydlpikkksDI 225
Cdd:cd05911 80 ISKPKVIFTDPDgleKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLG--EEDEDLPPPLKDGKD---------DT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 226 CTIMYTSGTTGDPKGVMISNESIvtlIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDrvieeCFIQHGAAIG------F 299
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNL---IANLSQVQTFLYGNDGSNDVILGFLPLYHIYG-----LFTTLASLLNgatviiM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 WRGDVKLLIEDLAELKPTIFCAVPRVLdrvysglqkklsdggflkkfifdSAFSykfgymkkgqshveASPLFDKLVFSk 379
Cdd:cd05911 221 PKFDSELFLDLIEKYKITFLYLVPPIA-----------------------AALA--------------KSPLLDKYDLS- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 380 vkqglggNVRIILSGAAPLASHVESFL-RVVACCHVLQGYGLTESCAGTFVSlPDELGMLGTVGPPVPNVDIRLesVPEM 458
Cdd:cd05911 263 -------SLRVILSGGAPLSKELQELLaKRFPNATIKQGYGMTETGGILTVN-PDGDDKPGSVGRLLPNVEAKI--VDDD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 459 EYDALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIEN 537
Cdd:cd05911 333 GKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEA 411
|
490
....*....|....*
gi 15236634 538 IYGEVQAVDSVWVYG 552
Cdd:cd05911 412 VLLEHPGVADAAVIG 426
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
224-552 |
4.88e-55 |
|
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: 190.96 E-value: 4.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFdrvieecfiQHGAAIGFW--- 300
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG-----LTEGDVFLSTLPLFHIG---------GLFGLLGALlag 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 301 -------RGDVKLLIEDLAELKPTIFCAVPRVLDRvysgLQKklsdggflkkfifdsafsykfgymkkgqshveaSPLFD 373
Cdd:cd04433 67 gtvvllpKFDPEAALELIEREKVTILLGVPTLLAR----LLK---------------------------------APESA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 374 KLVFSkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDEL-GMLGTVGPPVPNVDIRL 452
Cdd:cd04433 110 GYDLS--------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDaRKPGSVGRPVPGVEVRI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 453 ESVpemEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKlSQGEYVAV 532
Cdd:cd04433 182 VDP---DGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYP 257
|
330 340
....*....|....*....|
gi 15236634 533 ENIENIYGEVQAVDSVWVYG 552
Cdd:cd04433 258 AEVEAVLLGHPGVAEAAVVG 277
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
48-521 |
3.26e-54 |
|
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: 192.78 E-value: 3.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 48 WDVFRMSVEKYPNNPMLgrreIVDGKpgkyvWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAH 127
Cdd:cd05936 2 ADLLEEAARRFPDKTAL----IFMGR-----KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 128 GLYCVPLYDTLGADAVEFIISHSEVSIVFVeekkiselfktcpnsteymktVVSFggvsreqkeeaetfglviyawDEFL 207
Cdd:cd05936 73 GAVVVPLNPLYTPRELEHILNDSGAKALIV---------------------AVSF---------------------TDLL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 208 KLGEGKQYDlPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanEALTVKDVYLSYLPLAHIFD-RVI 286
Cdd:cd05936 111 AAGAPLGER-VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLE---DLLEGDDVVLAALPLFHVFGlTVA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 287 EECFIQHGAAIGFW-RGDVKLLIEDLAELKPTIFCAVPRVldrvYSGLQkklsdggflkkfifdsafsykfgymkkgqsh 365
Cdd:cd05936 187 LLLPLALGATIVLIpRFRPIGVLKEIRKHRVTIFPGVPTM----YIALL------------------------------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 366 veASPLFDKLVFSkvkqglggNVRIILSGAAPLA-SHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDELGMLGTVGPP 444
Cdd:cd05936 232 --NAPEFKKRDFS--------SLRLCISGGAPLPvEVAERFEELTGV-PIVEGYGLTETSPVVAVNPLDGPRKPGSIGIP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 445 VPNVDIRL-----ESVPEMEydalastaRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKK 519
Cdd:cd05936 301 LPGTEVKIvdddgEELPPGE--------VGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKK 372
|
..
gi 15236634 520 NI 521
Cdd:cd05936 373 DM 374
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
227-633 |
1.63e-52 |
|
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: 190.74 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 227 TIMYTSGTTGDPKGVMISNEsivtLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFW-RGDVK 305
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTER----LVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAaASDMS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 306 LLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSdggflkkfifdsafsykfgymKKGQSHVEASPLFDKLVFSKVKQGLG 385
Cdd:cd17632 303 TLFDDLALVRPTELFLVPRVCDMLFQRYQAELD---------------------RRSVAGADAETLAERVKAELRERVLG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 386 GNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTfVSLPDELgmlgtVGPPVpnVDIRLESVPEMEYDALAS 465
Cdd:cd17632 362 GRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGA-VILDGVI-----VRPPV--LDYKLVDVPELGYFRTDR 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 466 T-ARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDV-GEWQPDgSMKIIDRKKNIFKLSQGEYVAVENIENIYGEV 542
Cdd:cd17632 432 PhPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPD-RLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 543 QAVDSVWVYGNSFESFLIAIANPNQHILErwaaengvsgDYDAlcqnEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDP 622
Cdd:cd17632 511 PLVRQIFVYGNSERAYLLAVVVPTQDALA----------GEDT----ARLRAALAESLQRIAREAGLQSYEIPRDFLIET 576
|
410
....*....|.
gi 15236634 623 VPFDMERDLLT 633
Cdd:cd17632 577 EPFTIANGLLS 587
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
81-522 |
2.02e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 174.71 E-value: 2.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KIsELFKTCPNSTEYMKTVVSFggvsreQKEEAETFGLVIYAWDEFLKLGEGKqYDLPIKKKSDICTIMYTSGTTGDPKG 240
Cdd:PRK07656 112 FL-GVDYSATTRLPALEHVVIC------ETEEDDPHTEKMKTFTDFLAAGDPA-ERAPEVDPDDVADILFTSGTTGRPKG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFdrvieeCF-------IQHGAAI----GFwrgDVKLLIE 309
Cdd:PRK07656 184 AMLTHRQLLSNAADWAEYLG-----LTEGDRYLAANPFFHVF------GYkagvnapLMRGATIlplpVF---DPDEVFR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 310 DLAELKPTIFCAVPRVldrvysglqkklsdggflkkfifdsafsYKFGYmkkgqSHVEASPlFDklvFSkvkqglggNVR 389
Cdd:PRK07656 250 LIETERITVLPGPPTM----------------------------YNSLL-----QHPDRSA-ED---LS--------SLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 390 IILSGAA--PLAShVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDE-LGMLGTVGPPVPNVDIRLESVPEMEydaLAS 465
Cdd:PRK07656 285 LAVTGAAsmPVAL-LERFESELGVDIVLTGYGLSEASgVTTFNRLDDDrKTVAGTIGTAIAGVENKIVNELGEE---VPV 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15236634 466 TARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIF 522
Cdd:PRK07656 361 GEVGELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
51-552 |
9.62e-47 |
|
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: 171.25 E-value: 9.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 51 FRMSVEKYPNNPML---GRREivdgkpgkyvwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAH 127
Cdd:cd17631 1 LRRRARRHPDRTALvfgGRSL------------TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 128 GLYCVPLYDTLGADAVEFIISHSEVSIVFveekkiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdefl 207
Cdd:cd17631 69 GAVFVPLNFRLTPPEVAYILADSGAKVLF--------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 208 klgegkqydlpikkkSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANEALTVKDVYLSYLPLAHIfdrVIE 287
Cdd:cd17631 98 ---------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL-----AALDLGPDDVLLVVAPLFHI---GGL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 288 ECF----IQHGAAIGFWRG-DVKLLIEDLAELKPTIFCAVPRVLDRVysgLQkklsdggflkkfifdsafsykfgymkkg 362
Cdd:cd17631 155 GVFtlptLLRGGTVVILRKfDPETVLDLIERHRVTSFFLVPTMIQAL---LQ---------------------------- 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 363 qshveaSPLFDKLVFSkvkqglggNVRIILSGAAPLAshvESFLRVVACCHV--LQGYGLTESCAGTFVSLPDE-LGMLG 439
Cdd:cd17631 204 ------HPRFATTDLS--------SLRAVIYGGAPMP---ERLLRALQARGVkfVQGYGMTETSPGVTFLSPEDhRRKLG 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 440 TVGPPVPNVDIRL-----ESVPEMEydalastaRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKI 514
Cdd:cd17631 267 SAGRPVFFVEVRIvdpdgREVPPGE--------VGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYI 338
|
490 500 510
....*....|....*....|....*....|....*...
gi 15236634 515 IDRKKNIFKlSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd17631 339 VDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG 375
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-535 |
1.96e-44 |
|
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: 166.65 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 65 GRREIV-DGKPGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAV 143
Cdd:cd12119 10 GDREIVsRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 144 EFIISHSEVSIVFVE---EKKISELFKTCPNsteYMKTVVSFGGVsreqkEEAETFGLVIYAWDEFLKLGEGKqYDLPIK 220
Cdd:cd12119 90 AYIINHAEDRVVFVDrdfLPLLEAIAPRLPT---VEHVVVMTDDA-----AMPEPAGVGVLAYEELLAAESPE-YDWPDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 221 KKSDICTIMYTSGTTGDPKGVMISNESIV-----TLIAGVIrllksaneALTVKDVYLSYLPLAHIfdrvieecfiqHG- 294
Cdd:cd12119 161 DENTAAAICYTSGTTGNPKGVVYSHRSLVlhamaALLTDGL--------GLSESDVVLPVVPMFHV-----------NAw 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 295 --AAIGFWRG----------DVKLLIEDLAELKPTIFCAVPRVLDrvysglqkklsdgGFLkkfifdsafsykfgymkkg 362
Cdd:cd12119 222 glPYAAAMVGaklvlpgpylDPASLAELIEREGVTFAAGVPTVWQ-------------GLL------------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 363 qSHVEASPLfdklVFSKVKqglggnvRIILSGAAPLASHVESFLRvvACCHVLQGYGLTESCA-GTFVSLPDELGMLG-- 439
Cdd:cd12119 270 -DHLEANGR----DLSSLR-------RVVIGGSAVPRSLIEAFEE--RGVRVIHAWGMTETSPlGTVARPPSEHSNLSed 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 440 -------TVGPPVPNVDIRL--ESVPEMEYDalaSTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDG 510
Cdd:cd12119 336 eqlalraKQGRPVPGVELRIvdDDGRELPWD---GKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDG 412
|
490 500
....*....|....*....|....*...
gi 15236634 511 SMKIIDRKKNIFKlSQGEY---VAVENI 535
Cdd:cd12119 413 YLTITDRSKDVIK-SGGEWissVELENA 439
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
81-576 |
3.52e-35 |
|
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: 138.35 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFktcpnsteymkTVVSFGGVSREQKEEAEtfgLVIYAWDEflklgegkqydlpikkksDICTIMYTSGTTGDPKG 240
Cdd:TIGR01923 81 LEEKDF-----------QADSLDRIEAAGRYETS---LSASFNMD------------------QIATLMFTSGTTGKPKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAHIFD-RVIEECFIQhGAAIGFWRGDVKLLiEDLAELKPTIF 319
Cdd:TIGR01923 129 VPHTFRNHYASAVGSKENL-----GFTEDDNWLLSLPLYHISGlSILFRWLIE-GATLRIVDKFNQLL-EMIANERVTHI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 320 CAVPRVLDRvysglqkklsdggflkkfifdsafsykfgYMKKGQSHVeasplfdklvfskvkqglggNVRIILSGAAPLA 399
Cdd:TIGR01923 202 SLVPTQLNR-----------------------------LLDEGGHNE--------------------NLRKILLGGSAIP 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 400 ShveSFLRVVAC--CHVLQGYGLTESCAgTFVSLPDELGM-LGTVGPPVPNVDIRLEsVPEMEydalastARGEICIRGK 476
Cdd:TIGR01923 233 A---PLIEEAQQygLPIYLSYGMTETCS-QVTTATPEMLHaRPDVGRPLAGREIKIK-VDNKE-------GHGEIMVKGA 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 477 TLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWV------ 550
Cdd:TIGR01923 301 NLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpda 379
|
490 500
....*....|....*....|....*..
gi 15236634 551 -YGNSFESFLIAIANPNQHILERWAAE 576
Cdd:TIGR01923 380 eWGQVPVAYIVSESDISQAKLIAYLTE 406
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
221-523 |
4.74e-35 |
|
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: 139.29 E-value: 4.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRllkSANEALTVKDVYLSYLPLAHIFD-RVIEECFIQHGAAI-- 297
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVA---GEGSNSDSEDVFLCVLPMFHIYGlSSFALGLLRLGATVvv 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 298 --GFwrgDVKLLIEDLAELKPTIFCAVPRVLdrvySGLQKklsdggflkkfifdsafsykfgymkkgqshveaSPLFDKL 375
Cdd:cd05904 233 mpRF---DLEELLAAIERYKVTHLPVVPPIV----LALVK---------------------------------SPIVDKY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 376 VFSKVKQglggnvriILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGM--LGTVGPPVPNVDIRL 452
Cdd:cd05904 273 DLSSLRQ--------IMSGAAPLGKELiEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRakYGSVGRLVPNVEAKI 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236634 453 ESVPEMEydALASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFK 523
Cdd:cd05904 345 VDPETGE--SLPPNQTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
74-538 |
9.78e-35 |
|
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: 138.21 E-value: 9.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 74 PGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVS 153
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 154 IVFVEEKKISELFKTCPNSTEYMKTVVSFGGVsREQKEEAETFGlviyawdeFLKLGEGKQYDLPIKKKSDICTIMYTSG 233
Cdd:cd05926 89 LVLTPKGELGPASRAASKLGLAILELALDVGV-LIRAPSAESLS--------NLLADKKNAKSEGVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 234 TTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIfdrvieecfiqHGAAIG--------------- 298
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYK-----LTPDDRTLVVMPLFHV-----------HGLVASllstlaaggsvvlpp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 299 ------FWrgdvklliEDLAELKPTIFCAVPRVldrvysgLQKKLSdggflkkfifdsafsykfgyMKKGQSHVEASPLf 372
Cdd:cd05926 224 rfsastFW--------PDVRDYNATWYTAVPTI-------HQILLN--------------------RPEPNPESPPPKL- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 373 dklvfskvkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVS-LPDELGMLGTVGPPVpNVDIR 451
Cdd:cd05926 268 ----------------RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNpLPPGPRKPGSVGKPV-GVEVR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 452 LesVPEmEYDALASTARGEICIRGKTLFSGYYKREDLTKEV-LIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYV 530
Cdd:cd05926 331 I--LDE-DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKI 406
|
....*...
gi 15236634 531 AVENIENI 538
Cdd:cd05926 407 SPLEVDGV 414
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
58-624 |
9.54e-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: 135.12 E-value: 9.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 58 YPNnpmlgRREIVDGKpgkyVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDT 137
Cdd:cd12118 17 YPD-----RTSIVYGD----RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 138 LGADAVEFIISHSEVSIVFVEEKkiselfktcpnsteymktvvsfggvsreqkeeaetfglviYAWDEFLKLGEGKQYDL 217
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDRE----------------------------------------FEYEDLLAEGDPDFEWI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 218 PIKKKSDICTIMYTSGTTGDPKGVMISNES--IVTLIAGVI-RLLKSAnealtvkdVYLSYLPLAHIFDRvieeCFIQHG 294
Cdd:cd12118 128 PPADEWDPIALNYTSGTTGRPKGVVYHHRGayLNALANILEwEMKQHP--------VYLWTLPMFHCNGW----CFPWTV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 295 AAIG-----FWRGDVKLLIEDLAELKPTIFCAVPRVLDRVysglqkklsdggflkkfifdsafsykfgymkkgqshVEAS 369
Cdd:cd12118 196 AAVGgtnvcLRKVDAKAIYDLIEKHKVTHFCGAPTVLNML------------------------------------ANAP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 370 PLfdklvfskVKQGLGGNVRIILSGAAPLASHVES-----FlrvvaccHVLQGYGLTE------SCA--GTFVSLPDE-- 434
Cdd:cd12118 240 PS--------DARPLPHRVHVMTAGAPPPAAVLAKmeelgF-------DVTHVYGLTEtygpatVCAwkPEWDELPTEer 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 435 --------LGMLGTVGPPVPNVDIrLESVPemeydALASTArGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEW 506
Cdd:cd12118 305 arlkarqgVRYVGLEEVDVLDPET-MKPVP-----RDGKTI-GEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVI 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 507 QPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVygnsfesfliaIANPNQHILERWAAengvsgdYDAL 586
Cdd:cd12118 378 HPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAV-----------VARPDEKWGEVPCA-------FVEL 438
|
570 580 590
....*....|....*....|....*....|....*...
gi 15236634 587 CQNEKAKEfilGELVKMAKEkKMKGFEIIKAIHLDPVP 624
Cdd:cd12118 439 KEGAKVTE---EEIIAFCRE-HLAGFMVPKTVVFGELP 472
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
81-552 |
6.15e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 132.78 E-value: 6.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFKTCPnsteymktvVSFGGVSREQKEEAEtfglVIYAWDEflklgegkqydlpikkkSDICTIMYTSGTTGDPKG 240
Cdd:PRK03640 109 FEAKLIPGIS---------VKFAELMNGPKEEAE----IQEEFDL-----------------DEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNE----SIVTliagvirllkSA-NEALTVKDVYLSYLPLAHI------FDRVI-------EECFiqhgaaigfwrg 302
Cdd:PRK03640 159 VIQTYGnhwwSAVG----------SAlNLGLTEDDCWLAAVPIFHIsglsilMRSVIygmrvvlVEKF------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 DVKLLIEDLAELKPTIFCAVPRVLDRvysgLQKKLSDGGFlkkfifdsafsykfgymkkgqshveasplfdklvfskvkq 382
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVSTMLQR----LLERLGEGTY---------------------------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 383 glGGNVRIILSGAAPLAshvesfLRVVACCH-----VLQGYGLTESCAgTFVSLP--DELGMLGTVGPPVPNVDIRLESv 455
Cdd:PRK03640 253 --PSSFRCMLLGGGPAP------KPLLEQCKekgipVYQSYGMTETAS-QIVTLSpeDALTKLGSAGKPLFPCELKIEK- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 456 pemEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENI 535
Cdd:PRK03640 323 ---DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEI 398
|
490
....*....|....*..
gi 15236634 536 ENIYGEVQAVDSVWVYG 552
Cdd:PRK03640 399 EEVLLSHPGVAEAGVVG 415
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-552 |
9.13e-33 |
|
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: 131.26 E-value: 9.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVeek 160
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksDICTIMYTSGTTGDPKG 240
Cdd:cd05934 82 ---------------------------------------------------------------DPASILYTSGTTGPPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAHIFDRVieecfiqHGAAIGFWRGDVKLLIE---------DL 311
Cdd:cd05934 99 VVITHANLTFAGYYSARRF-----GLGEDDVYLTVLPLFHINAQA-------VSVLAALSVGATLVLLPrfsasrfwsDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 312 AELKPTIFCAVPRVLDRVYSglQKKLSDggflkkfifDSAfsykfgymkkgqshveasplfdklvfskvkqglgGNVRII 391
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLA--QPPSPD---------DRA----------------------------------HRLRAA 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 392 LSGAAPLASHVESFLRVvaCCHVLQGYGLTESCAGTfVSLPDELGMLGTVGPPVPNVDIRLesVPEMEYDALASTArGEI 471
Cdd:cd05934 202 YGAPNPPELHEEFEERF--GVRLLEGYGMTETIVGV-IGPRDEPRRPGSIGRPAPGYEVRI--VDDDGQELPAGEP-GEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 472 CIR---GKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSV 548
Cdd:cd05934 276 VIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREA 354
|
....
gi 15236634 549 WVYG 552
Cdd:cd05934 355 AVVA 358
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
81-552 |
1.67e-32 |
|
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: 130.16 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVsivfveek 160
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikKKSDICTIMYTSGTTGDPKG 240
Cdd:cd05912 75 ------------------------------------------------------------KLDDIATIMYTSGTTGKPKG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIvtliagvirlLKSA-----NEALTVKDVYLSYLPLAHI------FDRVIEECFIqhgaaIGFWRGDVKLLIE 309
Cdd:cd05912 95 VQQTFGNH----------WWSAigsalNLGLTEDDNWLCALPLFHIsglsilMRSVIYGMTV-----YLVDKFDAEQVLH 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 310 DLAELKPTIFCAVPRVLDRVYSglqkklsdggflkkfIFDSAFSYkfgymkkgqshveasplfdklvfskvkqglggNVR 389
Cdd:cd05912 160 LINSGKVTIISVVPTMLQRLLE---------------ILGEGYPN--------------------------------NLR 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 390 IILSGAAPLAshvesfLRVVACCH-----VLQGYGLTESCAgTFVSLP--DELGMLGTVGPPVPNVDIRLESVPEMEYDA 462
Cdd:cd05912 193 CILLGGGPAP------KPLLEQCKekgipVYQSYGMTETCS-QIVTLSpeDALNKIGSAGKPLFPVELKIEDDGQPPYEV 265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 463 lastarGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEV 542
Cdd:cd05912 266 ------GEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSH 338
|
490
....*....|
gi 15236634 543 QAVDSVWVYG 552
Cdd:cd05912 339 PAIKEAGVVG 348
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
49-550 |
3.29e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.21 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 49 DVFRMSVEKYPnnpmlGRREIVDGKpgkYVWqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
Cdd:PRK08316 15 DILRRSARRYP-----DKTALVFGD---RSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 129 LYCVPLYDTLGADAVEFIISHSEVSIVFVEekkiSELFKTCPNSTEYMKtVVSFGGVSREQKEEAETfglviyAWDEFLK 208
Cdd:PRK08316 86 AVHVPVNFMLTGEELAYILDHSGARAFLVD----PALAPTAEAALALLP-VDTLILSLVLGGREAPG------GWLDFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 209 L--GEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIV-----TLIAGvirllksaneALTVKDVYLSYLPLAHI 281
Cdd:PRK08316 155 WaeAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyvsCIVAG----------DMSADDIPLHALPLYHC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 282 FDRvieECFIQHGAAIGFW-----RGDVKLLIEDLAELKPTIFCAVPRV-----------------LDRVYSG------- 332
Cdd:PRK08316 225 AQL---DVFLGPYLYVGATnvildAPDPELILRTIEAERITSFFAPPTVwisllrhpdfdtrdlssLRKGYYGasimpve 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 333 ----LQKKLSDGGFlkkfifdsafsYKFgYmkkGQSHVeasplfdklvfskvkqglggnvriilsgaAPLAShvesflrv 408
Cdd:PRK08316 302 vlkeLRERLPGLRF-----------YNC-Y---GQTEI-----------------------------APLAT-------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 409 vacchVLQgygltescagtfvslPDE-LGMLGTVGPPVPNVDIRLESvPEMEydALASTARGEICIRGKTLFSGYYKRED 487
Cdd:PRK08316 330 -----VLG---------------PEEhLRRPGSAGRPVLNVETRVVD-DDGN--DVAPGEVGEIVHRSPQLMLGYWDDPE 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236634 488 LTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKlSQGEYVA---VEniENIY-----GEVqAV----DSVWV 550
Cdd:PRK08316 387 KTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVAsreVE--EALYthpavAEV-AViglpDPKWI 457
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
81-538 |
8.88e-31 |
|
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: 126.87 E-value: 8.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFKTcPNSTEYMKTVVSFGG-VSREQKEEAETFglviYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPK 239
Cdd:cd17642 126 GLQKVLNV-QKKLKIIKTIIILDSkEDYKGYQCLYTF----ITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAGVIR--LLKSANEALTVkdvyLSYLPLAHIFDrvieeCFIQHGAAI-GF-----WRGDVKLLIEDL 311
Cdd:cd17642 201 GVQLTHKNIVARFSHARDpiFGNQIIPDTAI----LTVIPFHHGFG-----MFTTLGYLIcGFrvvlmYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 312 AELKPTIFCAVPRVLdrvysglqkklsdgGFLKKfifdsafsykfgymkkgqshveaSPLFDKLVFSkvkqglggNVRII 391
Cdd:cd17642 272 QDYKVQSALLVPTLF--------------AFFAK-----------------------STLVDKYDLS--------NLHEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 392 LSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSlPDELGMLGTVGPPVPNVDIRLesVPEMEYDALASTARGE 470
Cdd:cd17642 307 ASGGAPLSKEVgEAVAKRFKLPGIRQGYGLTETTSAILIT-PEGDDKPGAVGKVVPFFYAKV--VDLDTGKTLGPNERGE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15236634 471 ICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
35-521 |
2.21e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 126.27 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 35 DGFPDPIE-GMDSCWDVFRMSVEKYPNNPML---GRReivdgkpgkyvwQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIY 110
Cdd:PRK05605 21 PWTPHDLDyGDTTLVDLYDNAVARFGDRPALdffGAT------------TTYAELGKQVRRAAAGLRALGVRPGDRVAIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 111 GANSPEWIISMEACNAHGLYCV---PLYDtlgADAVE--FIISHSEVSIVFveeKKISELFKTCPNSTEyMKTVVSFGGV 185
Cdd:PRK05605 89 LPNCPQHIVAFYAVLRLGAVVVehnPLYT---AHELEhpFEDHGARVAIVW---DKVAPTVERLRRTTP-LETIVSVNMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 186 S-----------------REQKEEAETFGLVIYAWDEFLK---LGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISN 245
Cdd:PRK05605 162 AampllqrlalrlpipalRKARAALTGPAPGTVPWETLVDaaiGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 246 ESIVT-LIAGV--IRLLKSANEaltvkdVYLSYLPLAHIFDRVIEECFiqhGAAIG-----FWRGDVKLLIEDLAELKPT 317
Cdd:PRK05605 242 RNLFAnAAQGKawVPGLGDGPE------RVLAALPMFHAYGLTLCLTL---AVSIGgelvlLPAPDIDLILDAMKKHPPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 318 IFCAVPrvldrvysglqkklsdggflkkfifdsafsykfgymkkgqshveasPLFDKLVFSKVKQGLG-GNVRIILSGAA 396
Cdd:PRK05605 313 WLPGVP----------------------------------------------PLYEKIAEAAEERGVDlSGVRNAFSGAM 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 397 PL-ASHVESFLRVVACcHVLQGYGLTEsCAGTFVSLP-DELGMLGTVGPPVPNVDIRLESvPEMEYDALASTARGEICIR 474
Cdd:PRK05605 347 ALpVSTVELWEKLTGG-LLVEGYGLTE-TSPIIVGNPmSDDRRPGYVGVPFPDTEVRIVD-PEDPDETMPDGEEGELLVR 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15236634 475 GKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNI 521
Cdd:PRK05605 424 GPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
224-607 |
1.04e-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: 122.49 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNEsivTLIAGVIRLLksANEALTVKDVYLSYLPLAHIfdrvieecfiqhgaaIGFWRGD 303
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHN---TLSASIRQYA--ERLGLGPGDVFLVASPMAHQ---------------TGFVYGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 304 VKLLIEdlaelkptifcAVPRVLDRVYS---GLQKKLSDGgflkkfifdsafsykfgymkkgQSHVEASPLF-DKLVFSK 379
Cdd:cd05903 154 TLPLLL-----------GAPVVLQDIWDpdkALALMREHG----------------------VTFMMGATPFlTDLLNAV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 380 VKQG-LGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDELGMLGTVGPPVPNVDIRLesVPE 457
Cdd:cd05903 201 EEAGePLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPgAVTSITPAPEDRRLYTDGRPLPGVEIKV--VDD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 458 mEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIEN 537
Cdd:cd05903 279 -TGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVED 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236634 538 IYGEVQAVDSVWVygnsfesfliaIANPNQHILERWAA----ENGVSGDYDALCqnekakEFILGelVKMAKEK 607
Cdd:cd05903 357 LLLGHPGVIEAAV-----------VALPDERLGERACAvvvtKSGALLTFDELV------AYLDR--QGVAKQY 411
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
49-552 |
1.31e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 123.73 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 49 DVFRMSVEKYPNNPMLGRREivdgkpgKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
Cdd:PRK12583 22 DAFDATVARFPDREALVVRH-------QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 129 LYCVPLYDTLGADAVEFIISHSEVSIVFVEEKkiselFKTC----------PNSTE------------YMKTVVSFGGvs 186
Cdd:PRK12583 95 AILVNINPAYRASELEYALGQSGVRWVICADA-----FKTSdyhamlqellPGLAEgqpgalacerlpELRGVVSLAP-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 187 reqkeeAETFGLViyAWDEFLKLGEG-KQYDLPIKKKS----DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLks 261
Cdd:PRK12583 168 ------APPPGFL--AWHELQARGETvSREALAERQASldrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESL-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 262 aneALTVKDVYLSYLPLAHIFDRVIEE--CfIQHGAAIGFWRGDVKLLI--EDLAELKPTIFCAVPRVldrvysglqkkl 337
Cdd:PRK12583 238 ---GLTEHDRLCVPVPLYHCFGMVLANlgC-MTVGACLVYPNEAFDPLAtlQAVEEERCTALYGVPTM------------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 338 sdggflkkFIfdsafsykfgymkkgqSHVEaSPLFDKLVFSKVKQGlggnvriILSGAAPLashVESFLRVVA---CCHV 414
Cdd:PRK12583 302 --------FI----------------AELD-HPQRGNFDLSSLRTG-------IMAGAPCP---IEVMRRVMDemhMAEV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 415 LQGYGLTESCAGTFVSLPDElgmlgtvgppvpNVDIRLESV----PEME---YDALAST----ARGEICIRGKTLFSGYY 483
Cdd:PRK12583 347 QIAYGMTETSPVSLQTTAAD------------DLERRVETVgrtqPHLEvkvVDPDGATvprgEIGELCTRGYSVMKGYW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 484 KREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK12583 415 NNPEATAESIDeDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
81-517 |
1.97e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 123.30 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEE- 159
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADg 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 -----------KKISELFKTCPNsteyMKTVVSFGGVSREQKEEAEtfglviYAWDEFLKlGEGKQYDLPIKKKSDICTI 228
Cdd:COG0365 121 glrggkvidlkEKVDEALEELPS----LEHVIVVGRTGADVPMEGD------LDWDELLA-AASAEFEPEPTDADDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 229 MYTSGTTGDPKGVMISNesivtliAGVI-RLLKSANEALTVK--DVY-----------LSYL---PLAhifdrvieecfi 291
Cdd:COG0365 190 LYTSGTTGKPKGVVHTH-------GGYLvHAATTAKYVLDLKpgDVFwctadigwatgHSYIvygPLL------------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 292 qHGAAIGFWRG-----DVKLLIEDLAELKPTIFCAVPRVLDrvysglqkklsdggflkkfifdsAFsykfgyMKKGQSHV 366
Cdd:COG0365 251 -NGATVVLYEGrpdfpDPGRLWELIEKYGVTVFFTAPTAIR-----------------------AL------MKAGDEPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 367 EASPLfdklvfskvkqglgGNVRIILSGAAPLAshVESFLRVVA--CCHVLQGYGLTESCaGTFVSLPDELGM-LGTVGP 443
Cdd:COG0365 301 KKYDL--------------SSLRLLGSAGEPLN--PEVWEWWYEavGVPIVDGWGQTETG-GIFISNLPGLPVkPGSMGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 444 PVPNVDIRL-----ESVPEMEydalastaRGEICIRGK--TLFSGYYKREDLTKEV---LIDGWLHTGDVGEWQPDGSMK 513
Cdd:COG0365 364 PVPGYDVAVvdedgNPVPPGE--------EGELVIKGPwpGMFRGYWNDPERYRETyfgRFPGWYRTGDGARRDEDGYFW 435
|
....
gi 15236634 514 IIDR 517
Cdd:COG0365 436 ILGR 439
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
205-525 |
6.10e-29 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 121.70 E-value: 6.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 205 EFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIvtlIAGVIRLLKSANEALTV-KDVYLSYLPLAHIFD 283
Cdd:PRK08974 188 SALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNM---LANLEQAKAAYGPLLHPgKELVVTALPLYHIFA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 284 RVIEeC--FIQHGAAigfwrgdvKLLIEDlaelkptifcavPRVLDRVYSGLQKklsdggflkkfifdsafsYKFGYMKK 361
Cdd:PRK08974 265 LTVN-CllFIELGGQ--------NLLITN------------PRDIPGFVKELKK------------------YPFTAITG 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 362 GQSHVEA---SPLFDKLVFSKVKQGLGGnvriilsGAAPLASHVESFLRVVACcHVLQGYGLTEsCAGTFVSLPDEL-GM 437
Cdd:PRK08974 306 VNTLFNAllnNEEFQELDFSSLKLSVGG-------GMAVQQAVAERWVKLTGQ-YLLEGYGLTE-CSPLVSVNPYDLdYY 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 438 LGTVGPPVPNVDIRLesVPEmEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDR 517
Cdd:PRK08974 377 SGSIGLPVPSTEIKL--VDD-DGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDR 453
|
....*...
gi 15236634 518 KKNIFKLS 525
Cdd:PRK08974 454 KKDMILVS 461
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
81-552 |
6.24e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 121.68 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCV---PLYDTlgaDAVEFIISHSEVSIVFV 157
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTE---RELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 158 EEKKISELfKTCPNSTEYMKTVVS-------------FGGVSREQK------EEAETfglvIYAWDEFLKlGEGKQYDLP 218
Cdd:PRK06710 128 LDLVFPRV-TNVQSATKIEHVIVTriadflpfpknllYPFVQKKQSnlvvkvSESET----IHLWNSVEK-EVNTGVEVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEAltvKDVYLSYLPLAHIF--DRVIEECFIQHGAA 296
Cdd:PRK06710 202 CDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG---EEVVLGVLPFFHVYgmTAVMNLSIMQGYKM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 297 IGFWRGDVKLLIEDLAELKPTIFCAVPRVldrvYSGLQKklsdggflkkfifdsafsykfgymkkgqshveaSPLFDKLV 376
Cdd:PRK06710 279 VLIPKFDMKMVFEAIKKHKVTLFPGAPTI----YIALLN---------------------------------SPLLKEYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 FSkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVP 456
Cdd:PRK06710 322 IS--------SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 457 EMEydALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIE 536
Cdd:PRK06710 394 TGE--ALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVE 470
|
490
....*....|....*.
gi 15236634 537 NIYGEVQAVDSVWVYG 552
Cdd:PRK06710 471 EVLYEHEKVQEVVTIG 486
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
224-552 |
1.36e-27 |
|
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: 116.24 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIvtliAGVIRLLKSANEaLTVKDVYLSYLPLAHIfdrvieecfiqHGAAIG----F 299
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANL----AANVRALVDAWR-WTEDDVLLHVLPLHHV-----------HGLVNAllcpL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 WRG---------DVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFdsafsykfgymkkgqshveasp 370
Cdd:cd05941 154 FAGasveflpkfDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA---------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 371 lfdklvfskvkqglgGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEScaGTFVSLP-DELGMLGTVGPPVPNVD 449
Cdd:cd05941 212 ---------------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEI--GMALSNPlDGERRPGTVGMPLPGVQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 450 IRLesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKK-NIFKlSQG 527
Cdd:cd05941 275 ARI--VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGG 351
|
330 340
....*....|....*....|....*
gi 15236634 528 EYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIG 376
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
207-525 |
3.06e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 116.79 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSA-NEAltvKDVYLSYLPLAHIFdrv 285
Cdd:PRK05677 191 LAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNlNEG---CEILIAPLPLYHIY--- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 286 ieeCFIQHGAAIgFWRGDVKLLIEDlaelkptifcavPRVLDRVYSGLQK-KLSdgGFLKkfiFDSAFSykfgymkkGQS 364
Cdd:PRK05677 265 ---AFTFHCMAM-MLIGNHNILISN------------PRDLPAMVKELGKwKFS--GFVG---LNTLFV--------ALC 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 365 HVEAsplFDKLVFSKVKqglggnvrIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELgMLGTVGPP 444
Cdd:PRK05677 316 NNEA---FRKLDFSALK--------LTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAI-QVGTIGIP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 445 VPNVDIRlesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFK 523
Cdd:PRK05677 384 VPSTLCK---VIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMIL 460
|
..
gi 15236634 524 LS 525
Cdd:PRK05677 461 VS 462
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
223-558 |
7.38e-27 |
|
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: 111.97 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTliagVIRLLKSANEALTVKDVYLSYLPLAHIFDRV-IEECFIQHGA-AIGFW 300
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA----VPDILQKEGLNWVVGDVTYLPLPATHIGGLWwILTCLIHGGLcVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 301 RGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFsykfgymkkgqshveasPLFDKLVFSKv 380
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR-----------------AIAADVRFIE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 381 kqgLGGNVRIIlsgaaplashvesflrvvacchvlQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVpemEY 460
Cdd:cd17635 139 ---ATGLTNTA------------------------QVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAAT---DG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 461 DALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYG 540
Cdd:cd17635 189 IAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAE 267
|
330
....*....|....*...
gi 15236634 541 EVQAVDSVWVYGNSFESF 558
Cdd:cd17635 268 GVSGVQECACYEISDEEF 285
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
220-548 |
2.79e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 112.81 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFDRVIEECF-IQHGAAIG 298
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD-----PNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 299 FWRG--DVKLLIEDLAELKPTIFCAVPRVLDrvysglqkklsdggflkkfifdsafsykfGYMKKGQSHVEASplfdklv 376
Cdd:cd05909 219 FHPNplDYKKIPELIYDKKATILLGTPTFLR-----------------------------GYARAAHPEDFSS------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 fskvkqglggnVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVP 456
Cdd:cd05909 263 -----------LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 457 EmeYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIE 536
Cdd:cd05909 332 T--HEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIE 408
|
330
....*....|..
gi 15236634 537 NIYGEVQAVDSV 548
Cdd:cd05909 409 DILSEILPEDNE 420
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
224-523 |
4.10e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 112.77 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIA----GvirllKSANEALTVKDVYLSYLPLAHIFD-RVIEECFIQHGAAIG 298
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdG-----ENPNLYFHSDDVILCVLPMFHIYSlNSVLLCGLRVGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 299 FWRG-DVKLLIEDLAELKPTIFCAVPRVLdrvysglqkkLSdggflkkfifdsafsykfgymkkgqshVEASPLFDKLVF 377
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV----------LA---------------------------IAKSPVVEKYDL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVL-QGYGLTEscAGTFVSL---------PDELGMLGTVgppVPN 447
Cdd:PLN02246 298 S--------SIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE--AGPVLAMclafakepfPVKSGSCGTV---VRN 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15236634 448 VDIRLESvPEMEyDALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFK 523
Cdd:PLN02246 365 AELKIVD-PETG-ASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIK 439
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
81-552 |
5.33e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 112.26 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLR-SVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEE 159
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiselfktcpnstEYMKTVVSFGGVSreqkeeaetfGLVIYAWDEFLK-LGEGKQYDLPIKKKSDICTIMYTSGTTGDP 238
Cdd:PRK06839 109 --------------TFQNMALSMQKVS----------YVQRVISITSLKeIEDRKIDNFVEKNESASFIICYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 239 KGVMISNESIV-TLIAGVIRLlksaneALTVKDVYLSYLPLAHIfdrvieecfiqhgAAIGFWRgdvklliedlaelKPT 317
Cdd:PRK06839 165 KGAVLTQENMFwNALNNTFAI------DLTMHDRSIVLLPLFHI-------------GGIGLFA-------------FPT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 318 IFCA----VPRVLDRvysglQKKLSdggflkkFIFDSAFSYKFGYMKKGQSHVEAsPLFDKLVFSkvkqglggNVRIILS 393
Cdd:PRK06839 213 LFAGgviiVPRKFEP-----TKALS-------MIEKHKVTVVMGVPTIHQALINC-SKFETTNLQ--------SVRWFYN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 394 GAAP-----LASHVESFLRVVacchvlQGYGLTESCAGTFVSLPDELG-MLGTVGPPVPNVDIRLES-----VPEMEYda 462
Cdd:PRK06839 272 GGAPcpeelMREFIDRGFLFG------QGFGMTETSPTVFMLSEEDARrKVGSIGKPVLFCDYELIDenknkVEVGEV-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 463 lastarGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEV 542
Cdd:PRK06839 344 ------GELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKL 416
|
490
....*....|
gi 15236634 543 QAVDSVWVYG 552
Cdd:PRK06839 417 SDVYEVAVVG 426
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
81-511 |
5.55e-26 |
|
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: 111.47 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFveek 160
Cdd:cd05930 14 TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfkTCPNSTEYmktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksdictIMYTSGTTGDPKG 240
Cdd:cd05930 90 -------TDPDDLAY----------------------------------------------------VIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAI----GFWRGDVKLLIEDLAEL 314
Cdd:cd05930 111 VMVEHRGLVNLLLWMQEAY-----PLTPGDRVLQFTSFS--FDVSVWEIFgaLLAGATLvvlpEEVRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 315 KPTIFCAVPRVLDRVysglqkkLSDGGFLkkfifdsafsykfgymkkgqshveasplfdklVFSKVKqglggnvRIILSG 394
Cdd:cd05930 184 GITVLHLTPSLLRLL-------LQELELA--------------------------------ALPSLR-------LVLVGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 395 AAPLASHVESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELGMLGTV--GPPVPNVDIR-----LESVPEmeydalasT 466
Cdd:cd05930 218 EALPPDLVRRWRELLPGARLVNLYGPTEATVDaTYYRVPPDDEEDGRVpiGRPIPNTRVYvldenLRPVPP--------G 289
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15236634 467 ARGEICIRGKTLFSGYYKREDLTKEVLID------GWLH-TGDVGEWQPDGS 511
Cdd:cd05930 290 VPGELYIGGAGLARGYLNRPELTAERFVPnpfgpgERMYrTGDLVRWLPDGN 341
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
81-510 |
1.27e-25 |
|
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: 109.66 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRS-VGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEE 159
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 KKISELfktcpnsteymktvvsfggvsreqkeEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKS--DICTIMYTSGTTGD 237
Cdd:TIGR01733 81 ALASRL--------------------------AGLVLPVILLDPLELAALDDAPAPPPPDAPSGpdDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 238 PKGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAA--------IGFWRGDVKLL 307
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRY-----GLDPDDRVLQFASLS--FDASVEEIFgaLLAGATlvvppedeERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 308 IedlAELKPTIFCAVPRVLDRVysgLQKKLSDGGFLKkfifdsafsykfgymkkgqshveasplfdklvfskvkqglggn 387
Cdd:TIGR01733 208 I---AEHPVTVLNLTPSLLALL---AAALPPALASLR------------------------------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 388 vRIILSGAAPLASHVESFLRVVACCHVLQGYGLTE----SCAGTFVSLPDELGMLGTVGPPVPNVDIRLESvPEMEYDAL 463
Cdd:TIGR01733 239 -LVILGGEALTPALVDRWRARGPGARLINLYGPTEttvwSTATLVDPDDAPRESPVPIGRPLANTRLYVLD-DDLRPVPV 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 464 ASTarGEICIRGKTLFSGYYKREDLTKEVLIDG---------WLHTGDVGEWQPDG 510
Cdd:TIGR01733 317 GVV--GELYIGGPGVARGYLNRPELTAERFVPDpfaggdgarLYRTGDLVRYLPDG 370
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
209-552 |
1.95e-25 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 111.12 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 209 LGEGKQYDLPIKK--KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVI 286
Cdd:PRK08751 192 LALGRKHSMPTLQiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 287 EE-CFIQHGAA---IGFWRgDVKLLIEDLAELKPTIFCAVprvlDRVYSGLQKklsdggflkkfifdsafsykfgymkkg 362
Cdd:PRK08751 272 NGlVFMKIGGCnhlISNPR-DMPGFVKELKKTRFTAFTGV----NTLFNGLLN--------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 363 qshveaSPLFDKLVFSKVKQGLGGnvriilsGAAPLASHVESFLRVVACCHVlQGYGLTESCAGTFVSLPDELGMLGTVG 442
Cdd:PRK08751 320 ------TPGFDQIDFSSLKMTLGG-------GMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAACINPLTLKEYNGSIG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 443 PPVPNVDIrleSVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNI 521
Cdd:PRK08751 386 LPIPSTDA---CIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDM 462
|
330 340 350
....*....|....*....|....*....|.
gi 15236634 522 FKLSqGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK08751 463 ILVS-GFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
81-552 |
2.45e-24 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 106.41 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEek 160
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiSELfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkkSDICTIMYTSGTTGDPKG 240
Cdd:cd05935 81 --SEL---------------------------------------------------------DDLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIvtlIAGVIRLLKSANeaLTVKDVYLSYLPLAHI--FDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTI 318
Cdd:cd05935 102 CMHTHFSA---AANALQSAVWTG--LTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 319 FCAVPRVLDRVYsglqkklsdggflkkfifdsafsykfgymkkgqshveASPLFDKLVFSKVKQgLGGnvriilsGAAPL 398
Cdd:cd05935 177 WTNIPTMLVDLL-------------------------------------ATPEFKTRDLSSLKV-LTG-------GGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 399 ASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELgMLGTVGPPVPNVDIRLESVPEMEydALASTARGEICIRGKTL 478
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRP-KLQCLGIP*FGVDARVIDIETGR--ELPPNEVGEIVVRGPQI 288
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236634 479 FSGYYKREDLTKE--VLIDG--WLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd05935 289 FKGYWNRPEETEEsfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
56-637 |
2.59e-24 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 107.80 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 56 EKYPNnpmlgRREIVDGKPgKYVWQtyqEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLY 135
Cdd:PLN03102 25 ECYPN-----RTSIIYGKT-RFTWP---QTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPIN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 136 DTLGADAVEFIISHSEVSIVFVE---EKKISELFKTCPNSTEYMKTVVSF----GGVSREQKEEAETFGLViyawdeflK 208
Cdd:PLN03102 96 TRLDATSIAAILRHAKPKILFVDrsfEPLAREVLHLLSSEDSNLNLPVIFiheiDFPKRPSSEELDYECLI--------Q 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 209 LGEGKQYDLP----IKKKSDICTIMYTSGTTGDPKGVMISNE----SIVTLIAGVirllksaneALTVKDVYLSYLPLAH 280
Cdd:PLN03102 168 RGEPTPSLVArmfrIQDEHDPISLNYTSGTTADPKGVVISHRgaylSTLSAIIGW---------EMGTCPVYLWTLPMFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 281 ifdrvieeC----FIQHGAAigfwRGDVKLLIEDLAelKPTIF-----------CAVPRVldrvysglqkklsdggflkk 345
Cdd:PLN03102 239 --------CngwtFTWGTAA----RGGTSVCMRHVT--APEIYkniemhnvthmCCVPTV-------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 346 fifdsafsykFGYMKKGQShVEASPLfdklvfskvkqglGGNVRIILSGAAPLASHVESFLRVvaCCHVLQGYGLTESCA 425
Cdd:PLN03102 285 ----------FNILLKGNS-LDLSPR-------------SGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 426 GT-FVSLPDELGML------------GTVGPPVPNVDIR----LESVPEmeydalASTARGEICIRGKTLFSGYYKREDL 488
Cdd:PLN03102 339 PVlFCEWQDEWNRLpenqqmelkarqGVSILGLADVDVKnketQESVPR------DGKTMGEIVIKGSSIMKGYLKNPKA 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 489 TKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIygevqavdsVWVYGNSFESFLIAIANPNQH 568
Cdd:PLN03102 413 TSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHPTWG 482
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 569 -------ILERwaAENGVSGDYDALCQNEkakefilGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFK 637
Cdd:PLN03102 483 etpcafvVLEK--GETTKEDRVDKLVTRE-------RDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-552 |
7.50e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 103.51 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVT--LIAGvIRLlksaneALTVKDVYLSYLPLAHIFDRVIE--ECfIQHGAAI-- 297
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNngYFIG-ERL------GLTEQDRLCIPVPLFHCFGSVLGvlAC-LTHGATMvf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 298 ---GFwrgDVKLLIEDLAELK-------PTIFCAVprvLDRvysglqkklsdggflkkfifdsafsykfgymkkgqshve 367
Cdd:cd05917 75 pspSF---DPLAVLEAIEKEKctalhgvPTMFIAE---LEH--------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 368 asPLFDKLVFSKVKQGlggnvriILSGA-APlashVESFLRVVACCH---VLQGYGLTESCAGTFVSLPD---ELgMLGT 440
Cdd:cd05917 110 --PDFDKFDLSSLRTG-------IMAGApCP----PELMKRVIEVMNmkdVTIAYGMTETSPVSTQTRTDdsiEK-RVNT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 441 VGPPVPNVDIRlesVPEMEYDALAST-ARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRK 518
Cdd:cd05917 176 VGRIMPHTEAK---IVDPEGGIVPPVgVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRI 252
|
330 340 350
....*....|....*....|....*....|....
gi 15236634 519 KNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd05917 253 KDMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
207-525 |
3.03e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 104.33 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVtliAGVIRLLKSANEALTVKD-----VYLSYLPLAHI 281
Cdd:PRK07059 188 LAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIV---ANVLQMEAWLQPAFEKKPrpdqlNFVCALPLYHI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 282 FdrVIEECFIQ------HGAAIGFWRgDVKLLIEDLAELKPTIFCAVprvlDRVYSGLQKklsdggflkkfifdsafsyk 355
Cdd:PRK07059 265 F--ALTVCGLLgmrtggRNILIPNPR-DIPGFIKELKKYQVHIFPAV----NTLYNALLN-------------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 356 fgymkkgqshveaSPLFDKLVFSKVKQGLGGnvriilsGAA---PLAshvESFLRVVACcHVLQGYGLTESCAGTFVSLP 432
Cdd:PRK07059 318 -------------NPDFDKLDFSKLIVANGG-------GMAvqrPVA---ERWLEMTGC-PITEGYGLSETSPVATCNPV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 433 DELGMLGTVGPPVPNVDIrleSVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGS 511
Cdd:PRK07059 374 DATEFSGTIGLPLPSTEV---SIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTaDGFFRTGDVGVMDERGY 450
|
330
....*....|....
gi 15236634 512 MKIIDRKKNIFKLS 525
Cdd:PRK07059 451 TKIVDRKKDMILVS 464
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
81-552 |
3.75e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 103.43 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEk 160
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kisELfkTCPNSTEYMKTVVSfggvsreqkeeaetfglvIYAWDEFLKLGEGKQYDLP--IKKKSDICTIMYTSGTTGDP 238
Cdd:PRK06145 108 ---EF--DAIVALETPKIVID------------------AAAQADSRRLAQGGLEIPPqaAVAPTDLVRLMYTSGTTDRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 239 KGVMISNESIVtliagvirlLKSANE----ALTVKDVYLSYLPLAHIfdrvieECFIQHGAAIgFWRGDVkLLIEdlAEL 314
Cdd:PRK06145 165 KGVMHSYGNLH---------WKSIDHvialGLTASERLLVVGPLYHV------GAFDLPGIAV-LWVGGT-LRIH--REF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 315 KP-TIFCAVPRvlDRVysglqkklsDGGFLKKFIFdsafsykfgymkkgqSHVEASPLFDKLVFSKVKQGLGGnvriils 393
Cdd:PRK06145 226 DPeAVLAAIER--HRL---------TCAWMAPVML---------------SRVLTVPDRDRFDLDSLAWCIGG------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 394 GAAPLASHVESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELGMLGTVGPPVPNVDIRLESvpeMEYDALASTARGEIC 472
Cdd:PRK06145 273 GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGdTLMEAGREIEKIGSTGRALAHVEIRIAD---GAGRWLPPNMKGEIC 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 473 IRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK06145 350 MRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
27-538 |
4.37e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 103.52 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 27 VYRSIFAKDGFPDPIegmdSCWDVFRMSVEKYPNNPMLgrreiVDGKPGKYVwqTYQEVYDIVMKLGNSLRSVGVKDEAK 106
Cdd:PLN02330 14 IFRSRYPSVPVPDKL----TLPDFVLQDAELYADKVAF-----VEAVTGKAV--TYGEVVRDTRRFAKALRSLGLRKGQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 107 CGIYGANSPEW-IISMEACNAHGLYCvplydtlGADAVEFIishSEVSivfvEEKKISELFKTCPNSTEYMKT------V 179
Cdd:PLN02330 83 VVVVLPNVAEYgIVALGIMAAGGVFS-------GANPTALE---SEIK----KQAEAAGAKLIVTNDTNYGKVkglglpV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 180 VSFGGVSREQKEEaetfglviyaWDEFLKLGE--GKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESivtLIAGVIR 257
Cdd:PLN02330 149 IVLGEEKIEGAVN----------WKELLEAADraGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRN---LVANLCS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 258 LLKSANEALTVKDVYLSYLPLAHIFDrVIEECFI---QHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPRVLdrvysglq 334
Cdd:PLN02330 216 SLFSVGPEMIGQVVTLGLIPFFHIYG-ITGICCAtlrNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPII-------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 335 kklsdggflkkfifdsafsykFGYMKkgqshveaSPLFDKLVFSKVKqglggnVRIILSGAAPLASHV-ESFLRVVACCH 413
Cdd:PLN02330 287 ---------------------LNLVK--------NPIVEEFDLSKLK------LQAIMTAAAPLAPELlTAFEAKFPGVQ 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 414 VLQGYGLTE-SCAGTFVSLPDE---LGMLGTVGPPVPNVDIRLESvPEMEYdALASTARGEICIRGKTLFSGYY-KREDL 488
Cdd:PLN02330 332 VQEAYGLTEhSCITLTHGDPEKghgIAKKNSVGFILPNLEVKFID-PDTGR-SLPKNTPGELCVRSQCVMQGYYnNKEET 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15236634 489 TKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
Cdd:PLN02330 410 DRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
224-552 |
8.22e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 99.71 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIfdrvieecfiqHGAAIgFWR-- 301
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-----FGGGDSWLLSLPLYHV-----------GGLAI-LVRsl 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 302 ---GDVKL------LIEDLAELKPTIFCAVPRVLDRVYsglqkklsdggflkkfifdsafsykfgymkkgQSHVEASPLF 372
Cdd:cd17630 64 lagAELVLlernqaLAEDLAPPGVTHVSLVPTQLQRLL--------------------------------DSGQGPAALK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 373 dklvfskvkqglggNVRIILSGAAPLASH-VESFL-RVVACChvlQGYGLTESCAGTFVSLPDELGmLGTVGPPVPNVDI 450
Cdd:cd17630 112 --------------SLRAVLLGGAPIPPElLERAAdRGIPLY---TTYGMTETASQVATKRPDGFG-RGGVGVLLPGREL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 451 RLesvpemeydalasTARGEICIRGKTLFSGYYKReDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYV 530
Cdd:cd17630 174 RI-------------VEDGEIWVGGASLAMGYLRG-QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENI 238
|
330 340
....*....|....*....|..
gi 15236634 531 AVENIENIYGEVQAVDSVWVYG 552
Cdd:cd17630 239 QPEEIEAALAAHPAVRDAFVVG 260
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
81-552 |
1.02e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 102.37 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISE----LFKTCPNsteyMKTVVSFG--GVSREQKEEAETFG---LViyawdeflklgegkQYDLPikkkSDICTIMYT 231
Cdd:PRK06188 119 PFVEralaLLARVPS----LKHVLTLGpvPDGVDLLAAAAKFGpapLV--------------AAALP----PDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 232 SGTTGDPKGVMISNESIVTLIagVIRLlksANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAI---GFWRGDVKLLI 308
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMA--QIQL---AEWEWPADPRFLMCTPLSHAGGAFFLPTLLRGGTVIvlaKFDPAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 309 ED----LAELKPTIFCAV---PRVLDRVYSGLQkklsdggflkkfifdsafsykfgymkkgqshveasplfdklvfskvk 381
Cdd:PRK06188 252 EEqritATFLVPTMIYALldhPDLRTRDLSSLE----------------------------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 382 qglggnvrIILSGAAP-----LASHVESFLRVVAcchvlQGYGLTEscAGTFVS-------LPDELGMLGTVGPPVPNVD 449
Cdd:PRK06188 285 --------TVYYGASPmspvrLAEAIERFGPIFA-----QYYGQTE--APMVITylrkrdhDPDDPKRLTSCGRPTPGLR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 450 IRL-----ESVPEMEYdalastarGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkL 524
Cdd:PRK06188 350 VALldedgREVAQGEV--------GEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMI-V 420
|
490 500
....*....|....*....|....*...
gi 15236634 525 SQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK06188 421 TGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
49-539 |
1.39e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 102.20 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 49 DVFRMSVEKYPNNPML-----GRReivdgkpgkyvwQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEA 123
Cdd:PRK08315 20 QLLDRTAARYPDREALvyrdqGLR------------WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 124 CNAHGLYCV---PLYDTlgaDAVEFIISHSEVS-IVFVEEKK-------ISEL---FKTCP----NSTE--YMKTVVSFG 183
Cdd:PRK08315 88 TAKIGAILVtinPAYRL---SELEYALNQSGCKaLIAADGFKdsdyvamLYELapeLATCEpgqlQSARlpELRRVIFLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 184 gvsreqkeEAETFGLviYAWDEFLKLGEGKQYD-LPIKKKS----DICTIMYTSGTTGDPKGVMISNESIVT---LIAGV 255
Cdd:PRK08315 165 --------DEKHPGM--LNFDELLALGRAVDDAeLAARQATldpdDPINIQYTSGTTGFPKGATLTHRNILNngyFIGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 256 IRLlksanealTVKDVYLSYLPLAHifdrvieeCF---------IQHGAAI-----GFwrgDVKLLIEDLAELK------ 315
Cdd:PRK08315 235 MKL--------TEEDRLCIPVPLYH--------CFgmvlgnlacVTHGATMvypgeGF---DPLATLAAVEEERctalyg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 316 -PTIFCAVprvLDrvysglqkklsdggflkkfifdsafsykfgymkkgqsHveasPLFDKLVFSKVKQGlggnvriILSG 394
Cdd:PRK08315 296 vPTMFIAE---LD-------------------------------------H----PDFARFDLSSLRTG-------IMAG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 395 AA-PlashVESFLRVVACCH---VLQGYGLTESCAGTFVSLPD---ELgMLGTVGPPVPNVDIRL------ESVPEMEyd 461
Cdd:PRK08315 325 SPcP----IEVMKRVIDKMHmseVTIAYGMTETSPVSTQTRTDdplEK-RVTTVGRALPHLEVKIvdpetgETVPRGE-- 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 462 alastaRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFklsqgeyvavenI---EN 537
Cdd:PRK08315 398 ------QGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMI------------IrggEN 459
|
..
gi 15236634 538 IY 539
Cdd:PRK08315 460 IY 461
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
81-577 |
3.56e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 100.62 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSL--RSVGVKDeaKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVE 158
Cdd:PRK07786 44 TWRELDDRVAALAGALsrRGVGFGD--RVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 159 EKkISELFKTCPNSTEYMKTVVSFGGVSREQkeeaetfglvIYAWDEFL-KLGEGKQY-DLPIKKKSdicTIMYTSGTTG 236
Cdd:PRK07786 122 AA-LAPVATAVRDIVPLLSTVVVAGGSSDDS----------VLGYEDLLaEAGPAHAPvDIPNDSPA---LIMYTSGTTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 237 DPKGVMISNESIVTLIAGVIRllksANEALTVKDVYLSYLPLAHIfdrvieecfiqhgAAIGfwrgdvklliedlaELKP 316
Cdd:PRK07786 188 RPKGAVLTHANLTGQAMTCLR----TNGADINSDVGFVGVPLFHI-------------AGIG--------------SMLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 317 TIFCAVPRVLdrvysglqkklsdggflkkfifdsafsYKFGYMKKGQshveaspLFDKLVFSKVK--------------- 381
Cdd:PRK07786 237 GLLLGAPTVI---------------------------YPLGAFDPGQ-------LLDVLEAEKVTgiflvpaqwqavcae 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 382 ---QGLGGNVRIILSGAAPlAShvESFLRVVACC----HVLQGYGLTESCAGTFVSL-PDELGMLGTVGPPVPNVDIRle 453
Cdd:PRK07786 283 qqaRPRDLALRVLSWGAAP-AS--DTLLRQMAATfpeaQILAAFGQTEMSPVTCMLLgEDAIRKLGSVGKVIPTVAAR-- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 454 sVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVE 533
Cdd:PRK07786 358 -VVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCA 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15236634 534 NIENIYGEVQAVDSVWVYGNSFESF------LIAIANPNQHI----LERWAAEN 577
Cdd:PRK07786 436 EVENVLASHPDIVEVAVIGRADEKWgevpvaVAAVRNDDAALtledLAEFLTDR 489
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
212-545 |
4.05e-22 |
|
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: 100.43 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 212 GKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirllKSANEALTVKDVYLSYLPLAHIfdRVIEECFI 291
Cdd:cd05906 156 AADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-----KIQHNGLTPQDVFLNWVPLDHV--GGLVELHL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 292 QhgaaigfwrgDVKLLIEDLAELKPTIFCAVPRVLDrvysglqkklsdggFLKKFIFDSAFSYKFGYMKKGQsHVEASPL 371
Cdd:cd05906 229 R----------AVYLGCQQVHVPTEEILADPLRWLD--------------LIDRYRVTITWAPNFAFALLND-LLEEIED 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 372 FDklvfskvkqGLGGNVRIILSGAAPL-ASHVESFLRVVACCHVLQ-----GYGLTESCAGTFVSLPDELGMLGT----- 440
Cdd:cd05906 284 GT---------WDLSSLRYLVNAGEAVvAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSFPTYDHSQalefv 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 441 -VGPPVPNVDIRL-----ESVPEMEydalastaRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGeWQPDGSMK 513
Cdd:cd05906 355 sLGRPIPGVSMRIvddegQLLPEGE--------VGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLG-FLDNGNLT 425
|
330 340 350
....*....|....*....|....*....|..
gi 15236634 514 IIDRKKNIFKLSQGEYVAVEnIENIYGEVQAV 545
Cdd:cd05906 426 ITGRTKDTIIVNGVNYYSHE-IEAAVEEVPGV 456
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
218-538 |
4.09e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 100.69 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 218 PIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFD-RVIEECFIQHGAA 296
Cdd:PLN02574 193 PVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGlSLFVVGLLSLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 297 IGFWRG-DVKLLIEDLAELKPTIFCAVPRVLdrvysglqkklsdggflkkfifdsafsykfgymkkgqshveasplfdkL 375
Cdd:PLN02574 273 IVVMRRfDASDMVKVIDRFKVTHFPVVPPIL------------------------------------------------M 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 376 VFSKVKQGLGGNV----RIILSGAAPLASH-VESFLRVVACCHVLQGYGLTESCA-GTFVSLPDELGMLGTVGPPVPNVD 449
Cdd:PLN02574 305 ALTKKAKGVCGEVlkslKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAvGTRGFNTEKLSKYSSVGLLAPNMQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 450 IRlesVPEMEYDA-LASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLsQG 527
Cdd:PLN02574 385 AK---VVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KG 460
|
330
....*....|.
gi 15236634 528 EYVAVENIENI 538
Cdd:PLN02574 461 FQIAPADLEAV 471
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
207-538 |
5.65e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 100.28 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVI-----------RLLKSANEaltvkdVYLSY 275
Cdd:PRK12492 191 LRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRaclsqlgpdgqPLMKEGQE------VMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 276 LPLAHIFdRVIEECFIQhgaaigFWRGDVKLLIEDlaelkptifcavPRVLdrvysglqkklsdGGFLKKFifdsaFSYK 355
Cdd:PRK12492 265 LPLYHIY-AFTANCMCM------MVSGNHNVLITN------------PRDI-------------PGFIKEL-----GKWR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 356 FGYMKKGQSHVEA---SPLFDKLVFSKVKqglggnvrIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLP 432
Cdd:PRK12492 308 FSALLGLNTLFVAlmdHPGFKDLDFSALK--------LTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPY 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 433 DELGMLGTVGPPVPNVDIRlesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGS 511
Cdd:PRK12492 380 GELARLGTVGIPVPGTALK---VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGF 456
|
330 340
....*....|....*....|....*..
gi 15236634 512 MKIIDRKKNIFKLSqGEYVAVENIENI 538
Cdd:PRK12492 457 VRIVDRKKDLIIVS-GFNVYPNEIEDV 482
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
58-545 |
1.71e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 98.48 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 58 YPNNPmlgrrEIVDGKpgkyVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIismeacNAHglYCVP---- 133
Cdd:PRK08162 31 YPDRP-----AVIHGD----RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMV------EAH--FGVPmaga 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 134 ----LYDTLGADAVEFIISHSEVSIVFVEE---KKISELFKTCPNSTeymKTVVsfgGVSREQKEEAETFGLVIYawDEF 206
Cdd:PRK08162 94 vlntLNTRLDAASIAFMLRHGEAKVLIVDTefaEVAREALALLPGPK---PLVI---DVDDPEYPGGRFIGALDY--EAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 207 LKLGE-GKQYDLPiKKKSDICTIMYTSGTTGDPKGVM----------ISNesivTLIAGvirllksaneaLTVKDVYLSY 275
Cdd:PRK08162 166 LASGDpDFAWTLP-ADEWDAIALNYTSGTTGNPKGVVyhhrgaylnaLSN----ILAWG-----------MPKHPVYLWT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 276 LPLAHIFDRvieeCF-----IQHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPRVldrvYSGLqkklsdggflkkfifds 350
Cdd:PRK08162 230 LPMFHCNGW----CFpwtvaARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIV----LSAL----------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 351 afsykfgymkkgqshVEASPlfdklvfsKVKQGLGGNVRIILSGAAPLASHVESFLRV-VACCHVlqgYGLTES------ 423
Cdd:PRK08162 285 ---------------INAPA--------EWRAGIDHPVHAMVAGAAPPAAVIAKMEEIgFDLTHV---YGLTETygpatv 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 424 CA--GTFVSLPDEL--GMLGTVGPPVPnvdiRLESVPEMEYDALASTAR-----GEICIRGKTLFSGYYKREDLTKEVLI 494
Cdd:PRK08162 339 CAwqPEWDALPLDEraQLKARQGVRYP----LQEGVTVLDPDTMQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFA 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15236634 495 DGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGeyvavENIENIygEVQAV 545
Cdd:PRK08162 415 GGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGG-----ENISSI--EVEDV 457
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
79-550 |
2.04e-21 |
|
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: 97.75 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 79 WQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVE 158
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 159 EKKISELFKTCPNSTEymktVVSFGGVSREQKEEAETFGLVIYawdeflklgegkqydlpikkksdictIMYTSGTTGDP 238
Cdd:cd12116 92 DALPDRLPAGLPVLLL----ALAAAAAAPAAPRTPVSPDDLAY--------------------------VIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 239 KGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDrvieecfiqhgaaigfwrgdvkllIEDLAELKPTI 318
Cdd:cd12116 142 KGVVVSHRNLVNFLHSMRERL-----GLGPGDRLLAVTTYA--FD------------------------ISLLELLLPLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 319 FCAVPRVLDRvysglqKKLSDGGFLKKFIFDsafsykfgymkKGQSHVEASPLFDKLVFSKVKQGLGGnVRIILSGAA-- 396
Cdd:cd12116 191 AGARVVIAPR------ETQRDPEALARLIEA-----------HSITVMQATPATWRMLLDAGWQGRAG-LTALCGGEAlp 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 397 -PLAshvESFLRVVACCHVLqgYGLTE----SCAgTFVSlpDELGMLgTVGPPVPN-----VDIRLESVPEMEYdalast 466
Cdd:cd12116 253 pDLA---ARLLSRVGSLWNL--YGPTEttiwSTA-ARVT--AAAGPI-PIGRPLANtqvyvLDAALRPVPPGVP------ 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 467 arGEICIRGKTLFSGYYKREDLTKEVLIDG--------WLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
Cdd:cd12116 318 --GELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAA 394
|
490
....*....|..
gi 15236634 539 YGEVQAVDSVWV 550
Cdd:cd12116 395 LAAHPGVAQAAV 406
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
81-538 |
4.29e-21 |
|
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: 97.01 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIIS-MEACNAHGLYcVPLYDTLGADAVEFIISHSEVSIVFVEE 159
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGiLGILKAGGAY-LPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 KKISELFKTcpnsteymktvvsfggvsreqkeeaetfGLVIYAWDEFLKLGEGKQYDlPIKKKSDICTIMYTSGTTGDPK 239
Cdd:cd17655 103 HLQPPIAFI----------------------------GLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAGVIRLLKSaNEALTVkdvyLSYLPLAhiFDRVIEECFiqHGAAIGfwrgdvklliedlaelkptif 319
Cdd:cd17655 154 GVMIEHRGVVNLVEWANKVIYQ-GEHLRV----ALFASIS--FDASVTEIF--ASLLSG--------------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 320 cavprvlDRVYSGLQKKLSDGGFLKKFIFDsafsYKFGYMKKGQSHVEASPLFDKLVFSKVKqglggnvRIILSGAAPLA 399
Cdd:cd17655 204 -------NTLYIVRKETVLDGQALTQYIRQ----NRITIIDLTPAHLKLLDAADDSEGLSLK-------HLIVGGEALST 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 400 SHVESFL-RVVACCHVLQGYGLTESCAGTFVSLPDELGMLGT---VGPPVPN-----VDIRLESVPEMEydalastaRGE 470
Cdd:cd17655 266 ELAKKIIeLFGTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPLGNtriyiLDQYGRPQPVGV--------AGE 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236634 471 ICIRGKTLFSGYYKREDLTKEVLID------GWLH-TGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
Cdd:cd17655 338 LYIGGEGVARGYLNRPELTAEKFVDdpfvpgERMYrTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEAR 411
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
81-511 |
9.02e-21 |
|
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: 97.62 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYcVPLYDTLGADAVEFIISHSEVSIVFVEE 159
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVlKAGAAY-VPLDPAYPAERLAYMLEDAGARLVLTQS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 KkiselfktcpnsteymktvvsfggvsreQKEEAETFGLVIYAWDEfLKLGEGKQYDLPIK-KKSDICTIMYTSGTTGDP 238
Cdd:COG1020 582 A----------------------------LAARLPELGVPVLALDA-LALAAEPATNPPVPvTPDDLAYVIYTSGSTGRP 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 239 KGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAI----GFWRGDVKLLIEDLA 312
Cdd:COG1020 633 KGVMVEHRALVNLLAWMQRRY-----GLGPGDRVLQFASLS--FDASVWEIFgaLLSGATLvlapPEARRDPAALAELLA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 313 ELKPTIFCAVPRVLDRVYSGLQKKLSDggfLKkfifdsafsykfgymkkgqshveasplfdklvfskvkqglggnvRIIL 392
Cdd:COG1020 706 RHRVTVLNLTPSLLRALLDAAPEALPS---LR--------------------------------------------LVLV 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 393 SGAAPLASHVESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELGMLGTV--GPPVPNV-----DIRLESVPEmeydala 464
Cdd:COG1020 739 GGEALPPELVRRWRARLPGARLVNLYGPTETTVDsTYYEVTPPDADGGSVpiGRPIANTrvyvlDAHLQPVPV------- 811
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15236634 465 sTARGEICIRGKTLFSGYYKREDLTKEVLIDG--------WLHTGDVGEWQPDGS 511
Cdd:COG1020 812 -GVPGELYIGGAGLARGYLNRPELTAERFVADpfgfpgarLYRTGDLARWLPDGN 865
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
39-655 |
9.20e-21 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 97.62 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 39 DPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVdgkpGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWI 118
Cdd:PTZ00297 421 NPLAGVRSLGEMWERSVTRHSTFRCLGQTSES----GESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIV 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 119 ISMEACNAHGLYCVPLYDTlgADAVEFIISHSEVSIVFVEEKKISELFkTCpNSTEYMKTVVSFGGVSREQKEEAETFGL 198
Cdd:PTZ00297 497 ILEVACALYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAIL-TC-RSRKLETVVYTHSFYDEDDHAVARDLNI 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 199 VIYAWDEFLKLGEGKQYDLPIKKKSDICTIMY----TSGTTGDPKGVMISNESI---VTLIAGVIRLLKSANEALTVKdv 271
Cdd:PTZ00297 573 TLIPYEFVEQKGRLCPVPLKEHVTTDTVFTYVvdntTSASGDGLAVVRVTHADVlrdISTLVMTGVLPSSFKKHLMVH-- 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 272 ylsYLPLAHIFDRVIEECFIQHGAAIGfwRGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSA 351
Cdd:PTZ00297 651 ---FTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERA 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 352 FSYKFGYMkkgQSHVEASPLFDKLVFSKVKQGLGGNVR-IILSGAAplASHVESFLRVVACCHVlqgyglteSCAGTFVS 430
Cdd:PTZ00297 726 FQLRSRLI---NIHRRDSSLLRFIFFRATQELLGGCVEkIVLCVSE--ESTSFSLLEHISVCYV--------PCLREVFF 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 431 LPDElGMLGTVGPPVPNVDIRLESVPEMEYDA----LASTARGEicirgktlfsgyyKREDLtkEVlidgwlhtgdVGEW 506
Cdd:PTZ00297 793 LPSE-GVFCVDGTPAPSLQVDLEPFDEPSDGAgigqLVLAKKGE-------------PRRTL--PI----------AAQW 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 507 QPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESfLIAIANPNQHILE-RW-AAENGVSGDYD 584
Cdd:PTZ00297 847 KRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWrQSHCMGEGGGP 925
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 585 ALCQN-----EKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
Cdd:PTZ00297 926 ARQLGwtelvAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
70-561 |
1.12e-20 |
|
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: 95.39 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 70 VDGKPGKYvwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISH 149
Cdd:cd05945 10 VVEGGRTL---TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 150 SEVSIVFVEekkiselfktcPNSTEYmktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksdictIM 229
Cdd:cd05945 87 AKPALLIAD-----------GDDNAY----------------------------------------------------II 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 230 YTSGTTGDPKGVMISNESIVTLIAGVIrllksANEALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIgfW------R 301
Cdd:cd05945 104 FTSGSTGRPKGVQISHDNLVSFTNWML-----SDFPLGPGDVFLNQAPFS--FDLSVMDLYpaLASGATL--VpvprdaT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 302 GDVKLLIEDLAELKPTIFCAVPRVLDRVysglqkkLSDGGF-------LKKFIFDSafsykfgymkkgqshvEASPLfdk 374
Cdd:cd05945 175 ADPKQLFRFLAEHGITVWVSTPSFAAMC-------LLSPTFtpeslpsLRHFLFCG----------------EVLPH--- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 375 lvfSKVKQglggnvriiLSGAAPLAshvesflrvvaccHVLQGYGLTESCAG-TFVSLPDE-LGMLGTV--GPPVPNVDI 450
Cdd:cd05945 229 ---KTARA---------LQQRFPDA-------------RIYNTYGPTEATVAvTYIEVTPEvLDGYDRLpiGYAKPGAKL 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 451 RLEsvpEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVL--IDG--WLHTGDVGEWQPDGSMKIIDRKKNIFKLsQ 526
Cdd:cd05945 284 VIL---DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKL-N 359
|
490 500 510
....*....|....*....|....*....|....*...
gi 15236634 527 GEYVAVENIENIYGEVQAVDS---VWVYGNSFESFLIA 561
Cdd:cd05945 360 GYRIELEEIEAALRQVPGVKEavvVPKYKGEKVTELIA 397
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
228-518 |
1.67e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 95.06 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESIvtliAGVIRLLKSAnEALTVKDVYLSYLPLAHIfdrvieecfiqHGAAIGFW----RGD 303
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAI----AADLDALAEA-WQWTADDVLVHGLPLFHV-----------HGLVLGVLgplrIGN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 304 -----VKLLIEDLAE---LKPTIFCAVPRVLDRVysglqkklsdggflkkfifdsafsykfgymkkgqshVEASPLFDKL 375
Cdd:PRK07787 197 rfvhtGRPTPEAYAQalsEGGTLYFGVPTVWSRI------------------------------------AADPEAARAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 376 vfskvkqglgGNVRIILSGAAPLASHVesFLRVVACC--HVLQGYGLTESCAgTFVSLPDELGMLGTVGPPVPNVDIRL- 452
Cdd:PRK07787 241 ----------RGARLLVSGSAALPVPV--FDRLAALTghRPVERYGMTETLI-TLSTRADGERRPGWVGLPLAGVETRLv 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236634 453 -ESVPEMEYDAlasTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRK 518
Cdd:PRK07787 308 dEDGGPVPHDG---ETVGELQVRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGRE 372
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
224-552 |
3.86e-20 |
|
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: 92.18 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVirllkSANEALTVKDVYLSYLPLAHIFdrvieecfiqhgaaiGFWRGD 303
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAW-----ADCADLTEDDRYLIINPFFHTF---------------GYKAGI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 304 VKLLIEDlAELKPTIFCAVPRVLDRVYSglqKKLSdggFL--KKFIFDSAFsykfgymkkgqshveASPLFDKLVFSKVK 381
Cdd:cd17638 61 VACLLTG-ATVVPVAVFDVDAILEAIER---ERIT---VLpgPPTLFQSLL---------------DHPGRKKFDLSSLR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 382 QGLGGNVRIilsgAAPLASHVESFLRVVAcchVLQGYGLTESCAGTFVSLPDELGMLG-TVGPPVPNVDIRLESvpemey 460
Cdd:cd17638 119 AAVTGAATV----PVELVRRMRSELGFET---VLTAYGLTEAGVATMCRPGDDAETVAtTCGRACPGFEVRIAD------ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 461 dalastaRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIY 539
Cdd:cd17638 186 -------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGAL 257
|
330
....*....|...
gi 15236634 540 GEVQAVDSVWVYG 552
Cdd:cd17638 258 AEHPGVAQVAVIG 270
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
66-538 |
9.17e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 93.23 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 66 RReiVDGKPGKYvwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEF 145
Cdd:PRK07008 31 RR--VEGDIHRY---TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 146 IISHSEVSIVFVEEK---KISELFKTCPNsteymktVVSFGGVSREQKEEAETFGLVIYawdEFLKLGEGKQYDLPIKKK 222
Cdd:PRK07008 106 IVNHAEDRYVLFDLTflpLVDALAPQCPN-------VKGWVAMTDAAHLPAGSTPLLCY---ETLVGAQDGDYDWPRFDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVtLIAGVIRLLKSANeaLTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwRG 302
Cdd:PRK07008 176 NQASSLCYTSGTTGNPKGALYSHRSTV-LHAYGAALPDAMG--LSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVL-PG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 ---DVKLLIEDLAELKPTIFCAVPRVldrvYSGLqkklsdggflkkfifdsafsykFGYMKKGQshveasplfdkLVFSK 379
Cdd:PRK07008 252 pdlDGKSLYELIEAERVTFSAGVPTV----WLGL----------------------LNHMREAG-----------LRFST 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 380 VKqglggnvRIILSGAAPLASHVESFLRVVACcHVLQGYGLTE-SCAGTFVSL-------PDELGM--LGTVGPPVPNVD 449
Cdd:PRK07008 295 LR-------RTVIGGSACPPAMIRTFEDEYGV-EVIHAWGMTEmSPLGTLCKLkwkhsqlPLDEQRklLEKQGRVIYGVD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 450 IRL--ESVPEMEYDALAStarGEICIRGKTLFSGYYKREDltkEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKlSQG 527
Cdd:PRK07008 367 MKIvgDDGRELPWDGKAF---GDLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDRSKDVIK-SGG 439
|
490
....*....|.
gi 15236634 528 EYVAVENIENI 538
Cdd:PRK07008 440 EWISSIDIENV 450
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-517 |
2.38e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 93.06 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 217 LPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFDRVIEECF------ 290
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN-----LRNDDVILSSLPFFHSFGLTVTLWLpllegi 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 291 --IQH-----GAAIGfwrgdvKLLiedlAELKPTIFCAVPRVLdRVYSGLQKklsdggfLKKFIFDSafsykfgymkkgq 363
Cdd:PRK08633 851 kvVYHpdptdALGIA------KLV----AKHRATILLGTPTFL-RLYLRNKK-------LHPLMFAS------------- 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 364 shveasplfdklvfskvkqglggnVRIILSGAAPLASHV-ESFLRVVACcHVLQGYGLTESCAGTFVSLPDEL------- 435
Cdd:PRK08633 900 ------------------------LRLVVAGAEKLKPEVaDAFEEKFGI-RILEGYGATETSPVASVNLPDVLaadfkrq 954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 436 --GMLGTVGPPVPNVDIRLesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLID----GWLHTGDVGEWQPD 509
Cdd:PRK08633 955 tgSKEGSVGMPLPGVAVRI--VDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDED 1032
|
....*...
gi 15236634 510 GSMKIIDR 517
Cdd:PRK08633 1033 GFLTITDR 1040
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
46-519 |
8.03e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 90.40 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 46 SCWDVFRMSVEKYPNNPML---GRReivdgkpgkyvwQTYQEVYDIVMKLGNSLRSV-GVKDEAKCGIYGANSPEWIISM 121
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIvfyGRA------------ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 122 EACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEekkiSELF---KTCPNSTEYMKTVV-SFGGVSREQ-------- 189
Cdd:PRK08314 79 YAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVG----SELApkvAPAVGNLRLRHVIVaQYSDYLPAEpeiavpaw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 190 -KEEAETFGLV---IYAWDEFLklgeGKQYDLPIKKKS--DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSan 263
Cdd:PRK08314 155 lRAEPPLQALApggVVAWKEAL----AAGLAPPPHTAGpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNS-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 264 ealTVKDVYLSYLPLAHIFDrvieecfIQHG--AAIgFWRGDVKLLI----EDLAEL----KPTIFCAVPR-VLDrvysg 332
Cdd:PRK08314 229 ---TPESVVLAVLPLFHVTG-------MVHSmnAPI-YAGATVVLMPrwdrEAAARLieryRVTHWTNIPTmVVD----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 333 lqkklsdggFLkkfifdsafsykfgymkkgqshveASPLFDKLVFSKVKqGLGGnvriilsGAAPLASHVESFLRVVACC 412
Cdd:PRK08314 293 ---------FL------------------------ASPGLAERDLSSLR-YIGG-------GGAAMPEAVAERLKELTGL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 413 HVLQGYGLTESCAGTFVSLPD--ELGMLGTvgpPVPNVDIR------LESVPEMEydalastaRGEICIRGKTLFSGYYK 484
Cdd:PRK08314 332 DYVEGYGLTETMAQTHSNPPDrpKLQCLGI---PTFGVDARvidpetLEELPPGE--------VGEIVVHGPQVFKGYWN 400
|
490 500 510
....*....|....*....|....*....|....*....
gi 15236634 485 REDLTKEVLI--DG--WLHTGDVGEWQPDGSMKIIDRKK 519
Cdd:PRK08314 401 RPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLK 439
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
43-538 |
1.49e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.42 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 43 GMDSCWDVFRMSVEKYPNnpmlgRREIVDGKPGKYvwqTYQEVYDIVMKLGNSLRSVGVK--DeakcgIYGANSPEW--- 117
Cdd:PRK06087 21 GDASLADYWQQTARAMPD-----KIAVVDNHGASY---TYSALDHAASRLANWLLAKGIEpgD-----RVAFQLPGWcef 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 118 -IISMeACNAHGLYCVPLYDTLGADAVEFII--SHSEVSIVFVEEKKIS--ELFKTCPNSTEYMKTVVsfgGVSREQKEE 192
Cdd:PRK06087 88 tIIYL-ACLKVGAVSVPLLPSWREAELVWVLnkCQAKMFFAPTLFKQTRpvDLILPLQNQLPQLQQIV---GVDKLAPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 193 AETfglviyAWDEFLKLGEGKQYDLPIKKkSDICTIMYTSGTTGDPKGVMISNESIvtlIAGVIRLLKSANeaLTVKDVY 272
Cdd:PRK06087 164 SSL------SLSQIIADYEPLTTAITTHG-DELAAVLFTSGTEGLPKGVMLTHNNI---LASERAYCARLN--LTWQDVF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 273 LSYLPLAHifdrviEECFIqHGAAIGFWRGDVKLLIEDLaelKPTifcAVPRVLDRvysglQK-KLSDGGflKKFIFDSA 351
Cdd:PRK06087 232 MMPAPLGH------ATGFL-HGVTAPFLIGARSVLLDIF---TPD---ACLALLEQ-----QRcTCMLGA--TPFIYDLL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 352 FSYKfgymkkgQSHVEASPLfdklvfskvkqglggnvRIILSGAAPLAShvesflRVVACCH-----VLQGYGLTESCAG 426
Cdd:PRK06087 292 NLLE-------KQPADLSAL-----------------RFFLCGGTTIPK------KVARECQqrgikLLSVYGSTESSPH 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 427 TFVSLPDELG-MLGTVGPPVPNVDIRlesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVG 504
Cdd:PRK06087 342 AVVNLDDPLSrFMHTDGYAAAGVEIK---VVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLC 418
|
490 500 510
....*....|....*....|....*....|....
gi 15236634 505 EWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
Cdd:PRK06087 419 RMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
224-552 |
1.54e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 89.34 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHifdrvieecfiQHGAAIGFwrgd 303
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG-----LGADDVILMASPMAH-----------QTGFMYGL---- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 304 vklliedlaeLKPTIFCAVPrVLDRVYSGLQkklsdggfLKKFIFDSAFSYKFGymkkgqshveASPLFDKLVfsKVKQG 383
Cdd:PRK13295 258 ----------MMPVMLGATA-VLQDIWDPAR--------AAELIRTEGVTFTMA----------STPFLTDLT--RAVKE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 384 LGGNV---RIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTV-GPPVPNVDIRlesVPEME 459
Cdd:PRK13295 307 SGRPVsslRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTdGCPLPGVEVR---VVDAD 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 460 YDALASTARGEICIRGKTLFSGYYKREDLTKeVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIY 539
Cdd:PRK13295 384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALL 461
|
330
....*....|...
gi 15236634 540 GEVQAVDSVWVYG 552
Cdd:PRK13295 462 YRHPAIAQVAIVA 474
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
81-565 |
2.04e-18 |
|
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: 88.14 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYCvPLYDTLGADAVEFIISHSEVSIVfvee 159
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAIlKAGAAYV-PLDAKLPSARIQAILRTSGATLL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiseLFKTCPNSTEYmktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksdictIMYTSGTTGDPK 239
Cdd:cd17653 99 -----LTTDSPDDLAY----------------------------------------------------IIFTSGSTGIPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIagvirLLKSANEALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFwRGDVKLLIEDLAELkpT 317
Cdd:cd17653 122 GVMVPHRGVLNYV-----SQPPARLDVGPGSRVAQVLSIA--FDACIGEIFstLCNGGTLVL-ADPSDPFAHVARTV--D 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 318 IFCAVPRVLdrvysglqkklsdggflkkfifdsafsykfgymkkgqSHVEASPlfdklvFSKVKqglggnvRIILSGAAP 397
Cdd:cd17653 192 ALMSTPSIL-------------------------------------STLSPQD------FPNLK-------TIFLGGEAV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 398 LASHVESFLRVVAcchVLQGYGLTE-SCAGTFVSLpdELGMLGTVGPPVPNVDIRL-----ESVPEMEydalastaRGEI 471
Cdd:cd17653 222 PPSLLDRWSPGRR---LYNAYGPTEcTISSTMTEL--LPGQPVTIGKPIPNSTCYIldadlQPVPEGV--------VGEI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 472 CIRGKTLFSGYYKREDLTKEVLI-----DGWLH--TGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENI----YG 540
Cdd:cd17653 289 CISGVQVARGYLGNPALTASKFVpdpfwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVvlqsQP 367
|
490 500
....*....|....*....|....*
gi 15236634 541 EVQAVDSVWVYGNsfesfLIAIANP 565
Cdd:cd17653 368 EVTQAAAIVVNGR-----LVAFVTP 387
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
224-643 |
2.06e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.09 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVtliagVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFW-RG 302
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALI-----VQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLpKF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 DVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFlkkfifdsafsykfgymkkgqshveasplfdklvfskvkq 382
Cdd:PLN02860 248 DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVF---------------------------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 383 glgGNVRIILSGAAPLASH-VESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELGML--------------------GT 440
Cdd:PLN02860 288 ---PSVRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEACSSlTFMTLHDPTLESpkqtlqtvnqtksssvhqpqGV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 441 -VGPPVPNVDIRLeSVPEmeydalaSTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRK 518
Cdd:PLN02860 365 cVGKPAPHVELKI-GLDE-------SSRVGRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKAGNLWLIGRS 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 519 KNIFKlSQGEYVAVENIENIYGEVQAVDSVWVYGNSfESFLIAIANPNQHILERWAAEngvsgdyDALCQNEKaKEFILG 598
Cdd:PLN02860 437 NDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGVP-DSRLTEMVVACVRLRDGWIWS-------DNEKENAK-KNLTLS 506
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15236634 599 E--LVKMAKEKKMKGFEIIKAIHLDPVPFDmerdlLTPTFKKKRPQL 643
Cdd:PLN02860 507 SetLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
79-536 |
2.97e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 88.33 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 79 WqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVfve 158
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 159 ekkiselfktcpnsteymktvvsfggVSREQKEEAETFGLviyAWDEFLKLGEGKQYDL-PIKKKSDICTIMYTSGTTGD 237
Cdd:PRK09088 99 --------------------------LGDDAVAAGRTDVE---DLAAFIASADALEPADtPSIPPERVSLILFTSGTSGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 238 PKGVMISNESIVTLIAGVIRLLKSANEAltvkdVYLSYLPLAHIFDRVIE-ECFIQHGAAI----GF-------WRGDVK 305
Cdd:PRK09088 150 PKGVMLSERNLQQTAHNFGVLGRVDAHS-----SFLCDAPMFHIIGLITSvRPVLAVGGSIlvsnGFepkrtlgRLGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 306 LLIedlaelkpTIFCAVPRVLDRVysglqkklsdggflkkfifdsafsykfgymkkgqshvEASPLFDKLVFskvkqglg 385
Cdd:PRK09088 225 LGI--------THYFCVPQMAQAF-------------------------------------RAQPGFDAAAL-------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 386 GNVRIILSGAAPlasHVESFLR--VVACCHVLQGYGLTEscAGTFVSLPDELGM----LGTVGPPVPNVDIRLesVPEME 459
Cdd:PRK09088 252 RHLTALFTGGAP---HAAEDILgwLDDGIPMVDGFGMSE--AGTVFGMSVDCDVirakAGAAGIPTPTVQTRV--VDDQG 324
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236634 460 YDALASTArGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIE 536
Cdd:PRK09088 325 NDCPAGVP-GELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
81-538 |
1.25e-17 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 86.27 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFglviyawDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
Cdd:PRK08008 119 -FYPMYRQIQQEDATPLRHICLTRVALPADDGVSSF-------TQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIvtLIAGvirLLKSANEALTVKDVYLSYLPLAHIfdrvieECfiQHGAAIG-FWRGDVKLLIE---------D 310
Cdd:PRK08008 191 VVITHYNL--RFAG---YYSAWQCALRDDDVYLTVMPAFHI------DC--QCTAAMAaFSAGATFVLLEkysarafwgQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 311 LAELKPTIFCAVPRVLDRVYsgLQKKLSD--GGFLKKFIF--------DSAFSYKFGymkkgqshveasplfdklvfskv 380
Cdd:PRK08008 258 VCKYRATITECIPMMIRTLM--VQPPSANdrQHCLREVMFylnlsdqeKDAFEERFG----------------------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 381 kqglggnVRIILSgaaplashvesflrvvacchvlqgYGLTESCAGTFVSLPDELGMLGTVGPP--VPNVDIRLEsvpem 458
Cdd:PRK08008 313 -------VRLLTS------------------------YGMTETIVGIIGDRPGDKRRWPSIGRPgfCYEAEIRDD----- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 459 EYDALASTARGEICIRG---KTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVEN 534
Cdd:PRK08008 357 HNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVE 435
|
....
gi 15236634 535 IENI 538
Cdd:PRK08008 436 LENI 439
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
65-624 |
1.54e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 86.44 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 65 GRREIVDGkPGKYVW-QTYQEVYDIVMKLGNslRSVGVKDEAkcGIYGANSP---EWIISMEACNAHgLYCVPLydTLGA 140
Cdd:PLN02479 35 TRKSVVHG-SVRYTWaQTYQRCRRLASALAK--RSIGPGSTV--AVIAPNIPamyEAHFGVPMAGAV-VNCVNI--RLNA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 141 DAVEFIISHSEVSIVFVEEK---KISELFKTCPNSTEY---MKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQ 214
Cdd:PLN02479 107 PTIAFLLEHSKSEVVMVDQEfftLAEEALKILAEKKKSsfkPPLLIVIGDPTCDPKSLQYALGKGAIEYEKFLETGDPEF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 215 YDLPIKKKSDICTIMYTSGTTGDPKGVMISNESiVTLIAGVIRLLKSANEALtvkdVYLSYLPLAHIFDRvieeCFIQHG 294
Cdd:PLN02479 187 AWKPPADEWQSIALGYTSGTTASPKGVVLHHRG-AYLMALSNALIWGMNEGA----VYLWTLPMFHCNGW----CFTWTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 295 AA-----IGFWRGDVKLLIEDLAELKPTIFCAVPRVLDRVysglqkklsdggflkkfifdsafsykfgymkkgqshVEAS 369
Cdd:PLN02479 258 AAlcgtnICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTI------------------------------------VNAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 370 PLFDKLVFSKVkqglggnVRIILSGAAP----LASHVESFLRVVACCHVLQGYGLTESCA--GTFVSLPDE--------- 434
Cdd:PLN02479 302 KSETILPLPRV-------VHVMTAGAAPppsvLFAMSEKGFRVTHTYGLSETYGPSTVCAwkPEWDSLPPEeqarlnarq 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 435 ----LGM--LGTVGP----PVPnvdirlesvpemeydALASTArGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVG 504
Cdd:PLN02479 375 gvryIGLegLDVVDTktmkPVP---------------ADGKTM-GEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 505 EWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIygevqavdsVWVYGNSFESFLIAIANpnqhilERW----------- 573
Cdd:PLN02479 439 VKHPDGYIEIKDRSKDII-ISGGENISSLEVENV---------VYTHPAVLEASVVARPD------ERWgespcafvtlk 502
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236634 574 -----AAENGVSGDYDALCQNEK-----AKEFILGELVKMAKEKKMKGFEIIKAIHLDPVP 624
Cdd:PLN02479 503 pgvdkSDEAALAEDIMKFCRERLpaywvPKSVVFGPLPKTATGKIQKHVLRAKAKEMGPVK 563
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
228-552 |
2.87e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 83.47 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFDRVIEECFIQHGAA-IGFWRGDVKL 306
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMG-----LTEADVYLNMLPLFHIAGLNLALATFHAGGAnVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 307 LIEDLAELKPTIFCAVPRVLDRvysglqkklsdggflkkfIFDSAfsykfgymkkGQSHVEASPLfdklvfskvkqglgg 386
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSN------------------LLDAA----------EKSGVDLSSL--------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 387 nvRIILSGAAPlaSHVESFLRVVACChVLQGYGLTESCAgtFVSLPDELGMLGTVGPPVPNVDIRLesVPEMEYDALAST 466
Cdd:cd17637 117 --RHVLGLDAP--ETIQRFEETTGAT-FWSLYGQTETSG--LVTLSPYRERPGSAGRPGPLVRVRI--VDDNDRPVPAGE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 467 ArGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRK--KNIFKlSQGEYVAVENIENIYGEVQA 544
Cdd:cd17637 188 T-GEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPA 265
|
....*...
gi 15236634 545 VDSVWVYG 552
Cdd:cd17637 266 IAEVCVIG 273
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
81-545 |
5.60e-17 |
|
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: 83.67 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEk 160
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkkSDICTIMYTSGTTGDPKG 240
Cdd:cd05919 91 --------------------------------------------------------------DDIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTliagVIRLLKSANEALTVKDVYLSylpLAHIF------DRVIEECFIQHGAAIGFWRGDVKLLIEDLAEL 314
Cdd:cd05919 109 VMHAHRDPLL----FADAMAREALGLTPGDRVFS---SAKMFfgyglgNSLWFPLAVGASAVLNPGWPTAERVLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 315 KPTIFCAVPRVLDRVYsglqkklsdggflkkfifdsafsykfgymkkgqshveASPLFDKLVFSkvkqglggNVRIILSG 394
Cdd:cd05919 182 RPTVLYGVPTFYANLL-------------------------------------DSCAGSPDALR--------SLRLCVSA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 395 AAPLASHVESFLRVVACCHVLQGYGLTEScAGTFVS-LPDELgMLGTVGPPVPNVDIRLesVPEMEYDALASTArGEICI 473
Cdd:cd05919 217 GEALPRGLGERWMEHFGGPILDGIGATEV-GHIFLSnRPGAW-RLGSTGRPVPGYEIRL--VDEEGHTIPPGEE-GDLLV 291
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236634 474 RGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAV 545
Cdd:cd05919 292 RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAV 362
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
65-538 |
6.95e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 84.03 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 65 GRREIVDGK-PGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAV 143
Cdd:PRK06018 24 GNREVVTRSvEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 144 EFIISHSEVSIVFVEEKKISELFKTCPNsTEYMKTVVSFGGvsREQKEEAETFGLViyAWDEFLKLGEG----KQYDlpi 219
Cdd:PRK06018 104 AWIINHAEDRVVITDLTFVPILEKIADK-LPSVERYVVLTD--AAHMPQTTLKNAV--AYEEWIAEADGdfawKTFD--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 220 kkKSDICTIMYTSGTTGDPKGVMISNESIV--TLIAGVIRLLksaneALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAI 297
Cdd:PRK06018 176 --ENTAAGMCYTSGTTGDPKGVLYSHRSNVlhALMANNGDAL-----GTSAADTMLPVVPLFHANSWGIAFSAPSMGTKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 298 GF--WRGDVKLLIEDLAELKPTIFCAVPRVLDRVysgLQkklsdggflkkfifdsafsykfgYMKKgqshveasplfDKL 375
Cdd:PRK06018 249 VMpgAKLDGASVYELLDTEKVTFTAGVPTVWLML---LQ-----------------------YMEK-----------EGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 376 VFSKVKqglggnvRIILSGAAPLASHVESFLRVvaCCHVLQGYGLTE-SCAGTFVSLPDE---------LGMLGTVGPPV 445
Cdd:PRK06018 292 KLPHLK-------MVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEmSPLGTLAALKPPfsklpgdarLDVLQKQGYPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 446 PNVDIRL-----ESVPemeYDALAStarGEICIRGKTLFSGYYKREDltkEVL-IDGWLHTGDVGEWQPDGSMKIIDRKK 519
Cdd:PRK06018 363 FGVEMKItddagKELP---WDGKTF---GRLKVRGPAVAAAYYRVDG---EILdDDGFFDTGDVATIDAYGYMRITDRSK 433
|
490
....*....|....*....
gi 15236634 520 NIFKlSQGEYVAVENIENI 538
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENL 451
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
81-517 |
1.36e-16 |
|
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: 83.02 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYcVPLYDTLGADAVEFIISHSEVSIVFVEE 159
Cdd:cd12117 24 TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVlKAGAAY-VPLDPELPAERLAFMLADAGAKVLLTDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 KkiselfktcpnsteymktvvsfggvSREQKEEAETFGLVIYAWDEflklgEGKQYDLPIKKKSDICTIMYTSGTTGDPK 239
Cdd:cd12117 103 S-------------------------LAGRAGGLEVAVVIDEALDA-----GPAGNPAVPVSPDDLAYVMYTSGSTGRPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNesivtliAGVIRLLKSANEA-LTVKDVYLSYLPLAhiFDrvieecfiqhGAAIGFWrgdVKLLieDLAELkpti 318
Cdd:cd12117 153 GVAVTH-------RGVVRLVKNTNYVtLGPDDRVLQTSPLA--FD----------ASTFEIW---GALL--NGARL---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 319 fcavpRVLDRvysglqKKLSDGGFLKKFIfdsafsykfgymkkGQSHVEA----SPLFDKLVfSKVKQGLGGnVRIILSG 394
Cdd:cd12117 205 -----VLAPK------GTLLDPDALGALI--------------AEEGVTVlwltAALFNQLA-DEDPECFAG-LRELLTG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 395 --AAPlASHVESFLRVVACCHVLQGYGLTES--CAGTFVSLPDELGMlGTV--GPPVPN-----VDIRLESVPEmeydal 463
Cdd:cd12117 258 geVVS-PPHVRRVLAACPGLRLVNGYGPTENttFTTSHVVTELDEVA-GSIpiGRPIANtrvyvLDEDGRPVPP------ 329
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236634 464 asTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWL------HTGDVGEWQPDGSMKIIDR 517
Cdd:cd12117 330 --GVPGELYVGGDGLALGYLNRPALTAERFVaDPFGpgerlyRTGDLARWLPDGRLEFLGR 388
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
70-522 |
1.69e-16 |
|
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: 83.06 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 70 VDGKPGKYVWQTYQEVYDIVMKLGNSLRSVGvkdeaKCG----IYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVE- 144
Cdd:cd05931 15 LDDEGGREETLTYAELDRRARAIAARLQAVG-----KPGdrvlLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAEr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 145 --FIISHSEVSIVFveekkiselfktcpnsteymkTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKK 222
Cdd:cd05931 90 laAILADAGPRVVL---------------------TTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIFdrvieecfiqhgAAIGFwrg 302
Cdd:cd05931 149 DDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG-----LDPGDVVVSWLPLYHDM------------GLIGG--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 dvkLLIedlaelkpTIFCAVPRVLdrvysglqkkLSDGGFLKKfifdsafsyKFGYMK---KGQSHVEASPLF--DkLVF 377
Cdd:cd05931 209 ---LLT--------PLYSGGPSVL----------MSPAAFLRR---------PLRWLRlisRYRATISAAPNFayD-LCV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SKVK-QGLGG----NVRIILSGAAPL-ASHVESFLRVVACC----HVLQ-GYGLTESCagTFVSL-------------PD 433
Cdd:cd05931 258 RRVRdEDLEGldlsSWRVALNGAEPVrPATLRRFAEAFAPFgfrpEAFRpSYGLAEAT--LFVSGgppgtgpvvlrvdRD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 434 ELGMLGTV--------------GPPVPNVDIRLesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLI----- 494
Cdd:cd05931 336 ALAGRAVAvaaddpaarelvscGRPLPDQEVRI--VDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaat 413
|
490 500 510
....*....|....*....|....*....|....*..
gi 15236634 495 --DGWLHTGDVG-----EWQPDGSMK--IIDRKKNIF 522
Cdd:cd05931 414 deGGWLRTGDLGflhdgELYITGRLKdlIIVRGRNHY 450
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
81-552 |
1.91e-16 |
|
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: 82.52 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:TIGR03098 27 TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFKTCPnSTEYMKTVVSFGGVSREQKEEAetfGLVIYAWDEFLKLGEgkQYDLPIKKKSDICTIMYTSGTTGDPKG 240
Cdd:TIGR03098 107 RLDLLHPALP-GCHDLRTLIIVGDPAHASEGHP---GEEPASWPKLLALGD--ADPPHPVIDSDMAAILYTSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAhiFDRVIEE---CFIQHGAAIGFWRGDVKLLIEDLAELKPT 317
Cdd:TIGR03098 181 VVLSHRNLVAGAQSVATYLE-----NRPDDRLLAVLPLS--FDYGFNQlttAFYVGATVVLHDYLLPRDVLKALEKHGIT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 318 IFCAVPRVLDRVYSgLQKKLSDGGFLkKFIFDSafsykfgymkkgqshveasplfdklvfskvkqglGGNV-RIILSGAA 396
Cdd:TIGR03098 254 GLAAVPPLWAQLAQ-LDWPESAAPSL-RYLTNS----------------------------------GGAMpRATLSRLR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 397 PLASHVESFLRvvacchvlqgYGLTESCAGTFVSlPDELGML-GTVGPPVPNVDIrleSVPEMEYDALASTARGEICIRG 475
Cdd:TIGR03098 298 SFLPNARLFLM----------YGLTEAFRSTYLP-PEEVDRRpDSIGKAIPNAEV---LVLREDGSECAPGEEGELVHRG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 476 KTLFSGYYKREDLTKEVL-----IDGWLH-------TGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQ 543
Cdd:TIGR03098 364 ALVAMGYWNDPEKTAERFrplppFPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATG 442
|
....*....
gi 15236634 544 AVDSVWVYG 552
Cdd:TIGR03098 443 LVAEAVAFG 451
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
81-519 |
3.97e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 81.46 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELFK-TCPNSTEYMKTVVSFGGVS--REQKEEAETFGLVIYAWDeflklgegkqydlpikkksDICTIMYTSGTTGD 237
Cdd:PRK07514 110 NFAWLSKiAAAAGAPHVETLDADGTGSllEAAAAAPDDFETVPRGAD-------------------DLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 238 PKGVMISNESivtliagvirlLKSANEAL------TVKDVYLSYLPLAH---IFdrVIEECFIQHGAAIgFW--RGDVKL 306
Cdd:PRK07514 171 SKGAMLSHGN-----------LLSNALTLvdywrfTPDDVLIHALPIFHthgLF--VATNVALLAGASM-IFlpKFDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 307 LIEDLAelKPTIFCAVP----RVLdrvysglqkklsdggflkkfifdsafsykfgymkkgqshveASPLFDKlvfskvkq 382
Cdd:PRK07514 237 VLALMP--RATVMMGVPtfytRLL-----------------------------------------QEPRLTR-------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 383 GLGGNVRIILSGAAPL--ASHVESFLRVvacCH-VLQGYGLTESCAGTfvSLP---DELGmlGTVGPPVPNVDIRLesvp 456
Cdd:PRK07514 266 EAAAHMRLFISGSAPLlaETHREFQERT---GHaILERYGMTETNMNT--SNPydgERRA--GTVGFPLPGVSLRV---- 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15236634 457 eMEYDALASTARGEIC---IRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPDGSMKIIDRKK 519
Cdd:PRK07514 335 -TDPETGAELPPGEIGmieVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
81-536 |
3.97e-16 |
|
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: 81.65 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kISELFKTCPNSTEYMK-TVVSFGGvsreqkeEAETFGLVIYAwdEFLKLGEGkqyDLPIKKKS--DICTIMYTSGTTGD 237
Cdd:cd05959 111 -LAPVLAAALTKSEHTLvVLIVSGG-------AGPEAGALLLA--ELVAAEAE---QLKPAATHadDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 238 PKGVMISNESI-VTLIAGVIRLLKsaneaLTVKDVYLSYLPLahifdrvieecFIQHGAAIG----FWRGDVKLLI---- 308
Cdd:cd05959 178 PKGVVHLHADIyWTAELYARNVLG-----IREDDVCFSAAKL-----------FFAYGLGNSltfpLSVGATTVLMperp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 309 ------EDLAELKPTIFCAVPRVldrvYSGLQKklSDGgfLKKFIFDSafsykfgymkkgqshveasplfdklvfskvkq 382
Cdd:cd05959 242 tpaavfKRIRRYRPTVFFGVPTL----YAAMLA--APN--LPSRDLSS-------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 383 glggnVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAgTFVS-LPDELgMLGTVGPPVPNVDIRLesVPEMEYD 461
Cdd:cd05959 282 -----LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLH-IFLSnRPGRV-RYGTTGKPVPGYEVEL--RDEDGGD 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236634 462 ALASTArGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIE 536
Cdd:cd05959 353 VADGEP-GELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVE 425
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
81-552 |
6.78e-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: 81.02 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEek 160
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcpnsteymktvvsfggVSREQKEEAETFGLVIYAWDEFLKLGE----GKQYDLPIKKKSDICTIMYTSGTTG 236
Cdd:cd05923 108 ------------------------VDAQVMDAIFQSGVRVLALSDLVGLGEpesaGPLIEDPPREPEQPAFVFYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 237 DPKGVMISN---ESIVTLIAGVIRLLKSANEaltvkdVYLSYLPLAHI--FDRVIEECFIQHGAAI---GFWRGDVKLLI 308
Cdd:cd05923 164 LPKGAVIPQraaESRVLFMSTQAGLRHGRHN------VVLGLMPLYHVigFFAVLVAALALDGTYVvveEFDPADALKLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 309 EdlaELKPTIFCAVPRVLDRVYSglqkklsdggflkkfifdsafsykfgymkkgqsHVEASPL----FDKLVFSkvkqgl 384
Cdd:cd05923 238 E---QERVTSLFATPTHLDALAA---------------------------------AAEFAGLklssLRHVTFA------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 385 ggnvriilsGAA---PLASHVESFLRVVACCHvlqgYGLTESCAGTFVSLPDElgmlGTVGPPVPNVDIRLESVPEMEYD 461
Cdd:cd05923 276 ---------GATmpdAVLERVNQHLPGEKVNI----YGTTEAMNSLYMRDART----GTEMRPGFFSEVRIVRIGGSPDE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 462 ALASTARGEICIR--GKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIY 539
Cdd:cd05923 339 ALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVL 417
|
490
....*....|...
gi 15236634 540 GEVQAVDSVWVYG 552
Cdd:cd05923 418 SRHPGVTEVVVIG 430
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-537 |
7.44e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 80.56 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 119 ISMEACnAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPnsteymktvvsfggVSREQKEEAETFGL 198
Cdd:cd05922 38 VAYAGG-RLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALP--------------ASPDPGTVLDADGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 199 ViyawdeflklGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPL 278
Cdd:cd05922 103 R----------AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG-----ITADDRALTVLPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 279 AHIFD-RVIEECFIQHGAAIGFWRGDV-KLLIEDLAELKPTIFCAVPrvldrvysglqkklSDGGFLKKFIFDSAfsykf 356
Cdd:cd05922 168 SYDYGlSVLNTHLLRGATLVLTNDGVLdDAFWEDLREHGATGLAGVP--------------STYAMLTRLGFDPA----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 357 gymkkgqshveASPlfdklvfskvkqglggNVRIILSGAAPLAShvesfLRVVACCHVLQG------YGLTESCAGTFVS 430
Cdd:cd05922 229 -----------KLP----------------SLRYLTQAGGRLPQ-----ETIARLRELLPGaqvyvmYGQTEATRRMTYL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 431 LPDELG-MLGTVGPPVPNVDIRLESVPEMEYdalASTARGEICIRGKTLFSGYYKRE-DLTKEVLIDGWLHTGDVGEWQP 508
Cdd:cd05922 277 PPERILeKPGSIGLAIPGGEFEILDDDGTPT---PPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDE 353
|
410 420
....*....|....*....|....*....
gi 15236634 509 DGSMKIIDRKKNIFKLSqGEYVAVENIEN 537
Cdd:cd05922 354 DGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
220-547 |
1.90e-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: 79.45 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAHifdrvieecfiqhgaaigf 299
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-----EWKTKDRILSWMPLTH------------------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 wrgDVKLLIEDLAELkptifcavprvldrvYSGLQKKLSDGG-FLKKFIFdsafsykfgYMKKGQSH---VEASPLFD-K 374
Cdd:cd05908 159 ---DMGLIAFHLAPL---------------IAGMNQYLMPTRlFIRRPIL---------WLKKASEHkatIVSSPNFGyK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 375 LVFSKVKQGLGGN-----VRIILSGAAPLASHV-ESFLRVVACCH-----VLQGYGLTESCAGtfVSLPD---------- 433
Cdd:cd05908 212 YFLKTLKPEKANDwdlssIRMILNGAEPIDYELcHEFLDHMSKYGlkrnaILPVYGLAEASVG--ASLPKaqspfktitl 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 434 -------------------ELGMLGTVGPPVPNVDIRlesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLI 494
Cdd:cd05908 290 grrhvthgepepevdkkdsECLTFVEVGKPIDETDIR---ICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFT 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15236634 495 -DGWLHTGDVGeWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDS 547
Cdd:cd05908 367 dDGWLKTGDLG-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGVEL 418
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
80-552 |
2.49e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 79.44 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 80 QTYQEVYDIVMKLGNSLR-SVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVE 158
Cdd:PRK05620 39 TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 159 E---KKISELFKTCPNsteyMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKlGEGKQYDLPIKKKSDICTIMYTSGTT 235
Cdd:PRK05620 119 PrlaEQLGEILKECPC----VRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVYDWPELDETTAAAICYSTGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 236 GDPKGVMISNESivtLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVkllieDLAELK 315
Cdd:PRK05620 194 GAPKGVVYSHRS---LYLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDL-----SAPTLA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 316 PTIFCAVPRVLDRVYSglqkklsdggflkkfIFDSAFSYkfgYMKKgqsHVEASPLfdklvfskvkqglggnvRIILSGA 395
Cdd:PRK05620 266 KIIATAMPRVAHGVPT---------------LWIQLMVH---YLKN---PPERMSL-----------------QEIYVGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 396 APLASHV-----ESF-LRVVACchvlqgYGLTESCAGTFVSLPDElgmlGTVGPPVPNVDIRLESVP-EMEY------DA 462
Cdd:PRK05620 308 SAVPPILikaweERYgVDVVHV------WGMTETSPVGTVARPPS----GVSGEARWAYRVSQGRFPaSLEYrivndgQV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 463 LASTAR--GEICIRGKTLFSGYYKR-----------------EDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFK 523
Cdd:PRK05620 378 MESTDRneGEIQVRGNWVTASYYHSpteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR 457
|
490 500
....*....|....*....|....*....
gi 15236634 524 lSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK05620 458 -SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
113-552 |
4.31e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 78.57 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 113 NSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPNsteymktvVSFGGVSREqkee 192
Cdd:PRK07867 63 NTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPG--------VRVINVDSP---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 193 aetfglviyAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVtlIAGVirlLKSANEALTVKDV- 271
Cdd:PRK07867 131 ---------AWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGV---MLAQRFGLGPDDVc 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 272 YLSyLPLahifdrvieecFiqHGAAIgfwrgdvklliedLAELKPTIFCAVPRVLDRvysglqkKLSDGGFL---KKFif 348
Cdd:PRK07867 197 YVS-MPL-----------F--HSNAV-------------MAGWAVALAAGASIALRR-------KFSASGFLpdvRRY-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 349 dsAFSYkFGYMKKGQSHVEASP---------LfdKLVFskvkqglgGNvriilSGAAPlasHVESFLRVVACcHVLQGYG 419
Cdd:PRK07867 241 --GATY-ANYVGKPLSYVLATPerpddadnpL--RIVY--------GN-----EGAPG---DIARFARRFGC-VVVDGFG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 420 LTESCAGtFVSLPDelGMLGTVGPPVPNVDIR----LESVPEMEYDAL----ASTARGEIC-IRGKTLFSGYYKREDLTK 490
Cdd:PRK07867 299 STEGGVA-ITRTPD--TPPGALGPLPPGVAIVdpdtGTECPPAEDADGrllnADEAIGELVnTAGPGGFEGYYNDPEADA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236634 491 EVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK07867 376 ERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD-GENLGTAPIERILLRYPDATEVAVYA 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-521 |
4.71e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 77.14 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSanealTVKDVYLSYLPLAHIFDRVIEECFIQH-GAAIGF-- 299
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLF-----DPDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 ---WRGdvKLLIEDLAEL----KPTIFCAVPRVldrvYSGLQKKLSDGGFlkkfifdsafsykfgymkkgqshveasplf 372
Cdd:cd05944 77 pagYRN--PGLFDNFWKLveryRITSLSTVPTV----YAALLQVPVNADI------------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 373 dklvfskvkqglgGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIR- 451
Cdd:cd05944 121 -------------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRi 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236634 452 --LESVPEMEYDALASTArGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNI 521
Cdd:cd05944 188 kvLDGVGRLLRDCAPDEV-GEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
418-577 |
7.87e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 77.77 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 418 YGLTES-CAGTFVS--LPDELGMLGT---VGPPVPNVDIRlesVPEMEYDALAST-ARGEICIRGKTLFSGYYKREDLTK 490
Cdd:PRK06178 360 WGMTEThTCDTFTAgfQDDDFDLLSQpvfVGLPVPGTEFK---ICDFETGELLPLgAEGEIVVRTPSLLKGYWNKPEATA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 491 EVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSVWVYGNSFE-------SF--LIA 561
Cdd:PRK06178 437 EALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAVLGSAVVGRPDPdkgqvpvAFvqLKP 515
|
170
....*....|....*.
gi 15236634 562 IANPNQHILERWAAEN 577
Cdd:PRK06178 516 GADLTAAALQAWCREN 531
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
81-525 |
3.08e-14 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 75.45 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEk 160
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkkSDICTIMYTSGTTGDPKG 240
Cdd:cd05972 81 --------------------------------------------------------------EDPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLI--AGVIRLLKSANEALTVKD------VYLSYL-PLAHifdrvieecfiqhGAAIGFWRG---DVKLLI 308
Cdd:cd05972 99 VLHTHSYPLGHIptAAYWLGLRPDDIHWNIADpgwakgAWSSFFgPWLL-------------GATVFVYEGprfDAERIL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 309 EDLAELKPTIFCAVPRVLDRvysgLQKKLSDggflkkfifdsafSYKFGYMKKGQSHVEasPLfDKLVFSKVKQGLGGNV 388
Cdd:cd05972 166 ELLERYGVTSFCGPPTAYRM----LIKQDLS-------------SYKFSHLRLVVSAGE--PL-NPEVIEWWRAATGLPI 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 389 RiilsgaaplashvesflrvvacchvlQGYGLTESCA--GTFVSLPDELGMLGTvgpPVPNVDIRL-----ESVPEMEyd 461
Cdd:cd05972 226 R--------------------------DGYGQTETGLtvGNFPDMPVKPGSMGR---PTPGYDVAIidddgRELPPGE-- 274
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 462 alastaRGEICIRGKT--LFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLS 525
Cdd:cd05972 275 ------EGDIAIKLPPpgLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
81-547 |
6.32e-14 |
|
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: 74.43 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYcVPLYDTLGADAVEFIISHSEVSIVFVEe 159
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVlKAGGAY-VPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiselfktcPNSTEYmktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksdictIMYTSGTTGDPK 239
Cdd:cd17650 92 ----------PEDLAY----------------------------------------------------VIYTSGTTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAG----------VIRLLKSANEALtvkDVYLSYLPLAHIFDRVIEECfiQHGAaigfwRGDVKLLIE 309
Cdd:cd17650 110 GVMVEHRNVAHAAHAwrreyeldsfPVRLLQMASFSF---DVFAGDFARSLLNGGTLVIC--PDEV-----KLDPAALYD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 310 DLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAfsykfgyMKKGQSHVEASPLFdklvfskvkqglGGNVR 389
Cdd:cd17650 180 LILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSD-------GCKAQDFKTLAARF------------GQGMR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 390 IILSgaaplashvesflrvvacchvlqgYGLTESC--AGTFVSLPDELGMLGTV--GPPVPN-----VDIRLESVPEMEY 460
Cdd:cd17650 241 IINS------------------------YGVTEATidSTYYEEGRDPLGDSANVpiGRPLPNtamyvLDERLQPQPVGVA 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 461 dalastarGEICIRGKTLFSGYYKREDLTKEVLIDGWL-------HTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVE 533
Cdd:cd17650 297 --------GELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
490
....*....|....
gi 15236634 534 NIENIYGEVQAVDS 547
Cdd:cd17650 368 EIESQLARHPAIDE 381
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
50-551 |
2.25e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 73.25 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 50 VFRMSVEKYPNNPMLgrreiVDGKpgkyVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
Cdd:PRK06155 26 MLARQAERYPDRPLL-----VFGG----TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 130 YCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELfKTCPNSTEYMKTVVSFGGVSReqkeeaetfglviYAWDEFLKL 209
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAAL-EAADPGDLPLPAVWLLDAPAS-------------VSVPAGWST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 210 GEGKQYDLPIK----KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAHIfdrV 285
Cdd:PRK06155 163 APLPPLDAPAPaaavQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLE-----IGADDVLYTTLPLFHT---N 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 286 IEECFIQ---HGA---------AIGFWrgdvklliEDLAELKPTIFcavprvldrvysglqkklsdggflkkfifdsafs 353
Cdd:PRK06155 235 ALNAFFQallAGAtyvleprfsASGFW--------PAVRRHGATVT---------------------------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 354 YKFGYMkkgQSHVEASPlfdklvfsKVKQGLGGNVRIILSGAAPLASHVESFLRV-VAcchVLQGYGLTESCAGTFVSLP 432
Cdd:PRK06155 273 YLLGAM---VSILLSQP--------ARESDRAHRVRVALGPGVPAALHAAFRERFgVD---LLDGYGSTETNFVIAVTHG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 433 DELGmlGTVGPPVPNVDIRlesVPEMEYDALASTARGEICIRGKTLF---SGYYKREDLTKEVLIDGWLHTGDVGEWQPD 509
Cdd:PRK06155 339 SQRP--GSMGRLAPGFEAR---VVDEHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTVEAWRNLWFHTGDRVVRDAD 413
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15236634 510 GSMKIIDRKKNIFKlSQGEYVAVENIENIYGEVQAVDSVWVY 551
Cdd:PRK06155 414 GWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVF 454
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
388-519 |
2.48e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 73.07 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 388 VRIILSGAAPLASHV-ESFLRVVACcHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVPE---MEYDAl 463
Cdd:PRK07529 335 LRYALCGAAPLPVEVfRRFEAATGV-RIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVILDDagrYLRDC- 412
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 464 ASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKK 519
Cdd:PRK07529 413 AVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
81-525 |
4.31e-13 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 72.14 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVS-IVFVEE 159
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKmIVAIAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 KKISELFK----TCPNSTEymktVVSFGGVSREqkeeaetfglviyAWDEFLKLGEGKQYDLP------IKKKSDICTIM 229
Cdd:cd05970 129 DNIPEEIEkaapECPSKPK----LVWVGDPVPE-------------GWIDFRKLIKNASPDFErptansYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 230 YTSGTTGDPKgvMISNE------SIVTliAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEecfiqhGAAI---GFW 300
Cdd:cd05970 192 FSSGTTGMPK--MVEHDftyplgHIVT--AKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIA------GAAVfvyDYD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 301 RGDVKLLIEDLAELKPTIFCAVPRVldrvYSGLQK-KLSDggflkkfifdsafsYKFGYMKKGqshVEASPLFDKLVFSK 379
Cdd:cd05970 262 KFDPKALLEKLSKYGVTTFCAPPTI----YRFLIReDLSR--------------YDLSSLRYC---TTAGEALNPEVFNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 380 VKQGLGGNVRiilsgaaplashvesflrvvacchvlQGYGLTEsCAGTFVSLPDELGMLGTVGPPVPNVDIRL-----ES 454
Cdd:cd05970 321 FKEKTGIKLM--------------------------EGFGQTE-TTLTIATFPWMEPKPGSMGKPAPGYEIDLidregRS 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 455 VPEMEydalastaRGEICIR---GKT--LFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLS 525
Cdd:cd05970 374 CEAGE--------EGEIVIRtskGKPvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
412-552 |
7.15e-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: 70.02 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 412 CHVLQGYGLTEscAGTFVSLPdELG--MLGTVGPPVPNVDIRL-----ESVPEMEYdalastarGEICIRGKTLFSGYYK 484
Cdd:cd17636 137 GRKPGGYGQTE--VMGLATFA-ALGggAIGGAGRPSPLVQVRIldedgREVPDGEV--------GEIVARGPTVMAGYWN 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 485 REDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKlsqgeyvavENIENIY-GEVQ-------AVDSVWVYG 552
Cdd:cd17636 206 RPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK---------SGAENIYpAEVErclrqhpAVADAAVIG 272
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
417-550 |
1.30e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 70.29 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 417 GYGLTES----CAGTFVSLPDelgmlgtVGPPVPNVDIRLESvpemeydalastarGEICIRGKTLFSGYY---KREDLT 489
Cdd:PRK09029 270 GYGLTEMastvCAKRADGLAG-------VGSPLPGREVKLVD--------------GEIWLRGASLALGYWrqgQLVPLV 328
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236634 490 KEvliDGWLHTGDVGEWQpDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWV 550
Cdd:PRK09029 329 ND---EGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
223-518 |
1.65e-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: 70.26 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEAltvkDVYLSYlplAHIFDRVIEECFI--QHGAAIgfw 300
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSES----RVLQFA---SYTFDVSILEIFTtlAAGGCL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 301 rgdvklliedlaelkptifCaVPRVLDRVySGLQkklsdgGFLKKFifdsafsykfgymkkGQSHVEASP----LFDKLV 376
Cdd:cd05918 176 -------------------C-IPSEEDRL-NDLA------GFINRL---------------RVTWAFLTPsvarLLDPED 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 FSKVKQglggnvrIILSGAAPLASHVESFLRVVaccHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPN----VDirl 452
Cdd:cd05918 214 VPSLRT-------LVLGGEALTQSDVDTWADRV---RLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAtcwvVD--- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 453 esvpEMEYDALAST-ARGEICIRGKTLFSGYYKREDLTKEVLIDG--WLH------------TGDVGEWQPDGSMKIIDR 517
Cdd:cd05918 281 ----PDNHDRLVPIgAVGELLIEGPILARGYLNDPEKTAAAFIEDpaWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGR 356
|
.
gi 15236634 518 K 518
Cdd:cd05918 357 K 357
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
81-545 |
3.04e-12 |
|
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: 69.39 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYcVPLYDTLGADAVEFIISHSEVSIVFvee 159
Cdd:cd17644 27 TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAIlKAGGAY-VPLDPNYPQERLTYILEDAQISVLL--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiselfkTCPNSTEYmktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksdictIMYTSGTTGDPK 239
Cdd:cd17644 103 --------TQPENLAY----------------------------------------------------VIYTSGSTGKPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECFIQhgaaigFWRGDVKLLIEDLAELKPTIF 319
Cdd:cd17644 123 GVMIEHQSLVNLSHGLIKEY-----GITSSDRVLQFASIA--FDVAAEEIYVT------LLSGATLVLRPEEMRSSLEDF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 320 CAVPRvldrvysglQKKLSdggflkkfIFDSAFSYKFGYMKKGQSHVEASPLFDKLVfskvkqglggnvriILSGAAPLA 399
Cdd:cd17644 190 VQYIQ---------QWQLT--------VLSLPPAYWHLLVLELLLSTIDLPSSLRLV--------------IVGGEAVQP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 400 SHVESFLRVVA-CCHVLQGYGLTESCAGTFVSLPDELGMLG----TVGPPVPNV-----DIRLESVPemeydalaSTARG 469
Cdd:cd17644 239 ELVRQWQKNVGnFIQLINVYGPTEATIAATVCRLTQLTERNitsvPIGRPIANTqvyilDENLQPVP--------VGVPG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 470 EICIRGKTLFSGYYKREDLTKEVLIDGWLH---------TGDVGEWQPDGSMKIIDR-----KKNIFKLSQGEYVAVENi 535
Cdd:cd17644 311 ELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGRidnqvKIRGFRIELGEIEAVLS- 389
|
490
....*....|
gi 15236634 536 ENIYGEVQAV 545
Cdd:cd17644 390 QHNDVKTAVV 399
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
82-545 |
3.69e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.27 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 82 YQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVE-FIISHSEVSIVFVEEK 160
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIErFCQITDPAAALVAPGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISElfKTCPNSTEYMKTV-VSFGGVSREQKEEAETfglviyawdEFLKLGEGKQYDLPIkkksdicTIMYTSGTTGDPK 239
Cdd:PRK05857 124 KMAS--SAVPEALHSIPVIaVDIAAVTRESEHSLDA---------ASLAGNADQGSEDPL-------AMIFTSGTTGEPK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTlIAGVIRllksaNEAL-----TVKDVYLSYLPLAHIFDRV-IEECFIQHGAAIGfwRGDVKL-LIEDLA 312
Cdd:PRK05857 186 AVLLANRTFFA-VPDILQ-----KEGLnwvtwVVGETTYSPLPATHIGGLWwILTCLMHGGLCVT--GGENTTsLLEILT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 313 ELKPTIFCAVPRVLDRVYSGLqkKLSDggflkkfifdsafsykfgymkkgqshVEASPLfdKLVFSKVKQGLGGNVRIIL 392
Cdd:PRK05857 258 TNAVATTCLVPTLLSKLVSEL--KSAN--------------------------ATVPSL--RLVGYGGSRAIAADVRFIE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 393 SGAAPLAshvesflrvvacchvlQGYGLTES-CagTFVSLPDELGML-----GTVGPPVPNVDIRLESV----PEMEyDA 462
Cdd:PRK05857 308 ATGVRTA----------------QVYGLSETgC--TALCLPTDDGSIvkieaGAVGRPYPGVDVYLAATdgigPTAP-GA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 463 LASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEV 542
Cdd:PRK05857 369 GPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIAEGV 447
|
...
gi 15236634 543 QAV 545
Cdd:PRK05857 448 SGV 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
81-517 |
9.70e-12 |
|
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: 67.75 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:cd17651 22 TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELfktcpnsteymkTVVSFGGVsreqkeeaetfglviyAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
Cdd:cd17651 102 LAGEL------------AVELVAVT----------------LLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLKSANEALTvkdvyLSYLPLAhiFDRVIEECF--IQHGAAIGF----WRGDVKLLIEDLAE- 313
Cdd:cd17651 154 VVMPHRSLANLVAWQARASSLGPGART-----LQFAGLG--FDVSVQEIFstLCAGATLVLppeeVRTDPPALAAWLDEq 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 314 -----LKPTIF----CAVPRVLDRVYSGLQKKLSDGgflkkfifdsafsykfgymkkgqshveasplfDKLVfskvkqgL 384
Cdd:cd17651 227 risrvFLPTVAlralAEHGRPLGVRLAALRYLLTGG--------------------------------EQLV-------L 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 385 GGNVRiilsgaAPLASHveSFLRVVacchvlQGYGLTES---CAGTFVSLPDELGMLGTVGPPVPNVDI-----RLESVP 456
Cdd:cd17651 268 TEDLR------EFCAGL--PGLRLH------NHYGPTEThvvTALSLPGDPAAWPAPPPIGRPIDNTRVyvldaALRPVP 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236634 457 EMEydalastaRGEICIRGKTLFSGYYKREDLTKEVLI-DGWL------HTGDVGEWQPDGSMKIIDR 517
Cdd:cd17651 334 PGV--------PGELYIGGAGLARGYLNRPELTAERFVpDPFVpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
224-532 |
1.51e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 67.60 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGV-----MISneSIVTLIAGVIRLLKSAnealtvKDVYLSYLPLAH------IFDRVIeecfiQ 292
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAVinthrMLC--ANQQMLAQTFPFLAEE------PPVLVDWLPWNHtfggnhNLGIVL-----Y 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 293 HGAAI----------GFWRgdvklLIEDLAELKPTIFCAVPRvldrvysglqkklsdgGF------LKKfifDSAFSYKF 356
Cdd:PRK08180 277 NGGTLyiddgkptpgGFDE-----TLRNLREISPTVYFNVPK----------------GWemlvpaLER---DAALRRRF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 357 gymkkgqshveasplfdklvFSKVkqglggnvRIILSGAAPLASHVESFLRVVACCHV------LQGYGLTESC-AGTFV 429
Cdd:PRK08180 333 --------------------FSRL--------KLLFYAGAALSQDVWDRLDRVAEATCgerirmMTGLGMTETApSATFT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 430 SLPDElgMLGTVGPPVPNVDIRLesVPemeydalaSTARGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEW-- 506
Cdd:PRK08180 385 TGPLS--RAGNIGLPAPGCEVKL--VP--------VGGKLEVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGDAVRFvd 452
|
330 340 350
....*....|....*....|....*....|....
gi 15236634 507 --QP------DGsmkiidRKKNIFKLSQGEYVAV 532
Cdd:PRK08180 453 paDPerglmfDG------RIAEDFKLSSGTWVSV 480
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
71-537 |
2.39e-11 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 66.30 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 71 DGKPGKYvwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHS 150
Cdd:cd05971 1 KGTPEKV---TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 151 EVSIVFVEEkkiselfktcpnsteymktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkKSDICTIMY 230
Cdd:cd05971 78 GASALVTDG--------------------------------------------------------------SDDPALIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 231 TSGTTGDPKGvmisnesivtliagvirllksaneALTVKDVYLSYLP---LAHIFDRVIEECFiqHGAAIGFWRGDVkll 307
Cdd:cd05971 96 TSGTTGPPKG------------------------ALHAHRVLLGHLPgvqFPFNLFPRDGDLY--WTPADWAWIGGL--- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 308 iedLAELKPTIFCAVPrVLDRVYSGLQKK-----LSDGGFLKKFIFDSAFSykfgYMKKgqshvEASPLFDKLVfskvkq 382
Cdd:cd05971 147 ---LDVLLPSLYFGVP-VLAHRMTKFDPKaaldlMSRYGVTTAFLPPTALK----MMRQ-----QGEQLKHAQV------ 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 383 glggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTE------SCAGTFVSLPdelgmlGTVGPPVPNVDIRLESVP 456
Cdd:cd05971 208 ----KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTEcnlvigNCSALFPIKP------GSMGKPIPGHRVAIVDDN 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 457 EMEydaLASTARGEICIR--GKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKlSQGEYVAVEN 534
Cdd:cd05971 278 GTP---LPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAE 353
|
...
gi 15236634 535 IEN 537
Cdd:cd05971 354 IEE 356
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
217-542 |
4.35e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.53 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 217 LPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVirllkSANEALTVKDVYLSYLPLAHIFdrvieecfiqhgaa 296
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQV-----AARIDFSPEDKVFNALPVFHSF-------------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 297 iGFWRGdvkLLIEDLAELK------PTIFCAVPRVldrVY-SGLQKKLSDGGFLKKFIfDSAFSYKFgymkkgqshveas 369
Cdd:PRK06814 848 -GLTGG---LVLPLLSGVKvflypsPLHYRIIPEL---IYdTNATILFGTDTFLNGYA-RYAHPYDF------------- 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 370 plfdklvFSkvkqglggnVRIILSGAAPLAS-----HVESF-LRVvacchvLQGYGLTESCAGTFVSLPdelgM---LGT 440
Cdd:PRK06814 907 -------RS---------LRYVFAGAEKVKEetrqtWMEKFgIRI------LEGYGVTETAPVIALNTP----MhnkAGT 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 441 VGPPVPNVDIRLESVPEMEydalastARGEICIRGKTLFSGYYKREDL-TKEVLIDGWLHTGDVGEWQPDGSMKIIDRKK 519
Cdd:PRK06814 961 VGRLLPGIEYRLEPVPGID-------EGGRLFVRGPNVMLGYLRAENPgVLEPPADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
330 340
....*....|....*....|...
gi 15236634 520 NIFKLSqGEYVAVENIENIYGEV 542
Cdd:PRK06814 1034 RFAKIA-GEMISLAAVEELAAEL 1055
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
81-569 |
7.01e-11 |
|
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: 64.80 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVfveek 160
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfglVIYAWDeflklgegkqydlpikkksDICTIMYTSGTTGDPKG 240
Cdd:cd17656 90 -LTQRHLKSKLSFNKSTILLEDPSISQEDTSNID----YINNSD-------------------DLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAgvirLLKSANEALTVKDVyLSYLPLAhiFDRVIEECF--IQHGAAIGFWRGDVKLLIEDLAELKPTi 318
Cdd:cd17656 146 VQLEHKNMVNLLH----FEREKTNINFSDKV-LQFATCS--FDVCYQEIFstLLSGGTLYIIREETKRDVEQLFDLVKR- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 319 fcavprvldrvySGLQKKLSDGGFLkKFIFdsafsykfgymkkgqSHVEASPLFdklvFSKVKQglggnvrIILSGAAPL 398
Cdd:cd17656 218 ------------HNIEVVFLPVAFL-KFIF---------------SEREFINRF----PTCVKH-------IITAGEQLV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 399 ASH--VESFLRvvACCHVLQGYGLTESCAGTF--VSLPDELGMLGTVGPPVPNVDIRLESvPEMEYDALASTarGEICIR 474
Cdd:cd17656 259 ITNefKEMLHE--HNVHLHNHYGPSETHVVTTytINPEAEIPELPPIGKPISNTWIYILD-QEQQLQPQGIV--GELYIS 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 475 GKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIE----NIYGEVQ 543
Cdd:cd17656 334 GASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEaqllNHPGVSE 412
|
490 500
....*....|....*....|....*..
gi 15236634 544 AVdsVWVYGNSF-ESFLIAIANPNQHI 569
Cdd:cd17656 413 AV--VLDKADDKgEKYLCAYFVMEQEL 437
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
49-536 |
8.44e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 64.91 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 49 DVFRMSVEKYPNNPML--GRREIvdgkpgkyvwqTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNA 126
Cdd:PRK07798 7 DLFEAVADAVPDRVALvcGDRRL-----------TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 127 HGLYCVPLYDTLGADAVEFIISHSEVSIVFVeEKKISELFKTCPNSTEYMKTVVSFGGVSreqkEEAETFGLVIYawDEF 206
Cdd:PRK07798 76 ARAVPVNVNYRYVEDELRYLLDDSDAVALVY-EREFAPRVAEVLPRLPKLRTLVVVEDGS----GNDLLPGAVDY--EDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 207 LKLGEGKQydLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSAnealTVKDVY-LSYLPLAHIFDRV 285
Cdd:PRK07798 149 LAAGSPER--DFGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGE----PIEDEEeLAKRAAAGPGMRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 286 IEECFIQHGAA-----IGFWRGDvKLLIEDLAELKPTifcAVPRVLDRVYSGLQkklsdggflkkFIFDSAFsykfgymk 360
Cdd:PRK07798 223 FPAPPLMHGAGqwaafAALFSGQ-TVVLLPDVRFDAD---EVWRTIEREKVNVI-----------TIVGDAM-------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 361 kgqshveASPLFDKLvfSKVKQGLGGNVRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSLPDelGMLG 439
Cdd:PRK07798 280 -------ARPLLDAL--EARGPYDLSSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAK--GAVH 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 440 TVGPPV---PNVDIRLESVPEMEYDalaSTARGEICIRGKtLFSGYYKREDLTKEVL--IDG--WLHTGDVGEWQPDGSM 512
Cdd:PRK07798 349 TGGPRFtigPRTVVLDEDGNPVEPG---SGEIGWIARRGH-IPLGYYKDPEKTAETFptIDGvrYAIPGDRARVEADGTI 424
|
490 500
....*....|....*....|....
gi 15236634 513 KIIDRKKNIFKlSQGEYVAVENIE 536
Cdd:PRK07798 425 TLLGRGSVCIN-TGGEKVFPEEVE 447
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
81-552 |
1.07e-10 |
|
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: 64.45 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEk 160
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kisELF-KTCPNsteymktvvsfggvsreqkeeaetfglviyawDEFLklgegkqydlpikkksdictIMYTSGTTGDPK 239
Cdd:cd05969 81 ---ELYeRTDPE--------------------------------DPTL--------------------LHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNEsivtliagvirllksanealtvkDVYLSYLPLAHIFDRVIEECFiQHGAAIGFWRGDVKLLIEDLAElkptif 319
Cdd:cd05969 106 GVLHVHD-----------------------AMIFYYFTGKYVLDLHPDDIY-WCTADPGWVTGTVYGIWAPWLN------ 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 320 cAVPRVLD-------RVYSGLQKklsdggfLKKFIFDSAFSYKFGYMKKGQSHVEASPLfdklvfskvkqglgGNVRIIL 392
Cdd:cd05969 156 -GVTNVVYegrfdaeSWYGIIER-------VKVTVWYTAPTAIRMLMKEGDELARKYDL--------------SSLRFIH 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 393 SGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDirlESVPEMEYDALASTARGEIC 472
Cdd:cd05969 214 SVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVK---AAVVDENGNELPPGTKGILA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 473 IRG--KTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSVWV 550
Cdd:cd05969 291 LKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGV 369
|
..
gi 15236634 551 YG 552
Cdd:cd05969 370 IG 371
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
81-523 |
1.33e-10 |
|
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: 64.03 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIY---GANSPEWIISMEACNAHGLYCVPLYDTlgaDAVEFIISHSEVSiVFV 157
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRcdrGTESPVAILAILFLGAAYAPIDPASPE---QRSLTVMKKCHVS-YLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 158 EEKKISELFKTCPNSTEYMKtvvsfggvsreqkeeaetfglviyawdefLKLGEGkqydlpikkksdICTIMYTSGTTGD 237
Cdd:cd17654 94 QNKELDNAPLSFTPEHRHFN-----------------------------IRTDEC------------LAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 238 PKGVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLahIFDRVIEECF--IQHGAAIGFWRGDVKLLIEDLAEL- 314
Cdd:cd17654 133 PKIVAVPHKCILPNIQHFRSLFN-----ITSEDILFLTSPL--TFDPSVVEIFlsLSSGATLLIVPTSVKVLPSKLADIl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 315 ----KPTIFCAVPRVLDRvysglqkklsdggFLKKFIFDSafsykfgymkkgqshveasplfdklVFSKVKqglggNVRI 390
Cdd:cd17654 206 fkrhRITVLQATPTLFRR-------------FGSQSIKST-------------------------VLSATS-----SLRV 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 391 ILSGAAPLASHV--ESFLRVVACCHVLQGYGLTE-SCAGTFVSLPDELGMLgTVGPPVPNVDIRLEsvpemeyDALASTA 467
Cdd:cd17654 243 LALGGEPFPSLVilSSWRGKGNRTRIFNIYGITEvSCWALAYKVPEEDSPV-QLGSPLLGTVIEVR-------DQNGSEG 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 468 RGEICIRGKTLfsGYYKREDLTkeVLIDGWLHTGDVGEWQpDGSMKIIDRKKNIFK 523
Cdd:cd17654 315 TGQVFLGGLNR--VCILDDEVT--VPKGTMRATGDFVTVK-DGELFFLGRKDSQIK 365
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
81-552 |
3.14e-10 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 62.98 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLyDTLGADAVEFIISHSE-VSIVFVEE 159
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL-DPALPIAEQRVRSQAAgARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 KKISElfkTCPNSTEYMKTVVSFGGVSreqkeeAETFGLVIYAWDEFLKLGEGKQYDLPIKkkSDICTIMYTSGTTGDPK 239
Cdd:PRK05852 124 DGPHD---RAEPTTRWWPLTVNVGGDS------GPSGGTLSVHLDAATEPTPATSTPEGLR--PDDAMIMFTGGTTGLPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAGVIrllksANEALTVKDVYLSYLPLAHifdrvieecfiQHGAaigfwrgdVKLLIEDLAelkptif 319
Cdd:PRK05852 193 MVPWTHANIASSVRAII-----TGYRLSPRDATVAVMPLYH-----------GHGL--------IAALLATLA------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 320 cavprvldrvySGLQKKLSDGGflkKFifdSAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGGN----VRIILSGA 395
Cdd:PRK05852 242 -----------SGGAVLLPARG---RF---SAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpaaLRFIRSCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 396 APLASHVESFLRVVACCHVLQGYGLTES---CAGTFVSLPDE-------LGMLGTVGPPvpnvDIRLESVPEMEydaLAS 465
Cdd:PRK05852 305 APLTAETAQALQTEFAAPVVCAFGMTEAthqVTTTQIEGIGQtenpvvsTGLVGRSTGA----QIRIVGSDGLP---LPA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 466 TARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAV 545
Cdd:PRK05852 378 GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNV 456
|
....*..
gi 15236634 546 DSVWVYG 552
Cdd:PRK05852 457 MEAAVFG 463
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
228-532 |
5.56e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 62.37 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLlkSANEALTVKDVYLSYLPLAHIFdrvieecfiqhGAAIGF----WRG- 302
Cdd:PRK12582 225 YLFTSGSTGMPKAVINTQRMMCANIAMQEQL--RPREPDPPPPVSLDWMPWNHTM-----------GGNANFngllWGGg 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 -----DVKLL-------IEDLAELKPTIFCAVPRVLDRVYSGLQKklsDGGFLKKFifdsaFSyKFGYMKKGQSHVeASP 370
Cdd:PRK12582 292 tlyidDGKPLpgmfeetIRNLREISPTVYGNVPAGYAMLAEAMEK---DDALRRSF-----FK-NLRLMAYGGATL-SDD 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 371 LFDKLvfskvkQGLGgnVRIILSgaaplashvesflRVVacchVLQGYGLTEScAGTFVSLPDELGMLGTVGPPVPNVDI 450
Cdd:PRK12582 362 LYERM------QALA--VRTTGH-------------RIP----FYTGYGATET-APTTTGTHWDTERVGLIGLPLPGVEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 451 RLesVPemeydalaSTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEW-QPDGSMK--IID-RKKNIFKLS 525
Cdd:PRK12582 416 KL--AP--------VGDKYEVRVKGPNVTPGYHKDPELTAAAFDeEGFYRLGDAARFvDPDDPEKglIFDgRVAEDFKLS 485
|
....*..
gi 15236634 526 QGEYVAV 532
Cdd:PRK12582 486 TGTWVSV 492
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
388-558 |
1.55e-09 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 59.73 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 388 VRIILSGAAPLASHVESFLRVVACCHVL-QGYGLTEScagTFVS--LPDELGMLGTVGPPVPNVDIRLEsvpemeydALA 464
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFPKANLiEFYGTSEL---SFITynFNQESRPPNSVGRPFPNVEIEIR--------NAD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 465 STARGEICIRGKTLFSGYYKREDLTKevliDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQA 544
Cdd:cd17633 181 GGEIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPG 255
|
170
....*....|....
gi 15236634 545 VDSVWVYGNSFESF 558
Cdd:cd17633 256 IEEAIVVGIPDARF 269
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
223-545 |
2.35e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.39 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllkSANEALTVKDVYLSYLPLAHifDRvieecfiqhgAAIGFwrg 302
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF----VAAEFDVETDVMVSWLPLFH--DM----------GMVGF--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 dvkLLIE-----DLAELKPTIFCAVPRvldrvysgLQKKLsdggflkkfifdsafsykfgyMKKGQSHVEASPLFDKLVF 377
Cdd:PRK07768 213 ---LTVPmyfgaELVKVTPMDFLRDPL--------LWAEL---------------------ISKYRGTMTAAPNFAYALL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SKV--KQGLGGN-----VRIILSGAAPL-ASHVESFLRVVA-------CchVLQGYGLTESC-AGTFVSL---------- 431
Cdd:PRK07768 261 ARRlrRQAKPGAfdlssLRFALNGAEPIdPADVEDLLDAGArfglrpeA--ILPAYGMAEATlAVSFSPCgaglvvdevd 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 432 PDELGMLG--------------TVGPPVPNVDIRLesVPEmEYDALASTARGEICIRGKTLFSGYykredLTKEVLI--- 494
Cdd:PRK07768 339 ADLLAALRravpatkgntrrlaTLGPPLPGLEVRV--VDE-DGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIpaq 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15236634 495 --DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAV 545
Cdd:PRK07768 411 daDGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIERAAARVEGV 462
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
81-240 |
4.66e-09 |
|
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: 59.43 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEE- 159
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 ----KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYaWDEFLKlgegKQYDLPIKKKS-DICTIMYTSGT 234
Cdd:cd05968 173 ftrrGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLS-YDEEKE----TAGDGAERTESeDPLMIIYTSGT 247
|
....*.
gi 15236634 235 TGDPKG 240
Cdd:cd05968 248 TGKPKG 253
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
81-562 |
5.41e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.79 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYcVPLYDTLGADAVEFIISHSEVSIVFVEe 159
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVlKAGGAY-VPLDPEYPQDRLAYMLDDSGVRLLLTQ- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiSELFKTCPNSTeymktvvsfgGVSreqkeeaetfGLVIYAWDEFLKLGEGKQYDLPIKKKSdICTIMYTSGTTGDPK 239
Cdd:PRK12467 617 ---SHLLAQLPVPA----------GLR----------SLCLDEPADLLCGYSGHNPEVALDPDN-LAYVIYTSGSTGQPK 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAGVIRLLKsaneaLTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFWRGDVKLLIEDLAEL--- 314
Cdd:PRK12467 673 GVAISHGALANYVCVIAERLQ-----LAADDSMLMVSTFA--FDLGVTELFgaLASGATLHLLPPDCARDAEAFAALmad 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 315 -KPTIFCAVPRVLDrvysglqkklsdgGFLkkfifdsafsykfgymkkgQSHVEASPLfdklvfskvkqglgGNVRIILS 393
Cdd:PRK12467 746 qGVTVLKIVPSHLQ-------------ALL-------------------QASRVALPR--------------PQRALVCG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 394 GAAPLASHVESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELGMLGTV--GPPVPNVDIRlesVPEMEYDALASTARGE 470
Cdd:PRK12467 780 GEALQVDLLARVRALGPGARLINHYGPTETTVGvSTYELSDEERDFGNVpiGQPLANLGLY---ILDHYLNPVPVGVVGE 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 471 ICIRGKTLFSGYYKREDLTKEVLI------DG--WLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENiygEV 542
Cdd:PRK12467 857 LYIGGAGLARGYHRRPALTAERFVpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEA---RL 932
|
490 500
....*....|....*....|
gi 15236634 543 QAVDSVWvygnsfESFLIAI 562
Cdd:PRK12467 933 LAQPGVR------EAVVLAQ 946
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
81-510 |
5.79e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 59.17 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFglviyawDEFLKLGEGKQydLPIKKKSDICTIMyTSGTTGDPKG 240
Cdd:PRK07788 156 -FTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETL-------DDLIAGSSTAP--LPKPPKPGGIVIL-TSGTTGTPKG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVI-RLLKSANEALtvkdvylsYLPlAHIFdrvieecfiqHG-----AAIGFWRG---------DVK 305
Cdd:PRK07788 225 APRPEPSPLAPLAGLLsRVPFRAGETT--------LLP-APMF----------HAtgwahLTLAMALGstvvlrrrfDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 306 LLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDggflkkfiFDsafsykfgymkkgqshveASPLfdKLVFSkvkqglg 385
Cdd:PRK07788 286 ATLEDIAKHKATALVVVPVMLSRILDLGPEVLAK--------YD------------------TSSL--KIIFV------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 386 gnvriilSGAA---PLASHV-ESFLRVVacCHVlqgYGLTESCAGTfVSLPDELGML-GTVGPPVPNVDIRLesvpemeY 460
Cdd:PRK07788 331 -------SGSAlspELATRAlEAFGPVL--YNL---YGSTEVAFAT-IATPEDLAEApGTVGRPPKGVTVKI-------L 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15236634 461 DA----LASTARGEICIRGKTLFSGYykREDLTKEVlIDGWLHTGDVGEWQPDG 510
Cdd:PRK07788 391 DEngneVPRGVVGRIFVGNGFPFEGY--TDGRDKQI-IDGLLSSGDVGYFDEDG 441
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
231-545 |
6.44e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.01 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 231 TSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEAltvkDVYLSYLPLAHifDRVIeeCFIQHGAAIG--FWrgdvklli 308
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAT----DVGCSWLPLYH--DMGL--AFLLTAALAGapLW-------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 309 edlaeLKPT-IFCAVP-RVLDRvysglqkkLSDGGFlkkfIFDSAFSYKFGYMKKGQSHVEASPLfdklvfskvkqglgG 386
Cdd:PRK05851 224 -----LAPTtAFSASPfRWLSW--------LSDSRA----TLTAAPNFAYNLIGKYARRVSDVDL--------------G 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 387 NVRIILSGAAPLasHVESFLRVVACCH--------VLQGYGLTES-CAGTF-----------VSLPDELGM--LGTVGPP 444
Cdd:PRK05851 273 ALRVALNGGEPV--DCDGFERFATAMApfgfdagaAAPSYGLAEStCAVTVpvpgiglrvdeVTTDDGSGArrHAVLGNP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 445 VPNVDIRLEsvPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKevliDGWLHTGDVGeWQPDGSMKIIDRKKNIFKL 524
Cdd:PRK05851 351 IPGMEVRIS--PGDGAAGVAGREIGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLG-YLVDGGLVVCGRAKELITV 423
|
330 340
....*....|....*....|.
gi 15236634 525 SqGEYVAVENIENIYGEVQAV 545
Cdd:PRK05851 424 A-GRNIFPTEIERVAAQVRGV 443
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
220-538 |
8.39e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.57 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 220 KKKSDICTIMYTSGTTGDPKGVMISNESivtLIAGVIRLLKSANeaLTVKDVYLSYLPLAHIFdrvieecfiqhGAAIGF 299
Cdd:PRK08043 362 QQPEDAALILFTSGSEGHPKGVVHSHKS---LLANVEQIKTIAD--FTPNDRFMSALPLFHSF-----------GLTVGL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 WrgdVKLLIEDLAELKPTI--FCAVPR-VLDR---VYSGLQKKLsdgGFLKKFifdsAFSYKFGymkkgqshveasplfd 373
Cdd:PRK08043 426 F---TPLLTGAEVFLYPSPlhYRIVPElVYDRnctVLFGTSTFL---GNYARF----ANPYDFA---------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 374 klvfskvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAgTFVSLPDELGM-LGTVGPPVPNVDIRL 452
Cdd:PRK08043 480 -------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CA-PVVSINVPMAAkPGTVGRILPGMDARL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 453 ESVPEMEYDalastarGEICIRGKTLFSGYYKRE----------DLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIF 522
Cdd:PRK08043 545 LSVPGIEQG-------GRLQLKGPNIMNGYLRVEkpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFA 617
|
330
....*....|....*.
gi 15236634 523 KLSqGEYVAVENIENI 538
Cdd:PRK08043 618 KIA-GEMVSLEMVEQL 632
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
228-524 |
9.90e-09 |
|
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: 58.03 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAigfwrgdvk 305
Cdd:cd17652 98 VIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF-----DVGPGSRVLQFASPS--FDASVWELLmaLLAGAT--------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 306 LLIEDLAELKPTifcavprvldrvySGLQKKLSDGGFLKKFIFDSAFSYkfgymkkgqshVEASPLFDKLVfskvkqglg 385
Cdd:cd17652 162 LVLAPAEELLPG-------------EPLADLLREHRITHVTLPPAALAA-----------LPPDDLPDLRT--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 386 gnvrIILSGAAPLASHVEsflRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNV-----DIRLESVPemey 460
Cdd:cd17652 209 ----LVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTrvyvlDARLRPVP---- 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236634 461 dalaSTARGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLH-TGDVGEWQPDGSMKIIDRKKNIFKL 524
Cdd:cd17652 278 ----PGVPGELYIAGAGLARGYLNRPGLTAERFVadpfgapGSRMYrTGDLARWRADGQLEFLGRADDQVKI 345
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
223-545 |
1.04e-08 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 58.18 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYlplahIFDRVIEECFIqhgAAIGfwrG 302
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFSNY-----VFDFFVEQMTL---ALLN---G 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 303 DVKLLIEDLAELKPTIFCAVPRVLDRVY-SGlqkklsDGGFLKKFIFDSAFSYKfgymkkgqshveasplfdklvfskvk 381
Cdd:cd17648 163 QKLVVPPDEMRFDPDRFYAYINREKVTYlSG------TPSVLQQYDLARLPHLK-------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 382 qglggnvRIILSGAAPLASHVESfLRVVACCHVLQGYGLTESCAGTFVSL---PDELGMlgTVGPPVPNV-----DIRLE 453
Cdd:cd17648 211 -------RVDAAGEEFTAPVFEK-LRSRFAGLIINAYGPTETTVTNHKRFfpgDQRFDK--SLGRPVRNTkcyvlNDAMK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 454 SVPemeydalaSTARGEICIRGKTLFSGYYKREDLTKEVLI--------------DGWLH-TGDVGEWQPDGSMKIIDRK 518
Cdd:cd17648 281 RVP--------VGAVGELYLGGDGVARGYLNRPELTAERFLpnpfqteqerargrNARLYkTGDLVRWLPSGELEYLGRN 352
|
330 340
....*....|....*....|....*..
gi 15236634 519 KNIFKLsQGEYVAVENIENIYGEVQAV 545
Cdd:cd17648 353 DFQVKI-RGQRIEPGEVEAALASYPGV 378
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
224-532 |
1.23e-08 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 57.83 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVkdvYLSYLPLAHIFdrvieecfiqhGAAIGF---- 299
Cdd:cd05921 166 TVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPV---LVDWLPWNHTF-----------GGNHNFnlvl 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 WRGDVKLL-------------IEDLAELKPTIFCAVPRVLDRVYSGLQKklsdggflkkfifDSAFSYKFgymkkgqshv 366
Cdd:cd05921 232 YNGGTLYIddgkpmpggfeetLRNLREISPTVYFNVPAGWEMLVAALEK-------------DEALRRRF---------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 367 easplFDklvfskvkqglggNVRIILSGAAPLASHVESFLRVVACCHV------LQGYGLTEScAGTFVSLPDELGMLGT 440
Cdd:cd05921 289 -----FK-------------RLKLMFYAGAGLSQDVWDRLQALAVATVgeripmMAGLGATET-APTATFTHWPTERSGL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 441 VGPPVPNVDIRLesVPemeydalaSTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEW-QPDGSMKIID-- 516
Cdd:cd05921 350 IGLPAPGTELKL--VP--------SGGKYEVRVKGPNVTPGYWRQPELTAQAFDeEGFYCLGDAAKLaDPDDPAKGLVfd 419
|
330
....*....|....*..
gi 15236634 517 -RKKNIFKLSQGEYVAV 532
Cdd:cd05921 420 gRVAEDFKLASGTWVSV 436
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
418-545 |
1.50e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 57.79 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 418 YGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRL-----ESVPEMEydalastaRGEICIR--GKTLFSgYYKREDLTK 490
Cdd:PRK12406 303 YGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFvdedgRPLPQGE--------IGEIYSRiaGNPDFT-YHNKPEKRA 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 491 EVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGeyvaveniENIY-GEVQAV 545
Cdd:PRK12406 374 EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGG--------VNIYpAEIEAV 420
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
228-517 |
1.72e-08 |
|
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: 57.32 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNesivtliAGVIRLLKSANEALTV--KDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFWRGD 303
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSH-------ANVLALFAATQRWFGFneDDVWTLFHSYA--FDFSVWEIWgaLLHGGRLVVVPYE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 304 VKLLIEDLAEL----KPTIFCAVPrvldrvysglqkklsdggflkkfifdSAFSykfGYMKKGQSHVEASPlfdklvfsk 379
Cdd:cd17643 169 VARSPEDFARLlrdeGVTVLNQTP--------------------------SAFY---QLVEAADRDGRDPL--------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 380 vkqglggNVR-IILSG----AAPLASHVESFlrVVACCHVLQGYGLTESCA-GTFVSL-PDEL--GMLGTVGPPVPN--- 447
Cdd:cd17643 211 -------ALRyVIFGGealeAAMLRPWAGRF--GLDRPQLVNMYGITETTVhVTFRPLdAADLpaAAASPIGRPLPGlrv 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 448 --VDIRLESVPEMEYdalastarGEICIRGKTLFSGYYKREDLTKEVLIDG--------WLHTGDVGEWQPDGSMKIIDR 517
Cdd:cd17643 282 yvLDADGRPVPPGVV--------GELYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGR 353
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
228-537 |
1.74e-08 |
|
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: 57.29 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESIVTliagviRLLKSANE-ALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFWR--- 301
Cdd:cd17646 143 VIYTSGSTGRPKGVMVTHAGIVN------RLLWMQDEyPLGPGDRVLQKTPLS--FDVSVWELFwpLVAGARLVVARpgg 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 302 -GDVKLLIEDLAELKPTIFCAVPRVLDRvysglqkklsdggFLKkfifdsafsykfgymkkgqshvEASPlfdklvfskv 380
Cdd:cd17646 215 hRDPAYLAALIREHGVTTCHFVPSMLRV-------------FLA----------------------EPAA---------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 381 kqGLGGNVRIILSGAAPL-ASHVESFLRVV-ACCHVLqgYGLTES--------CAGTFV--SLPdelgmlgtVGPPVPN- 447
Cdd:cd17646 250 --GSCASLRRVFCSGEALpPELAARFLALPgAELHNL--YGPTEAaidvthwpVRGPAEtpSVP--------IGRPVPNt 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 448 ----VDIRLESVPemeydalASTArGEICIRGKTLFSGYYKREDLTKEVLIDGWL-------HTGDVGEWQPDGSMKIID 516
Cdd:cd17646 318 rlyvLDDALRPVP-------VGVP-GELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLG 389
|
330 340
....*....|....*....|.
gi 15236634 517 RKKNIFKLsQGEYVAVENIEN 537
Cdd:cd17646 390 RSDDQVKI-RGFRVEPGEIEA 409
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
81-242 |
1.91e-08 |
|
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: 57.59 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIV----- 155
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLitadg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 156 FVEEKKISELFKTC-----PNSTEYMKTVVsfggVSREQKEEAETFGLVIYaWDEFLKLGEGKQYDLPIkKKSDICTIMY 230
Cdd:cd17634 166 GVRAGRSVPLKKNVddalnPNVTSVEHVIV----LKRTGSDIDWQEGRDLW-WRDLIAKASPEHQPEAM-NAEDPLFILY 239
|
170
....*....|..
gi 15236634 231 TSGTTGDPKGVM 242
Cdd:cd17634 240 TSGTTGKPKGVL 251
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
442-521 |
2.54e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 442 GPPVPN--VDIRLES---VPEMEYdalastarGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGeWQPDGSMKIID 516
Cdd:PRK09192 388 GKALPGheIEIRNEAgmpLPERVV--------GHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLG-YLLDGYLYITG 458
|
....*
gi 15236634 517 RKKNI 521
Cdd:PRK09192 459 RAKDL 463
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-517 |
2.74e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC-NAHGLYcVPLYDTLGADAVEFIISHSEVSIVFVEe 159
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAIlKAGGAY-VPLDPEYPAERLAYMLEDSGVQLLLSQ- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiSELFKTCPNSTEYMKTVVSFGGVSRE-QKEEAETFGLViyawdeflklGEGKQYdlpikkksdictIMYTSGTTGDP 238
Cdd:PRK12316 616 ---SHLGRKLPLAAGVQVLDLDRPAAWLEgYSEENPGTELN----------PENLAY------------VIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 239 KGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECFIQ-------HGAAIGFWRgdvkllieDL 311
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-----GLGVGDTVLQKTPFS--FDVSVWEFFWPlmsgarlVVAAPGDHR--------DP 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 312 AELKPTIFCAVPRVLDRVYSGLQKKLSDGGFlkkfifDSAFSYKfgymkkgqshveasplfdklvfskvkqglggnvRII 391
Cdd:PRK12316 736 AKLVELINREGVDTLHFVPSMLQAFLQDEDV------ASCTSLR---------------------------------RIV 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 392 LSGAAPLASHVESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELGMLGTVGPPVPNV-----DIRLESVPemeydalaS 465
Cdd:PRK12316 777 CSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDvTHWTCVEEGGDSVPIGRPIANLacyilDANLEPVP--------V 848
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15236634 466 TARGEICIRGKTLFSGYYKREDLTKEVLI-----DG--WLHTGDVGEWQPDGSMKIIDR 517
Cdd:PRK12316 849 GVLGELYLAGRGLARGYHGRPGLTAERFVpspfvAGerMYRTGDLARYRADGVIEYAGR 907
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
416-552 |
3.26e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 56.59 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 416 QGYGLTEsCAGTFVSLPDEL--------GMLGTVGPPVPNVDIrleSVPEMEYDALASTARGEICIRGKTLFSGYYKRED 487
Cdd:PRK07470 310 QYFGLGE-VTGNITVLPPALhdaedgpdARIGTCGFERTGMEV---QIQDDEGRELPPGETGEICVIGPAVFAGYYNNPE 385
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236634 488 LTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK07470 386 ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
223-552 |
3.59e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.57 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISnESIVTLIAGVIrllkSANEALTVKDV-YLSyLPLahifdrvieecFiqHGAAIgfwr 301
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCS-HGRLAFAGRAL----TERFGLTRDDVcYVS-MPL-----------F--HSNAV---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 302 gdvklliedLAELKPTifcavprvldrVYSG----LQKKLSDGGFLKKFIFDSAfSYkFGYMKKGQSHVEASPLFDKLVF 377
Cdd:PRK13388 207 ---------MAGWAPA-----------VASGaavaLPAKFSASGFLDDVRRYGA-TY-FNYVGKPLAYILATPERPDDAD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SKVKQGLGgnvriilSGAAPlaSHVESFLRVVACcHVLQGYGLTEScAGTFVSLPDELGmlGTVGPPVPNVDI----RLE 453
Cdd:PRK13388 265 NPLRVAFG-------NEASP--RDIAEFSRRFGC-QVEDGYGSSEG-AVIVVREPGTPP--GSIGRGAPGVAIynpeTLT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 454 SVPEMEYDAL-----ASTARGEICIR-GKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqG 527
Cdd:PRK13388 332 ECAVARFDAHgallnADEAIGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVD-G 410
|
330 340
....*....|....*....|....*
gi 15236634 528 EYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK13388 411 ENLSAAPIERILLRHPAINRVAVYA 435
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
81-504 |
5.85e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 55.67 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFveek 160
Cdd:PRK04813 29 TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 KISELfktcPNSTEYMKTVvsfggvSREQKEEAETFGLVIyawdeflklgegkQYDLPIKKKsDICTIMYTSGTTGDPKG 240
Cdd:PRK04813 105 ATEEL----PLEILGIPVI------TLDELKDIFATGNPY-------------DFDHAVKGD-DNYYIIFTSGTTGKPKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIAGVIRLLKSA------NEA-----LTVKDVYLSylpLA-----HIFDRVIeecfIQhgaaigfwrgDV 304
Cdd:PRK04813 161 VQISHDNLVSFTNWMLEDFALPegpqflNQApysfdLSVMDLYPT---LAsggtlVALPKDM----TA----------NF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 305 KLLIEDLAELKPTIFCAVPR-----VLDRVYSglQKKLSDggfLKKFIFDsafsykfgymkkGQ--SHVEASPLFDKLvf 377
Cdd:PRK04813 224 KQLFETLPQLPINVWVSTPSfadmcLLDPSFN--EEHLPN---LTHFLFC------------GEelPHKTAKKLLERF-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 skvkqglggnvriilsgaaPLAshvesflrvvaccHVLQGYGLTESC-AGTFVSLPDElgMLGT-----VGPPVPNVDIr 451
Cdd:PRK04813 285 -------------------PSA-------------TIYNTYGPTEATvAVTSIEITDE--MLDQykrlpIGYAKPDSPL- 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15236634 452 leSVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVL--IDGW--LHTGDVG 504
Cdd:PRK04813 330 --LIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAG 384
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
219-537 |
6.26e-08 |
|
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: 55.64 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAgvirLLKSANEaLTVKDVYLSYLPLAhiFDRVIEECF--IQHGAA 296
Cdd:cd17645 100 LTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCE----WHRPYFG-VTPADKSLVYASFS--FDASAWEIFphLTAGAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 297 IGFWRGDVKLLIEdlaelkptifcavprvldrvysglqkKLSDggflkkfifdsafsykfgYMKkgQSHVEASPLFDKLV 376
Cdd:cd17645 173 LHVVPSERRLDLD--------------------------ALND------------------YFN--QEGITISFLPTGAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 fSKVKQGLGGNVRIILSGAAPLASHVESFLRVVacchvlQGYGLTE-SCAGTFVSLPDELGMLgTVGPPVPNVDI----- 450
Cdd:cd17645 207 -EQFMQLDNQSLRVLLTGGDKLKKIERKGYKLV------NNYGPTEnTVVATSFEIDKPYANI-PIGKPIDNTRVyilde 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 451 RLESVPEmeydalasTARGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGEWQPDGSMKIIDRKKNIFK 523
Cdd:cd17645 279 ALQLQPI--------GVAGELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVK 350
|
330
....*....|....
gi 15236634 524 LsQGEYVAVENIEN 537
Cdd:cd17645 351 I-RGYRIEPGEIEP 363
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
224-552 |
7.33e-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: 55.44 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEaltvkDVYLSYLPLAHIFDRVIeeCF---IQHGAAIGfw 300
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS-----DVLYTCLPLYHSTALIV--GWsacLASGATLV-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 301 rgdvklliedlaelkptifcavprvldrvysgLQKKLSDGGFlkkfiFDSAFSYK---FGYMKKGQSHVEASPLFDKLVF 377
Cdd:cd05940 153 --------------------------------IRKKFSASNF-----WDDIRKYQatiFQYIGELCRYLLNQPPKPTERK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SKVKQGLGGNVRiilsgaaplASHVESFLRVVACCHVLQGYGLTESCAGtFVSLPDELGMLGTVGP-------------- 443
Cdd:cd05940 196 HKVRMIFGNGLR---------PDIWEEFKERFGVPRIAEFYAATEGNSG-FINFFGKPGAIGRNPSllrkvaplalvkyd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 444 -----PVPNVDIRLESVPEMEYDALASTargeicIRGKTLFSGYYKREDLTKEVLI------DGWLHTGDVGEWQPDGSM 512
Cdd:cd05940 266 lesgePIRDAEGRCIKVPRGEPGLLISR------INPLEPFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFW 339
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15236634 513 KIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd05940 340 YFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
220-541 |
7.48e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.59 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 220 KKKSDICTIMYTSGTTGDPKGVMISNESivtLIAGVIRLLKSANEalTVKDVYLSYLPLAHIFDRVIEECF-IQHGAAIG 298
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHAN---LLANQRACLKFFSP--KEDDVMMSFLPPFHAYGFNSCTLFpLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 299 FWRGDV--KLLIEDLAELKPTIFCAVPrvldrvysglqkklsdggflkkfIFdsaFSYKFGYMKKGQSHVEAsplfdkLV 376
Cdd:PRK06334 255 FAYNPLypKKIVEMIDEAKVTFLGSTP-----------------------VF---FDYILKTAKKQESCLPS------LR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 FSKVkqglGGNV--RIILSGAAPLASHVEsfLRvvacchvlQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLes 454
Cdd:PRK06334 303 FVVI----GGDAfkDSLYQEALKTFPHIQ--LR--------QGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLI-- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 455 VPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDG--WLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAV 532
Cdd:PRK06334 367 VSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSL 445
|
....*....
gi 15236634 533 ENIENIYGE 541
Cdd:PRK06334 446 EALESILME 454
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-558 |
1.93e-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: 53.97 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWI-ISMEACNAHGLYCVpLYDTLGADAVEFIISHSEVSIVFVEe 159
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLeAYFAVPGMGAVLHT-ANPRLSPKEIAYILNHAEDKVLLFD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 160 kkiSELFKTCPNSTEYMKTVVSfgGVSREQKEEAetfglviyaWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPK 239
Cdd:cd05915 104 ---PNLLPLVEAIRGELKTVQH--FVVMDEKAPE---------GYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 240 GVMISNESIVTLIAGVIRLLKSANEALTVkdvYLSYLPLAHIFDRVIEECFIQHGAAIGFWR--GDVKLLIEDLAELKPT 317
Cdd:cd05915 170 GVVYSHRALVLHSLAASLVDGTALSEKDV---VLPVVPMFHVNAWCLPYAATLVGAKQVLPGprLDPASLVELFDGEGVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 318 IFCAVPRVLDRVYSGLQKklsdggfLKKfifdsAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGgnvriilsgaap 397
Cdd:cd05915 247 FTAGVPTVWLALADYLES-------TGH-----RLKTLRRLVVGGSAAPRSLIARFERMGVEVRQGYG------------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 398 lashvesflrvvaCCHVlqgYGLTESC--AGTFVSLPDELGM-------LGTVGPPVPNVDIRLESVPemeYDAlaSTAR 468
Cdd:cd05915 303 -------------LTET---SPVVVQNfvKSHLESLSEEEKLtlkaktgLPIPLVRLRVADEEGRPVP---KDG--KALG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 469 gEICIRGKTLFSGYYKREDLTK-EVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDS 547
Cdd:cd05915 362 -EVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKE 439
|
490
....*....|.
gi 15236634 548 VWVYGNSFESF 558
Cdd:cd05915 440 AAVVAIPHPKW 450
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
204-504 |
6.71e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.59 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 204 DEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIvtliAGVIRLLKSAnEALTVKDVYLSYLPLahifd 283
Cdd:PRK09274 155 ATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMF----EAQIEALRED-YGIEPGEIDLPTFPL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 284 rvieecFIQHGAAIGfwrgdVKLLIEDLAELKPtIFCavprvldrvysglqkklsDGGFLKKFIFDSAFSYKFG---YMK 360
Cdd:PRK09274 225 ------FALFGPALG-----MTSVIPDMDPTRP-ATV------------------DPAKLFAAIERYGVTNLFGspaLLE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 361 K----GQSHVEASPlfdklvfskvkqglggNVRIILSGAAPL-ASHVESFLRVVA-CCHVLQGYGLTESCAGTFVSLPDE 434
Cdd:PRK09274 275 RlgryGEANGIKLP----------------SLRRVISAGAPVpIAVIERFRAMLPpDAEILTPYGATEALPISSIESREI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 435 LGML--------GT-VGPPVPNVDIRL-----ESVPEMEYD-ALASTARGEICIRGKTLFSGYYKREDLTKEVLI-DG-- 496
Cdd:PRK09274 339 LFATraatdngaGIcVGRPVDGVEVRIiaisdAPIPEWDDAlRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIpDGqg 418
|
330
....*....|
gi 15236634 497 --WLHTGDVG 504
Cdd:PRK09274 419 dvWHRMGDLG 428
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
224-560 |
8.61e-07 |
|
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: 51.71 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAG----VIRllksaneaLTVKDVYLSYLPLAHIFDRVIEECFIQH-GAA-I 297
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRyavnVLR--------LREDDRFVGSPPLAFTFGLGGVLLFPFGvGASgV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 298 GFWRGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIfdsafsykfgymkkgqSHVEASPlfdKLVF 377
Cdd:cd05958 170 LLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCV----------------SAGEALP---AALH 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SKVKQGLGgnVRIIlsgaaplashvesflrvvacchvlQGYGLTESCAgTFVSLPDELGMLGTVGPPVPNvdIRLESVPE 457
Cdd:cd05958 231 RAWKEATG--IPII------------------------DGIGSTEMFH-IFISARPGDARPGATGKPVPG--YEAKVVDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 458 MEYDALASTArGEICIRGKTLFsgYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKlSQGEYVAVENIEN 537
Cdd:cd05958 282 EGNPVPDGTI-GRLAVRGPTGC--RYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVED 357
|
330 340
....*....|....*....|...
gi 15236634 538 IYGEVQAVDSVWVYGNSFESFLI 560
Cdd:cd05958 358 VLLQHPAVAECAVVGHPDESRGV 380
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
81-586 |
1.54e-06 |
|
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: 51.16 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEek 160
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcPNSTEYmktvvsfggvsreqkeeaetfglviyawdeflklgegkqydlpikkksdictIMYTSGTTGDPKG 240
Cdd:cd12115 104 ---------PDDLAY----------------------------------------------------VIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 241 VMISNESIVTLIagvirllKSANEALTvKDVYLSYLPLAHI-FDRVIEECF--IQHGAAIgFWRGDVKLLIEDLAELKPT 317
Cdd:cd12115 123 VAIEHRNAAAFL-------QWAAAAFS-AEELAGVLASTSIcFDLSVFELFgpLATGGKV-VLADNVLALPDLPAAAEVT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 318 IFCAVPRVLDRVysglqkklsdggflkkfifdsafsykfgymkkgqshVEASplfdklvfskvkqGLGGNVRII-LSGAa 396
Cdd:cd12115 194 LINTVPSAAAEL------------------------------------LRHD-------------ALPASVRVVnLAGE- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 397 PLASH-VESFLRV--VACCHVLqgYGLTESCA-GTFVSLPDELGMLGTVGPPVPN-----VDIRLESVPemeydalaSTA 467
Cdd:cd12115 224 PLPRDlVQRLYARlqVERVVNL--YGPSEDTTySTVAPVPPGASGEVSIGRPLANtqayvLDRALQPVP--------LGV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 468 RGEICIRGKTLFSGYYKREDLTKE-VLIDGWL------HTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIENIYG 540
Cdd:cd12115 294 PGELYIGGAGVARGYLGRPGLTAErFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALR 372
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15236634 541 EVQAVDSVWVygnsfesFLIAIANPNQHILERWAAENGVSGDYDAL 586
Cdd:cd12115 373 SIPGVREAVV-------VAIGDAAGERRLVAYIVAEPGAAGLVEDL 411
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
228-517 |
2.47e-06 |
|
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: 50.44 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAI-----GFW 300
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERY-----GLTPGDRELQFASFN--FDGAHEQLLppLICGACVvlrpdELW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 301 rGDVKLLIEDLAELKPTifcavprVLDrvysglqkklsdggflkkfiFDSAFSYKFGymkkgqshveasplfdkLVFSKV 380
Cdd:cd17649 172 -ASADELAEMVRELGVT-------VLD--------------------LPPAYLQQLA-----------------EEADRT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 381 KQGLGGNVRIILSGAAPLASHvesFLRVVACCHV--LQGYGLTEscaGTFVSL----PDELGMLGT---VGPPVPNV--- 448
Cdd:cd17649 207 GDGRPPSLRLYIFGGEALSPE---LLRRWLKAPVrlFNAYGPTE---ATVTPLvwkcEAGAARAGAsmpIGRPLGGRsay 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15236634 449 --DIRLESVPEmeydalasTARGEICIRGKTLFSGYYKREDLTKEVLIDG--------WLHTGDVGEWQPDGSMKIIDR 517
Cdd:cd17649 281 ilDADLNPVPV--------GVTGELYIGGEGLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGR 351
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
386-537 |
2.78e-06 |
|
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: 50.40 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 386 GNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAgTFVSL--PDELgMLGTVGPPV-PNVDIRlesVPEMEYDA 462
Cdd:cd05920 255 SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL-NYTRLddPDEV-IIHTQGRPMsPDDEIR---VVDEEGNP 329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236634 463 LASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIEN 537
Cdd:cd05920 330 VPPGEEGELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-546 |
3.49e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.15 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEaltvkDVYLSYLPLAHIFdrvieecfiqhGAAIG 298
Cdd:cd05910 81 IPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG-----EVDLATFPLFALF-----------GPALG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 299 fwrgdVKLLIEDLAELKPTifCAVPRVLDrvysglqkklsdgGFLKKFifdsafsykfgymkkGQSHVEASP-LFDKLVF 377
Cdd:cd05910 145 -----LTSVIPDMDPTRPA--RADPQKLV-------------GAIRQY---------------GVSIVFGSPaLLERVAR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 378 SKVKQGLG-GNVRIILSGAAPLASHV-ESFLRVVA-CCHVLQGYGLTESCAGTFVS----------LPDELGmlGT-VGP 443
Cdd:cd05910 190 YCAQHGITlPSLRRVLSAGAPVPIALaARLRKMLSdEAEILTPYGATEALPVSSIGsrellatttaATSGGA--GTcVGR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 444 PVPNVDIRL-----ESVPEMEYD-ALASTARGEICIRGKTLFSGYYKREDLTKEVLID----GWLH-TGDVGEWQPDGSM 512
Cdd:cd05910 268 PIPGVRVRIieiddEPIAEWDDTlELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDdnseGFWHrMGDLGYLDDEGRL 347
|
330 340 350
....*....|....*....|....*....|....
gi 15236634 513 KIIDRKKNIFKLSQGEYVAvENIENIYGEVQAVD 546
Cdd:cd05910 348 WFCGRKAHRVITTGGTLYT-EPVERVFNTHPGVR 380
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
377-552 |
4.85e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.39 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 FSKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVP 456
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 457 EMEYDAlasTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIE 536
Cdd:PRK07638 325 GEEVQK---GEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIE 400
|
170
....*....|....*.
gi 15236634 537 NIYGEVQAVDSVWVYG 552
Cdd:PRK07638 401 SVLHEHPAVDEIVVIG 416
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
418-552 |
7.22e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 48.84 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 418 YGLTESCAGTFVSLPDELgMLG--TVGPPVPNVDIRLESvpemeydalasTARGEICIRGKTLFSGYYKREDLTKEVLId 495
Cdd:PRK07445 261 YGMTETASQIATLKPDDF-LAGnnSSGQVLPHAQITIPA-----------NQTGNITIQAQSLALGYYPQILDSQGIFE- 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15236634 496 gwlhTGDVGEWQPDGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:PRK07445 328 ----TDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLG 379
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
220-552 |
1.00e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 48.28 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 220 KKKSDICTIMYTSGTTGDPKGVMISnesiVTLIAGVIRLLKSANEaLTVKDVYLsylplahifdrvieeCFIQHGAAIGF 299
Cdd:cd05973 85 KLDSDPFVMMFTSGTTGLPKGVPVP----LRALAAFGAYLRDAVD-LRPEDSFW---------------NAADPGWAYGL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 WRGdvklLIEDLAELKPTIFCAvprvldrvysglqkklsdGGFLKKFIFDSAFSYkfgymkkGQSHVEASPLFDKLVFS- 378
Cdd:cd05973 145 YYA----ITGPLALGHPTILLE------------------GGFSVESTWRVIERL-------GVTNLAGSPTAYRLLMAa 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 379 --KVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVS----LPDELgMLGTVGPPVPN----- 447
Cdd:cd05973 196 gaEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE--LGMVLAnhhaLEHPV-HAGSAGRAMPGwrvav 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 448 VDIRLESVPEMEYDALAstargeICIRGKTL--FSGYYKREDLTkevlIDG-WLHTGDVGEWQPDGSMKIIDRKKNIFKL 524
Cdd:cd05973 273 LDDDGDELGPGEPGRLA------IDIANSPLmwFRGYQLPDTPA----IDGgYYLTGDTVEFDPDGSFSFIGRADDVITM 342
|
330 340
....*....|....*....|....*...
gi 15236634 525 SqGEYVAVENIENIYGEVQAVDSVWVYG 552
Cdd:cd05973 343 S-GYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
389-525 |
2.12e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 47.56 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 389 RIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSlPDELGMLGTVGPPVPNVDIRLesvpemeYDALASTAR 468
Cdd:cd05974 203 REVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQPVKAGSMGRPLPGYRVAL-------LDPDGAPAT 274
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15236634 469 -GEICI-----RGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLS 525
Cdd:cd05974 275 eGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
389-537 |
2.19e-05 |
|
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: 47.45 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 389 RIILSGAAPLAShvESFLRVVAC--CHVLQGYGLTEscaG--TFVSL--PDELgMLGTVGPPVPNVD-IRL-----ESVP 456
Cdd:COG1021 303 RVLQVGGAKLSP--ELARRVRPAlgCTLQQVFGMAE---GlvNYTRLddPEEV-ILTTQGRPISPDDeVRIvdedgNPVP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 457 EMEYdalastarGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNifklsQ----GEYVA 531
Cdd:COG1021 377 PGEV--------GELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEKIA 443
|
....*.
gi 15236634 532 VENIEN 537
Cdd:COG1021 444 AEEVEN 449
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
81-280 |
3.37e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 46.99 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEK 160
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 K---ISELFKTCPNSTEYMkTVVSFGGVSReqkeeaetfglvIYAWDEFLKlgegKQYDLPIKKKSDICTIMYTSGTTGD 237
Cdd:PRK13391 106 KldvARALLKQCPGVRHRL-VLDGDGELEG------------FVGYAEAVA----GLPATPIADESLGTDMLYSSGTTGR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15236634 238 PKGVM--ISNESIVT---LIAGVIRLLKSANEAltvkdVYLSYLPLAH 280
Cdd:PRK13391 169 PKGIKrpLPEQPPDTplpLTAFLQRLWGFRSDM-----VYLSPAPLYH 211
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
223-561 |
3.39e-05 |
|
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: 46.88 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksaneALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGF- 299
Cdd:cd12114 126 DDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF-----AVGPDDRVLALSSLS--FDLSVYDIFgaLSAGATLVLp 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 300 ---WRGDVKLLIEDLAELKPTIFCAVPRVLDrvysglqkklsdggflkkfifdsafsykfgyMkkgqshveaspLFDKLV 376
Cdd:cd12114 199 deaRRRDPAHWAELIERHGVTLWNSVPALLE-------------------------------M-----------LLDVLE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 377 fskVKQGLGGNVR-IILSG---AAPLASHVEsflRVVACCHVLQGYGLTE----SCAGTFVSLPDELGMLgTVGPPVPN- 447
Cdd:cd12114 237 ---AAQALLPSLRlVLLSGdwiPLDLPARLR---ALAPDARLISLGGATEasiwSIYHPIDEVPPDWRSI-PYGRPLANq 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 448 ----VDIRLESVPEMeydalastARGEICIRGKTLFSGYYKREDLTKEVLID-----GWLHTGDVGEWQPDGSMKIIDRK 518
Cdd:cd12114 310 ryrvLDPRGRDCPDW--------VPGELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRR 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15236634 519 KNIFKLsQGEYVAVENIENIYGEVQAVDS--VWVYGNSFESFLIA 561
Cdd:cd12114 382 DGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAA 425
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
218-521 |
4.38e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 218 PIKKKSDICTIMYTSGTTGDPKGVMISNESIVtliagvirllksANEALTVK---------DVYLSYLPLAHifdrviee 288
Cdd:PRK05691 161 PALQPDDIAFLQYTSGSTALPKGVQVSHGNLV------------ANEQLIRHgfgidlnpdDVIVSWLPLYH-------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 289 cfiqhgaaigfwrgDVKlLIEDLaeLKPtIFCAVPRVLdrvysglqkkLSDGGFLKKFI-FDSAFSYKFGYMKKGQSHve 367
Cdd:PRK05691 221 --------------DMG-LIGGL--LQP-IFSGVPCVL----------MSPAYFLERPLrWLEAISEYGGTISGGPDF-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 368 ASPLFDKLVFSKVKQGLG-GNVRIILSGAAPL-ASHVESFLRVVACC-----HVLQGYGLTEscAGTFVS---------- 430
Cdd:PRK05691 271 AYRLCSERVSESALERLDlSRWRVAYSGSEPIrQDSLERFAEKFAACgfdpdSFFASYGLAE--ATLFVSggrrgqgipa 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 431 -------------LPDELGMLGTVGPPVPNVDIRLesVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLI--D 495
Cdd:PRK05691 349 leldaealarnraEPGTGSVLMSCGRSQPGHAVLI--VDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVehD 426
|
330 340
....*....|....*....|....*...
gi 15236634 496 G--WLHTGDVGeWQPDGSMKIIDRKKNI 521
Cdd:PRK05691 427 GrtWLRTGDLG-FLRDGELFVTGRLKDM 453
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
469-552 |
6.53e-05 |
|
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: 45.89 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 469 GEICIR----GKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLsQGEYVAVENIEN 537
Cdd:cd05937 300 GEMLGRvpfkNREAFQGYLHNEDATESKLVrdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRW-KSENVSTTEVAD 378
|
90
....*....|....*
gi 15236634 538 IYGEVQAVDSVWVYG 552
Cdd:cd05937 379 VLGAHPDIAEANVYG 393
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
81-242 |
1.21e-04 |
|
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: 45.24 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIV----- 155
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVitadg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 156 ------FVEEKKI-SELFKTCPnSTEymKTVVsfggVSREQKEEAETFGLVIYaWDEFLKlgEGKQYDLPIKKKS-DICT 227
Cdd:cd05966 166 gyrggkVIPLKEIvDEALEKCP-SVE--KVLV----VKRTGGEVPMTEGRDLW-WHDLMA--KQSPECEPEWMDSeDPLF 235
|
170
....*....|....*
gi 15236634 228 IMYTSGTTGDPKGVM 242
Cdd:cd05966 236 ILYTSGSTGKPKGVV 250
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
228-528 |
1.29e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.54 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 228 IMYTSGTTGDPKGVMISNESivtliagVIRLLKSANEA--LTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAI-----G 298
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGA-------LVNRLCATQEAyqLSAADVVLQFTSFA--FDVSVWELFwpLINGARLviappG 1793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 299 FWRgDVKLLIEDLAELKPTIFCAVPrvldrvySGLQKKLSDGGflkkfifdsafsykfgymkkgqsHVEASPlfdklvfs 378
Cdd:PRK12467 1794 AHR-DPEQLIQLIERQQVTTLHFVP-------SMLQQLLQMDE-----------------------QVEHPL-------- 1834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 379 KVKqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAG----TFVSLPDELGMLGTVGPPVPN-----VD 449
Cdd:PRK12467 1835 SLR-------RVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDvthwTCRRKDLEGRDSVPIGQPIANlstyiLD 1907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 450 IRLESVPemeydalaSTARGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLH-TGDVGEWQPDGSMKI---IDRK 518
Cdd:PRK12467 1908 ASLNPVP--------IGVAGELYLGGVGLARGYLNRPALTAERFVadpfgtvGSRLYrTGDLARYRADGVIEYlgrIDHQ 1979
|
330
....*....|..
gi 15236634 519 KNI--FKLSQGE 528
Cdd:PRK12467 1980 VKIrgFRIELGE 1991
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
462-552 |
2.91e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 43.96 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 462 ALASTARGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSqGEYVAVENIENIYG 540
Cdd:PRK06164 371 LLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALE 449
|
90
....*....|..
gi 15236634 541 EVQAVDSVWVYG 552
Cdd:PRK06164 450 ALPGVAAAQVVG 461
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
191-290 |
6.55e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.11 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 191 EEAETF----GLVIYAWDEFLKLGEGKqyDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTliagviRLLKSANE-A 265
Cdd:PRK10252 564 DQLPRFadvpDLTSLCYNAPLAPQGAA--PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN------RLLWMQNHyP 635
|
90 100
....*....|....*....|....*
gi 15236634 266 LTVKDVYLSYLPLAhiFDRVIEECF 290
Cdd:PRK10252 636 LTADDVVLQKTPCS--FDVSVWEFF 658
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
81-242 |
2.20e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.28 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACnAHglycvplydtLGAdavefiiSHSevsivfveek 160
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-AR----------IGA-------VHS---------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 161 kiselfktcpnsteymktVVsFGGVS----REQKEEAETfGLVIYAwDEFLKLG-------------------------- 210
Cdd:PRK00174 152 ------------------VV-FGGFSaealADRIIDAGA-KLVITA-DEGVRGGkpiplkanvdealancpsvekvivvr 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15236634 211 ---------EGKQY---DLpIKKKSDICT-----------IMYTSGTTGDPKGVM 242
Cdd:PRK00174 211 rtggdvdwvEGRDLwwhEL-VAGASDECEpepmdaedplfILYTSGSTGKPKGVL 264
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
81-242 |
4.09e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 40.26 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 81 TYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIV----- 155
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLittpa 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236634 156 FVEEKKISELfktcPNsteyMKTVVSFGGVSREQKEEAETFGLVIYAWDEFlklgegkqyDLPIKKKSDICTIMYTSGTT 235
Cdd:PRK04319 155 LLERKPADDL----PS----LKHVLLVGEDVEEGPGTLDFNALMEQASDEF---------DIEWTDREDGAILHYTSGST 217
|
....*..
gi 15236634 236 GDPKGVM 242
Cdd:PRK04319 218 GKPKGVL 224
|
|
| |
