|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
6-665 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 1275.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 6 KNTFTIKVEDGKPGKDGRLAVGPVFRSVLAKDGFPQLEPDMKTSWDVFRVAAVKYADNRMLGWRPFKDGVPGPYLWKSYK 85
Cdd:PLN02430 1 MKSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 86 EIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIK 165
Cdd:PLN02430 81 EVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 166 EILSPNCKSAKRLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVML 245
Cdd:PLN02430 161 ELLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 246 THESHAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPTLLVGVP 325
Cdd:PLN02430 241 THEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 326 RVYERIYEGILKAIAELRPLRRVIFNALYNRKLASMKAGYSHKTASPFADMLAFRKVKARLGGRLRLLISGGAPLSNEIE 405
Cdd:PLN02430 321 RVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 406 EFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLEEVPEMGYNPLGVPSRGEICIRGKSLFAGYY 485
Cdd:PLN02430 401 EFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 486 KSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSFRSSLVAVV 565
Cdd:PLN02430 481 KNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 566 NPHQENTMKWAESNGYKGSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERDLVTATMKKKRKNM 645
Cdd:PLN02430 561 VPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNL 640
|
650 660
....*....|....*....|
gi 226491570 646 LNYYQSEIDTIYKKLEAQKS 665
Cdd:PLN02430 641 LKYYQVEIDEMYRKLAEKRI 660
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
9-663 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 774.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 9 FTIKVEDGKPGKDGRLAVGPVFRSVLAKDGFPQLEPDMKTSWDVFRVAAVKYADNRMLGWRPFKDGVPGPYLWKSYKEIY 88
Cdd:PLN02614 7 FIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPNPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 89 DEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIKEIL 168
Cdd:PLN02614 87 DIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 169 SPNCKSAKRLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHE 248
Cdd:PLN02614 167 KTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 249 SHAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPTLLVGVPRVY 328
Cdd:PLN02614 247 SIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 329 ERIYEGILKAIAELRPLRRVIFNALYNRKLASMKAGYSHKTASPFADMLAFRKVKARLGGRLRLLISGGAPLSNEIEEFM 408
Cdd:PLN02614 327 DRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 409 RVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLEEVPEMGYNPLGVPSRGEICIRGKSLFAGYYKSP 488
Cdd:PLN02614 407 RVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKRE 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 489 ELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSFRSSLVAVVNPH 568
Cdd:PLN02614 487 DLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPN 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 569 QENTMKWAESNGYKGSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERDLVTATMKKKRKNMLNY 648
Cdd:PLN02614 567 QQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKY 646
|
650
....*....|....*
gi 226491570 649 YQSEIDTIYKKLEAQ 663
Cdd:PLN02614 647 YQSVIDEMYKTTNEK 661
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
8-665 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 766.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 8 TFTIKVEDGKPGKDGRLAVGPVFRSVLAKDGFPQLEPDMKTSWDVFRVAAVKYADNRMLGWRPFKDGVPGPYLWKSYKEI 87
Cdd:PLN02861 4 TYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTYKEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 88 YDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIKEI 167
Cdd:PLN02861 84 YDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 168 LS--PNCKSakRLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKVGKDNPRQPcPPQASDICTVMYTSGTSGQPKGVML 245
Cdd:PLN02861 164 LSclPKCSS--NLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 246 THESHAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPTLLVGVP 325
Cdd:PLN02861 241 TNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 326 RVYERIYEGILKAIAELRPLRRVIFNALYNRKLASMKAGYSHKTASPFADMLAFRKVKARLGGRLRLLISGGAPLSNEIE 405
Cdd:PLN02861 321 RVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 406 EFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLEEVPEMGYNPLGVPSRGEICIRGKSLFAGYY 485
Cdd:PLN02861 401 EFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 486 KSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSFRSSLVAVV 565
Cdd:PLN02861 481 KRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 566 NPHQENTMKWAESNGYKGSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERDLVTATMKKKRKNM 645
Cdd:PLN02861 561 VPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQL 640
|
650 660
....*....|....*....|
gi 226491570 646 LNYYQSEIDTIYKKLEAQKS 665
Cdd:PLN02861 641 LKYYKDCIDQLYSEAKGGKA 660
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
77-658 |
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: 757.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWKSYKEIYDEVLQAGSALQKLGV--QPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEI 154
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 155 DVVFIQDkkikeilspncksakrlkalvaftsatteqnkeadqiGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTS 234
Cdd:cd05927 81 SIVFCDA-------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 235 GTSGQPKGVMLTHESHAMYVKGVDLFMDQFDdKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIV 314
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILN-KINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 315 ELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNALYNRKLASMKAGysHKTASPFADMLAFRKVKARLGGRLRLLI 394
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSG--VVRASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 395 SGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRLEEVPEMGYNPLGVPSRGEIC 474
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDVPEMNYDAKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 475 IRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVY 553
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 554 GDSFRSSLVAVVNPHQENTMKWAESN-GYKGSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERD 632
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
570 580
....*....|....*....|....*.
gi 226491570 633 LVTATMKKKRKNMLNYYQSEIDTIYK 658
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
23-660 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 594.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 23 RLAVGP--VFRSVLA----KDGFPQlEPDMKTSWDVFRVAAVKYADNRMLGWRPFKDGVPGPYLWKSYKEIYDEVLQAGS 96
Cdd:PLN02736 15 KLQTGKwnVYRSARSplklVSRFPD-HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDGTVGEYKWMTYGEAGTARTAIGS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 97 ALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIKEILS--PNCKS 174
Cdd:PLN02736 94 GLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSclSEIPS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 175 akrLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYV 254
Cdd:PLN02736 174 ---VRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 255 KGVDLfmdqfDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPTLLVGVPRVYERIYEG 334
Cdd:PLN02736 251 AGSSL-----STKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 335 ILKAIAELRPLRRVIFNALYNRKLASMKAGyshKTASPFADMLAFRKVKARLGGRLRLLISGGAPLSNEIEEFMRVTTCA 414
Cdd:PLN02736 326 ITNAVKESGGLKERLFNAAYNAKKQALENG---KNPSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 415 YFIQGYGLTETLGPSTVCYIDDMaLVGSAGVPATYTEIRLEEVPEMGYNPLGVP-SRGEICIRGKSLFAGYYKSPELTNE 493
Cdd:PLN02736 403 RVLEGYGMTETSCVISGMDEGDN-LSGHVGSPNPACEVKLVDVPEMNYTSEDQPyPRGEICVRGPIIFKGYYKDEVQTRE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 494 AI-VDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSFRSSLVAVVNPHQENT 572
Cdd:PLN02736 482 VIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 573 MKWAESNGYK-GSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERDLVTATMKKKRKNMLNYYQS 651
Cdd:PLN02736 562 KAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAK 641
|
....*....
gi 226491570 652 EIDTIYKKL 660
Cdd:PLN02736 642 AISDMYAEL 650
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
77-644 |
2.73e-171 |
|
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: 499.05 E-value: 2.73e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDV 156
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 157 VFiqdkkikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpCPPQASDICTVMYTSGT 236
Cdd:cd17639 81 IF-------------------------------------------------------------TDGKPDDLACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHEShamYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYyhGDLNALRD----- 311
Cdd:cd17639 100 TGNPKGVMLTHGN---LVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 ---DIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNALYNRKLASMKAGYShktaSPFADMLAFRKVKARLGG 388
Cdd:cd17639 175 ckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG----TPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 389 RLRLLISGGAPLSNEIEEFMRVTtCAYFIQGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRLEEVPEMGYNPLGVP 468
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIV-LCPVIQGYGLTETCAGGTVQDPGDLE-TGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 469 SRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLV 547
Cdd:cd17639 329 PRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 548 EDIWVYGDSFRSSLVAVVNPHQENTMKWAESNGYKGS-FDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVP 626
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSeWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*...
gi 226491570 627 FDIERDLVTATMKKKRKN 644
Cdd:cd17639 489 WTPENGLVTAAQKLKRKE 506
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
51-659 |
1.10e-169 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 498.09 E-value: 1.10e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 51 DVFRVAAVKYADNRMLGWRPFkdgvpGPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYS 130
Cdd:COG1022 15 DLLRRRAARFPDRVALREKED-----GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 131 LVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIKEILSPNCKSAKRLKALVAFtsatteqNKEADQIGIKMYAWDDFLK 210
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVL-------DPRGLRDDPRLLSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 211 VGKDNP------RQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHIL 284
Cdd:COG1022 163 LGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-----LGPGDRTLSFLPLAHVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 285 DRMIEEYFFHKGASIgYYHGDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFN-------ALYNRK 357
Cdd:COG1022 238 ERTVSYYALAAGATV-AFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRwalavgrRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 358 LASMKAGYSHKTASPFADMLAFRKVKARLGGRLRLLISGGAPLSNEIEEFMR---VTtcayFIQGYGLTETLGPSTVCYI 434
Cdd:COG1022 317 LAGKSPSLLLRLKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRalgIP----VLEGYGLTETSPVITVNRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 435 DDMaLVGSAGVPATYTEIRLEEvpemgynplgvpsRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGI 513
Cdd:COG1022 393 GDN-RIGTVGPPLPGVEVKIAE-------------DGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 514 LKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSfRSSLVAVVNPHQENTMKWAESNGYK-GSFDEICKLE 592
Cdd:COG1022 459 LRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDP 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 593 GLKEYILKELAAVaqKNKLRGFEYIKGVVLDPVPFDIERDLVTATMKKKRKNMLNYYQSEIDTIYKK 659
Cdd:COG1022 538 EVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
39-657 |
2.70e-127 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 392.56 E-value: 2.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 39 FPQLepdMKTSWD-------VFRVAAVKYADNRMLGWRPF--------KDGVP------GPYLWKSYKEIYDEVLQAGSA 97
Cdd:PLN02387 46 FPEL---VETPWEgattlaaLFEQSCKKYSDKRLLGTRKLisrefetsSDGRKfeklhlGEYEWITYGQVFERVCNFASG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 98 LQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIKEI--LSPNCKSA 175
Cdd:PLN02387 123 LVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLidISSQLETV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 176 KRLKALvaftsatTEQNKEADQIGIKMYAW-----DDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESH 250
Cdd:PLN02387 203 KRVIYM-------DDEGVDSDSSLSGSSNWtvssfSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 251 AMYVKGVDLFMDqfddKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYyhGDLNALRD-----------DIVELKPT 319
Cdd:PLN02387 276 VATVAGVMTVVP----KLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 320 LLVGVPRVYERIYEGILKAIAELRPLRRVIFNALYNRKLASMKAGY--SHKTASPFADMLAFRKVKARLGGRLRLLISGG 397
Cdd:PLN02387 350 LMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGSWfgAWGLEKLLWDALVFKKIRAVLGGRIRFMLSGG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRLEEVPEMGYNPLGVP-SRGEICIR 476
Cdd:PLN02387 430 APLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTS-VGRVGPPLPCCYVKLVSWEEGGYLISDKPmPRGEIVIG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 477 GKSLFAGYYKSPELTNEAI-VDG----WFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIW 551
Cdd:PLN02387 509 GPSVTLGYFKNQEKTDEVYkVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 552 VYGDSFRSSLVAVVNPHQENTMKWAESNGYK-GSFDEIC-KLEGLKEyILKELAAVAQKNKLRGFEYIKGVVLDPVPFDI 629
Cdd:PLN02387 589 VHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCeKEEAVKE-VQQSLSKAAKAARLEKFEIPAKIKLLPEPWTP 667
|
650 660
....*....|....*....|....*...
gi 226491570 630 ERDLVTATMKKKRKNMLNYYQSEIDTIY 657
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 ... |
77-643 |
5.04e-126 |
|
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: 380.79 E-value: 5.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDV 156
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 157 VFIQDkkikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqASDICTVMYTSGT 236
Cdd:cd05907 81 LFVED--------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHILDRMIEEYF-FHKGASIGYYHGDlNALRDDIVE 315
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLP-----ATEGDRHLSFLPLAHVFERRAGLYVpLLAGARIYFASSA-ETLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 316 LKPTLLVGVPRVYERIYEGIlkAIAELRPLRRVIFnalynrklasmkagyshktaspfadMLAfrkvkarLGGRLRLLIS 395
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLF-------------------------DLA-------VGGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 GGAPLSNEIEEFMRvTTCAYFIQGYGLTETLGPSTVCYIDD--MALVGSAGVPatyTEIRLEEvpemgynplgvpsRGEI 473
Cdd:cd05907 219 GGAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDnrIGTVGKPLPG---VEVRIAD-------------DGEI 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 474 CIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWV 552
Cdd:cd05907 282 LVRGPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 553 YGDSfRSSLVAVVNPHQENTMKWAESNGYKG-SFDEICKLEGLKEYILKELAAVAQknKLRGFEYIKGVVLDPVPFDIER 631
Cdd:cd05907 362 IGDG-RPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIEN 438
|
570
....*....|..
gi 226491570 632 DLVTATMKKKRK 643
Cdd:cd05907 439 GELTPTLKLKRP 450
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
75-527 |
9.85e-114 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 347.76 E-value: 9.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 75 VPGPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEI 154
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 155 DVVFIQDKKIKEILSPNCKSAKRLKALVAftsatteqnkeADQIGIKMYAWDDFLKVGKDN-PRQPCPPQASDICTVMYT 233
Cdd:pfam00501 95 KVLITDDALKLEELLEALGKLEVVKLVLV-----------LDRDPVLKEEPLPEEAKPADVpPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 234 SGTSGQPKGVMLTHESHAMYVKGVDLfMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYF-FHKGASIGYYHG----DLNA 308
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKR-VRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGpLLAGATVVLPPGfpalDPAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 309 LRDDIVELKPTLLVGVPRVYERIyegilkaiaelrplrrvifnalynrklasmkagyshktaspfadmLAFRKVKARLGG 388
Cdd:pfam00501 243 LLELIERYKVTVLYGVPTLLNML---------------------------------------------LEAGAPKRALLS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 389 RLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCY--IDDMALVGSAGVPATYTEIRLEEVPEMGYNPLG 466
Cdd:pfam00501 278 SLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLplDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPG 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 467 VPsrGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:pfam00501 358 EP--GELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
83-660 |
9.97e-108 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 341.57 E-value: 9.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILspncksakRLKALVAFTSATTEQNKE----ADQIGIKMYAWDDFLKVGKDNPRQ-PCPPQAS--DICTVMYTSG 235
Cdd:PTZ00216 203 NVPNLL--------RLMKSGGMPNTTIIYLDSlpasVDTEGCRLVAWTDVVAKGHSAGSHhPLNIPENndDLALIMYTSG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 236 TSGQPKGVMLTHESHAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYyhGDLNALRD---- 311
Cdd:PTZ00216 275 TTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfar 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 ---DIVELKPTLLVGVPRvyerIYEGILKAI-AELRP---LRRVIFNALYNRKLASMKAGYShktaSPFADMLAFRKVKA 384
Cdd:PTZ00216 353 phgDLTEFRPVFLIGVPR----IFDTIKKAVeAKLPPvgsLKRRVFDHAYQSRLRALKEGKD----TPYWNEKVFSAPRA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 385 RLGGRLRLLISGGAPLSNEIEEFMRVTTcAYFIQGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRLEEVPEmgYNP 464
Cdd:PTZ00216 425 VLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGGIQRTGDLE-PNAVGQLLKGVEMKLLDTEE--YKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 465 LGVPS-RGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYG 542
Cdd:PTZ00216 501 TDTPEpRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYG 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 543 FPPLV--EDIWVYGDSFRSSLVAVVNPHQENTMKWAESNGYKGSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGV 620
Cdd:PTZ00216 581 QNELVvpNGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHV 660
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 226491570 621 VLDPVPFDIERDLVTATMKKKRknmlnyyqSEIDTIYKKL 660
Cdd:PTZ00216 661 RVLSDEWTPENGVLTAAMKLKR--------RVIDERYADL 692
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
77-642 |
2.25e-85 |
|
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: 275.78 E-value: 2.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAcngyslvcvplydTLGAGAVD---------- 146
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQG-------------IMALGAVDvvrgsdssve 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 147 ---YIIDHAEIDVVFIQDkkikeilSPNcksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppq 223
Cdd:cd17640 68 ellYILNHSESVALVVEN-------DSD---------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 224 asDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDDKMTtdDVFLSFLPLAHILDRMIEEYFFHKGASIGYyh 303
Cdd:cd17640 89 --DLATIIYTSGTTGNPKGVMLTHAN---LLHQIRSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAY-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 304 GDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNALYnrklasmkagyshktaspfadmlafrkvk 383
Cdd:cd17640 160 TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFL----------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 384 arLGGRLRLLISGGAPLSNEIEEFMRVTTCAyFIQGYGLTETlGPSTVCYIDDMALVGSAGVPATYTEIRLeeVPEMGYN 463
Cdd:cd17640 211 --SGGIFKFGISGGGALPPHVDTFFEAIGIE-VLNGYGLTET-SPVVSARRLKCNVRGSVGRPLPGTEIKI--VDPEGNV 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 464 PLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYG 542
Cdd:cd17640 285 VLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALM 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 543 FPPLVEDIWVYGDSFRsSLVAVVNPHQENTMKWAESNGYKGSFDEICKLEGLKE---YILKELAAVAQKNKLRGFEYIKG 619
Cdd:cd17640 365 RSPFIEQIMVVGQDQK-RLGALIVPNFEELEKWAKESGVKLANDRSQLLASKKVlklYKNEIKDEISNRPGFKSFEQIAP 443
|
570 580
....*....|....*....|...
gi 226491570 620 VVLDPVPFdIERDLVTATMKKKR 642
Cdd:cd17640 444 FALLEEPF-IENGEMTQTMKIKR 465
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
83-657 |
7.16e-76 |
|
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: 254.59 E-value: 7.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 ----KIKEILspncKSAKRLKALVAFTSATTEQNkeadqigIKMYAWDDFLKVGKDNP---------RQpcppQASDICT 229
Cdd:cd05933 90 kqlqKILQIQ----DKLPHLKAIIQYKEPLKEKE-------PNLYSWDEFMELGRSIPdeqldaiisSQ----KPNQCCT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 230 VMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqFDDKMTTDDVFLSFLPLAHILDRMIEeyfFHKGASIG--YYHGDLN 307
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMD-LRPATVGQESVVSYLPLSHIAAQILD---IWLPIKVGgqVYFAQPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 308 ALRDDIV----ELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIF----NALYNRKLASMKAGYSHKTASPFADMLAF 379
Cdd:cd05933 231 ALKGTLVktlrEVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLMGGESPSPLFYRLAKKLVF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 380 RKVKARLG-GRLRLLISGGAPLSNEIEEFMRVTTCAYFiQGYGLTETLGPSTVCyIDDMALVGSAGVPATYTEIRLEEVP 458
Cdd:cd05933 311 KKVRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIM-ELYGMSETSGPHTIS-NPQAYRLLSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 459 EMGYnplgvpsrGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVA-VEY 536
Cdd:cd05933 389 ADGI--------GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPpVPI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 537 LEKVYGFPPLVEDIWVYGDS--FRSSLVAV---VNPH--------QENTMKWAESNGYKGS-FDEIC--KLEGLKEYILK 600
Cdd:cd05933 461 EDAVKKELPIISNAMLIGDKrkFLSMLLTLkceVNPEtgepldelTEEAIEFCRKLGSQATrVSEIAggKDPKVYEAIEE 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 601 ELAAVAQKNKLRGFEYIKGVVLDpVPFDIERDLVTATMKKKRKNMLNYYQSEIDTIY 657
Cdd:cd05933 541 GIKRVNKKAISNAQKIQKWVILE-KDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
77-646 |
1.57e-75 |
|
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: 251.23 E-value: 1.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDV 156
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 157 VFIQDKKIKEILSPNCKSAKRLKALVAFTSATTEqnkeadqigikmYAWDDFLKVGkdNPRQPCPPQASD-ICTVMYTSG 235
Cdd:cd05932 82 LFVGKLDDWKAMAPGVPEGLISISLPPPSAANCQ------------YQWDDLIAQH--PPLEERPTRFPEqLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 236 TSGQPKGVMLTHESHAMYV-KGVDLFMDQFDDKMttddvfLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIV 314
Cdd:cd05932 148 TTGQPKGVMLTFGSFAWAAqAGIEHIGTEENDRM------LSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 315 ELKPTLLVGVPRVYERIYEGILKAIaelrPLRRVifnalyNRKLasmkagyshktASPFADMLAFRKVKARLG-GRLRLL 393
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQDKI----PQQKL------NLLL-----------KIPVVNSLVKRKVLKGLGlDQCRLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 394 ISGGAPLSNEIEEFMRvTTCAYFIQGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRLEEvpemgynplgvpsRGEI 473
Cdd:cd05932 281 GCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDK-IGTVGNAGPGVEVRISE-------------DGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 474 CIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWV 552
Cdd:cd05932 346 LVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCV 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 553 YGDSFrSSLVAVVNPHQENTMKwaESNGYKGSFDeicklEGLKEYIlkelaavAQKNK-LRGFEYIKGVVLDPVPFDIER 631
Cdd:cd05932 426 IGSGL-PAPLALVVLSEEARLR--ADAFARAELE-----ASLRAHL-------ARVNStLDSHEQLAGIVVVKDPWSIDN 490
|
570
....*....|....*
gi 226491570 632 DLVTATMKKKRkNML 646
Cdd:cd05932 491 GILTPTLKIKR-NVL 504
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
50-530 |
1.66e-68 |
|
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: 230.85 E-value: 1.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 50 WDVFRVAAVKYADNRML--GWRPFkdgvpgpylwkSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACN 127
Cdd:COG0318 2 ADLLRRAAARHPDRPALvfGGRRL-----------TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 128 GYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIqdkkikeilspncksakrlkalvaftsatteqnkeadqigikmyawdd 207
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 208 flkvgkdnprqpcppqasdiCTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHILDRM 287
Cdd:COG0318 103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG-----LTPGDVVLVALPLFHVFGLT 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 288 IEEYF-FHKGASIgYYHGDLNALR--DDIVELKPTLLVGVPRVYERIyegilkaiaelrpLRRVIFNAlynRKLASmkag 364
Cdd:COG0318 158 VGLLApLLAGATL-VLLPRFDPERvlELIERERVTVLFGVPTMLARL-------------LRHPEFAR---YDLSS---- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 365 yshktaspfadmlafrkvkarlggrLRLLISGGAPLSNE-IEEFMRVTTCAyFIQGYGLTETLGPSTVCYIDDM-ALVGS 442
Cdd:COG0318 217 -------------------------LRLVVSGGAPLPPElLERFEERFGVR-IVEGYGLTETSPVVTVNPEDPGeRRPGS 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 443 AGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKN 522
Cdd:COG0318 271 VGRPLPGVEVRI--VDEDG-RELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKD 347
|
....*...
gi 226491570 523 IFKLSqGE 530
Cdd:COG0318 348 MIISG-GE 354
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
80-580 |
1.19e-63 |
|
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: 221.14 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 80 LWK--SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWI---VAMQACNGYSlvcVPLYDTLGAGAVDYIIDHAEI 154
Cdd:cd17641 8 IWQefTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVwaeLAAQAIGALS---LGIYQDSMAEEVAYLLNYTGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 155 DVVFIQDK----KIKEILSpnckSAKRLKALVAFTSATTEQNKEAdqigiKMYAWDDFLKVGKDNPRQPcpPQA------ 224
Cdd:cd17641 85 RVVIAEDEeqvdKLLEIAD----RIPSVRYVIYCDPRGMRKYDDP-----RLISFEDVVALGRALDRRD--PGLyereva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 225 ----SDICTVMYTSGTSGQPKGVMLTHEshAMYVKGVDLFmdQFDDKMTTDDVFlSFLPLAHILDRMIEEYFFHKGASIG 300
Cdd:cd17641 154 agkgEDVAVLCTTSGTTGKPKLAMLSHG--NFLGHCAAYL--AADPLGPGDEYV-SVLPLPWIGEQMYSVGQALVCGFIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 301 YYHGDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNALY-------NRKLASMKAGYSHKTASPF 373
Cdd:cd17641 229 NFPEEPETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMklglralDRGKRGRPVSLWLRLASWL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 374 ADMLAFRKVKARLG-GRLRLLISGGAPLSNEIEEFMRvttcAYFI---QGYGLTETLGPSTVcYIDDMALVGSAGVPATY 449
Cdd:cd17641 309 ADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFH----AIGVplkQLYGQTELAGAYTV-HRDGDVDPDTVGVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 450 TEIRLEEVpemgynplgvpsrGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQ 528
Cdd:cd17641 384 TEVRIDEV-------------GEILVRSPGVFVGYYKNPEATAEDFDeDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSD 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 226491570 529 GEYVAVEYLEKVYGFPPLVEDIWVYGDSfRSSLVAVVNPHQENTMKWAESNG 580
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRG 501
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
60-636 |
5.99e-62 |
|
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: 216.94 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 60 YADNRMLGWRPFkDGVPGPY--------LWK----SYKEIYDEVLQAGSALQ-KLGVQPGSRVGIYGANCPQWIVAMQAC 126
Cdd:cd17632 35 YADRPALGQRAT-ELVTDPAtgrttlrlLPRfetiTYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 127 NGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQ----DKKIKEILSPNckSAKRL------KALVAFTSATTEQNKEAD 196
Cdd:cd17632 114 TRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSaehlDLAVEAVLEGG--TPPRLvvfdhrPEVDAHRAALESARERLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 197 QIGIKMYAWDDFLKVGKDNPRQPCPPQASD---ICTVMYTSGTSGQPKGVMLTHESHAMYvkGVDLFMDQFDDKMTTddV 273
Cdd:cd17632 192 AVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVATF--WLKVSSIQDIRPPAS--I 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 274 FLSFLPLAHILDRMIEEYFFHKGAsIGYYHG--DLNALRDDIVELKPTLLVGVPRVYERIYEGILkaiAELRplRRVifn 351
Cdd:cd17632 268 TLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQ---AELD--RRS--- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 352 alynrklasmkagyshkTASPFADMLAfRKVKARL-----GGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETl 426
Cdd:cd17632 339 -----------------VAGADAETLA-ERVKAELrervlGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEA- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 427 gpstvcyidDMALVGSAGVPATYTEIRLEEVPEMGYNPLGVP-SRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGD 504
Cdd:cd17632 400 ---------GAVILDGVIVRPPVLDYKLVDVPELGYFRTDRPhPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 505 I-GEMTPDGiLKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSFRSSLVAVVNPHQENTMKWAEsngykg 583
Cdd:cd17632 471 VmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDT------ 543
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 226491570 584 sfdeicklEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERDLVTA 636
Cdd:cd17632 544 --------ARLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLSG 588
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
83-577 |
3.55e-59 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 205.15 E-value: 3.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFiqdk 162
Cdd:cd17631 22 TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqaSDICTVMYTSGTSGQPKG 242
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES-HAMYVKGVdlfmdqFDDKMTTDDVFLSFLPLAHIldrmieeyffhkgASIGYYhgdlnalrddiveLKPTLL 321
Cdd:cd17631 116 AMLTHRNlLWNAVNAL------AALDLGPDDVLLVVAPLFHI-------------GGLGVF-------------TLPTLL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 322 VGVPRVYERIYEG--ILKAIAELRP----LRRVIFNALYNrklasmkagyshktaSPFADMLAFrkvkarlgGRLRLLIS 395
Cdd:cd17631 164 RGGTVVILRKFDPetVLDLIERHRVtsffLVPTMIQALLQ---------------HPRFATTDL--------SSLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 GGAPLSNEIEEFMRVTTCAyFIQGYGLTETLGPSTVCYIDD-MALVGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEIC 474
Cdd:cd17631 221 GGAPMPERLLRALQARGVK-FVQGYGMTETSPGVTFLSPEDhRRKLGSAGRPVFFVEVRI--VDPDG-REVPPGEVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 475 IRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYVA---VEylEKVYGFPPLVEdiw 551
Cdd:cd17631 297 VRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYpaeVE--DVLYEHPAVAE--- 370
|
490 500
....*....|....*....|....*..
gi 226491570 552 vygdsfrsslVAVVN-PHQentmKWAE 577
Cdd:cd17631 371 ----------VAVIGvPDE----KWGE 383
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
83-565 |
9.83e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 206.19 E-value: 9.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEIlspncKSAKRLKALVAFTSATTEqnKEADQIGIKMYAWDDFLKVGKDNPRQPcPPQASDICTVMYTSGTSGQPKG 242
Cdd:PRK06187 113 FVPLL-----AAILPQLPTVRTVIVEGD--GPAAPLAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES---HAMYVKGVDlfmdqfddKMTTDDVFLSFLPLAHIldrmieeyffhkGAS-IGY---YHG---------DL 306
Cdd:PRK06187 185 VVLSHRNlflHSLAVCAWL--------KLSRDDVYLVIVPMFHV------------HAWgLPYlalMAGakqviprrfDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 307 NALRDDIVELKPTLLVGVPRvyerIYEGILKaiaelrplrrvifnalynrklasmkagysHKTAsPFADMlafrkvkarl 386
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVPT----IWQMLLK-----------------------------APRA-YFVDF---------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 387 gGRLRLLISGGAPLSNE-IEEFMRVTTCaYFIQGYGLTETLGPSTVCYIDD-----MALVGSAGVPATYTEIRL-----E 455
Cdd:PRK06187 281 -SSLRLVIYGGAALPPAlLREFKEKFGI-DLVQGYGMTETSPVVSVLPPEDqlpgqWTKRRSAGRPLPGVEARIvdddgD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 456 EVPEMGYnplgvpSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYV-AV 534
Cdd:PRK06187 359 ELPPDGG------EVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIyPR 431
|
490 500 510
....*....|....*....|....*....|..
gi 226491570 535 EyLEKV-YGFPPLVEdiwvygdsfrsslVAVV 565
Cdd:PRK06187 432 E-LEDAlYGHPAVAE-------------VAVI 449
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
193-661 |
1.06e-58 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 210.73 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 193 KEADQIGIKMYAWDDFLKVGKDNPR-QPCPPQAsdICTVMYTSGTSGQPKGVMLTHEshAMYVKGVDLFMDQFDDKMTTD 271
Cdd:PTZ00342 273 EKAKKLGISIILFDDMTKNKTTNYKiQNEDPDF--ITSIVYTSGTSGKPKGVMLSNK--NLYNTVVPLCKHSIFKKYNPK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 272 DvFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFn 351
Cdd:PTZ00342 349 T-HLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLV- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 352 alynRKLASMKAGYSHKTASPFADMLAF--RKVKARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPS 429
Cdd:PTZ00342 427 ----KKILSLRKSNNNGGFSKFLEGITHisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPI 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 430 TVCYIDDMAL--VGSAGVPATYTEIRLEEVpemgYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIG 506
Cdd:PTZ00342 503 FVQHADDNNTesIGGPISPNTKYKVRTWET----YKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIV 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 507 EMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVEDIWVYGDSFRSSLVAVVNPHQE---------NTMKWA- 576
Cdd:PTZ00342 579 QINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYllfkclkddNMLESTg 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 577 --ESNGYKGSFDEICKLEGLKEYILKELAAVAQKNKLRGFEYIKGVVLDPVPFDIERDLvTATMKKKRKNMLNYYQSEID 654
Cdd:PTZ00342 659 inEKNYLEKLTDETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNNYL-TPTFKVKRFYVFKDYAFFID 737
|
....*..
gi 226491570 655 TIYKKLE 661
Cdd:PTZ00342 738 QVKKIYK 744
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
83-642 |
5.76e-58 |
|
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: 202.67 E-value: 5.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqasDICTVMYTSGTSGQPKG 242
Cdd:cd05914 89 D--------------------------------------------------------------DVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVDLFmdqfdDKMTTDDVFLSFLPLAHILDRMIEE-YFFHKGASIgYYHGDL-NALRDDIVELKPTL 320
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEV-----VLLGKGDKILSILPLHHIYPLTFTLlLPLLNGAHV-VFLDKIpSAKIIALAFAQVTP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 321 LVGVPRVYEriyegilkaiaelrpLRRVIFNALYNRKlasMKAGYSHKTASPFADM----LAFRKVKARLGGRLRLLISG 396
Cdd:cd05914 181 TLGVPVPLV---------------IEKIFKMDIIPKL---TLKKFKFKLAKKINNRkirkLAFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 397 GAPLSNEIEEFMRvTTCAYFIQGYGLTETlGPsTVCYIDDMALV-GSAGVPATYTEIRLeevpemgYNPLGVPSRGEICI 475
Cdd:cd05914 243 GAKINPDVEEFLR-TIGFPYTIGYGMTET-AP-IISYSPPNRIRlGSAGKVIDGVEVRI-------DSPDPATGEGEIIV 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 476 RGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLE-KVYGFP-PLVEDIWV 552
Cdd:cd05914 313 RGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEaKINNMPfVLESLVVV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 553 YGDsfRSSLVAVVNPHQENTMKWAESNgykgsfdeicKLEGLKEYILKELaavaqKNKLRGFEYIKGVVLDPVPFDierd 632
Cdd:cd05914 393 QEK--KLVALAYIDPDFLDVKALKQRN----------IIDAIKWEVRDKV-----NQKVPNYKKISKVKIVKEEFE---- 451
|
570
....*....|
gi 226491570 633 lVTATMKKKR 642
Cdd:cd05914 452 -KTPKGKIKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
50-523 |
2.97e-56 |
|
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: 198.17 E-value: 2.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 50 WDVFRVAAVKYADNRMLGWrpfkDGVpgpylWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGY 129
Cdd:cd05936 2 ADLLEEAARRFPDKTALIF----MGR-----KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 130 SLVCVPLYDTLGAGAVDYIIDhaeidvvfiqdkkikeilspNCKSakrlKALVAFTSatteqnkeadqigikmyaWDDFL 209
Cdd:cd05936 73 GAVVVPLNPLYTPRELEHILN--------------------DSGA----KALIVAVS------------------FTDLL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 210 KVGKDnPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqfdDKMTTDDVFLSFLPLAHILDRMIE 289
Cdd:cd05936 111 AAGAP-LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLE---DLLEGDDVVLAALPLFHVFGLTVA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 290 -EYFFHKGASIGYYHG--DLNALrDDIVELKPTLLVGVPrvyeriyegilkaiaelrplrrVIFNALynrklasmkagys 366
Cdd:cd05936 187 lLLPLALGATIVLIPRfrPIGVL-KEIRKHRVTIFPGVP----------------------TMYIAL------------- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 367 hktaspfadmLAFRKVKARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVP 446
Cdd:cd05936 231 ----------LNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIP 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 447 ATYTEIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:cd05936 301 LPGTEVKI--VDDDG-EELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
226-570 |
4.18e-56 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 194.04 E-value: 4.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDlfmdqFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIgYYHGD 305
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALA-----ASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTV-VLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 306 LNA--LRDDIVELKPTLLVGVPRVYERIyegilkaiaelrplrrvifnalynrklasMKAGYSHKTASPfadmlafrkvk 383
Cdd:cd04433 75 FDPeaALELIEREKVTILLGVPTLLARL-----------------------------LKAPESAGYDLS----------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 384 arlggRLRLLISGGAPLSNE-IEEFMRVTTCAyFIQGYGLTETLGPSTVCYIDD-MALVGSAGVPATYTEIRLeeVPEMG 461
Cdd:cd04433 115 -----SLRALVSGGAPLPPElLERFEEAPGIK-LVNGYGLTETGGTVATGPPDDdARKPGSVGRPVPGVEVRI--VDPDG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 462 yNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYVAVEYLEKV- 540
Cdd:cd04433 187 -GELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVl 264
|
330 340 350
....*....|....*....|....*....|...
gi 226491570 541 YGFpPLVEDIWVYG---DSFRSSLVAVVNPHQE 570
Cdd:cd04433 265 LGH-PGVAEAAVVGvpdPEWGERVVAVVVLRPG 296
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
83-524 |
3.47e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 193.58 E-value: 3.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDk 162
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeILSPNCKSAK-RLKALVAFTSATTEQNKEAdqiGIKMYAWDDFLKVGKDNPRQPcPPQASDICTVMYTSGTSGQPK 241
Cdd:PRK07656 111 ----LFLGVDYSATtRLPALEHVVICETEEDDPH---TEKMKTFTDFLAAGDPAERAP-EVDPDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHEShamyvkgvdlFMDQFDD-----KMTTDDVFLSFLPlahildrmieeyFFHkgaSIGYYHGDLNALR------ 310
Cdd:PRK07656 183 GAMLTHRQ----------LLSNAADwaeylGLTEGDRYLAANP------------FFH---VFGYKAGVNAPLMrgatil 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 311 -------DDIVEL----KPTLLVGVPRVYeriyegilkaiaelrplrrvifNALYNrklasmkagysHKTASPFaDMlaf 379
Cdd:PRK07656 238 plpvfdpDEVFRLieteRITVLPGPPTMY----------------------NSLLQ-----------HPDRSAE-DL--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 380 rkvkarlgGRLRLLISGGAPLSNEIEEFMR-------VTTcayfiqGYGLTETLGPSTVCYIDDMALV--GSAGVPATYT 450
Cdd:PRK07656 281 --------SSLRLAVTGAASMPVALLERFEselgvdiVLT------GYGLSEASGVTTFNRLDDDRKTvaGTIGTAIAGV 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 451 EIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIF 524
Cdd:PRK07656 347 ENKI--VNELG-EEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
83-554 |
9.99e-54 |
|
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: 191.66 E-value: 9.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIqDK 162
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT-DP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNCKSAKRLKALVAFTSatteqnKEADQIGIKMyaWDDFLKVGKDNPRQPCPPQ-ASDICTVMYTSGTSGQPK 241
Cdd:cd05911 91 DGLEKVKEAAKELGPKDKIIVLDD------KPDGVLSIED--LLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHEShamYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHIldrmieeyffhkgASIGYYHGdlnalrddivelkpTLL 321
Cdd:cd05911 163 GVCLSHRN---LIANLSQVQTFLYGNDGSNDVILGFLPLYHI-------------YGLFTTLA--------------SLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 322 VGVPRVYERIYEGI--LKAIAElrplRRVIFNALYNRKLASMkagyshkTASPFADmlafrkvKARLGGrLRLLISGGAP 399
Cdd:cd05911 213 NGATVIIMPKFDSElfLDLIEK----YKITFLYLVPPIAAAL-------AKSPLLD-------KYDLSS-LRVILSGGAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 400 LSNEIEEFM-RVTTCAYFIQGYGLTETlGPSTVCYIDDMALVGSAGVPATYTEIRLeeVPEMGYNPLGVPSRGEICIRGK 478
Cdd:cd05911 274 LSKELQELLaKRFPNATIKQGYGMTET-GGILTVNPDGDDKPGSVGRLLPNVEAKI--VDDDGKDSLGPNEPGEICVRGP 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 479 SLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:cd05911 351 QVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
83-577 |
2.53e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 166.26 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeiLSPNCKSAKRLKALVAFTSATTEQNKEADQigiKMYAWDDFLKVGKDNPRQPcPPQASDICTVMYTSGTSGQPKG 242
Cdd:PRK08316 118 -----LAPTAEAALALLPVDTLILSLVLGGREAPG---GWLDFADWAEAGSVAEPDV-ELADDDLAQILYTSGTESLPKG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES-HAMYVKGVdlfmdqFDDKMTTDDVFLSFLPLAHI--LDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPT 319
Cdd:PRK08316 189 AMLTHRAlIAEYVSCI------VAGDMSADDIPLHALPLYHCaqLDVFLGPYLYVGATNVILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 320 LLVGVPRVYeriyegilkaIAELR-PLrrviFNAlynRKLASMKAGYSHKTASPfadmlafRKVKARLGGRLRLLisgga 398
Cdd:PRK08316 263 SFFAPPTVW----------ISLLRhPD----FDT---RDLSSLRKGYYGASIMP-------VEVLKELRERLPGL----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 399 plsneieefmRVTTCayfiqgYGLTEtLGP-STVCYIDD-MALVGSAGVPATYTEIRL-----EEVPEmgynplGVPsrG 471
Cdd:PRK08316 314 ----------RFYNC------YGQTE-IAPlATVLGPEEhLRRPGSAGRPVLNVETRVvdddgNDVAP------GEV--G 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 472 EICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYVA---VEylEKVYGFPPLVE 548
Cdd:PRK08316 369 EIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVAsreVE--EALYTHPAVAE 445
|
490 500 510
....*....|....*....|....*....|
gi 226491570 549 diwvygdsfrsslVAVVN-PHQentmKWAE 577
Cdd:PRK08316 446 -------------VAVIGlPDP----KWIE 458
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
83-577 |
3.61e-43 |
|
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: 163.19 E-value: 3.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIqDK 162
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV-DR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNCKSAKRLKALVAFTSAtteqNKEADQIGIKMYAWDDFLKVG---KDNPRQPcPPQASDICtvmYTSGTSGQ 239
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMTDD----AAMPEPAGVGVLAYEELLAAEspeYDWPDFD-ENTAAAIC---YTSGTTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHES---HAMYVKGVDLFmdqfddKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNAlrDDIVEL 316
Cdd:cd12119 178 PKGVVYSHRSlvlHAMAALLTDGL------GLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDP--ASLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 317 ----KPTLLVGVPRVYERIYEGILKAIAELRPLRRVIfnalynrklasmkagyshktaspfadmlafrkvkarlggrlrl 392
Cdd:cd12119 250 iereGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVV------------------------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 393 lISGGAPLSNEIEEFMRVTTcaYFIQGYGLTETLGPSTVCYI----------DDMALVGSAGVPATYTEIRLEEvPEMGY 462
Cdd:cd12119 287 -IGGSAVPRSLIEAFEERGV--RVIHAWGMTETSPLGTVARPpsehsnlsedEQLALRAKQGRPVPGVELRIVD-DDGRE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 463 NPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYV-AVEyLEKV- 540
Cdd:cd12119 363 LPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWIsSVE-LENAi 440
|
490 500 510
....*....|....*....|....*....|....*...
gi 226491570 541 YGFPPLVEdiwvygdsfrsslVAVVN-PHQentmKWAE 577
Cdd:cd12119 441 MAHPAVAE-------------AAVIGvPHP----KWGE 461
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
83-565 |
1.94e-41 |
|
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: 155.91 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIqdk 162
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqasDICTVMYTSGTSGQPKG 242
Cdd:cd05934 82 ---------------------------------------------------------------DPASILYTSGTTGPPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHeshAMYVKGVDLFMDQFDdkMTTDDVFLSFLPLAHIldrmieeyffhkgasigyyhgdlNALrddIVELKPTLLV 322
Cdd:cd05934 99 VVITH---ANLTFAGYYSARRFG--LGEDDVYLTVLPLFHI-----------------------NAQ---AVSVLAALSV 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 G-----VPRVYERIYegilkaIAELRPLRRVIFNALynrklaSMKAGYSHKTAsPFADMLAfrkvkarlgGRLRLlISGG 397
Cdd:cd05934 148 GatlvlLPRFSASRF------WSDVRRYGATVTNYL------GAMLSYLLAQP-PSPDDRA---------HRLRA-AYGA 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSNEIEEFMRVTTCAyFIQGYGLTETLGPSTVCYiDDMALVGSAGVPATYTEIRLeeVPEMGY-NPLGVPsrGEICIR 476
Cdd:cd05934 205 PNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGPR-DEPRRPGSIGRPAPGYEVRI--VDDDGQeLPAGEP--GELVIR 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 477 ---GKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYGFPPLVEDIWVY 553
Cdd:cd05934 279 glrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVV 357
|
490
....*....|....
gi 226491570 554 G--DSFRSSLVAVV 565
Cdd:cd05934 358 AvpDEVGEDEVKAV 371
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
83-512 |
4.26e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 157.97 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACngYSL--VCVPLYDTLGAGAVDYIIDHAEIDVVFIQ 160
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLAC--ARIgaVHSPVFPGFGAEALADRIEDAEAKVLITA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 161 D------KKI--KEILSPNCKSAKRLKALVAFTSATTEQNKEADqigikmYAWDDFLkvgkDNPRQPCPP---QASDICT 229
Cdd:COG0365 119 DgglrggKVIdlKEKVDEALEELPSLEHVIVVGRTGADVPMEGD------LDWDELL----AAASAEFEPeptDADDPLF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 230 VMYTSGTSGQPKGVMLTHES----HAMYVKGVdlfmdqFDdkMTTDDVFLS--------------FLPLAHildrmieey 291
Cdd:COG0365 189 ILYTSGTTGKPKGVVHTHGGylvhAATTAKYV------LD--LKPGDVFWCtadigwatghsyivYGPLLN--------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 292 ffhkGASIGYYHG-----DLNALRDDIVELKPTLLVGVPRVYeriyegilkaiaelrplrrvifnalynRKLasMKAGYS 366
Cdd:COG0365 252 ----GATVVLYEGrpdfpDPGRLWELIEKYGVTVFFTAPTAI---------------------------RAL--MKAGDE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 367 HKTASPFAdmlafrkvkarlggRLRLLISGGAPLSNE-IEEFMRVTTCAyFIQGYGLTETLGPsTVCYIDDMALV-GSAG 444
Cdd:COG0365 299 PLKKYDLS--------------SLRLLGSAGEPLNPEvWEWWYEAVGVP-IVDGWGQTETGGI-FISNLPGLPVKpGSMG 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226491570 445 VPATYTEIRLeeVPEMGyNPLGVPSRGEICIRGK--SLFAGYYKSPELTNEAIVD---GWFHTGDIGEMTPDG 512
Cdd:COG0365 363 KPVPGYDVAV--VDEDG-NPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDG 432
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
83-604 |
7.93e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 157.47 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCV---PLYDTL---------GAGAV---DY 147
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAHelehpfedhGARVAivwDK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 148 IIDHAEIDVvfiQDKKIKEILSPNCKSA----KRLKALVAFTSATTEQNK---EADQIgikmYAWDDFLK--VGKDNPRQ 218
Cdd:PRK05605 139 VAPTVERLR---RTTPLETIVSVNMIAAmpllQRLALRLPIPALRKARAAltgPAPGT----VPWETLVDaaIGGDGSDV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 219 PCP-PQASDICTVMYTSGTSGQPKGVMLTH---ESHAM----YVKGVDlfmDQfddkmttDDVFLSFLPLAHILDRMIEE 290
Cdd:PRK05605 212 SHPrPTPDDVALILYTSGTTGKPKGAQLTHrnlFANAAqgkaWVPGLG---DG-------PERVLAALPMFHAYGLTLCL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 291 YFfhkGASIGyyhGDLNAL-RDDIVEL-------KPTLLVGVPRVYERIyegiLKAIAElrplRRVifnalynrKLASMK 362
Cdd:PRK05605 282 TL---AVSIG---GELVLLpAPDIDLIldamkkhPPTWLPGVPPLYEKI----AEAAEE----RGV--------DLSGVR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 363 agYShktaspfadmlafrkvkarlggrlrllISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETlGPSTVCY-IDDMALVG 441
Cdd:PRK05605 340 --NA---------------------------FSGAMALPVSTVELWEKLTGGLLVEGYGLTET-SPIIVGNpMSDDRRPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 442 SAGVPATYTEIRLEEvPEmgyNP---LGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVID 518
Cdd:PRK05605 390 YVGVPFPDTEVRIVD-PE---DPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 519 RKKNI-----FKLSQGEyvaveyLEKVYGFPPLVEDIWVYG---DSFRSSLVAVVNPHQENTmkwaesngykgsFDEick 590
Cdd:PRK05605 466 RIKELiitggFNVYPAE------VEEVLREHPGVEDAAVVGlprEDGSEEVVAAVVLEPGAA------------LDP--- 524
|
570
....*....|....
gi 226491570 591 lEGLKEYILKELAA 604
Cdd:PRK05605 525 -EGLRAYCREHLTR 537
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
80-646 |
2.90e-38 |
|
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: 148.22 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 80 LWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFi 159
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 qdkkikeilspncksakrlkalvaftsatteqnkeADQigikMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQ 239
Cdd:cd12118 107 -----------------------------------VDR----EFEYEDLLAEGDPDFEWIPPADEWDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHEShaMYVKGVDlfmDQFDDKMTTDDVFLSFLPLahildrmieeyfFH-------------KGASIGYYHGDL 306
Cdd:cd12118 148 PKGVVYHHRG--AYLNALA---NILEWEMKQHPVYLWTLPM------------FHcngwcfpwtvaavGGTNVCLRKVDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 307 NALRDDIVELKPTLLVGVPRVyeriyegiLKAIAELRPLRRVIFNalynRKLASMKAGyshktASPFADMLAfrKVKaRL 386
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTV--------LNMLANAPPSDARPLP----HRVHVMTAG-----APPPAAVLA--KME-EL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 387 GGRLrllisggaplsneieefmrvttcayfIQGYGLTETLGPSTVCY---------IDDMA-LVGSAGVPAtyteIRLEE 456
Cdd:cd12118 271 GFDV--------------------------THVYGLTETYGPATVCAwkpewdelpTEERArLKARQGVRY----VGLEE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 457 VpeMGYNPLG---VP----SRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQG 529
Cdd:cd12118 321 V--DVLDPETmkpVPrdgkTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 530 EYVAVEYLEKV-YGFPPLVEdiwvygdsfrsslVAVV-NPHQentmKWAES--------NGYKGSFDEICKLeglkeyil 599
Cdd:cd12118 398 ENISSVEVEGVlYKHPAVLE-------------AAVVaRPDE----KWGEVpcafvelkEGAKVTEEEIIAF-------- 452
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 226491570 600 kelaavaQKNKLRGFEYIKGVVLDPVPfdierdlVTATmKKKRKNML 646
Cdd:cd12118 453 -------CREHLAGFMVPKTVVFGELP-------KTST-GKIQKFVL 484
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
75-523 |
4.25e-38 |
|
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: 147.84 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 75 VPGPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEI 154
Cdd:cd05926 8 VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 155 DVVFIQdkkiKEILSPNCKSAKRLKAL---VAFTSATTEQNKEADQIGikmyawddFLKVGKDNPRQPCPPQASDICTVM 231
Cdd:cd05926 88 KLVLTP----KGELGPASRAASKLGLAileLALDVGVLIRAPSAESLS--------NLLADKKNAKSEGVPLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 232 YTSGTSGQPKGVMLTHESHAMYVKGVdlfmdQFDDKMTTDDVFLSFLPLAHI--LDRMIEEYFFHKGASIGYYHGDLNAL 309
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASATNI-----TNTYKLTPDDRTLVVMPLFHVhgLVASLLSTLAAGGSVVLPPRFSASTF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 310 RDDIVELKPTLLVGVPrvyeriyegilkaiaelrplrrVIFNALYNRKLAsmkagyshKTASPFAdmlafrkvkarlggR 389
Cdd:cd05926 231 WPDVRDYNATWYTAVP----------------------TIHQILLNRPEP--------NPESPPP--------------K 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYID-DMALVGSAGVPATyTEIRLeeVPEMGYN-PLGV 467
Cdd:cd05926 267 LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLPpGPRKPGSVGKPVG-VEVRI--LDEDGEIlPPGV 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 468 psRGEICIRGKSLFAGYYKSPELTNE-AIVDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:cd05926 344 --VGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRIKEL 398
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
202-525 |
1.03e-36 |
|
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: 144.30 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 202 MYAWDDFLKVGKDNPRQPCPPQaSDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDDKMTTDDVFLSFLPLA 281
Cdd:cd05904 136 LSFSDLLFEADEAEPPVVVIKQ-DDVAALLYSSGTTGRSKGVMLTHRN---LIAMVAQFVAGEGSNSDSEDVFLCVLPMF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 282 HIldrmieeyffhkgasigyyHGdLNALRDDIVELKPTLLVgVPRvYEriYEGILKAIAElrplRRVifnalynrklasm 361
Cdd:cd05904 212 HI-------------------YG-LSSFALGLLRLGATVVV-MPR-FD--LEELLAAIER----YKV------------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 362 kagySHKTASP--FADMLAFRKVKARLGGRLRLLISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMA 438
Cdd:cd05904 251 ----THLPVVPpiVLALVKSPIVDKYDLSSLRQIMSGAAPLGKElIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 439 LV--GSAGVPATYTEIRLEEvPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILK 515
Cdd:cd05904 327 RAkyGSVGRLVPNVEAKIVD-PETG-ESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLF 404
|
330
....*....|
gi 226491570 516 VIDRKKNIFK 525
Cdd:cd05904 405 IVDRLKELIK 414
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
83-554 |
1.00e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 141.15 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQ-KLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQD 161
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 KKIKEILSPNCKSAkrLKALVAFTSATteqnkeadqiGIKMYAWDDFLKVGKDNPRQPCppqasdictvmYTSGTSGQPK 241
Cdd:PRK06839 109 TFQNMALSMQKVSY--VQRVISITSLK----------EIEDRKIDNFVEKNESASFIIC-----------YTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHEShaMYVKGVDlfmDQFDDKMTTDDVFLSFLPLAHI--LDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPT 319
Cdd:PRK06839 166 GAVLTQEN--MFWNALN---NTFAIDLTMHDRSIVLLPLFHIggIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 320 LLVGVPRVYERIYEGILKAIAELRplrrvifnalynrklasmkagyshktaspfadmlafrkvkarlggRLRLLISGGAP 399
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETTNLQ---------------------------------------------SVRWFYNGGAP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 400 LSNE-IEEFMRvtTCAYFIQGYGLTETlGPSTVCYIDDMAL--VGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIR 476
Cdd:PRK06839 276 CPEElMREFID--RGFLFGQGFGMTET-SPTVFMLSEEDARrkVGSIGKPVLFCDYEL--IDENK-NKVEVGEVGELLIR 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 477 GKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:PRK06839 350 GPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
82-554 |
1.57e-35 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 139.02 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 82 KSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACngyslvcvplydtLGAGAVdyiidhaeidVVFIQD 161
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHAL-------------WLLGAE----------AVLLNT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 KkikeiLSPNcksakrlkalvaftsATTEQNKEADqigikmyawddflkvgkdnprqpcpPQASDICTVMYTSGTSGQPK 241
Cdd:cd05912 59 R-----LTPN---------------ELAFQLKDSD-------------------------VKLDDIATIMYTSGTTGKPK 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHIldrmieeyffhKGASIgyyhgdlnalrddiveLKPTLL 321
Cdd:cd05912 94 GVQQTFGNHWWSAIGSALNLG-----LTEDDNWLCALPLFHI-----------SGLSI----------------LMRSVI 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 322 VGVP-RVYERIYEgilkaiaelrplrRVIFNALYNRKLASMkagyshktaSPFADMLAfrKVKARLGGR----LRLLISG 396
Cdd:cd05912 142 YGMTvYLVDKFDA-------------EQVLHLINSGKVTII---------SVVPTMLQ--RLLEILGEGypnnLRCILLG 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 397 GAPLSNEIEEfmrvtTCAY----FIQGYGLTETLGPSTVCYIDDMAL-VGSAGVPATYTEIRLEEVpemGYNPLGVpsrG 471
Cdd:cd05912 198 GGPAPKPLLE-----QCKEkgipVYQSYGMTETCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDD---GQPPYEV---G 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 472 EICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDIW 551
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAG 345
|
...
gi 226491570 552 VYG 554
Cdd:cd05912 346 VVG 348
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
83-544 |
2.68e-34 |
|
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: 136.04 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIdhAEIDVVFIqdk 162
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQL--EDLDVQLL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeiLSPNCKSAKRLKALVAftSATTEQNKEADQIGIKMyawddflkvgkdnprqpcppQASDICTVMYTSGTSGQPKG 242
Cdd:TIGR01923 76 -----LTDSLLEEKDFQADSL--DRIEAAGRYETSLSASF--------------------NMDQIATLMFTSGTTGKPKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVDLFMdQFDDkmttDDVFLSFLPLAHILDRMIEEYFFHKGASIgYYHGDLNALRDDIVELKPTLLV 322
Cdd:TIGR01923 129 VPHTFRNHYASAVGSKENL-GFTE----DDNWLLSLPLYHISGLSILFRWLIEGATL-RIVDKFNQLLEMIANERVTHIS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 GVPRVYERIYEgilkaiAELRPLRrvifnalynrklasmkagyshktaspfadmlafrkvkarlggrLRLLISGGAPLSN 402
Cdd:TIGR01923 203 LVPTQLNRLLD------EGGHNEN-------------------------------------------LRKILLGGSAIPA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 403 E-IEEFMRVTTCAYfiQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLEEVPEMGYnplgvpsrGEICIRGKSLF 481
Cdd:TIGR01923 234 PlIEEAQQYGLPIY--LSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH--------GEIMVKGANLM 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 482 AGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKV-YGFP 544
Cdd:TIGR01923 304 KGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVlYQHP 366
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
50-521 |
5.55e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 136.63 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 50 WDVFRVAAVKYADNrmlgwrpfkdgvpgPYLW-----KSYKEIYDEVLQ-AGSALQKLGVQPGSRVGIYGANCPQWIVAM 123
Cdd:PRK08314 13 FHNLEVSARRYPDK--------------TAIVfygraISYRELLEEAERlAGYLQQECGVRKGDRVLLYMQNSPQFVIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 124 QACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFI-QDkkikeiLSPNCKSAK---RLKALVA--FTSATTEQNKEA-- 195
Cdd:PRK08314 79 YAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVgSE------LAPKVAPAVgnlRLRHVIVaqYSDYLPAEPEIAvp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 196 ----------DQIGIKMYAWDDFLKVGKDNPrqPCPPQASDICTVMYTSGTSGQPKGVMLTHES-HAMYVKGVDLFMdqf 264
Cdd:PRK08314 153 awlraepplqALAPGGVVAWKEALAAGLAPP--PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTvMANAVGSVLWSN--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 265 ddkMTTDDVFLSFLPLAHILdrmieeyffhkgasiGYYHGdLNALrddiVELKPTLLVgVPRvYERiyegilKAIAELRP 344
Cdd:PRK08314 228 ---STPESVVLAVLPLFHVT---------------GMVHS-MNAP----IYAGATVVL-MPR-WDR------EAAARLIE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 345 LRRVifnalynrklasmkagySHKTASP--FADMLAFRKVKARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGL 422
Cdd:PRK08314 277 RYRV-----------------THWTNIPtmVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 423 TETLGPSTV---------CyiddmalvgsAGVPATYTEIRLEEvPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNE 493
Cdd:PRK08314 340 TETMAQTHSnppdrpklqC----------LGIPTFGVDARVID-PETL-EELPPGEVGEIVVHGPQVFKGYWNRPEATAE 407
|
490 500 510
....*....|....*....|....*....|..
gi 226491570 494 AIV--DG--WFHTGDIGEMTPDGILKVIDRKK 521
Cdd:PRK08314 408 AFIeiDGkrFFRTGDLGRMDEEGYFFITDRLK 439
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
83-604 |
1.61e-33 |
|
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: 133.57 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQ-KLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDhaeidvvfiqD 161
Cdd:cd05941 13 TYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT----------D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 KKIKEILspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqasDICTVMYTSGTSGQPK 241
Cdd:cd05941 83 SEPSLVL---------------------------------------------------------DPALILYTSGTTGRPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHESHAMYVKG-VDLFmdqfddKMTTDDVFLSFLPLAHIldrmieeyffH-----------KGASIgYYHGDLNAL 309
Cdd:cd05941 106 GVVLTHANLAANVRAlVDAW------RWTEDDVLLHVLPLHHV----------HglvnallcplfAGASV-EFLPKFDPK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 310 RDDIVELKP--TLLVGVPRVYERIYEGilkaiaelrplrrvifnalYNRKlasmkagyshktaspFADMLAFRKVKARlg 387
Cdd:cd05941 169 EVAISRLMPsiTVFMGVPTIYTRLLQY-------------------YEAH---------------FTDPQFARAAAAE-- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 388 gRLRLLISGGAPLSNEI-EEFMRVTTCAyFIQGYGLTETlGPSTVCYIDDMALVGSAGVPATYTEIRLeeVPEMGYNPLG 466
Cdd:cd05941 213 -RLRLMVSGSAALPVPTlEEWEAITGHT-LLERYGMTEI-GMALSNPLDGERRPGTVGMPLPGVQARI--VDEETGEPLP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 467 VPSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKK-NIFKlSQGEYV-AVEYLEKVYGF 543
Cdd:cd05941 288 RGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVsALEIERVLLAH 366
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 544 PPLVEdIWVYG---DSFRSSLVAVVNPHQENTMKwaesngykgsfdeicKLEGLKEYILKELAA 604
Cdd:cd05941 367 PGVSE-CAVIGvpdPDWGERVVAVVVLRAGAAAL---------------SLEELKEWAKQRLAP 414
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-604 |
6.90e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 133.62 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQA---CNGYSLVCVPLYDTLgagAVDYIIDHAEIDVVFI 159
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGtllAGGIVVQTNPLYTER---ELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 QDKKIKEIlsPNCKSAKRLKALVAFTSATT-----------EQNKEADQI-----GIKMYAWDDFLKVGKDNPRQPCPPQ 223
Cdd:PRK06710 128 LDLVFPRV--TNVQSATKIEHVIVTRIADFlpfpknllypfVQKKQSNLVvkvseSETIHLWNSVEKEVNTGVEVPCDPE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 224 aSDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDDKMTTDDVFLSFLPlahildrmieeyFFHkgasigyYH 303
Cdd:PRK06710 206 -NDLALLQYTGGTTGFPKGVMLTHKN---LVSNTLMGVQWLYNCKEGEEVVLGVLP------------FFH-------VY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 304 GDLNALRDDIVELKPTLLVgvPRV-YERIYEGILKAIAELRPLRRVIFNALYNRKLasmkagyshktaspfadmlafrkV 382
Cdd:PRK06710 263 GMTAVMNLSIMQGYKMVLI--PKFdMKMVFEAIKKHKVTLFPGAPTIYIALLNSPL-----------------------L 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 383 KARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLEEVPEMGY 462
Cdd:PRK06710 318 KEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 463 NPLGvpSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVaveylekvyg 542
Cdd:PRK06710 398 LPPG--EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNV---------- 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 543 FPPLVEDIWVYGDSFRSSLV-AVVNPHQENTMKwaesngykgSF-----DEICKLEGLKEYILKELAA 604
Cdd:PRK06710 465 YPREVEEVLYEHEKVQEVVTiGVPDPYRGETVK---------AFvvlkeGTECSEEELNQFARKYLAA 523
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
82-554 |
1.44e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 131.62 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 82 KSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFiqd 161
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLI--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 kkikeilspncksakrlkalvaftsatTEQNKEADQIGIKMYAWDDFLKVgkdnPRQPCPPQA----SDICTVMYTSGTS 237
Cdd:PRK03640 105 ---------------------------TDDDFEAKLIPGISVKFAELMNG----PKEEAEIQEefdlDEVATIMYTSGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHIldrmieeyffhKGASIgyyhgdlnalrddiveLK 317
Cdd:PRK03640 154 GKPKGVIQTYGNHWWSAVGSALNLG-----LTEDDCWLAAVPIFHI-----------SGLSI----------------LM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 318 PTLLVGVPRVYERIY--EGILKAIAElrplRRVifnalynrklasmkagyshKTASPFADMLAfrKVKARLGGR-----L 390
Cdd:PRK03640 202 RSVIYGMRVVLVEKFdaEKINKLLQT----GGV-------------------TIISVVSTMLQ--RLLERLGEGtypssF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 391 RLLISGGAPLSNEIEEfmrvtTCAY----FIQGYGLTETlgPSTVCYI--DDMAL-VGSAGVPATYTEIRLEEvpemGYN 463
Cdd:PRK03640 257 RCMLLGGGPAPKPLLE-----QCKEkgipVYQSYGMTET--ASQIVTLspEDALTkLGSAGKPLFPCELKIEK----DGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 464 PLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGF 543
Cdd:PRK03640 326 VVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLS 404
|
490
....*....|.
gi 226491570 544 PPLVEDIWVYG 554
Cdd:PRK03640 405 HPGVAEAGVVG 415
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
83-588 |
4.69e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 131.05 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 -------KIKEILSPNCKSAK----------RLKALVAFTSATTEQnkeadqigikMYAWDDFLKVGKDNPRQPCPP--- 222
Cdd:PRK12583 127 fktsdyhAMLQELLPGLAEGQpgalacerlpELRGVVSLAPAPPPG----------FLAWHELQARGETVSREALAErqa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 --QASDICTVMYTSGTSGQPKGVMLTHES--HAMYVKGVDLfmdqfddKMTTDDVFLSFLPLAHILDRMIEEYF-FHKGA 297
Cdd:PRK12583 197 slDRDDPINIQYTSGTTGFPKGATLSHHNilNNGYFVAESL-------GLTEHDRLCVPVPLYHCFGMVLANLGcMTVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 298 SIGY--YHGDLNALRDDIVELKPTLLVGVPRVYeriyegilkaIAELRPLRRVIFNalynrkLASMKAGyshktaspfad 375
Cdd:PRK12583 270 CLVYpnEAFDPLATLQAVEEERCTALYGVPTMF----------IAELDHPQRGNFD------LSSLRTG----------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 376 mlafrkvkarlggrlrllISGGAPLSNEI-EEFMRVTTCAYFIQGYGLTETLGPST-VCYIDDMAL-VGSAGVPATYTEI 452
Cdd:PRK12583 323 ------------------IMAGAPCPIEVmRRVMDEMHMAEVQIAYGMTETSPVSLqTTAADDLERrVETVGRTQPHLEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 453 RLEEvPEMGYNPLGvpSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEY 531
Cdd:PRK12583 385 KVVD-PDGATVPRG--EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGEN 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 532 VAVEYLEKVYGFPPLVEDIWVYG--DSFrsslvavvnpHQENTMKWAE-SNGYKGSFDEI 588
Cdd:PRK12583 461 IYPREIEEFLFTHPAVADVQVFGvpDEK----------YGEEIVAWVRlHPGHAASEEEL 510
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
81-548 |
5.26e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 130.31 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 81 WkSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAgavdyiidhAEIDVVfIQ 160
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA---------SELDAL-LQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 161 DKKIKEILSPNCKSAKRLK--ALVAFTSatteqnkEADQIGIkmyawddflkvgkdNPRQPCPPQASDIctVMYTSGTSG 238
Cdd:PRK09088 92 DAEPRLLLGDDAVAAGRTDveDLAAFIA-------SADALEP--------------ADTPSIPPERVSL--ILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLT-----HESHAMYVKGvdlfmdqfddKMTTDDVFLSFLPLAHIldrmieeyffhkgasIGYyhgdlnalrddI 313
Cdd:PRK09088 149 QPKGVMLSernlqQTAHNFGVLG----------RVDAHSSFLCDAPMFHI---------------IGL-----------I 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 314 VELKPTLLVGvprvyeriyeGILKAIAELRPLRRvifnalyNRKLASMKAGYSHKTASP-FADML----AFRKvkARLGg 388
Cdd:PRK09088 193 TSVRPVLAVG----------GSILVSNGFEPKRT-------LGRLGDPALGITHYFCVPqMAQAFraqpGFDA--AALR- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 389 RLRLLISGGAPLSNE-----IEEFMRVttcayfIQGYGLTET---LGPSTVCYIDDmALVGSAGVPATYTEIRLeeVPEM 460
Cdd:PRK09088 253 HLTALFTGGAPHAAEdilgwLDDGIPM------VDGFGMSEAgtvFGMSVDCDVIR-AKAGAAGIPTPTVQTRV--VDDQ 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 461 GYN-PLGVPsrGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLE 538
Cdd:PRK09088 324 GNDcPAGVP--GELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
490
....*....|.
gi 226491570 539 KVYG-FPPLVE 548
Cdd:PRK09088 401 AVLAdHPGIRE 411
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
83-565 |
5.81e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.01 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrLKALVAFtsatteqnkEADQIGIKMYAWDDFLKVGKdnPRQPCPPQA----SDICTVMYTSGTSG 238
Cdd:PRK06145 109 ---------------FDAIVAL---------ETPKIVIDAAAQADSRRLAQ--GGLEIPPQAavapTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHEShaMYVKGVDLFMDQfddKMTTDDVFLSFLPLAHIldrmieEYFFHKGASIGYYHGDLNALRDdiveLKP 318
Cdd:PRK06145 163 RPKGVMHSYGN--LHWKSIDHVIAL---GLTASERLLVVGPLYHV------GAFDLPGIAVLWVGGTLRIHRE----FDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 tllvgvprvyeriyEGILKAIAELRPLRRVIFNALYNRKLASmkagyshktasPFADMLAFrkvkarlgGRLRLLISGG- 397
Cdd:PRK06145 228 --------------EAVLAAIERHRLTCAWMAPVMLSRVLTV-----------PDRDRFDL--------DSLAWCIGGGe 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 -APLSnEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYID-DMALVGSAGVPATYTEIRLEEvPEMGYNPLGVpsRGEICI 475
Cdd:PRK06145 275 kTPES-RIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGrEIEKIGSTGRALAHVEIRIAD-GAGRWLPPNM--KGEICM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 476 RGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKV-YGFPPLVED--IWV 552
Cdd:PRK06145 351 RGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERViYELPEVAEAavIGV 429
|
490
....*....|...
gi 226491570 553 YGDSFRSSLVAVV 565
Cdd:PRK06145 430 HDDRWGERITAVV 442
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
83-514 |
1.08e-31 |
|
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: 127.77 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQ-AGSALQKLGVQPGSRVGIYGANCPQWIVAMQACngysL----VCVPLYDTLGAGAVDYIIDHAEIDVV 157
Cdd:TIGR01733 1 TYRELDERANRlARHLRAAGGVGPGDRVAVLLERSAELVVAILAV----LkagaAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 158 FiqdkkikeilspncksakrlkalvaftsATTEQNKEADQIGIKMYAWD-DFLKVGKDNPRQPCP---PQASDICTVMYT 233
Cdd:TIGR01733 77 L----------------------------TDSALASRLAGLVLPVILLDpLELAALDDAPAPPPPdapSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 234 SGTSGQPKGVMLTHESHAMYVKGvdlfMDQFDDkMTTDDVFLSFLPLAHilDRMIEEYFfhkgasigyyhgdlnalrddi 313
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAW----LARRYG-LDPDDRVLQFASLSF--DASVEEIF--------------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 314 velkPTLLVGVPRVYerIYEGILKAIAELrpLRRVIfnalynrklASMKAGYSHKTASPFADMLAfrkVKARLGGRLRLL 393
Cdd:TIGR01733 181 ----GALLAGATLVV--PPEDEERDDAAL--LAALI---------AEHPVTVLNLTPSLLALLAA---ALPPALASLRLV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 394 ISGG-APLSNEIEEFMRVTTCAYFIQGYGLTETlgpsTVC-----YIDDMALVGSA---GVPATYTEIRLEEvPEMGYNP 464
Cdd:TIGR01733 241 ILGGeALTPALVDRWRARGPGARLINLYGPTET----TVWstatlVDPDDAPRESPvpiGRPLANTRLYVLD-DDLRPVP 315
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 465 LGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWF---------HTGDIGEMTPDGIL 514
Cdd:TIGR01733 316 VGVV--GELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRTGDLVRYLPDGNL 372
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
83-554 |
1.76e-30 |
|
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: 124.80 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkVGKDNPRqpcpPQASDICTVMYTSGTSGQPKG 242
Cdd:cd05903 83 ------------------------------------------------FRQFDPA----AMPDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES-HA---MYVKGVDLfmdqfddkmTTDDVFLSFLPLAHIldrmieeyffhkgasIGYYHGdlnalrddiVELkP 318
Cdd:cd05903 111 VMHSHNTlSAsirQYAERLGL---------GPGDVFLVASPMAHQ---------------TGFVYG---------FTL-P 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 TLLvGVPRVYERIYEGIlKAIAELRPLRRVIFNAlynrklasmkagyshktASPF-ADMLAFRKVKARLGGRLRLLISGG 397
Cdd:cd05903 157 LLL-GAPVVLQDIWDPD-KALALMREHGVTFMMG-----------------ATPFlTDLLNAVEEAGEPLSRLRTFVCGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSNEIEEfmRVTTC--AYFIQGYGLTETLGPSTVCYIDD-MALVGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEIC 474
Cdd:cd05903 218 ATVPRSLAR--RAAELlgAKVCSAYGSTECPGAVTSITPAPeDRRLYTDGRPLPGVEIKV--VDDTG-ATLAPGVEGELL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 475 IRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
83-527 |
4.38e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 125.13 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAC--NGYSLVCV-PLY----------DTlGAGAVDYII 149
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVlrAGYVVVNVnPLYtprelehqlkDS-GAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 150 DHAEIDVVFIQDKKIKEILSPNCKSAKRLK-ALVAFTSATTEqnkeadqigiKMY-AW--------DDFLKVGKDNPRQP 219
Cdd:PRK07059 129 NFATTVQQVLAKTAVKHVVVASMGDLLGFKgHIVNFVVRRVK----------KMVpAWslpghvrfNDALAEGARQTFKP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 220 CPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDQFDDKMTTDD--VFLSFLPLAHILDRMIeeyffhkGA 297
Cdd:PRK07059 199 VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDqlNFVCALPLYHIFALTV-------CG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 298 SIGYYHGDLNalrddivelkptLLVGVPRvyeriyeGILKAIAELRPLRRVIF---NALYNrklASMKagyshktaSPFA 374
Cdd:PRK07059 272 LLGMRTGGRN------------ILIPNPR-------DIPGFIKELKKYQVHIFpavNTLYN---ALLN--------NPDF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 375 DMLAFRKVKARLGGrlrllisGGAPLSNEIEEFMRVTTCAyFIQGYGLTETlGPSTVCY-IDDMALVGSAGVP--ATYTE 451
Cdd:PRK07059 322 DKLDFSKLIVANGG-------GMAVQRPVAERWLEMTGCP-ITEGYGLSET-SPVATCNpVDATEFSGTIGLPlpSTEVS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 452 IRLEEVPEMgynPLGVPsrGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:PRK07059 393 IRDDDGNDL---PLGEP--GEICIRGPQVMAGYWNRPDETAKVMTaDGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
83-548 |
1.11e-29 |
|
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: 122.20 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIqdk 162
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsaTTEQNkeadqigikmyawddflkvgkdnprqpcppqasDICTVMYTSGTSGQPKG 242
Cdd:cd05935 80 -------------------------GSELD---------------------------------DLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVdlfmdQFDDKMTTDDVFLSFLPLAHILDrmieeyffhkgasigyYHGDLNAlrddivelkptllv 322
Cdd:cd05935 102 CMHTHFSAAANALQS-----AVWTGLTPSDVILACLPLFHVTG----------------FVGSLNT-------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 gvprvyeRIYEGilkaiaelrplRRVIFNALYNRKLAS---MKAGYSHKTASPFA--DMLAFRKVKARLGGRLRLLISGG 397
Cdd:cd05935 147 -------AVYVG-----------GTYVLMARWDRETALeliEKYKVTFWTNIPTMlvDLLATPEFKTRDLSSLKVLTGGG 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVcyiDDMALVGSA--GVPATYTEIRLEEvPEMGyNPLGVPSRGEICI 475
Cdd:cd05935 209 APMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT---NPPLRPKLQclGIP*FGVDARVID-IETG-RELPPNEVGEIVV 283
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 476 RGKSLFAGYYKSPELTNEAI--VDG--WFHTGDIGEMTPDGILKVIDRKKNIFKLSQGEYVAVEYLEKVYGFPPLVE 548
Cdd:cd05935 284 RGPQIFKGYWNRPEETEESFieIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E 360
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
83-530 |
1.48e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 123.52 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVfIQDK 162
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL-IVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNCKSAKRLKALVafTSATTEQNKEADQIGIKMYawDDFLKVGkDNPRQPCPPQAS-DICTVMYTSGTSGQPK 241
Cdd:PRK08162 124 EFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIGALDY--EAFLASG-DPDFAWTLPADEwDAIALNYTSGTTGNPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLahildrmieeyfFH-------------KGASIGYYHGDLNA 308
Cdd:PRK08162 199 GVVYHHRGAYLNALSNILAWG-----MPKHPVYLWTLPM------------FHcngwcfpwtvaarAGTNVCLRKVDPKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 309 LRDDIVELKPTLLVGVPRVYeriyegilkaiaelrplrrvifNALYNRKlASMKAGYSHKtaspfadmlafrkVKArlgg 388
Cdd:PRK08162 262 IFDLIREHGVTHYCGAPIVL----------------------SALINAP-AEWRAGIDHP-------------VHA---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 389 rlrlLISGGAPLSNEIE--EFM--RVTtcayfiQGYGLTETLGPSTVCY---------IDDMA-LVGSAGV--------- 445
Cdd:PRK08162 302 ----MVAGAAPPAAVIAkmEEIgfDLT------HVYGLTETYGPATVCAwqpewdalpLDERAqLKARQGVryplqegvt 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 446 ---PATyteirLEEVPEMGynplgvPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKN 522
Cdd:PRK08162 372 vldPDT-----MQPVPADG------ETIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKD 440
|
....*...
gi 226491570 523 IFkLSQGE 530
Cdd:PRK08162 441 II-ISGGE 447
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
88-538 |
2.51e-29 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 122.05 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 88 YDEVLQAGSALQKL---GVQPGSRVGIY---GANCPQWIVAMQAcNGYslVCVPLYDTLGAGAVDYIIDHAEIDVVFIQD 161
Cdd:cd05909 10 YRKLLTGAIALARKlakMTKEGENVGVMlppSAGGALANFALAL-SGK--VPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 ---KKIKEILSPNCKSAKRLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKVGKdNPRQPcppqaSDICTVMYTSGTSG 238
Cdd:cd05909 87 qfiEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPKWLLRIFGV-APVQP-----DDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHEShamYVKGVDLFMDQFDdkMTTDDVFLSFLPlahildrmieeyFFHkgaSIGYyhgdlnalrddIVELKP 318
Cdd:cd05909 161 LPKGVVLSHKN---LLANVEQITAIFD--PNPEDVVFGALP------------FFH---SFGL-----------TGCLWL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 TLLVGVPRVYEriyegilkaiaelrplrrviFNALYNRKLASM--KAGYSHKTASP-FADMLAFRKVKARLGgRLRLLIS 395
Cdd:cd05909 210 PLLSGIKVVFH--------------------PNPLDYKKIPELiyDKKATILLGTPtFLRGYARAAHPEDFS-SLRLVVA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 GGAPLSNEIEEFMRVTTCAYFIQGYGLTEtLGPSTVCYIDDMALV-GSAGVPATYTEIRLEEVPemGYNPLGVPSRGEIC 474
Cdd:cd05909 269 GAEKLKDTLRQEFQEKFGIRILEGYGTTE-CSPVISVNTPQSPNKeGTVGRPLPGMEVKIVSVE--THEEVPIGEGGLLL 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 475 IRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLE 538
Cdd:cd05909 346 VRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIE 408
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
83-524 |
5.84e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 121.63 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQ-WIVAMQAC-NGYSLVCV-PLydtlgaGAVD---YIIDHAEIDV 156
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLMAIGAAQlAGLRRTALhPL------GSLDdhaYVLEDAGIST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 157 VFIQDKKIKE---ILSPNCKSAKRLKALVAFTSATteqnkeadqigikmyawdDFLKVGKDNPRQPCPPQA--SDICTVM 231
Cdd:PRK06188 113 LIVDPAPFVEralALLARVPSLKHVLTLGPVPDGV------------------DLLAAAAKFGPAPLVAAAlpPDIAGLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 232 YTSGTSGQPKGVMLTHESHAMYVkgvDLFMDQFDdkMTTDDVFLSFLPLAH-----ILDRMIeeyffhKGASIGYYHG-D 305
Cdd:PRK06188 175 YTGGTTGKPKGVMGTHRSIATMA---QIQLAEWE--WPADPRFLMCTPLSHaggafFLPTLL------RGGTVIVLAKfD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 306 LNALRDDIVELKPTLLVGVPRVyerIYegilkAIAELRPLRRvifnalynRKLASmkagyshktaspfadmlafrkvkar 385
Cdd:PRK06188 244 PAEVLRAIEEQRITATFLVPTM---IY-----ALLDHPDLRT--------RDLSS------------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 386 lggrLRLLISGGAPLS-----NEIEEFMRVttcayFIQGYGLTETlgPSTVCYI-------DDMALVGSAGVPATYTEIR 453
Cdd:PRK06188 283 ----LETVYYGASPMSpvrlaEAIERFGPI-----FAQYYGQTEA--PMVITYLrkrdhdpDDPKRLTSCGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 454 L-----EEVPemgynpLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKK------- 521
Cdd:PRK06188 352 LldedgREVA------QGEV--GEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKdmivtgg 423
|
....
gi 226491570 522 -NIF 524
Cdd:PRK06188 424 fNVF 427
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
83-554 |
2.73e-28 |
|
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: 119.55 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNcKSAKRLKALVAFTSATTEQNKEADQIGIKMYAWDDFlkvgkdNPRQPCPPQAS---DICTVMYTSGTSGQ 239
Cdd:cd17642 126 GLQKVLNVQ-KKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGF------NEYDFKPPSFDrdeQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHE------SHAMyvkgvdlfMDQFDDKMTTDDVFLSFLPLAHIldrmieeyfFHKGASIGYYhgdlnalrddI 313
Cdd:cd17642 199 PKGVQLTHKnivarfSHAR--------DPIFGNQIIPDTAILTVIPFHHG---------FGMFTTLGYL----------I 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 314 VELKptlLVGVPRVYERIYegiLKAIAELRplrrvIFNALYNRKLASMKAgyshktASPFADmlafrkvKARLGgRLRLL 393
Cdd:cd17642 252 CGFR---VVLMYKFEEELF---LRSLQDYK-----VQSALLVPTLFAFFA------KSTLVD-------KYDLS-NLHEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 394 ISGGAPLSNEIEEFMRVTTCAYFI-QGYGLTETLGpSTVCYIDDMALVGSAGVPATYTEIRLEEvPEMGyNPLGVPSRGE 472
Cdd:cd17642 307 ASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTS-AILITPEGDDKPGAVGKVVPFFYAKVVD-LDTG-KTLGPNERGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 473 ICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVEYLEKVYGFPPLVEDIW 551
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAG 462
|
...
gi 226491570 552 VYG 554
Cdd:cd17642 463 VAG 465
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
83-521 |
3.01e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 119.53 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACN--GYSLVCV-PLYDTlgaGAVDYIIDHAEIDVVFI 159
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAkiGAILVTInPAYRL---SELEYALNQSGCKALIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 QDK-------KIKEILSPNCKSAKRlkalVAFTSATTEQNKEADQIGIK----MYAWDDFLKVGKDNPRQPCPP-----Q 223
Cdd:PRK08315 122 ADGfkdsdyvAMLYELAPELATCEP----GQLQSARLPELRRVIFLGDEkhpgMLNFDELLALGRAVDDAELAArqatlD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 224 ASDICTVMYTSGTSGQPKGVMLTHES---HAMYVKGVDLFMDQfddkmttddvflsflplahilDRM-IEEYFFH----- 294
Cdd:PRK08315 198 PDDPINIQYTSGTTGFPKGATLTHRNilnNGYFIGEAMKLTEE---------------------DRLcIPVPLYHcfgmv 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 295 --------KGASIgYYHGD----LNALRDdIVELKPTLLVGVPRVYeriyegilkaIAELrplrrvifnalynrklasmk 362
Cdd:PRK08315 257 lgnlacvtHGATM-VYPGEgfdpLATLAA-VEEERCTALYGVPTMF----------IAEL-------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 363 agySHKTASPFaDMlafrkvkarlgGRLRLLISGGAPLSneiEEFMR----------VTTCayfiqgYGLTETLGPSTVC 432
Cdd:PRK08315 305 ---DHPDFARF-DL-----------SSLRTGIMAGSPCP---IEVMKrvidkmhmseVTIA------YGMTETSPVSTQT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 433 YIDDmAL---VGSAGVPATYTEIRLEEvPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEM 508
Cdd:PRK08315 361 RTDD-PLekrVTTVGRALPHLEVKIVD-PETG-ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVM 437
|
490
....*....|...
gi 226491570 509 TPDGILKVIDRKK 521
Cdd:PRK08315 438 DEEGYVNIVGRIK 450
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
226-572 |
3.71e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 115.51 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMdQFDDKmttdDVFLSFLPLAHILDRMIeeyfFHKGASIG---YY 302
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL-GFGGG----DSWLLSLPLYHVGGLAI----LVRSLLAGaelVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 HGDLNALRDDIVELKPTLLVGVPRVYERIYEgilkaiaelrplrrvifnalynrklasmkagySHKTASPFAdmlafrkv 382
Cdd:cd17630 72 LERNQALAEDLAPPGVTHVSLVPTQLQRLLD--------------------------------SGQGPAALK-------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 383 karlggRLRLLISGGAPLSNEI-EEF--MRVTTCayfiQGYGLTETLGPSTVCYIDDMALvGSAGVPATYTEIRLEEvpe 459
Cdd:cd17630 112 ------SLRAVLLGGAPIPPELlERAadRGIPLY----TTYGMTETASQVATKRPDGFGR-GGVGVLLPGRELRIVE--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 460 mgynplgvpsRGEICIRGKSLFAGYYK--SPELTNEaivDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYL 537
Cdd:cd17630 178 ----------DGEIWVGGASLAMGYLRgqLVPEFNE---DGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEI 243
|
330 340 350
....*....|....*....|....*....|....*...
gi 226491570 538 EKVYGFPPLVEDIWVYG---DSFRSSLVAVVNPHQENT 572
Cdd:cd17630 244 EAALAAHPAVRDAFVVGvpdEELGQRPVAVIVGRGPAD 281
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
83-526 |
3.96e-28 |
|
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: 118.01 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQA---CNGyslVCVPLYDTLGAGAVDYIIDHAEIDVVFI 159
Cdd:cd05930 14 TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAvlkAGA---AYVPLDPSYPAERLAYILEDSGAKLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 QdkkikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqASDICTVMYTSGTSGQ 239
Cdd:cd05930 91 D---------------------------------------------------------------PDDLAYVIYTSGSTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHESHAMYVKGVDlfmDQFDdkMTTDDVFLSFLPLAHilDRMIEEYFFH--KGASIgyY------HGDLNALRD 311
Cdd:cd05930 108 PKGVMVEHRGLVNLLLWMQ---EAYP--LTPGDRVLQFTSFSF--DVSVWEIFGAllAGATL--VvlpeevRKDPEALAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 DIVELKPTLLVGVPRVYeriyegilkaiaelrplrRVIFNALYNRKLASmkagyshktaspfadmlafrkvkarlggrLR 391
Cdd:cd05930 179 LLAEEGITVLHLTPSLL------------------RLLLQELELAALPS-----------------------------LR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 392 LLISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSA---GVPATYTEIR-----LEEVPemgy 462
Cdd:cd05930 212 LVLVGGEALPPDlVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRvpiGRPIPNTRVYvldenLRPVP---- 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226491570 463 npLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWFH-------TGDIGEMTPDGILKVIDRKKNIFKL 526
Cdd:cd05930 288 --PGVP--GELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVKI 354
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
98-548 |
1.83e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 117.45 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 98 LQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKkikeiLSPNCKSAKR 177
Cdd:PRK06178 75 LRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQ-----LAPVVEQVRA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 178 LKAL--VAFTSA--------TTEQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQAS--DICTVMYTSGTSGQPKGVML 245
Cdd:PRK06178 150 ETSLrhVIVTSLadvlpaepTLPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPAldALAALNYTGGTTGMPKGCEH 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 246 THeSHAMYVK----GVDLFMDQfddkmttDDVFLSFLPLahildrmieeyFFHKGASIG-----YYHGDLNAL-RDDIVe 315
Cdd:PRK06178 230 TQ-RDMVYTAaaayAVAVVGGE-------DSVFLSFLPE-----------FWIAGENFGllfplFSGATLVLLaRWDAV- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 316 lkpTLLVGVPRVYERIYEGILKAIAELRPLRRVifnalYNRKLASMKagysHKTASPFAdmlafRKVKARLGGRLRLLis 395
Cdd:PRK06178 290 ---AFMAAVERYRVTRTVMLVDNAVELMDHPRF-----AEYDLSSLR----QVRVVSFV-----KKLNPDYRQRWRAL-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 ggaplsneieefmrvTTCAYFIQGYGLTETLGPSTVC---YIDDMALVGS---AGVPATYTEIRLEEVPEMGYNPLGVPs 469
Cdd:PRK06178 351 ---------------TGSVLAEAAWGMTETHTCDTFTagfQDDDFDLLSQpvfVGLPVPGTEFKICDFETGELLPLGAE- 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 470 rGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVaveylekvygFPPLVE 548
Cdd:PRK06178 415 -GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSV----------FPSEVE 481
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
209-527 |
3.23e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 116.69 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 209 LKVGKDnpRQPCPPQAS--DICTVMYTSGTSGQPKGVMLTHE---SHAMYVKGV-DLFMDQFDDKMTTDdvflsfLPLAH 282
Cdd:PRK08974 190 LHKGRR--MQYVKPELVpeDLAFLQYTGGTTGVAKGAMLTHRnmlANLEQAKAAyGPLLHPGKELVVTA------LPLYH 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 283 ILDRMIE-EYFFHKGASigyyhgdlnalrddivelkpTLLVGVPRvyeriyeGILKAIAELRPLRRV-------IFNALY 354
Cdd:PRK08974 262 IFALTVNcLLFIELGGQ--------------------NLLITNPR-------DIPGFVKELKKYPFTaitgvntLFNALL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 355 NRKlasmkagyshktaspfadmlAFRKVKArlgGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYI 434
Cdd:PRK08974 315 NNE--------------------EFQELDF---SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 435 DDMALVGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGIL 514
Cdd:PRK08974 372 DLDYYSGSIGLPVPSTEIKL--VDDDG-NEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFL 448
|
330
....*....|...
gi 226491570 515 KVIDRKKNIFKLS 527
Cdd:PRK08974 449 RIVDRKKDMILVS 461
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
218-523 |
3.23e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 116.39 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 218 QPCPPQASDICTVMYTSGTSGQPKGVMLTHE----SHAMYVKGVDLfmdqfddkmTTDDVFLSFLPLAHildrmieeyff 293
Cdd:PRK06087 180 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNnilaSERAYCARLNL---------TWQDVFMMPAPLGH----------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 294 hkgaSIGYYHGdlnalrddiveLKPTLLVGVPRVYERIYegilKAIAELRPLRRvifnalynrklasMKAGYSHKtASPF 373
Cdd:PRK06087 240 ----ATGFLHG-----------VTAPFLIGARSVLLDIF----TPDACLALLEQ-------------QRCTCMLG-ATPF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 374 A-DML-AFRKVKARLGGrLRLLISGGAPLSNeieefmRVTTCAY-----FIQGYGLTETLgPSTVCYIDDMA--LVGSAG 444
Cdd:PRK06087 287 IyDLLnLLEKQPADLSA-LRFFLCGGTTIPK------KVARECQqrgikLLSVYGSTESS-PHAVVNLDDPLsrFMHTDG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 445 VPATYTEIRleeVPEMGYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:PRK06087 359 YAAAGVEIK---VVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDI 435
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
83-540 |
4.02e-27 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 116.31 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVF---- 158
Cdd:PRK13295 57 TYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVvpkt 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 ------------IQDK--KIKEILSPNCKSAKRLKALvaFTSATTEQNKEADQIgikmyawddflkvgKDNPRqpcpPQA 224
Cdd:PRK13295 137 frgfdhaamarrLRPElpALRHVVVVGGDGADSFEAL--LITPAWEQEPDAPAI--------------LARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 225 SDICTVMYTSGTSGQPKGVMLTHESH----AMYVKGVDLfmdqfddkmTTDDVFLSFLPLAHIldrmieeyffhkgasIG 300
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLmaniVPYAERLGL---------GADDVILMASPMAHQ---------------TG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 301 YYHGdlnalrddiveLKPTLLVGVPRVYERIYEgILKAIAELRPlRRVIFnalynrklaSMkagyshkTASPF-ADMLAF 379
Cdd:PRK13295 253 FMYG-----------LMMPVMLGATAVLQDIWD-PARAAELIRT-EGVTF---------TM-------ASTPFlTDLTRA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 380 RKVKARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYID-DMALVGSAGVPATYTEIRleeVP 458
Cdd:PRK13295 304 VKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDpDERASTTDGCPLPGVEVR---VV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 459 EMGYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAiVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLE 538
Cdd:PRK13295 381 DADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD-ADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIE 458
|
..
gi 226491570 539 KV 540
Cdd:PRK13295 459 AL 460
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
79-642 |
6.72e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 115.71 E-value: 6.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 79 YLWKsykEIYDEVLQAGSALQKLGVQPGSRVGIYGANCP-----QWIVAMQacnGYSLVCVPLydTLGAGAVDYIIDHAE 153
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPamyeaHFGVPMA---GAVVNCVNI--RLNAPTIAFLLEHSK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 154 IDVVFIQDKKIK------EILSPNCKSAKRLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKVGkdNPRQPCPPQASDI 227
Cdd:PLN02479 118 SEVVMVDQEFFTlaeealKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGAIEYEKFLETG--DPEFAWKPPADEW 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 228 CTVM--YTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHIldrmiEEYFF------HKGASI 299
Cdd:PLN02479 196 QSIAlgYTSGTTASPKGVVLHHRGAYLMALSNALIWG-----MNEGAVYLWTLPMFHC-----NGWCFtwtlaaLCGTNI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 300 GYYHGDLNALRDDIVELKPTLLVGVPRVYERIyegiLKAIAE--LRPLRRVIfnalynrklASMKAGyshktASPFADML 377
Cdd:PLN02479 266 CLRQVTAKAIYSAIANYGVTHFCAAPVVLNTI----VNAPKSetILPLPRVV---------HVMTAG-----AAPPPSVL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 378 AfrkvkarlggrlrllisggaplSNEIEEFmRVTtcayfiQGYGLTETLGPSTVCY----------IDDMALVGSAGVPA 447
Cdd:PLN02479 328 F----------------------AMSEKGF-RVT------HTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGVRY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 448 TYTEiRLEEVPEMGYNPlgVP----SRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:PLN02479 379 IGLE-GLDVVDTKTMKP--VPadgkTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 524 FkLSQGEYVAVEYLEKV-YGFPPLVEdiwvygdsfrSSLVAvvNPHQentmKWAESNgykgsfdeiCKLEGLKEYILK-E 601
Cdd:PLN02479 456 I-ISGGENISSLEVENVvYTHPAVLE----------ASVVA--RPDE----RWGESP---------CAFVTLKPGVDKsD 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 226491570 602 LAAVAQ------KNKLRGFEYIKGVVLDPVPfdierdlVTATMKKKR 642
Cdd:PLN02479 510 EAALAEdimkfcRERLPAYWVPKSVVFGPLP-------KTATGKIQK 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-524 |
8.88e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 114.75 E-value: 8.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 75 VPGPYLWkSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIiDHAEI 154
Cdd:PRK07470 27 VWGDRSW-TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYL-AEASG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 155 DVVFIQDKKIKEILSPNCKSAKRLKALVAFTSATTEQNKEAdqigikmyawddflkVGKDNPRQPCPPQA---SDICTVM 231
Cdd:PRK07470 105 ARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEA---------------LVARHLGARVANAAvdhDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 232 YTSGTSGQPKGVMLTHESHAMYVKG--VDLFMDqfddkMTTDDVFLSFLPLAHildrmieeyffhkGASIgyyHGDLNAL 309
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNhlADLMPG-----TTEQDASLVVAPLSH-------------GAGI---HQLCQVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 310 RDDIVELKPTLLVGVPRVYERIYE----------GILKAIAELRPLRRvifnalynrklasmkagYSHKTaspfadmlaf 379
Cdd:PRK07470 229 RGAATVLLPSERFDPAEVWALVERhrvtnlftvpTILKMLVEHPAVDR-----------------YDHSS---------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 380 rkvkarlggrLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVC-----YIDD--MALVGSAGVPATYTEI 452
Cdd:PRK07470 282 ----------LRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLppalhDAEDgpDARIGTCGFERTGMEV 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 453 RLEEvpEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIF 524
Cdd:PRK07470 352 QIQD--DEG-RELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY 420
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
47-565 |
1.63e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 114.20 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 47 KTSWDVFRVAAVKYADnrmlgwRPFKDGVpGPYLwkSYKEIYDEVLQ-AGSALQKLGVQPGSRVGIYGANCPQWIVAMQA 125
Cdd:PRK08751 25 RTVAEVFATSVAKFAD------RPAYHSF-GKTI--TYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 126 --CNGYSLVCV-PLYDT-------LGAGA-VDYIIDHAEIDVV-FIQDKKIKEILSPNCKS----AKRlkALVAFTSATT 189
Cdd:PRK08751 96 vlRAGLTVVNVnPLYTPrelkhqlIDSGAsVLVVIDNFGTTVQqVIADTPVKQVITTGLGDmlgfPKA--ALVNFVVKYV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 190 EQNKEADQIGiKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDQFDDKMT 269
Cdd:PRK08751 174 KKLVPEYRIN-GAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 270 TDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNALRDDIVELKPTLLVGVPRVyeriyegilkaiaelrplrRVI 349
Cdd:PRK08751 253 GCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-------------------NTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 350 FNALYNrklasmkagyshktaSPFADMLAFRKVKARLGgrlrllisGGAPLSNEIEEFMRVTTCAYFIQGYGLTETlgpS 429
Cdd:PRK08751 314 FNGLLN---------------TPGFDQIDFSSLKMTLG--------GGMAVQRSVAERWKQVTGLTLVEAYGLTET---S 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 430 TVCYIDDMALV---GSAGVPATYTEIRLEEvpEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDI 505
Cdd:PRK08751 368 PAACINPLTLKeynGSIGLPIPSTDACIKD--DAG-TVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDI 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 506 GEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYGFPPLVEDIWVYG--DSFRSSLVAVV 565
Cdd:PRK08751 445 ARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEVAAVGvpDEKSGEIVKVV 505
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
83-577 |
2.56e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 113.72 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDk 162
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeILSPNCKSAKRLKALVAfTSATTEQNKEADQIGikmyaWDDFLKvgKDNPrqpcPPQASDI-----CTVMYTSGTS 237
Cdd:PRK07786 123 ----ALAPVATAVRDIVPLLS-TVVVAGGSSDDSVLG-----YEDLLA--EAGP----AHAPVDIpndspALIMYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTH---ESHAM---YVKGVDlfmdqfddkmTTDDVFLSFLPLAHIldrmieeyffhkgASIGyyhgdlnalrd 311
Cdd:PRK07786 187 GRPKGAVLTHanlTGQAMtclRTNGAD----------INSDVGFVGVPLFHI-------------AGIG----------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 divELKPTLLVGVPRVyeriyegilkaiaeLRPLRRVIFNALYNrKLASMKAGYSHKTASPFADMLAFRKVKARlGGRLR 391
Cdd:PRK07786 233 ---SMLPGLLLGAPTV--------------IYPLGAFDPGQLLD-VLEAEKVTGIFLVPAQWQAVCAEQQARPR-DLALR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 392 LLISGGAPLSNEIEEFMRVT-TCAYFIQGYGLTEtLGPSTVCYIDDMAL--VGSAGVPATYTEIRLEEvPEMgyNPLGVP 468
Cdd:PRK07786 294 VLSWGAAPASDTLLRQMAATfPEAQILAAFGQTE-MSPVTCMLLGEDAIrkLGSVGKVIPTVAARVVD-ENM--NDVPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 469 SRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKV-YGFPPLV 547
Cdd:PRK07786 370 EVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVlASHPDIV 448
|
490 500 510
....*....|....*....|....*....|.
gi 226491570 548 EdiwvygdsfrsslVAVVN-PHQentmKWAE 577
Cdd:PRK07786 449 E-------------VAVIGrADE----KWGE 462
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
83-601 |
2.73e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 113.54 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCV---PLY-------DTLGAGA-------- 144
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTtanPFYtpaeiakQAKASGAkliitqsc 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 145 -VDYIIDHAEIDVVfiqdkKIKEILSP--NCksakrlkalVAFTSATTEQNKEADQIGIkmyawddflkvgkdnprqpcp 221
Cdd:PLN02246 132 yVDKLKGLAEDDGV-----TVVTIDDPpeGC---------LHFSELTQADENELPEVEI--------------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 222 pQASDICTVMYTSGTSGQPKGVMLTHE----SHAMYVKGvdlfmDQFDDKMTTDDVFLSFLPLAHIldrmieeyffhkga 297
Cdd:PLN02246 177 -SPDDVVALPYSSGTTGLPKGVMLTHKglvtSVAQQVDG-----ENPNLYFHSDDVILCVLPMFHI-------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 298 sigyYhgDLNALrddivelkptLLVGvprvyeriyegiLKAIAELRPLRRVIFNALynrklasMKAGYSHK-TASPFAD- 375
Cdd:PLN02246 237 ----Y--SLNSV----------LLCG------------LRVGAAILIMPKFEIGAL-------LELIQRHKvTIAPFVPp 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 376 -MLAFRK---VKARLGGRLRLLISGGAPLSNEIEE-FMRVTTCAYFIQGYGLTETlGPstvcyIDDMALV---------- 440
Cdd:PLN02246 282 iVLAIAKspvVEKYDLSSIRMVLSGAAPLGKELEDaFRAKLPNAVLGQGYGMTEA-GP-----VLAMCLAfakepfpvks 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 441 GSAGvpatyTEIRLEEV----PEMGYN-PLGVPsrGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGIL 514
Cdd:PLN02246 356 GSCG-----TVVRNAELkivdPETGASlPRNQP--GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDEL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 515 KVIDRKKNIFKLsQGEYVAVEYLEKVYGFPPLVEDIWVYG---DSFRSSLVAVVnphqentmkwAESNGYKGSFDEIckl 591
Cdd:PLN02246 429 FIVDRLKELIKY-KGFQVAPAELEALLISHPSIADAAVVPmkdEVAGEVPVAFV----------VRSNGSEITEDEI--- 494
|
570
....*....|
gi 226491570 592 eglKEYILKE 601
Cdd:PLN02246 495 ---KQFVAKQ 501
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
83-578 |
2.88e-26 |
|
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: 112.34 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACngyslvcvplydtLGAGAVdYI-IDhAEIDVVFIQd 161
Cdd:cd05945 18 TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAA-------------LKAGHA-YVpLD-ASSPAERIR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 kKIKEILSPncksakrlKALVAftsatteqnkeadqigikmyawddflkVGKDNprqpcppqasdiCTVMYTSGTSGQPK 241
Cdd:cd05945 82 -EILDAAKP--------ALLIA---------------------------DGDDN------------AYIIFTSGSTGRPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHESHAMYVKGvdlfMDQfDDKMTTDDVFLSFLPlahildrmieeyffhkgasigyYHGDLNalrddIVELKPTLL 321
Cdd:cd05945 114 GVQISHDNLVSFTNW----MLS-DFPLGPGDVFLNQAP----------------------FSFDLS-----VMDLYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 322 VGvprvyeriyegilkaiAELRPLRRVI---FNALYnRKLASMKAGYSHKTASpFADMLAFRK-VKARLGGRLRLLISGG 397
Cdd:cd05945 162 SG----------------ATLVPVPRDAtadPKQLF-RFLAEHGITVWVSTPS-FAAMCLLSPtFTPESLPSLRHFLFCG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSN-EIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATY--TEIRLEEVPEMGyNPLGVPSRGEIC 474
Cdd:cd05945 224 EVLPHkTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYakPGAKLVILDEDG-RPVPPGEKGELV 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 475 IRGKSLFAGYYKSPELTNEAIVD----GWFHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVEYLEKVYGFPPLVED- 549
Cdd:cd05945 303 ISGPSVSKGYLNNPEKTAAAFFPdegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEa 381
|
490 500 510
....*....|....*....|....*....|....*
gi 226491570 550 --IWVYGDSFRSSLVAVVNPH----QENTMKWAES 578
Cdd:cd05945 382 vvVPKYKGEKVTELIAFVVPKpgaeAGLTKAIKAE 416
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
209-527 |
4.96e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 112.99 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 209 LKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDQFDDKMTT-----DDVFLSFLPLAHI 283
Cdd:PRK12492 191 LRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPlmkegQEVMIAPLPLYHI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 284 ldrmieeYFFHKGASIGYYHGDLNalrddivelkptLLVGVPRvyeriyeGILKAIAELRPLRRVIFNALYNRKLASMka 363
Cdd:PRK12492 271 -------YAFTANCMCMMVSGNHN------------VLITNPR-------DIPGFIKELGKWRFSALLGLNTLFVALM-- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 364 gyshktaspfaDMLAFRKVKArlgGRLRLLISGGAPL-SNEIEEFMRVTTCAyFIQGYGLTETLGPSTVCYIDDMALVGS 442
Cdd:PRK12492 323 -----------DHPGFKDLDF---SALKLTNSGGTALvKATAERWEQLTGCT-IVEGYGLTETSPVASTNPYGELARLGT 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 443 AGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKK 521
Cdd:PRK12492 388 VGIPVPGTALKV--IDDDG-NELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKK 464
|
....*.
gi 226491570 522 NIFKLS 527
Cdd:PRK12492 465 DLIIVS 470
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
83-527 |
9.20e-26 |
|
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: 110.50 E-value: 9.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAeidvvfiqdk 162
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakRLKALVAftsatteqnkeadqigikmyawddflkvgkdnprqpcppQASDICTVMYTSGTSGQPKG 242
Cdd:cd05972 72 --------------GAKAIVT---------------------------------------DAEDPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHE---SHAMYVKGV-DLfmdqfddkmTTDDVFLSFlplahildrmieeyffhkgASIGYYHGDLNALrddiveLKP 318
Cdd:cd05972 99 VLHTHSyplGHIPTAAYWlGL---------RPDDIHWNI-------------------ADPGWAKGAWSSF------FGP 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 tLLVGVPRVyerIYEGilkaiAELRPLRrvIFNALYNRKLASMkagyshkTASPFA-DMLAFRKVKARLGGRLRLLISGG 397
Cdd:cd05972 145 -WLLGATVF---VYEG-----PRFDAER--ILELLERYGVTSF-------CGPPTAyRMLIKQDLSSYKFSHLRLVVSAG 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSNEIEEFMRVTTCAYFIQGYGLTETlGPSTVCYIDDMALVGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRG 477
Cdd:cd05972 207 EPLNPEVIEWWRAATGLPIRDGYGQTET-GLTVGNFPDMPVKPGSMGRPTPGYDVAI--IDDDG-RELPPGEEGDIAIKL 282
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 226491570 478 K--SLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:cd05972 283 PppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
207-527 |
4.29e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 109.85 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 207 DFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHE---SHAMYVKGvdLFMDQFDDKMttdDVFLSFLPLAHI 283
Cdd:PRK05677 189 DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRnlvANMLQCRA--LMGSNLNEGC---EILIAPLPLYHI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 284 LdrmieEYFFHKGAS--IGYYH------GDLNALRDDIVELKPTLLVGVprvyeriyegilkaiaelrplrRVIFNALYN 355
Cdd:PRK05677 264 Y-----AFTFHCMAMmlIGNHNilisnpRDLPAMVKELGKWKFSGFVGL----------------------NTLFVALCN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 356 RKlasmkagyshktaspfadmlAFRKVKArlgGRLRLLISGGAPLSNEI-EEFMRVTTCAyFIQGYGLTETLGPSTVCYI 434
Cdd:PRK05677 317 NE--------------------AFRKLDF---SALKLTLSGGMALQLATaERWKEVTGCA-ICEGYGMTETSPVVSVNPS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 435 DDMALvGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGI 513
Cdd:PRK05677 373 QAIQV-GTIGIPVPSTLCKV--IDDDG-NELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGY 448
|
330
....*....|....
gi 226491570 514 LKVIDRKKNIFKLS 527
Cdd:PRK05677 449 MRIVDRKKDMILVS 462
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-523 |
1.46e-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: 105.44 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTHES---------HAMyvkgvdlfmdqfddKMTTDDVFLSFLPLAHILdrmieeyffhkG 296
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNivnngyfigERL--------------GLTEQDRLCIPVPLFHCF-----------G 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 297 ASIGYY----HG----------DLNALRDDIVELKPTLLVGVPRVYeriyegilkaIAELRPLRRVIFNalynrkLASMK 362
Cdd:cd05917 58 SVLGVLacltHGatmvfpspsfDPLAVLEAIEKEKCTALHGVPTMF----------IAELEHPDFDKFD------LSSLR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 363 AGyshktaspfadmlafrkvkarlggrlrllISGGAPLSNE----IEEFMRVTTcayFIQGYGLTETLGPSTVCYIDDMA 438
Cdd:cd05917 122 TG-----------------------------IMAGAPCPPElmkrVIEVMNMKD---VTIAYGMTETSPVSTQTRTDDSI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 439 --LVGSAGVPATYTEIRL-----EEVPemgynPLGVPsrGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTP 510
Cdd:cd05917 170 ekRVNTVGRIMPHTEAKIvdpegGIVP-----PVGVP--GELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDE 242
|
330
....*....|...
gi 226491570 511 DGILKVIDRKKNI 523
Cdd:cd05917 243 DGYCRIVGRIKDM 255
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-524 |
2.08e-24 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 104.89 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTH-ESHAMYVKGVDLfmdqfdDKMTTDDVFLSFLPlahildrmieeyFFHkgaSIGYYHG 304
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADC------ADLTEDDRYLIINP------------FFH---TFGYKAG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 305 DLNALrddivelkptlLVGVPRVYERIYE--GILKAIAELR----PLRRVIFNALY------NRKLASMKAGYSHKTASP 372
Cdd:cd17638 60 IVACL-----------LTGATVVPVAVFDvdAILEAIERERitvlPGPPTLFQSLLdhpgrkKFDLSSLRAAVTGAATVP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 373 FAdmlAFRKVKARLGgrlrllisggaplsneieeFMRVTTcayfiqGYGLTETlGPSTVCYIDDMA--LVGSAGVPATYT 450
Cdd:cd17638 129 VE---LVRRMRSELG-------------------FETVLT------AYGLTEA-GVATMCRPGDDAetVATTCGRACPGF 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 451 EIRLEEvpemgynplgvpsRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIF 524
Cdd:cd17638 180 EVRIAD-------------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY 241
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
83-642 |
4.32e-24 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 106.30 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIV----AMQAcngySLVCVPLYDTLGAGAVDYIIDHAEIDVVF 158
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTaflgAIRA----GIVPVPVNTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 IQDKkikeiLSPNCKSA--KRLKALVAFTSAtteqNKEADQIGIKMYAwdDFLKVGKDNpRQPCPPQASDICTVMYTSGT 236
Cdd:cd05959 107 VSGE-----LAPVLAAAltKSEHTLVVLIVS----GGAGPEAGALLLA--ELVAAEAEQ-LKPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHESHA----MYVKGVDlfmdqfddKMTTDDVFLSFLPLAHILDRMIEEYF-FHKGASIGYYHGDLNALR- 310
Cdd:cd05959 175 TGRPKGVVHLHADIYwtaeLYARNVL--------GIREDDVCFSAAKLFFAYGLGNSLTFpLSVGATTVLMPERPTPAAv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 311 -DDIVELKPTLLVGVPRVYeriyegilkaiaelrplrrvifnalynrklasmkagyshktaspfADMLAFRKVKARLGGR 389
Cdd:cd05959 247 fKRIRRYRPTVFFGVPTLY---------------------------------------------AAMLAAPNLPSRDLSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLG------PSTVCYiddmalvGSAGVPATYTEIRLeeVPEMGyN 463
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHiflsnrPGRVRY-------GTTGKPVPGYEVEL--RDEDG-G 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 464 PLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYGF 543
Cdd:cd05959 352 DVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 544 PPLVEDIWVYG---DSFRSSLVAVVNPHQentmkwaesnGYKGSfdEICKlEGLKEYIlkelaavaqKNKLRGFEYIKGV 620
Cdd:cd05959 431 HPAVLEAAVVGvedEDGLTKPKAFVVLRP----------GYEDS--EALE-EELKEFV---------KDRLAPYKYPRWI 488
|
570 580
....*....|....*....|...
gi 226491570 621 V-LDPVPfdierdlVTATMKKKR 642
Cdd:cd05959 489 VfVDELP-------KTATGKIQR 504
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
83-597 |
9.14e-24 |
|
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: 105.28 E-value: 9.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDk 162
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kIKEILSPNCKSAKRLKALvaftsatteqnkeADQIGIKM-YAWDDFLKvgkdnPRQPCPPQASdicTVMYTSGTSGQPK 241
Cdd:cd05923 109 -DAQVMDAIFQSGVRVLAL-------------SDLVGLGEpESAGPLIE-----DPPREPEQPA---FVFYTSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHESHAMYVkgvdLFM-DQFDDKMTTDDVFLSFLPLAHILDrmieeyFFHKGASIGYYHGDLNALRDD-------- 312
Cdd:cd05923 167 GAVIPQRAAESRV----LFMsTQAGLRHGRHNVVLGLMPLYHVIG------FFAVLVAALALDGTYVVVEEFdpadalkl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 313 IVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNAlynrklASMKAGyshktaspfadmlAFRKVKARLGGRlrl 392
Cdd:cd05923 237 IEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAG------ATMPDA-------------VLERVNQHLPGE--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 393 lisggaplsneieefmrvttcayFIQGYGLTETLGpSTvcyIDDMALVGSAGVPATYTEIRLEEVPEMGYNPLGVPSRGE 472
Cdd:cd05923 295 -----------------------KVNIYGTTEAMN-SL---YMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 473 ICIR--GKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDI 550
Cdd:cd05923 348 LIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 226491570 551 WVYG---DSFRSSLVAVVNPHqentmkwaESNGYKGSFDEICKLEGLKEY 597
Cdd:cd05923 427 VVIGvadERWGQSVTACVVPR--------EGTLSADELDQFCRASELADF 468
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
83-558 |
1.61e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 104.76 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAM--QACNGysLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQ 160
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWfgLAKIG--AIMVPINARLLREESAWILQNSQASLLVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 161 DKKIKEILSPNCKSAKRLKALVAftsaTTEQNKEADqiGIKmyawdDFLKVGKDNPRQPC---PPQASDICTVMYTSGTS 237
Cdd:PRK08008 117 AQFYPMYRQIQQEDATPLRHICL----TRVALPADD--GVS-----SFTQLKAQQPATLCyapPLSTDDTAEILFTSGTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTHESHamyvkgvdLFMDQFDD---KMTTDDVFLSFLPLAHIlD----------------RMIEEYffhkgaS 298
Cdd:PRK08008 186 SRPKGVVITHYNL--------RFAGYYSAwqcALRDDDVYLTVMPAFHI-DcqctaamaafsagatfVLLEKY------S 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 299 IGYYHGDLNALRDDIVELKP----TLLVGVPRVYERIYEgilkaiaelrpLRRVIFnalynrklasmkagYSHKTAspfA 374
Cdd:PRK08008 251 ARAFWGQVCKYRATITECIPmmirTLMVQPPSANDRQHC-----------LREVMF--------------YLNLSD---Q 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 375 DMLAFrkvKARLGgrLRLLISggaplsneieefmrvttcayfiqgYGLTETLG-------------PStvcyiddmalVG 441
Cdd:PRK08008 303 EKDAF---EERFG--VRLLTS------------------------YGMTETIVgiigdrpgdkrrwPS----------IG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 442 SAGVpaTY-TEIRLEEvpemgYNPLGVPSRGEICIRG---KSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKV 516
Cdd:PRK08008 344 RPGF--CYeAEIRDDH-----NRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYF 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 226491570 517 IDRKKNIFKLSqGEYVAVEYLEKVYGFPPLVEDIWVYG--DSFR 558
Cdd:PRK08008 417 VDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikDSIR 459
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
83-521 |
4.00e-23 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 103.90 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLydtlGAGAVDYIIDHAEidvvfiqdK 162
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL----TVPPTYDEPNARL--------R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEIL----SPNCKSAKRLKALVAftsattEQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQasDICTVMYTSGTSG 238
Cdd:cd05906 109 KLRHIWqllgSPVVLTDAELVAEFA------GLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHES--HAMYVKGVdlfMDQFddkmTTDDVFLSFLPLAHIldrmieeyffhkgASIGYYHgdlnalrddiveL 316
Cdd:cd05906 181 FPKAVPLTHRNilARSAGKIQ---HNGL----TPQDVFLNWVPLDHV-------------GGLVELH------------L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 317 KPTLL----VGVPRVYeriyegILKaiaelRPLRrviFNALYNRklasmkagysHKTASPFADMLAFRKVKARLG----- 387
Cdd:cd05906 229 RAVYLgcqqVHVPTEE------ILA-----DPLR---WLDLIDR----------YRVTITWAPNFAFALLNDLLEeiedg 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 388 ----GRLRLLISGGAPLSNE-IEEFMR-------VTTCayFIQGYGLTET-------LGPSTVCYIDDMALVgSAGVPAT 448
Cdd:cd05906 285 twdlSSLRYLVNAGEAVVAKtIRRLLRllepyglPPDA--IRPAFGMTETcsgviysRSFPTYDHSQALEFV-SLGRPIP 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 449 YTEIRLeeVPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTpDGILKVIDRKK 521
Cdd:cd05906 362 GVSMRI--VDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTK 431
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
81-553 |
1.40e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 102.14 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 81 WKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQ 160
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 161 DKKIKEI--LSPNCKSAKRLKALVAFTSATTEQnkeadqigikmyAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSG 238
Cdd:PRK06155 126 AALLAALeaADPGDLPLPAVWLLDAPASVSVPA------------GWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHEShaMYVKGVdlfMDQFDDKMTTDDVFLSFLPLahildrmieeyfFHKGAsigyyhgdLNALrddivelKP 318
Cdd:PRK06155 194 PSKGVCCPHAQ--FYWWGR---NSAEDLEIGADDVLYTTLPL------------FHTNA--------LNAF-------FQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 TLLVGVPRVYERIYE--GILKAIAELRPLRRVIFNALYNRKLAsmkagyshKTASPfadmlafrkvkARLGGRLRLLISG 396
Cdd:PRK06155 242 ALLAGATYVLEPRFSasGFWPAVRRHGATVTYLLGAMVSILLS--------QPARE-----------SDRAHRVRVALGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 397 GAPlSNEIEEFmRVTTCAYFIQGYGLTETlgpSTVCYID-DMALVGSAGVPATYTEIRL-----EEVPEmgynplGVPsr 470
Cdd:PRK06155 303 GVP-AALHAAF-RERFGVDLLDGYGSTET---NFVIAVThGSQRPGSMGRLAPGFEARVvdehdQELPD------GEP-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 471 GEICIRGKSLFA---GYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYVAVEYLEKVYGFPPLV 547
Cdd:PRK06155 370 GELLLRADEPFAfatGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAV 448
|
....*.
gi 226491570 548 EDIWVY 553
Cdd:PRK06155 449 AAAAVF 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
83-532 |
1.86e-22 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 100.61 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACngyslvcvplydtLGAGAVDYIIdhaeidvvfiqdk 162
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGC-------------LARGAIAVVI------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspNCKSAKRLKALVAftsatteQNKEADQIGIkmyawddflkvgkdnprqpcppQASDICTVMYTSGTSGQPKG 242
Cdd:cd05919 66 --------NPLLHPDDYAYIA-------RDCEARLVVT----------------------SADDIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMlthESHAMYVKGVDLFMDQFDDKMTTDDVFLSflplahilDRMieeyFFhkgasiGYYHGdlNALRDDIVELKPTLLV 322
Cdd:cd05919 109 VM---HAHRDPLLFADAMAREALGLTPGDRVFSS--------AKM----FF------GYGLG--NSLWFPLAVGASAVLN 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 GVPRVYERIyegiLKAIAELRPlrRVIFNalynrklasmkagyshkTASPFADMLAFRKVKARLGGRLRLLISGGAPLSN 402
Cdd:cd05919 166 PGWPTAERV----LATLARFRP--TVLYG-----------------VPTFYANLLDSCAGSPDALRSLRLCVSAGEALPR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 403 EIEEFMRVTTCAYFIQGYGLTETlGPSTVCYIDDMALVGSAGVPATYTEIRLeeVPEMGYN-PLGVPsrGEICIRGKSLF 481
Cdd:cd05919 223 GLGERWMEHFGGPILDGIGATEV-GHIFLSNRPGAWRLGSTGRPVPGYEIRL--VDEEGHTiPPGEE--GDLLVRGPSAA 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 226491570 482 AGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYV 532
Cdd:cd05919 298 VGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWV 347
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
83-514 |
3.20e-22 |
|
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: 102.24 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACngysL----VCVPLYDTLGAGAVDYIIDHAEIDVVF 158
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAV----LkagaAYVPLDPAYPAERLAYMLEDAGARLVL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 IQDKkikeilspnckSAKRLKALvaftsatteqnkeadqiGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSG 238
Cdd:COG1020 579 TQSA-----------LAARLPEL-----------------GVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHESHAMYVKGvdlFMDQFDdkMTTDDVFLSFLPLAHilDrmieeyffhkgASIGyyhgdlnalrddivELKP 318
Cdd:COG1020 631 RPKGVMVEHRALVNLLAW---MQRRYG--LGPGDRVLQFASLSF--D-----------ASVW--------------EIFG 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 TLLVG-----VPRVYERIYEGILKAIAElrplRRV-IFNAlynrklasmkagyshkTASPFADMLAfrkVKARLGGRLRL 392
Cdd:COG1020 679 ALLSGatlvlAPPEARRDPAALAELLAR----HRVtVLNL----------------TPSLLRALLD---AAPEALPSLRL 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 393 LISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSA---GVPATYTEI-----RLEEVPemgyn 463
Cdd:COG1020 736 VLVGGEALPPElVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSvpiGRPIANTRVyvldaHLQPVP----- 810
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 464 pLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDG--------WFHTGDIGEMTPDGIL 514
Cdd:COG1020 811 -VGVP--GELYIGGAGLARGYLNRPELTAERFVADpfgfpgarLYRTGDLARWLPDGNL 866
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
83-634 |
4.37e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 100.86 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQ-- 160
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDrs 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 161 -DKKIKEILSPNCKSAKRLKALVAFT----SATTEQNKEADqigikmyaWDDFLKVGKDNP----RQPCPPQASDICTVM 231
Cdd:PLN03102 121 fEPLAREVLHLLSSEDSNLNLPVIFIheidFPKRPSSEELD--------YECLIQRGEPTPslvaRMFRIQDEHDPISLN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 232 YTSGTSGQPKGVMLTHEshAMYVKGVDLFMDQfddKMTTDDVFLSFLPLAHIldrmiEEYFF------HKGASIGYYHgd 305
Cdd:PLN03102 193 YTSGTTADPKGVVISHR--GAYLSTLSAIIGW---EMGTCPVYLWTLPMFHC-----NGWTFtwgtaaRGGTSVCMRH-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 306 lnalrddivelkptllVGVPRVYERIYegiLKAIAELRPLRRViFNALynrkLASMKAGYSHKTaspfadmlafrkvkar 385
Cdd:PLN03102 261 ----------------VTAPEIYKNIE---MHNVTHMCCVPTV-FNIL----LKGNSLDLSPRS---------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 386 lgGRLRLLISGGAPLSNEIEEFMRVTTcaYFIQGYGLTETLGPSTVCYIDD----------MALVGSAGVPA-TYTEIRL 454
Cdd:PLN03102 301 --GPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDewnrlpenqqMELKARQGVSIlGLADVDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 455 EEVPEMGYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAV 534
Cdd:PLN03102 377 KNKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 535 EYLEKV-YGFPPLVEdiwvygdsfrSSLVAVVNPhqentmKWAES--------NGYKGSFDEICKL---EG-LKEYILKE 601
Cdd:PLN03102 456 VEVENVlYKYPKVLE----------TAVVAMPHP------TWGETpcafvvleKGETTKEDRVDKLvtrERdLIEYCREN 519
|
570 580 590
....*....|....*....|....*....|....*..
gi 226491570 602 LAAVAQKNKLRGFEYI----KGVVLDPVPFDIERDLV 634
Cdd:PLN03102 520 LPHFMCPRKVVFLQELpkngNGKILKPKLRDIAKGLV 556
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
69-521 |
5.18e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.95 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 69 RPFKDGVPGPYLwkSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYI 148
Cdd:PRK07514 18 APFIETPDGLRY--TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 149 IDHAEIDVVfIQDKKIKEILSPnckSAKRLKALVAFTsatteqnKEADQIGikmyawdDFLKVGKDNP--RQPCPPQASD 226
Cdd:PRK07514 96 IGDAEPALV-VCDPANFAWLSK---IAAAAGAPHVET-------LDADGTG-------SLLEAAAAAPddFETVPRGADD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 227 ICTVMYTSGTSGQPKGVMLTHE---SHAMYVKGVDLFmdqfddkmTTDDVFLSFLPLAH----------IL---DRMIee 290
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGnllSNALTLVDYWRF--------TPDDVLIHALPIFHthglfvatnvALlagASMI-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 291 yFFHKgasigyyhgdLNAlrDDIVELKP--TLLVGVPrvyeriyegilkaiaelrplrrvifnALYNRKLASmkAGYSHK 368
Cdd:PRK07514 228 -FLPK----------FDP--DAVLALMPraTVMMGVP--------------------------TFYTRLLQE--PRLTRE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 369 TASpfadmlafrkvkarlggRLRLLISGGAPLSNEI-EEFMRVTTCAyFIQGYGLTETLGPSTVCYiDDMALVGSAGVPA 447
Cdd:PRK07514 267 AAA-----------------HMRLFISGSAPLLAEThREFQERTGHA-ILERYGMTETNMNTSNPY-DGERRAGTVGFPL 327
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 448 TYTEIRLEEvPEMGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKK 521
Cdd:PRK07514 328 PGVSLRVTD-PETG-AELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
217-520 |
5.71e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 99.68 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 217 RQPCPPQASdICTVMYTSGTSGQPKGVMLTHESHAmyvKGVDLFMDQFDdkMTTDDVFLSFLPLAHIldrmieeyffHkg 296
Cdd:PRK07787 121 RYPEPDPDA-PALIVYTSGTTGPPKGVVLSRRAIA---ADLDALAEAWQ--WTADDVLVHGLPLFHV----------H-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 297 asiGYYHGDLNALR----------------DDIVELKPTLLVGVPRVYERIyegilkaiaelrplrrvifnalynrklas 360
Cdd:PRK07787 183 ---GLVLGVLGPLRignrfvhtgrptpeayAQALSEGGTLYFGVPTVWSRI----------------------------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 361 mkagyshkTASPFAdmlafrkvkARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLgPSTVCYIDDMALV 440
Cdd:PRK07787 231 --------AADPEA---------ARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETL-ITLSTRADGERRP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 441 GSAGVPATYTEIRL-----EEVPEMGynplgvPSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGIL 514
Cdd:PRK07787 293 GWVGLPLAGVETRLvdedgGPVPHDG------ETVGELQVRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMH 366
|
....*.
gi 226491570 515 KVIDRK 520
Cdd:PRK07787 367 RIVGRE 372
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
83-540 |
1.54e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 98.63 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVF--IQ 160
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLfdLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 161 DKKIKEILSPNCKSAKRLKALvaftsaTTEQNKEADQIGIKMY-AWddflkVGKDNPRQPCPP----QASDICtvmYTSG 235
Cdd:PRK07008 121 FLPLVDALAPQCPNVKGWVAM------TDAAHLPAGSTPLLCYeTL-----VGAQDGDYDWPRfdenQASSLC---YTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 236 TSGQPKGVMLTHESHAMYVKGVDLfmdqfDDKM--TTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLN--ALRD 311
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGAAL-----PDAMglSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDgkSLYE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 DIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIfnalynrklasmkAGYShktASPFADMLAFRkvkarlggrlr 391
Cdd:PRK07008 262 LIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTV-------------IGGS---ACPPAMIRTFE----------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 392 llisggaplsneiEEF-MRVttcayfIQGYGLTETLGPSTVC-------------------------YIDDMALVGSAGv 445
Cdd:PRK07008 315 -------------DEYgVEV------IHAWGMTEMSPLGTLCklkwkhsqlpldeqrkllekqgrviYGVDMKIVGDDG- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 446 patyteirlEEVPEMGynplgvPSRGEICIRGKSLFAGYYKSpelTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFK 525
Cdd:PRK07008 375 ---------RELPWDG------KAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIK 436
|
490
....*....|....*
gi 226491570 526 lSQGEYVAVEYLEKV 540
Cdd:PRK07008 437 -SGGEWISSIDIENV 450
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
230-554 |
3.45e-21 |
|
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: 95.03 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 230 VMYTSGTSGQPKGVMLTHES------HAMYVKGVdlfmdqfddkmTTDDVFLSFLPLAHILDRMIEEYFFHKGAS---IG 300
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNliaanlQLIHAMGL-----------TEADVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 301 YYhgDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVifnalynrklasmkagyshktaspfadmlafr 380
Cdd:cd17637 74 KF--DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV-------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 381 kvkarlggrlrllisGGAPLSNEIEEFmRVTTCAYFIQGYGLTETLGPSTVCYIDDMAlvGSAGVPATYTEIRLeeVPEM 460
Cdd:cd17637 120 ---------------LGLDAPETIQRF-EETTGATFWSLYGQTETSGLVTLSPYRERP--GSAGRPGPLVRVRI--VDDN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 461 GyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRK--KNIFKlSQGEYVAVEYLE 538
Cdd:cd17637 180 D-RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVE 257
|
330
....*....|....*.
gi 226491570 539 KVYGFPPLVEDIWVYG 554
Cdd:cd17637 258 KVILEHPAIAEVCVIG 273
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-523 |
4.78e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 95.02 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 225 SDICTVMYTSGTSGQPKGVMLTHEShaMYVKGVDLFMDQFDdkMTTDDVFLSFLPLAHI--LDRMIEEYFFHKGASIGYY 302
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKT--FFAVPDILQKEGLN--WVVGDVTYLPLPATHIggLWWILTCLIHGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 HGDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNAlynrklasmkagyshktASPFADMLAFrkv 382
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGG-----------------SRAIAADVRF--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 383 karlggrlrllisggaplsneIEEFMRVTTcayfIQGYGLTETlgpSTVCYI---DDMALVGSAGVPATYTEIRLE---- 455
Cdd:cd17635 137 ---------------------IEATGLTNT----AQVYGLSET---GTALCLptdDDSIEINAVGRPYPGVDVYLAatdg 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 456 -EVPEMGYnplgvpsrGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:cd17635 189 iAGPSASF--------GTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSES 249
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
81-667 |
8.07e-21 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 98.00 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 81 WKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLydtLGAG-AVDYIIDHAEIDVVFI 159
Cdd:PTZ00297 457 WLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPL---VGKGsTMRTLIDEHKIKVVFA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 QDKKIKEILSpnCKSAKrLKALVAFTS-ATTEQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQASD-ICTVMYTSGTS 237
Cdd:PTZ00297 534 DRNSVAAILT--CRSRK-LETVVYTHSfYDEDDHAVARDLNITLIPYEFVEQKGRLCPVPLKEHVTTDtVFTYVVDNTTS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTHESHAMYVKGVD-LFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYhgDLNALRDDIVEL 316
Cdd:PTZ00297 611 ASGDGLAVVRVTHADVLRDIStLVMTGVLPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATV--DAAHLQRAFVKF 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 317 KPTLLVGVPRVYeriyegilkAIAELRPLRR-----VIFNALYNR--KLASMKAgYSHKTASPFADMLAFRKVKARLGGR 389
Cdd:PTZ00297 689 QPTILVAAPSLF---------STSRLQLSRAnerysAVYSWLFERafQLRSRLI-NIHRRDSSLLRFIFFRATQELLGGC 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LR--LLISGGAPLSNEIEEFMRV--TTC---AYFIQGYGltetlgpstVCYIDdmalvgsaGVPATYTEIRLEevpemgy 462
Cdd:PTZ00297 759 VEkiVLCVSEESTSFSLLEHISVcyVPClreVFFLPSEG---------VFCVD--------GTPAPSLQVDLE------- 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 463 nPLGVPSR----GEICIRGKSlfagyykSPELTNEaIVDGWFHTGDIGEM-TPDGILKVIdrkknifklsQGEYVAVEYL 537
Cdd:PTZ00297 815 -PFDEPSDgagiGQLVLAKKG-------EPRRTLP-IAAQWKRDRTLRLLgPPLGILLPV----------AYEYVIAAEL 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 538 EKVYGFPPLVEDIWVYGDSFRsSLVAVVNPHQENT-MKWAESNGyKGSFDEICKLEGLKEY-------ILKELAAVAQKN 609
Cdd:PTZ00297 876 ERIFSQSRYVNDIFLYADPSR-PIIAIVSPNRDTVeFEWRQSHC-MGEGGGPARQLGWTELvayasslLTADFACIAKEN 953
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 610 KLRGFEYIKGVVLDPVPFDIERDLVTATMKKKRKNMLNYYQSEIDTIYKKLEAQKSAA 667
Cdd:PTZ00297 954 GLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDVETTPLPT 1011
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
219-554 |
1.05e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 96.45 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 219 PCPP-QASDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMdQFDDKM----TTDDVFLSFLPLAHILdrmieeyff 293
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRN---LIAMVELFV-RFEASQyeypGSDNVYLAALPMFHIY--------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 294 hkGASIgyYHGDLNALRDDIVELKPTLLVGVPRVYERIyegilkaiaelrplrrvifnalynrklasmkaGYSHKTASPF 373
Cdd:PLN02574 258 --GLSL--FVVGLLSLGSTIVVMRRFDASDMVKVIDRF--------------------------------KVTHFPVVPP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 374 ADMLAFRKVKARLGG---RLRLLISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCY-IDDMALVGSAGVPAT 448
Cdd:PLN02574 302 ILMALTKKAKGVCGEvlkSLKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAVGTRGFnTEKLSKYSSVGLLAP 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 449 YTEIRLEEVPEMGYNPLGvpSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLs 527
Cdd:PLN02574 382 NMQAKVVDWSTGCLLPPG--NCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY- 458
|
330 340
....*....|....*....|....*..
gi 226491570 528 QGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:PLN02574 459 KGFQIAPADLEAVLISHPEIIDAAVTA 485
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
83-521 |
1.17e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 96.56 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCvPLYDTLGAGAVDYIIDHAEIDVV----- 157
Cdd:PRK07529 60 TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLvtlgp 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 158 -FIQD--KKIKEILSPncksAKRLKALVAFTSA---TTEQNKEADQI----GIKMYAWDDFLKVGKDN-PRQPCPPQASD 226
Cdd:PRK07529 139 fPGTDiwQKVAEVLAA----LPELRTVVEVDLArylPGPKRLAVPLIrrkaHARILDFDAELARQPGDrLFSGRPIGPDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 227 ICTVMYTSGTSGQPKGVMLTH--ESHAMYVKGVDLFMDQfddkmttDDVFLSFLPLAHILDRM-IEEYFFHKGASI---- 299
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHgnEVANAWLGALLLGLGP-------GDTVFCGLPLFHVNALLvTGLAPLARGAHVvlat 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 300 --GYyhgdlnalRDD--------IVE-LKPTLLVGVPRVYEriyegilkaiaelrplrrvifnalynrklasmkagyshk 368
Cdd:PRK07529 288 pqGY--------RGPgvianfwkIVErYRINFLSGVPTVYA--------------------------------------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 369 taspfadMLAFRKVKARLGGRLRLLISGGAPLSNE-IEEFMRVTTCAyFIQGYGLTETLGPSTVCYIDDMALVGSAGVPA 447
Cdd:PRK07529 321 -------ALLQVPVDGHDISSLRYALCGAAPLPVEvFRRFEAATGVR-IVEGYGLTEATCVSSVNPPDGERRIGSVGLRL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 448 TYTEIRLEEVPEMGYNP--LGVPSRGEICIRGKSLFAGYykspelTNEA------IVDGWFHTGDIGEMTPDGILKVIDR 519
Cdd:PRK07529 393 PYQRVRVVILDDAGRYLrdCAVDEVGVLCIAGPNVFSGY------LEAAhnkglwLEDGWLNTGDLGRIDADGYFWLTGR 466
|
..
gi 226491570 520 KK 521
Cdd:PRK07529 467 AK 468
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-519 |
1.58e-20 |
|
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: 95.35 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAM----QACNGYslvcVPLYDTLGAGAVDYIIdhaeidvvf 158
Cdd:cd12117 24 TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALlavlKAGAAY----VPLDPELPAERLAFML--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 iQDKKIKEILSpnCKSAKRLKALVAFTSATTEQNKEADQigikmyawddflkvgkDNPRqpCPPQASDICTVMYTSGTSG 238
Cdd:cd12117 91 -ADAGAKVLLT--DRSLAGRAGGLEVAVVIDEALDAGPA----------------GNPA--VPVSPDDLAYVMYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHESHAMYVKGVDlFMDqfddkMTTDDVFLSFLPLAhiLDRMIEEYFfhkGASigyyhgdLNALRddivelkp 318
Cdd:cd12117 150 RPKGVAVTHRGVVRLVKNTN-YVT-----LGPDDRVLQTSPLA--FDASTFEIW---GAL-------LNGAR-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 tlLVGVPrvyeriyEGILKAIAELRplrrvifNALYNRKLASMkagysHKTASPFaDMLAfRKVKARLGGrLRLLISGGA 398
Cdd:cd12117 204 --LVLAP-------KGTLLDPDALG-------ALIAEEGVTVL-----WLTAALF-NQLA-DEDPECFAG-LRELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 399 PLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSA---GVPATYTEIRLeevpeMGYN----PLGVPsr 470
Cdd:cd12117 260 VVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSipiGRPIANTRVYV-----LDEDgrpvPPGVP-- 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 226491570 471 GEICIRGKSLFAGYYKSPELTNEAIV-----DG--WFHTGDIGEMTPDGILKVIDR 519
Cdd:cd12117 333 GELYVGGDGLALGYLNRPALTAERFVadpfgPGerLYRTGDLARWLPDGRLEFLGR 388
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
83-526 |
4.69e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 93.51 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDk 162
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakRLKALVAFTSATTEQNKEADqigikmyawddflKVGKDNPRQPCPPqaSDICTVMYTSGTSGQPKG 242
Cdd:cd12116 93 --------------ALPDRLPAGLPVLLLALAAA-------------AAAPAAPRTPVSP--DDLAYVIYTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES-----HAMyvkgvdlfMDQFDdkMTTDDVFLSflplahildrmIEEYFFhkgasigyyhgDLNALrddivELK 317
Cdd:cd12116 144 VVVSHRNlvnflHSM--------RERLG--LGPGDRLLA-----------VTTYAF-----------DISLL-----ELL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 318 PTLLVGVpRVYERIYEGILKAIAELRPLRRvifnalynrklasmkAGYSHKTASP-FADMLAFRKVKARLGgrLRLLIsG 396
Cdd:cd12116 187 LPLLAGA-RVVIAPRETQRDPEALARLIEA---------------HSITVMQATPaTWRMLLDAGWQGRAG--LTALC-G 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 397 GAPLSNEIEEFMRVTTCAyFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEI-----RLEEVPEmgynplGVPsrG 471
Cdd:cd12116 248 GEALPPDLAARLLSRVGS-LWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVyvldaALRPVPP------GVP--G 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226491570 472 EICIRGKSLFAGYYKSPELTNEAIVDG--------WFHTGDIGEMTPDGILKVIDRKKNIFKL 526
Cdd:cd12116 319 ELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI 381
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
75-548 |
9.53e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 93.28 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 75 VPGPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEi 154
Cdd:PRK06018 33 VEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 155 DVVFIQDKKIKEILSPNCKSAKRLKALVAFTSA-----TTEQNKEADQIGIKM----YAWDDFlkvgKDNprqpcppQAS 225
Cdd:PRK06018 112 DRVVITDLTFVPILEKIADKLPSVERYVVLTDAahmpqTTLKNAVAYEEWIAEadgdFAWKTF----DEN-------TAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICtvmYTSGTSGQPKGVMLTHES---HAMYVKGVDLFmdqfddKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYY 302
Cdd:PRK06018 181 GMC---YTSGTTGDPKGVLYSHRSnvlHALMANNGDAL------GTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 HGDLNALrdDIVEL----KPTLLVGVPRVYERIYEGILKAIAELRPLRRVIFNAlynrklasmkagyshkTASPFADMLA 378
Cdd:PRK06018 252 GAKLDGA--SVYELldteKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGG----------------SAMPRSMIKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 379 FRKVKARLggrlrllisggaplsneieefmrvttcayfIQGYGLTETLGPSTVCYIdDMALVGSAGvpatytEIRLEEVP 458
Cdd:PRK06018 314 FEDMGVEV------------------------------RHAWGMTEMSPLGTLAAL-KPPFSKLPG------DARLDVLQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 459 EMGYNPLGV------------PSRGEIC----IRGKSLFAGYYKSpeltNEAIVD--GWFHTGDIGEMTPDGILKVIDRK 520
Cdd:PRK06018 357 KQGYPPFGVemkitddagkelPWDGKTFgrlkVRGPAVAAAYYRV----DGEILDddGFFDTGDVATIDAYGYMRITDRS 432
|
490 500
....*....|....*....|....*....
gi 226491570 521 KNIFKlSQGEYVAVEYLEKV-YGFPPLVE 548
Cdd:PRK06018 433 KDVIK-SGGEWISSIDLENLaVGHPKVAE 460
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
83-577 |
3.46e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.77 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQ-KLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEiDVVFIQD 161
Cdd:PRK05620 40 TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAE-DEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 KKIKEILSPNCKSAKRLKALVAFTSATTEQNKEADQIGIKMYAWDDFLKvGK----DNPRQPcPPQASDICtvmYTSGTS 237
Cdd:PRK05620 119 PRLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRstvyDWPELD-ETTAAAIC---YSTGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTHES---HAMYVKGVDLFmdqfddKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIGYYHGDLNA--LRDD 312
Cdd:PRK05620 194 GAPKGVVYSHRSlylQSLSLRTTDSL------AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSAptLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 313 IVELKPTLLVGVPRVYERIYEGILKaiaelRPLRRVifnalynrklasmkagyshktaspfadmlafrkvkarlggRLRL 392
Cdd:PRK05620 268 IATAMPRVAHGVPTLWIQLMVHYLK-----NPPERM----------------------------------------SLQE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 393 LISGGAPLSNEI----EEFMRVTTcayfIQGYGLTETLGPSTVCYiddmalvGSAGVPAtytEIRLEEVPEMGYNPLGVP 468
Cdd:PRK05620 303 IYVGGSAVPPILikawEERYGVDV----VHVWGMTETSPVGTVAR-------PPSGVSG---EARWAYRVSQGRFPASLE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 469 SR---------------GEICIRGKSLFAGYYKSPELTNEA-----------------IVDGWFHTGDIGEMTPDGILKV 516
Cdd:PRK05620 369 YRivndgqvmestdrneGEIQVRGNWVTASYYHSPTEEGGGaastfrgedvedandrfTADGWLRTGDVGSVTRDGFLTI 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226491570 517 IDRKKNIFKlSQGEYVAVEYLEK------------VYGFPplvEDIWVYgdsfRSSLVAVVNPHQENTMKWAE 577
Cdd:PRK05620 449 HDRARDVIR-SGGEWIYSAQLENyimaapevvecaVIGYP---DDKWGE----RPLAVTVLAPGIEPTRETAE 513
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
221-519 |
3.75e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 92.29 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 221 PPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGV-DLFMdqfddkMTTDDVFLSFLPlahildrmieeyFFHkgaSI 299
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQIsDVFN------LRNDDVILSSLP------------FFH---SF 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 300 GYyhgdlnalrddIVELKPTLLVGVPRVYE---RIYEGILKAIAELRplrrvifnalynrklASMKAGyshkTASPFADM 376
Cdd:PRK08633 837 GL-----------TVTLWLPLLEGIKVVYHpdpTDALGIAKLVAKHR---------------ATILLG----TPTFLRLY 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 377 LAFRKVKARLGGRLRLLISGGAPLSNEI-EEF-MRvttcayF----IQGYGLTETLGPSTVCYIDDMA---------LVG 441
Cdd:PRK08633 887 LRNKKLHPLMFASLRLVVAGAEKLKPEVaDAFeEK------FgiriLEGYGATETSPVASVNLPDVLAadfkrqtgsKEG 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 442 SAGVPATYTEIRLeeVPEMGYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVD----GWFHTGDIGEMTPDGILKVI 517
Cdd:PRK08633 961 SVGMPLPGVAVRI--VDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTIT 1038
|
..
gi 226491570 518 DR 519
Cdd:PRK08633 1039 DR 1040
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-523 |
9.55e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 88.31 E-value: 9.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 225 SDICTVMYTSGTSGQPKGVMLTHeSHAMYvkgvDLFMDQFDDKMTTDDVFLSFLPLAHILDRMIEEYF-FHKGASI---- 299
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTH-SNEVY----NAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVvlag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 300 --GYYHgdlNALRDDIVEL----KPTLLVGVPRVYeriyegilkAIAELRPLrrvifnalyNRKLASmkagyshktaspf 373
Cdd:cd05944 77 paGYRN---PGLFDNFWKLveryRITSLSTVPTVY---------AALLQVPV---------NADISS------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 374 admlafrkvkarlggrLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIR 453
Cdd:cd05944 123 ----------------LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVR 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 454 LEEVPEMGYN--PLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:cd05944 187 IKVLDGVGRLlrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-527 |
1.47e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 89.04 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 93 QAGSALQKLGVQPGSRVGIYGANCPQWI-----VAMQACNgYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDkkikei 167
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIelsfaVAYAGGR-LGLVFVPLNPTLKESVLRYLVADAGGRIVLADA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 168 lspncKSAKRLK-ALVAFTSATTEQNKEAdqigikmyAWDDflkvGKDNPRQPCPPQasDICTVMYTSGTSGQPKGVMLT 246
Cdd:cd05922 78 -----GAADRLRdALPASPDPGTVLDADG--------IRAA----RASAPAHEVSHE--DLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 247 HESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAHILDRMIEEYFFHKGASI----GYYHGDlnALRDDIVELKPTLLV 322
Cdd:cd05922 139 HQNLLANARSIAEYLG-----ITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDD--AFWEDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 GVPRVYERiyegilkaiaelrpLRRVIFNalynrklasmKAGYSHktaspfadmlafrkvkarlggrLRLLISGGAPLSN 402
Cdd:cd05922 212 GVPSTYAM--------------LTRLGFD----------PAKLPS----------------------LRYLTQAGGRLPQ 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 403 E-IEEFMRVTTCAYFIQGYGLTETLGPSTvcYID-DMAL--VGSAGVPATYTEIRLEEVPEmgyNPLGVPSRGEICIRGK 478
Cdd:cd05922 246 EtIARLRELLPGAQVYVMYGQTEATRRMT--YLPpERILekPGSIGLAIPGGEFEILDDDG---TPTPPGEPGEIVHRGP 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 226491570 479 SLFAGYYKSP-ELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:cd05922 321 NVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF 370
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
83-519 |
1.82e-18 |
|
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: 88.92 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVA----MQACNGYslvcVPLYDTLGAGAVDYIIDHAEIDVVF 158
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGilgiLKAGGAY----LPIDPDYPEERIQYILEDSGADILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 IQdkkikeilspncksaKRLKALVAFTSATTEQNKEADQIGikmyawddflkvGKDNPRQPCppQASDICTVMYTSGTSG 238
Cdd:cd17655 100 TQ---------------SHLQPPIAFIGLIDLLDEDTIYHE------------ESENLEPVS--KSDDLAYVIYTSGSTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHESHAMYVKGVDLFMDQfddkmTTDDVFLSFLPLAhiLDRMIEEYFfhkgasigyyhgdlnalrddivelkP 318
Cdd:cd17655 151 KPKGVMIEHRGVVNLVEWANKVIYQ-----GEHLRVALFASIS--FDASVTEIF-------------------------A 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 TLLVGvprvyERIYEGILKAIAELRPLRRVIfnalynrklasMKAGYSHKTASP-FADMLAfrKVKARLGGRLRLLISGG 397
Cdd:cd17655 199 SLLSG-----NTLYIVRKETVLDGQALTQYI-----------RQNRITIIDLTPaHLKLLD--AADDSEGLSLKHLIVGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 398 APLSNEIEE--FMRVTTCAYFIQGYGLTETlgpsTVC---YIDDMALVGSA----GVPATYTEIRLEEvPEMGYNPLGVP 468
Cdd:cd17655 261 EALSTELAKkiIELFGTNPTITNAYGPTET----TVDasiYQYEPETDQQVsvpiGKPLGNTRIYILD-QYGRPQPVGVA 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 469 srGEICIRGKSLFAGYYKSPELTNEAIVDGWF-------HTGDIGEMTPDGILKVIDR 519
Cdd:cd17655 336 --GELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermyRTGDLARWLPDGNIEFLGR 391
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
83-506 |
2.08e-18 |
|
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: 89.22 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGvQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDY---IIDHAEIDVVFI 159
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERlaaILADAGPRVVLT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 qdkkikeilspnckSAKRLKALVAFTSATTEQnkEADQIgikmyAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQ 239
Cdd:cd05931 105 --------------TAAALAAVRAFAASRPAA--GTPRL-----LVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHES----HAMYVKGVDLfmdqfddkmTTDDVFLSFLPLAHildrmieeyffhkgasigyyhgDLnALrddIVE 315
Cdd:cd05931 164 PKGVVVTHRNllanVRQIRRAYGL---------DPGDVVVSWLPLYH----------------------DM-GL---IGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 316 LKPTLLVGVPRVYeriyegiLKAIAEL-RPLR--RVIfnalyNRKLASMkagyshkTASP-FADMLAFRKVKAR-LGG-- 388
Cdd:cd05931 209 LLTPLYSGGPSVL-------MSPAAFLrRPLRwlRLI-----SRYRATI-------SAAPnFAYDLCVRRVRDEdLEGld 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 389 --RLRLLISGGAPLSNE-IEEF--------MRVTTcayFIQGYGLTE-TL--------GPSTVCYIDDMALVGSAGVPAT 448
Cdd:cd05931 270 lsSWRVALNGAEPVRPAtLRRFaeafapfgFRPEA---FRPSYGLAEaTLfvsggppgTGPVVLRVDRDALAGRAVAVAA 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 449 YTEIRLE------EVPEMGY---NPLG---VPSR--GEICIRGKSLFAGYYKSPELTNEAIV-------DGWFHTGDIG 506
Cdd:cd05931 347 DDPAARElvscgrPLPDQEVrivDPETgreLPDGevGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLG 425
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
83-567 |
5.79e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 87.63 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPnckSAKRLKALVAFTSATTeqnkeadqigikmyAWDDFLKVGKDNPRQPCPPQAS------DICTVMYTSGT 236
Cdd:PRK05852 125 GPHDRAEP---TTRWWPLTVNVGGDSG--------------PSGGTLSVHLDAATEPTPATSTpeglrpDDAMIMFTGGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHESHAMYVKGVDLFMdqfddKMTTDDVFLSFLPL--AHILDRMIEEYFFHKGASIGYYHGDLNA--LRDD 312
Cdd:PRK05852 188 TGLPKMVPWTHANIASSVRAIITGY-----RLSPRDATVAVMPLyhGHGLIAALLATLASGGAVLLPARGRFSAhtFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 313 IVELKPTLLVGVPRVYEriyegILKAIAELRPLRRvifnalynrklasmkagyshKTASpfadmlafrkvkarlggrLRL 392
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQ-----ILLERAATEPSGR--------------------KPAA------------------LRF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 393 LISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDM----------ALVGSAGVPatytEIRLeeVPEMGy 462
Cdd:PRK05852 300 IRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIgqtenpvvstGLVGRSTGA----QIRI--VGSDG- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 463 NPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYG 542
Cdd:PRK05852 373 LPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLA 451
|
490 500
....*....|....*....|....*...
gi 226491570 543 FPPLVEDIWVYGD---SFRSSLVAVVNP 567
Cdd:PRK05852 452 SHPNVMEAAVFGVpdqLYGEAVAAVIVP 479
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
77-554 |
1.40e-17 |
|
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: 86.33 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWK--SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIV----AMQACNGYSLVCvPLYDTLGA--GAVDYI 148
Cdd:cd05921 19 GNGGWRrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALmalaAMYAGVPAAPVS-PAYSLMSQdlAKLKHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 149 IDHAEIDVVFIQD-----KKIKEILSPNcKSAKRLKALVAFTSATTEQNKEADQIGIKMYAwdDFLKVGKDnprqpcppq 223
Cdd:cd05921 98 FELLKPGLVFAQDaapfaRALAAIFPLG-TPLVVSRNAVAGRGAISFAELAATPPTAAVDA--AFAAVGPD--------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 224 asDICTVMYTSGTSGQPKGVMLTHeshAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILdrmieeyffhkGASIGY-- 301
Cdd:cd05921 166 --TVAKFLFTSGSTGLPKAVINTQ---RMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTF-----------GGNHNFnl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 302 --YHGDLNALRDDivelKPTllvgvPRVYERIyegiLKAIAELRPLrrVIFNAlynrklasmKAGYshktaspfaDML-- 377
Cdd:cd05921 230 vlYNGGTLYIDDG----KPM-----PGGFEET----LRNLREISPT--VYFNV---------PAGW---------EMLva 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 378 AFRK---VKARLGGRLRLLISGGAPLSNEIEEFMR---VTTCAY---FIQGYGLTETLGPSTVCYiDDMALVGSAGVPAT 448
Cdd:cd05921 277 ALEKdeaLRRRFFKRLKLMFYAGAGLSQDVWDRLQalaVATVGEripMMAGLGATETAPTATFTH-WPTERSGLIGLPAP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 449 YTEIRLeevpemgynplgVPSRG--EICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMT-PDGILKVID---RKK 521
Cdd:cd05921 356 GTELKL------------VPSGGkyEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAKLAdPDDPAKGLVfdgRVA 423
|
490 500 510
....*....|....*....|....*....|....*
gi 226491570 522 NIFKLSQGEYVAVEYL--EKVYGFPPLVEDIWVYG 554
Cdd:cd05921 424 EDFKLASGTWVSVGPLraRAVAACAPLVHDAVVAG 458
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
83-554 |
2.66e-17 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 85.83 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMqacngysLVCVPLydtlgaGAVdyiidHAeidVVF---- 158
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAM-------LACARI------GAI-----HS---VVFggfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 -------IQDKKIKEILSPNC--KSAKR--LKALV--AFTSATTEQNK-----------EADQIGiKMYAWDDFLKvgKD 214
Cdd:cd05967 143 akelasrIDDAKPKLIVTASCgiEPGKVvpYKPLLdkALELSGHKPHHvlvlnrpqvpaDLTKPG-RDLDWSELLA--KA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 215 NPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVdlfMDQFDDkMTTDDVFLSflplahildrmieeyffh 294
Cdd:cd05967 220 EPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWS---MRNIYG-IKPGDVWWA------------------ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 295 kGASIGYYHGdlnalRDDIVeLKPtLLVGVPRVyerIYEGilkaiaelRPLR--------RVIfnalynrklasmkagYS 366
Cdd:cd05967 278 -ASDVGWVVG-----HSYIV-YGP-LLHGATTV---LYEG--------KPVGtpdpgafwRVI---------------EK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 367 HKTASPFADMLAFRKVK-----ARLG-----GRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCY--I 434
Cdd:cd05967 324 YQVNALFTAPTAIRAIRkedpdGKYIkkydlSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPvgL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 435 DDMAL-VGSAGVPAT-YteiRLEEVPEMGyNPLGVPSRGEICIRG---KSLFAGYYKSPELTNEAIV---DGWFHTGDIG 506
Cdd:cd05967 404 EPLPIkAGSPGKPVPgY---QVQVLDEDG-EPVGPNELGNIVIKLplpPGCLLTLWKNDERFKKLYLskfPGYYDTGDAG 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 226491570 507 EMTPDGILKVIDRKKNIF-----KLSQGEyvaveyLEKVYGFPPLVEDIWVYG 554
Cdd:cd05967 480 YKDEDGYLFIMGRTDDVInvaghRLSTGE------MEESVLSHPAVAECAVVG 526
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
77-523 |
5.21e-17 |
|
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: 84.46 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 77 GPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLydtlgagAVDYIIDHaEIDV 156
Cdd:cd05908 11 KKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV-------SIGSNEEH-KLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 157 VFIQDKKIKEILSPNCKSAKRLKALVAFtsatteqnkeadqigikmyawddflkvgkdnprqpcppqasdictVMYTSGT 236
Cdd:cd05908 83 NKVWNTLKNPYLITEEEVLCELADELAF---------------------------------------------IQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHEShamYVKGVDLFMDQFDdkMTTDDVFLSFLPLAHILDrMIEeyfFHkgasigyyhgdlnalrddiveL 316
Cdd:cd05908 118 TGDPKGVMLTHEN---LVHNMFAILNSTE--WKTKDRILSWMPLTHDMG-LIA---FH---------------------L 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 317 KPtLLVGVPRVyeriyegilkaiaeLRPLRRVIfnalyNRKLASMKAGYSHK---TASP-FADMLAFRKVKARLG----- 387
Cdd:cd05908 168 AP-LIAGMNQY--------------LMPTRLFI-----RRPILWLKKASEHKatiVSSPnFGYKYFLKTLKPEKAndwdl 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 388 GRLRLLISGGAPLSNE-IEEFMrvTTCAYF-------IQGYGLTE-TLG--------PSTVCYIDDMALVGSAGVPAT-- 448
Cdd:cd05908 228 SSIRMILNGAEPIDYElCHEFL--DHMSKYglkrnaiLPVYGLAEaSVGaslpkaqsPFKTITLGRRHVTHGEPEPEVdk 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 449 ----------------YTEIRL-----EEVPEMGYnplgvpsrGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIG 506
Cdd:cd05908 306 kdsecltfvevgkpidETDIRIcdednKILPDGYI--------GHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLG 377
|
490
....*....|....*..
gi 226491570 507 EMTpDGILKVIDRKKNI 523
Cdd:cd05908 378 FIR-NGRLVITGREKDI 393
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
83-281 |
7.28e-17 |
|
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: 84.06 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVfIQDK 162
Cdd:TIGR03098 27 TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNCKSAKRLKALVAFTSATTEQNKEAdqiGIKMYAWDDFLKVGKDNPRQPCPPqaSDICTVMYTSGTSGQPKG 242
Cdd:TIGR03098 106 ERLDLLHPALPGCHDLRTLIIVGDPAHASEGHP---GEEPASWPKLLALGDADPPHPVID--SDMAAILYTSGSTGRPKG 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 226491570 243 VMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLA 281
Cdd:TIGR03098 181 VVLSHRNLVAGAQSVATYLE-----NRPDDRLLAVLPLS 214
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
82-642 |
1.55e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 83.31 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 82 KSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCP---QWIVAMqACNGYslVCVPL----------YDTLGAGAVDYI 148
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDlylEWLLAV-ACAGG--IVAPLnyrwsfeeakSAMLLVRPVMLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 149 IDHA------EIDVVFIQDKKIKEILSPNCKSakrlKALVAFTSATTEQNKeadQIGIK----MYAWddflkvgkdnprq 218
Cdd:PLN02860 110 TDETcsswyeELQNDRLPSLMWQVFLESPSSS----VFIFLNSFLTTEMLK---QRALGttelDYAW------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 219 pCPPQASDICtvmYTSGTSGQPKGVMLTHEShamyvkgvdlFMDQFDDKMT-----TDDVFLSFLPLAHIldrmieeyff 293
Cdd:PLN02860 170 -APDDAVLIC---FTSGTTGRPKGVTISHSA----------LIVQSLAKIAivgygEDDVYLHTAPLCHI---------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 294 hKGASigyyhgdlNALrddivelkPTLLVGVPRVYeriyegILKAIAELrplrrvIFNALYNRKLASMKAgyshkTASPF 373
Cdd:PLN02860 226 -GGLS--------SAL--------AMLMVGACHVL------LPKFDAKA------ALQAIKQHNVTSMIT-----VPAMM 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 374 ADMLAF-RKVKARLGGR-LRLLISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYT 450
Cdd:PLN02860 272 ADLISLtRKSMTWKVFPsVRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVN 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 451 EIRLEEVPEMGYNPLGVP-------------SR-GEICIRGKSLFAGYY-KSPELTNEAIVDGWFHTGDIGEMTPDGILK 515
Cdd:PLN02860 352 QTKSSSVHQPQGVCVGKPaphvelkigldesSRvGRILTRGPHVMLGYWgQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 516 VIDRKKNIFKlSQGEYVAVEYLEKVYGFPPLVEDIWVYG--DSFRSSLV-AVVNPHQENTMKWAESNGYKGSFdEICKlE 592
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGvpDSRLTEMVvACVRLRDGWIWSDNEKENAKKNL-TLSS-E 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 226491570 593 GLKEYilkelaavAQKNKLRGFEYIKGVVLDPVPFDierdlVTATMKKKR 642
Cdd:PLN02860 509 TLRHH--------CREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRR 545
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
83-554 |
2.16e-16 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 82.14 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQ-KLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQD 161
Cdd:cd05958 12 TYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALCAH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 kkikeilspncksakrlkALVAftsatteqnkeadqigikmyawddflkvgkdnprqpcppqASDICTVMYTSGTSGQPK 241
Cdd:cd05958 92 ------------------ALTA----------------------------------------SDDICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHEShamYVKGVDLFMDQFdDKMTTDDVFLSFLPLAHILDRMIEEYF-FHKGASIgyyhgdlnalrddivelkptl 320
Cdd:cd05958 114 ATMHFHRD---PLASADRYAVNV-LRLREDDRFVGSPPLAFTFGLGGVLLFpFGVGASG--------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 321 lVGVPRvyeRIYEGILKAIAELRPlrRVIFNAlynrklasmkagyshKTAspFADMLAFRKVKARLGGRLRLLISGGAPL 400
Cdd:cd05958 169 -VLLEE---ATPDLLLSAIARYKP--TVLFTA---------------PTA--YRAMLAHPDAAGPDLSSLRKCVSAGEAL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 401 SNEIEEFMRVTTCAYFIQGYGLTETLGpstvCYI---DDMALVGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRG 477
Cdd:cd05958 226 PAALHRAWKEATGIPIIDGIGSTEMFH----IFIsarPGDARPGATGKPVPGYEAKV--VDDEG-NPVPDGTIGRLAVRG 298
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 478 KSLFagYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:cd05958 299 PTGC--RYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
97-519 |
5.65e-16 |
|
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: 81.24 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 97 ALQKLGVQPGSRVGIYGANCPQWIVAMQAcngyslvcvplydTLGAGAVDYIIDHAEidvvfiqdkkikeilsPncksAK 176
Cdd:cd17651 36 RLRARGVGPGDLVALCARRSAELVVALLA-------------ILKAGAAYVPLDPAY----------------P----AE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 177 RLKALVAFTSATT-----EQNKEADQIGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHA 251
Cdd:cd17651 83 RLAFMLADAGPVLvlthpALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 252 MYVKGVDLFMDqfddkMTTDDVFLSFLPLAhiLDRMIEEYFfhkgasigyyhgdlnalrddivelkPTLLVG----VPRV 327
Cdd:cd17651 163 NLVAWQARASS-----LGPGARTLQFAGLG--FDVSVQEIF-------------------------STLCAGatlvLPPE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 328 YERIYEGILKAIAELRPLRRVIFNALYNRKLAsmKAGYSHKTASPfadmlafrkvkarlggRLRLLISGGAPLS--NEIE 405
Cdd:cd17651 211 EVRTDPPALAAWLDEQRISRVFLPTVALRALA--EHGRPLGVRLA----------------ALRYLLTGGEQLVltEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 406 EFMRVTTCAYFIQGYGLTETlgpsTV--CYIDDMALVG-----SAGVPATYTEI-----RLEEVpemgynPLGVPsrGEI 473
Cdd:cd17651 273 EFCAGLPGLRLHNHYGPTET----HVvtALSLPGDPAAwpappPIGRPIDNTRVyvldaALRPV------PPGVP--GEL 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 226491570 474 CIRGKSLFAGYYKSPELTNEAIVDGWF-------HTGDIGEMTPDGILKVIDR 519
Cdd:cd17651 341 YIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
32-601 |
7.10e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 81.25 E-value: 7.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 32 SVLAKDGFPqLEPDMKTSWDVFRVAAVKYADNRMLGWRpfkDGVPGPYLWKSYKEIYDEVLQAGSALQKLGVQPGSRVGI 111
Cdd:PRK12582 35 SIVIKSRHP-LGPYPRSIPHLLAKWAAEAPDRPWLAQR---EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 112 YGANCPQWIVAMQACNGYSLVCVPL---YDTL--GAGAVDYIIDHAEIDVVFIQD-----KKIKEI-----------LSP 170
Cdd:PRK12582 111 LSGNSIEHALMTLAAMQAGVPAAPVspaYSLMshDHAKLKHLFDLVKPRVVFAQSgapfaRALAALdlldvtvvhvtGPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 171 NCKSAKRLKALVAfTSATTEQNKEADQIGIKMyawddflkVGKdnprqpcppqasdictVMYTSGTSGQPKGVMLTHESH 250
Cdd:PRK12582 191 EGIASIAFADLAA-TPPTAAVAAAIAAITPDT--------VAK----------------YLFTSGSTGMPKAVINTQRMM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 251 AMYVKGVDLFMDqfDDKMTTDDVFLSFLPLAHILdrmieeyffhkGASIGYyHGDLNA---LRDDivELKPtllvgVPRV 327
Cdd:PRK12582 246 CANIAMQEQLRP--REPDPPPPVSLDWMPWNHTM-----------GGNANF-NGLLWGggtLYID--DGKP-----LPGM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 328 YEriyegilKAIAELRPLRRVIFnalynrklASMKAGYShktaspfadMLAF-----RKVKARLGGRLRLLISGGAPLSN 402
Cdd:PRK12582 305 FE-------ETIRNLREISPTVY--------GNVPAGYA---------MLAEamekdDALRRSFFKNLRLMAYGGATLSD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 403 EIEEFMRVTTCAY------FIQGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRLeeVPemgynplgVPSRGEICIR 476
Cdd:PRK12582 361 DLYERMQALAVRTtghripFYTGYGATETAPTTTGTHWDTER-VGLIGLPLPGVELKL--AP--------VGDKYEVRVK 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 477 GKSLFAGYYKSPELTNEAI-VDGWFHTGDIGE-MTPDGILK--VID-RKKNIFKLSQGEYVAVEYL--EKVYGFPPLVED 549
Cdd:PRK12582 430 GPNVTPGYHKDPELTAAAFdEEGFYRLGDAARfVDPDDPEKglIFDgRVAEDFKLSTGTWVSVGTLrpDAVAACSPVIHD 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 226491570 550 IWVYGDSfRSSLVAVVNPHQENTMKWAESNGykGSFDEICKLEGLKEyILKE 601
Cdd:PRK12582 510 AVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLA-ILRE 557
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
228-525 |
1.25e-15 |
|
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: 78.50 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 228 CTVMYTSGTSGQPKGVMLTHEshAMYVKGVDLFMDQfddKMTTDDVFLSFLPLAHILDRMIEEYFFHKGASigyyhgdlN 307
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQ--ALLAQALVLAVLQ---AIDEGTVFLNSGPLFHIGTLMFTLATFHAGGT--------N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 308 alrddivelkptllVGVPRV----------YERIYEGIL--KAIAELRPLrrvifNALYNRKLASMkagYSHKTASPFAD 375
Cdd:cd17636 70 --------------VFVRRVdaeevlelieAERCTHAFLlpPTIDQIVEL-----NADGLYDLSSL---RSSPAAPEWND 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 376 MLAfrkVKARLGGRlrlliSGGaplsneieefmrvttcayfiqGYGLTETLGPSTVCYIDDMAlVGSAGVPATYTEIRL- 454
Cdd:cd17636 128 MAT---VDTSPWGR-----KPG---------------------GYGQTEVMGLATFAALGGGA-IGGAGRPSPLVQVRIl 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 455 ----EEVPEmgynplGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFK 525
Cdd:cd17636 178 dedgREVPD------GEV--GEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK 244
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
225-552 |
1.38e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 80.02 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 225 SDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHI--LDRMIEEYFFHKGASIGYY 302
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRN---LVANLCSSLFSVGPEMIGQVVTLGLIPFFHIygITGICCATLRNKGKVVVMS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 HGDLNALRDDIVELKPTLLVGVPrvyeriyegilkaiaelrPlrrVIFNALYNrklasmkagyshktasPFADMLAFRKV 382
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVP------------------P---IILNLVKN----------------PIVEEFDLSKL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 383 KarlggrLRLLISGGAPLSNEI-EEFMRVTTCAYFIQGYGLTE----TLGPSTVCYIDDMALVGSAGVPATYTEIRLEEv 457
Cdd:PLN02330 304 K------LQAIMTAAAPLAPELlTAFEAKFPGVQVQEAYGLTEhsciTLTHGDPEKGHGIAKKNSVGFILPNLEVKFID- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 458 PEMGYN-PLGVPsrGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVE 535
Cdd:PLN02330 377 PDTGRSlPKNTP--GELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPA 453
|
330
....*....|....*..
gi 226491570 536 YLEKVYGFPPLVEDIWV 552
Cdd:PLN02330 454 ELEAILLTHPSVEDAAV 470
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
83-253 |
1.40e-15 |
|
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: 80.31 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNCKSAKRLKALVAFTSATTEQNKEADQIGI-----KMYAWDDFlkVGKDNPR-QPCPPQASDICTVMYTSGT 236
Cdd:cd17634 166 GVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIdwqegRDLWWRDL--IAKASPEhQPEAMNAEDPLFILYTSGT 243
|
170
....*....|....*..
gi 226491570 237 SGQPKGVMLTHESHAMY 253
Cdd:cd17634 244 TGKPKGVLHTTGGYLVY 260
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
83-527 |
3.04e-15 |
|
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: 79.08 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEID-VVFIQD 161
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKmIVAIAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 KKIKEILS---PNCKSAKRLkALVAftsatteqnkeadqiGIKMYAWDDFLKVGKDNPRQPCPPQAS------DICTVMY 232
Cdd:cd05970 129 DNIPEEIEkaaPECPSKPKL-VWVG---------------DPVPEGWIDFRKLIKNASPDFERPTANsypcgeDILLVYF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 233 TSGTSGQPKgvMLTHEShaMYvkgvdlfmdqfddkmttddvflsflPLAHILDRMieeyffhkgasigYYHGdlnaLRDD 312
Cdd:cd05970 193 SSGTTGMPK--MVEHDF--TY-------------------------PLGHIVTAK-------------YWQN----VREG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 313 IVELKPTLLVGVPRVYERIY-EGILKAIAELRPLRRVIFNALYNrKLAsmKAGYSHKTASPfadmLAFR-KVKARLG--- 387
Cdd:cd05970 227 GLHLTVADTGWGKAVWGKIYgQWIAGAAVFVYDYDKFDPKALLE-KLS--KYGVTTFCAPP----TIYRfLIREDLSryd 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 388 -GRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETlgpsTVCyIDDMALV----GSAGVPATYTEIRLEEvPEMGY 462
Cdd:cd05970 300 lSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTET----TLT-IATFPWMepkpGSMGKPAPGYEIDLID-REGRS 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 463 NPLGvpSRGEICIR---GK--SLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:cd05970 374 CEAG--EEGEIVIRtskGKpvGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
209-552 |
3.43e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 78.37 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 209 LKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqFDDKmttDDVFLSfLPLAH-----I 283
Cdd:PRK09029 119 LHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMP-FTAQ---DSWLLS-LPLFHvsgqgI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 284 LDRmieeyFFHKGASIgyYHGDLNALRDDI-----VELKPTLLvgvprvyeriyegilkaiaelrplrrvifnalynRKL 358
Cdd:PRK09029 194 VWR-----WLYAGATL--VVRDKQPLEQALagcthASLVPTQL----------------------------------WRL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 359 ASMKAGYshktaspfadmLAFRKVkarlggrlrLLisGGAPLSNEIEEFMRvttcAYFIQ---GYGLTETlgPSTVCY-- 433
Cdd:PRK09029 233 LDNRSEP-----------LSLKAV---------LL--GGAAIPVELTEQAE----QQGIRcwcGYGLTEM--ASTVCAkr 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 434 IDDMALVGSagvPATYTEIRLEEvpemgynplgvpsrGEICIRGKSLFAGYYKSPE---LTNEaivDGWFHTGDIGEMTp 510
Cdd:PRK09029 285 ADGLAGVGS---PLPGREVKLVD--------------GEIWLRGASLALGYWRQGQlvpLVND---EGWFATRDRGEWQ- 343
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 226491570 511 DGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDIWV 552
Cdd:PRK09029 344 NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
83-512 |
6.32e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 77.86 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQD- 161
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPg 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 -KKIK--EILSPNCKSA-KRLKALVAFTSATTEqnkeadqigikmyAWDDFLKVGKDNPRQP--CPPQAS-------DIC 228
Cdd:PRK06164 117 fKGIDfaAILAAVPPDAlPPLRAIAVVDDAADA-------------TPAPAPGARVQLFALPdpAPPAAAgeraadpDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 229 TVMYT-SGTSGQPKGVM------LTHESHAMYVKGVDlfmdqfddkmtTDDVFLSFLPLAHIldrmieeyfFHKGASIGY 301
Cdd:PRK06164 184 ALLFTtSGTTSGPKLVLhrqatlLRHARAIARAYGYD-----------PGAVLLAALPFCGV---------FGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 302 YHGdlnalrddivelkptllvGVPRVYERIYEG--ILKAIAELRPLRRVIFNALYNR--KLASMKAGYSHKTASPFADML 377
Cdd:PRK06164 244 LAG------------------GAPLVCEPVFDAarTARALRRHRVTHTFGNDEMLRRilDTAGERADFPSARLFGFASFA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 378 -AFRKVKARLGGRlrllisgGAPL-----SNEIEEFMrvttcayfiqgyglteTLGPSTvcyiDDMALVGSAGVPATYTE 451
Cdd:PRK06164 306 pALGELAALARAR-------GVPLtglygSSEVQALV----------------ALQPAT----DPVSVRIEGGGRPASPE 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 452 IRLEEV-PEMG-YNPLGVPsrGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDG 512
Cdd:PRK06164 359 ARVRARdPQDGaLLPDGES--GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDG 420
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
83-526 |
1.13e-14 |
|
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: 76.93 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:cd17646 25 TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspnckSAKRLKALVAFTSATTEQNKEADqigikmyawddflkvgkDNPRQPcPPQASDICTVMYTSGTSGQPKG 242
Cdd:cd17646 105 -----------LAARLPAGGDVALLGDEALAAPP-----------------ATPPLV-PPRPDNLAYVIYTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVkgvdLFM-DQFDdkMTTDDVFLSFLPLAhiLDRMIEEYF--FHKGASI------GyyHGDLNALRDDI 313
Cdd:cd17646 156 VMVTHAGIVNRL----LWMqDEYP--LGPGDRVLQKTPLS--FDVSVWELFwpLVAGARLvvarpgG--HRDPAYLAALI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 314 VELKPTLLVGVPrvyeriyegilkaiaelrplrrvifnalynrklaSMKAgyshktasPFADMLAfrkvkARLGGRLRLL 393
Cdd:cd17646 226 REHGVTTCHFVP----------------------------------SMLR--------VFLAEPA-----AGSCASLRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 394 ISGGAPLSNEI-EEFMRVTTCAyFIQGYGLTETLGPSTVCYIDDMALVGSA--GVPATYTEI-----RLEEVPemgynpL 465
Cdd:cd17646 259 FCSGEALPPELaARFLALPGAE-LHNLYGPTEAAIDVTHWPVRGPAETPSVpiGRPVPNTRLyvlddALRPVP------V 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 466 GVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWF-------HTGDIGEMTPDGILKVIDRKKNIFKL 526
Cdd:cd17646 332 GVP--GELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKI 397
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
83-554 |
1.73e-14 |
|
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: 76.00 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFiqdk 162
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsaTTEQNKEadqigiKMYAWDDFLkvgkdnprqpcppqasdictVMYTSGTSGQPKG 242
Cdd:cd05969 78 -------------------------TTEELYE------RTDPEDPTL--------------------LHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHE---SHAMYVKGV------DLFMDQFDDKMTTDDVFLSFLPLAHildrmieeyffhkGASIGYYHGDLNALR--D 311
Cdd:cd05969 107 VLHVHDamiFYYFTGKYVldlhpdDIYWCTADPGWVTGTVYGIWAPWLN-------------GVTNVVYEGRFDAESwyG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 DIVELKPTLLVGVPRVYERIyegilkaiaelrplrrvifnalynrklasMKAGyshktaspfADMLAFRKVKArlggrLR 391
Cdd:cd05969 174 IIERVKVTVWYTAPTAIRML-----------------------------MKEG---------DELARKYDLSS-----LR 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 392 LLISGGAPLSNEI----EEFMRVTtcayFIQGYGLTETLGPSTVCYIDDMALVGSAGVPatYTEIRLEEVPEMGyNPLGV 467
Cdd:cd05969 211 FIHSVGEPLNPEAirwgMEVFGVP----IHDTWWQTETGSIMIANYPCMPIKPGSMGKP--LPGVKAAVVDENG-NELPP 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 468 PSRGEICIRG--KSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYGFPP 545
Cdd:cd05969 284 GTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHP 362
|
....*....
gi 226491570 546 LVEDIWVYG 554
Cdd:cd05969 363 AVAEAGVIG 371
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
83-519 |
4.49e-14 |
|
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: 75.10 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDk 162
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTHH- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnPRQPCppqasdicTVMYTSGTSGQPKG 242
Cdd:cd17649 93 -----------------------------------------------------PRQLA--------YVIYTSGSTGTPKG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAhiLDRMIEEYF--FHKGASIgyyhgdlnALRDdivelkPTL 320
Cdd:cd17649 112 VAVSHGPLAAHCQATAERYG-----LTPGDRELQFASFN--FDGAHEQLLppLICGACV--------VLRP------DEL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 321 LVGVPRVYERIYEGILkAIAELRPLrrvifnalYNRKLAsmkagyshktaspfadmLAFRKVKARLGGRLRLLISGGAPL 400
Cdd:cd17649 171 WASADELAEMVRELGV-TVLDLPPA--------YLQQLA-----------------EEADRTGDGRPPSLRLYIFGGEAL 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 401 SneIEEFMRVTTCA-YFIQGYGLTETLGPSTVCYIDDMALVGSAGVP-----ATYTEIRLEEvpEMGYNPLGVPsrGEIC 474
Cdd:cd17649 225 S--PELLRRWLKAPvRLFNAYGPTEATVTPLVWKCEAGAARAGASMPigrplGGRSAYILDA--DLNPVPVGVT--GELY 298
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 226491570 475 IRGKSLFAGYYKSPELTNEAIVDG--------WFHTGDIGEMTPDGILKVIDR 519
Cdd:cd17649 299 IGGEGLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGR 351
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
83-247 |
5.13e-14 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 75.39 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLV---CVPlyDTLGAGAVD------------- 146
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwssCSP--DFGVPGVLDrfgqiepkvlfav 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 147 --YIIDHAEIDVvfiqDKKIKEILspncKSAKRLKALVAFTSATTEQNKEADQIGiKMYAWDDFLKVGKDNPRQPCPPQA 224
Cdd:cd05943 178 daYTYNGKRHDV----REKVAELV----KGLPSLLAVVVVPYTVAAGQPDLSKIA-KALTLEDFLATGAAGELEFEPLPF 248
|
170 180
....*....|....*....|...
gi 226491570 225 SDICTVMYTSGTSGQPKGVMLTH 247
Cdd:cd05943 249 DHPLYILYSSGTTGLPKCIVHGA 271
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-567 |
5.30e-14 |
|
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: 74.65 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAcngyslvcvplydTLGAGAVdYI-IDHAeidvvfiqd 161
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILA-------------ILKAGAA-YVpLDAK--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 kkikeilSPncksAKRLKALVAFTSATteqnkeadqigikmyawddfLKVgkdnprqpCPPQASDICTVMYTSGTSGQPK 241
Cdd:cd17653 81 -------LP----SARIQAILRTSGAT--------------------LLL--------TTDSPDDLAYIIFTSGSTGIPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 242 GVMLTHESHAMYVKGVDLFMD-------------QFDdkMTTDDVFLSFLPLAHILDRMIEEYFFHKGASIgyyhgdlna 308
Cdd:cd17653 122 GVMVPHRGVLNYVSQPPARLDvgpgsrvaqvlsiAFD--ACIGEIFSTLCNGGTLVLADPSDPFAHVARTV--------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 309 lrdDIVELKPTLLVGV-PRVY---ERIY---EGILKAIAELRPLRRVIFNAlYnrklasmkaGYSHKT-ASPFADMLAFR 380
Cdd:cd17653 191 ---DALMSTPSILSTLsPQDFpnlKTIFlggEAVPPSLLDRWSPGRRLYNA-Y---------GPTECTiSSTMTELLPGQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 381 KVkarlggrlrlliSGGAPLSNeieefmrvttcayfiqgygltetlgpsTVCYIDDmalvgsAGvpatyteirLEEVPEm 460
Cdd:cd17653 258 PV------------TIGKPIPN---------------------------STCYILD------AD---------LQPVPE- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 461 gynplGVPsrGEICIRGKSLFAGYYKSPELTNEAIV-----DGW--FHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVA 533
Cdd:cd17653 283 -----GVV--GEICISGVQVARGYLGNPALTASKFVpdpfwPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKV-RGFRIN 354
|
490 500 510
....*....|....*....|....*....|....*..
gi 226491570 534 VEYLEK-VYGFPPLVED--IWVYGDsfrsSLVAVVNP 567
Cdd:cd17653 355 LEEIEEvVLQSQPEVTQaaAIVVNG----RLVAFVTP 387
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
82-573 |
8.89e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 74.35 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 82 KSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQD 161
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 ---KKIKEILSPNCK-----------SAKRLKALVAFTSATTEqnkeadqigikmyAWDDFLKVGK--DNPRQPCPPqas 225
Cdd:PRK12406 92 dllHGLASALPAGVTvlsvptppeiaAAYRISPALLTPPAGAI-------------DWEGWLAQQEpyDGPPVPQPQ--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 dicTVMYTSGTSGQPKGVML---THESHAMYVKGVDLFMDQfddkmTTDDVFLSFLPLAHildrmieeyffhkgaSIGYY 302
Cdd:PRK12406 156 ---SMIYTSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGL-----KPGIRALLTGPLYH---------------SAPNA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 HGdLNALRDDIVelkptlLVGVPRVYEriyEGILKAIAELRPLRRVIFNALYNR--KL-ASMKAGYSHKTaspfadmlaf 379
Cdd:PRK12406 213 YG-LRAGRLGGV------LVLQPRFDP---EELLQLIERHRITHMHMVPTMFIRllKLpEEVRAKYDVSS---------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 380 rkvkarlggrLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETlGPSTVCYIDD-MALVGSAGVPATYTEIRLeeVP 458
Cdd:PRK12406 273 ----------LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTES-GAVTFATSEDaLSHPGTVGKAAPGAELRF--VD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 459 EMGyNPLGVPSRGEICIR--GKSLFAgYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEY 536
Cdd:PRK12406 340 EDG-RPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAE 416
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 226491570 537 LEKVYGFPPLVEDIWVYG--DS-FRSSLVAVVNPHQENTM 573
Cdd:PRK12406 417 IEAVLHAVPGVHDCAVFGipDAeFGEALMAVVEPQPGATL 456
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-519 |
1.17e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.20 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSPNCKSAKRLKALVAFTSATTEQNKEadqigikmyawddfLKVGKDNprqpcppqasdICTVMYTSGTSGQPKG 242
Cdd:PRK12467 619 LLAQLPVPAGLRSLCLDEPADLLCGYSGHNPE--------------VALDPDN-----------LAYVIYTSGSTGQPKG 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAhiLDRMIEEYF--FHKGASI---GY-YHGDLNALRDDIVEL 316
Cdd:PRK12467 674 VAISHGALANYVCVIAERLQ-----LAADDSMLMVSTFA--FDLGVTELFgaLASGATLhllPPdCARDAEAFAALMADQ 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 317 KPTLLVGVPRVyeriYEGILKA--IAELRPLRRVIFNAlynrklasmkagyshkTASPFAdmLAFRKVKARLGGRLrlli 394
Cdd:PRK12467 747 GVTVLKIVPSH----LQALLQAsrVALPRPQRALVCGG----------------EALQVD--LLARVRALGPGARL---- 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 395 sggaplsneieefmrvttcayfIQGYGLTETLGPSTVCYIDDMALVGSA---GVPATYTEIRleeVPEMGYNPLGVPSRG 471
Cdd:PRK12467 801 ----------------------INHYGPTETTVGVSTYELSDEERDFGNvpiGQPLANLGLY---ILDHYLNPVPVGVVG 855
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 226491570 472 EICIRGKSLFAGYYKSPELTNEAIV------DG--WFHTGDIGEMTPDGILKVIDR 519
Cdd:PRK12467 856 ELYIGGAGLARGYHRRPALTAERFVpdpfgaDGgrLYRTGDLARYRADGVIEYLGR 911
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
226-554 |
1.69e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 73.76 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTHeshAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILdrmieeyffhkGAS--IGY-- 301
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAVINTH---RMLCANQQMLAQTFPFLAEEPPVLVDWLPWNHTF-----------GGNhnLGIvl 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 302 YHG-----D------------LNALRddivELKPTLLVGVPRVYERIyegilkaIAELR---PLRRVIFnalynrklasm 361
Cdd:PRK08180 276 YNGgtlyiDdgkptpggfdetLRNLR----EISPTVYFNVPKGWEML-------VPALErdaALRRRFF----------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 362 kagyshktaspfadmlafrkvkarlgGRLRLLISGGAPLSNEI-EEFMRVT--TCAY---FIQGYGLTETlGPSTVCYID 435
Cdd:PRK08180 334 --------------------------SRLKLLFYAGAALSQDVwDRLDRVAeaTCGErirMMTGLGMTET-APSATFTTG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 436 DMALVGSAGVPATYTEIRLeevpemgynplgVPSRG--EICIRGKSLFAGYYKSPELTNEAIVD-GWFHTGDIGEMT-PD 511
Cdd:PRK08180 387 PLSRAGNIGLPAPGCEVKL------------VPVGGklEVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGDAVRFVdPA 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 226491570 512 ----GIlkVID-RKKNIFKLSQGEYVAVEYL--EKVYGFPPLVEDIWVYG 554
Cdd:PRK08180 455 dperGL--MFDgRIAEDFKLSSGTWVSVGPLraRAVSAGAPLVQDVVITG 502
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
223-534 |
2.00e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 72.85 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVdlfMDQFDdkMTTDDVFLSFLPLAhiLDRMIEEYF--FHKGASig 300
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGL---IKEYG--ITSSDRVLQFASIA--FDVAAEEIYvtLLSGAT-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 301 yyhgdlnalrddivelkptlLVGVPrvyeriyegilkaiAELRPLRRVIFNALYNRKLA--SMKAGYSHKTASpfadmlA 378
Cdd:cd17644 175 --------------------LVLRP--------------EEMRSSLEDFVQYIQQWQLTvlSLPPAYWHLLVL------E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 379 FRKVKARLGGRLRLLISGGAPLSNEIEEFMRVTTCAY--FIQGYGLTETLGPSTVCYIDDMALVGSAGVP--------AT 448
Cdd:cd17644 215 LLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFiqLINVYGPTEATIAATVCRLTQLTERNITSVPigrpiantQV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 449 YT-EIRLEEVPemgynpLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWFH---------TGDIGEMTPDGILKVID 518
Cdd:cd17644 295 YIlDENLQPVP------VGVP--GELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLG 366
|
330 340
....*....|....*....|.
gi 226491570 519 R-----KKNIFKLSQGEYVAV 534
Cdd:cd17644 367 RidnqvKIRGFRIELGEIEAV 387
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-643 |
3.14e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 72.08 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVfIQDk 162
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL-VTD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvGKDNPRQpcppqasdictVMYTSGTSGQPKG 242
Cdd:cd05971 86 -------------------------------------------------GSDDPAL-----------IIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVDLFMDQFDDkmtTDDVFlsFLPlahildrmieeyffhkgASIGYYHGDLNALRddivelkPTLLV 322
Cdd:cd05971 106 ALHAHRVLLGHLPGVQFPFNLFPR---DGDLY--WTP-----------------ADWAWIGGLLDVLL-------PSLYF 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 GVPRVYERiyegilkaiaelrpLRRviFNAlynRKLASMKAGYSHKTA--SPFA-DMLAFRKV-KARLGGRLRLLISGGA 398
Cdd:cd05971 157 GVPVLAHR--------------MTK--FDP---KAALDLMSRYGVTTAflPPTAlKMMRQQGEqLKHAQVKLRAIATGGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 399 PLSNEIEEFMRVTTCAYFIQGYGLTET---LGPSTVCY-IDDmalvGSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEIC 474
Cdd:cd05971 218 SLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFpIKP----GSMGKPIPGHRVAI--VDDNG-TPLPPGEVGEIA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 475 IR--GKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKlSQGEYVAVEYLEKVYGFPPLVEDIWV 552
Cdd:cd05971 291 VElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAAV 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 553 YG--DSFRSSLV---AVVNPhqentmkwaesnGYKGSfDEICKleGLKEYILKELAAVAQKnklRGFEYIkgvvlDPVPf 627
Cdd:cd05971 370 VGipDPIRGEIVkafVVLNP------------GETPS-DALAR--EIQELVKTRLAAHEYP---REIEFV-----NELP- 425
|
570
....*....|....*.
gi 226491570 628 dierdlVTATMKKKRK 643
Cdd:cd05971 426 ------RTATGKIRRR 435
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
83-530 |
3.22e-13 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 72.11 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQdk 162
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqASDICTVMYTSGTSGQPKG 242
Cdd:cd17650 92 -------------------------------------------------------------PEDLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES--HAMYVKGVDLFMDQFDDKMT-----TDDVFLSFLPLAHILDRMIeeYFFHKGASIgyyhgDLNALRDDIVE 315
Cdd:cd17650 111 VMVEHRNvaHAAHAWRREYELDSFPVRLLqmasfSFDVFAGDFARSLLNGGTL--VICPDEVKL-----DPAALYDLILK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 316 LKPTLLVGVPrvyeriyegilkaiAELRPLrrvifnalynrklasMKAGYSHKTASPFadmlafrkvkarlggrLRLLIS 395
Cdd:cd17650 184 SRITLMESTP--------------ALIRPV---------------MAYVYRNGLDLSA----------------MRLLIV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 G--GAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVP--ATYTEIRLEEV-PEMGYNPLGVPsr 470
Cdd:cd17650 219 GsdGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPigRPLPNTAMYVLdERLQPQPVGVA-- 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 471 GEICIRGKSLFAGYYKSPELTNEAIVDGWF-------HTGDIGEMTPDGILKVIDR-----KKNIFKLSQGE 530
Cdd:cd17650 297 GELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRvdhqvKIRGFRIELGE 368
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
390-572 |
6.28e-13 |
|
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: 71.59 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LRLLISGGAPLSNEI-EEFMRVTTCAyFIQGYGLTETLgpstVCY--IDDMA--LVGSAGVPAT-YTEIRLeeVPEMGyN 463
Cdd:cd05920 257 LRLLQVGGARLSPALaRRVPPVLGCT-LQQVFGMAEGL----LNYtrLDDPDevIIHTQGRPMSpDDEIRV--VDEEG-N 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 464 PLGVPSRGEICIRGKSLFAGYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYG 542
Cdd:cd05920 329 PVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLL 407
|
170 180 190
....*....|....*....|....*....|....*
gi 226491570 543 FPPLVEDIWVYG--DSF---RSSLVAVVNPHQENT 572
Cdd:cd05920 408 RHPAVHDAAVVAmpDELlgeRSCAFVVLRDPPPSA 442
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
226-540 |
1.11e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.00 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDQfddkmTTDDVFLSFLPLAHildrmieEYFFHKGAsigyyhgd 305
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSP-----KEDDVMMSFLPPFH-------AYGFNSCT-------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 306 lnalrddiveLKPtLLVGVPRVYEriyegilkaiaelrplrrviFNALYNRKLASM----KAGYSHKTASPFADMLAFRK 381
Cdd:PRK06334 244 ----------LFP-LLSGVPVVFA--------------------YNPLYPKKIVEMideaKVTFLGSTPVFFDYILKTAK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 382 VKARLGGRLRLLISGGAPLSNEI-EEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLeeVPEM 460
Cdd:PRK06334 293 KQESCLPSLRFVVIGGDAFKDSLyQEALKTFPHIQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLI--VSEE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 461 GYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDG--WFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLE 538
Cdd:PRK06334 371 TKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALE 449
|
..
gi 226491570 539 KV 540
Cdd:PRK06334 450 SI 451
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
390-538 |
1.14e-12 |
|
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: 70.94 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LRLLISGGAPLSNEIeeFMRVTT---CAyFIQGYGLTETLgpstVCY--IDD--MALVGSAGVP-ATYTEIRL-----EE 456
Cdd:COG1021 302 LRVLQVGGAKLSPEL--ARRVRPalgCT-LQQVFGMAEGL----VNYtrLDDpeEVILTTQGRPiSPDDEVRIvdedgNP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 457 VPEmgynplGVPsrGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNifklsQ----GEY 531
Cdd:COG1021 375 VPP------GEV--GELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEK 441
|
....*..
gi 226491570 532 VAVEYLE 538
Cdd:COG1021 442 IAAEEVE 448
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
83-520 |
1.22e-12 |
|
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: 70.38 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAmqacngyslvcvpLYDTLGAGAVdYI-IDhaeidvvfiqd 161
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVA-------------VLGILAAGAA-YVpVD----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 kkikeILSPncksAKRLKALVAFTSATT-----EQNKEADQIGIKMYAWDDFLKVGKDNPrqPCPPQASDICTVMYTSGT 236
Cdd:cd12114 69 -----IDQP----AARREAILADAGARLvltdgPDAQLDVAVFDVLILDLDALAAPAPPP--PVDVAPDDLAYVIFTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHEShAMYVkgVDLFMDQFddKMTTDDVFLSFLPLAHilDRMIEEYF--FHKGASI----GYYHGDLNALR 310
Cdd:cd12114 138 TGTPKGVMISHRA-ALNT--ILDINRRF--AVGPDDRVLALSSLSF--DLSVYDIFgaLSAGATLvlpdEARRRDPAHWA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 311 DDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVifnalynrklasmkagyshktaspfadMLAFRKVKARLGGRL 390
Cdd:cd12114 211 ELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLV---------------------------LLSGDWIPLDLPARL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 391 RLLISGGAPLSneieefmrvttcayfiQGyGLTETLGPSTVCYIDDM-ALVGSA--GVPATYTEIRLeeVPEMGYN-PLG 466
Cdd:cd12114 264 RALAPDARLIS----------------LG-GATEASIWSIYHPIDEVpPDWRSIpyGRPLANQRYRV--LDPRGRDcPDW 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 467 VPsrGEICIRGKSLFAGYYKSPELTNEAIVD-----GWFHTGDIGEMTPDGILKVIDRK 520
Cdd:cd12114 325 VP--GELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRR 381
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-527 |
2.32e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 69.47 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFiqdk 162
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspnCKSAKRLKAlvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqASDICTVMYTSGTSGQPKG 242
Cdd:cd05973 78 ---------TDAANRHKL-------------------------------------------DSDPFVMMFTSGTTGLPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES----HAMYVKGVDLfmdqfddkmTTDDVFLSFlplahildrmieeyffhkgASIGYYHGDLNALrddiveLKP 318
Cdd:cd05973 106 VPVPLRAlaafGAYLRDAVDL---------RPEDSFWNA-------------------ADPGWAYGLYYAI------TGP 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 319 tLLVGVPRVyerIYEGILKAIAELRPLRRVifnalynrklasmkaGYSHKTASPFAD---MLAFRKVKARLGGRLRLLIS 395
Cdd:cd05973 152 -LALGHPTI---LLEGGFSVESTWRVIERL---------------GVTNLAGSPTAYrllMAAGAEVPARPKGRLRRVSS 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 GGAPLSNEIEEFMRVTTCAYFIQGYGLTEtLGpSTVC---YIDDMALVGSAGVP-----ATYTEIRLEEVPEmgynplGV 467
Cdd:cd05973 213 AGEPLTPEVIRWFDAALGVPIHDHYGQTE-LG-MVLAnhhALEHPVHAGSAGRAmpgwrVAVLDDDGDELGP------GE 284
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 468 PSRGEICIRGKSL--FAGYYKSPEltnEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:cd05973 285 PGRLAIDIANSPLmwFRGYQLPDT---PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
79-590 |
2.97e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 69.38 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 79 YLWKSYKeiyDEVLQAGSALQKLGVQPGSRVGIYGANCPQWI-VAMQACNGYSLVCVpLYDTLGAGAVDYIIDHAEIDVV 157
Cdd:cd05915 25 TTYAEVY---QRARRLMGGLRALGVGVGDRVATLGFNHFRHLeAYFAVPGMGAVLHT-ANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 158 FIQdkkiKEILSpncKSAKRLKALVAFTSATTEQNKEADqigikmyaWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTS 237
Cdd:cd05915 101 LFD----PNLLP---LVEAIRGELKTVQHFVVMDEKAPE--------GYLAYEEALGEEADPVRVPERAACGMAYTTGTT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTHESHAMYVKGVDLFMDQFDDKMTtddVFLSFLPLAHildrmieeyffhkgASIGYYHGDLNAlrddivelk 317
Cdd:cd05915 166 GLPKGVVYSHRALVLHSLAASLVDGTALSEKD---VVLPVVPMFH--------------VNAWCLPYAATL--------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 318 ptllvgvprvyeriYEGILKAIAELRPlRRVIFNALYNRKLASMKAgyshktASPFADMLAFRK--VKARLGGRLRLLIS 395
Cdd:cd05915 220 --------------VGAKQVLPGPRLD-PASLVELFDGEGVTFTAG------VPTVWLALADYLesTGHRLKTLRRLVVG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 GGAPlsneIEEFMRVTTCAYF--IQGYGLTETLGPSTVCyiddMALVGSAGVPATYTeIRL----------EEVPEMGYN 463
Cdd:cd05915 279 GSAA----PRSLIARFERMGVevRQGYGLTETSPVVVQN----FVKSHLESLSEEEK-LTLkaktglpiplVRLRVADEE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 464 PLGVPSRGE----ICIRGKSLFAGYYKSPELTN-EAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLE 538
Cdd:cd05915 350 GRPVPKDGKalgeVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLE 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 539 KVYGFPPLVEDIWVYG---DSFRSSLVAVVnphqentmKWAESNGYKGSFDEICK 590
Cdd:cd05915 429 NALMGHPKVKEAAVVAiphPKWQERPLAVV--------VPRGEKPTPEELNEHLL 475
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
83-247 |
3.33e-12 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 69.44 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQD- 161
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 162 --KKIKEI-LSPNCKSAKRLKALV-----------AFTSATTEQNKEADQigiKMYAWDDFLKVGKDNPrqpcppqasdi 227
Cdd:cd05968 173 ftRRGREVnLKEEADKACAQCPTVekvvvvrhlgnDFTPAKGRDLSYDEE---KETAGDGAERTESEDP----------- 238
|
170 180
....*....|....*....|
gi 226491570 228 CTVMYTSGTSGQPKGVMLTH 247
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
109-512 |
3.71e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 69.32 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 109 VGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIkEILSPncksakrLKALVAFTSAT 188
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHA-ELLDG-------LDPGVRVINVD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 189 TEqnkeadqigikmyAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSGQPKGVMLTHESHAmyVKGVDLfMDQFDdkM 268
Cdd:PRK07867 129 SP-------------AWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVML-AQRFG--L 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 269 TTDDVFLSFLPLahildrmieeyfFHKGASIGYYhgdlnalrddivelKPTLLVGVprvyeriyegilkAIAelrpLRRV 348
Cdd:PRK07867 191 GPDDVCYVSMPL------------FHSNAVMAGW--------------AVALAAGA-------------SIA----LRRK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 349 iFNAlyNRKLASMK---AGYSHKTASPFADMLAFRKVKARLGGRLRLLI--SGGAPlsnEIEEFMRVTTCAyFIQGYGLT 423
Cdd:PRK07867 228 -FSA--SGFLPDVRrygATYANYVGKPLSYVLATPERPDDADNPLRIVYgnEGAPG---DIARFARRFGCV-VVDGFGST 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 424 E-----TLGPSTVcyiddmalVGSAGVPATYTEIR----LEEVPEMGYNPLGVPSR----GEIC-IRGKSLFAGYYKSPE 489
Cdd:PRK07867 301 EggvaiTRTPDTP--------PGALGPLPPGVAIVdpdtGTECPPAEDADGRLLNAdeaiGELVnTAGPGGFEGYYNDPE 372
|
410 420
....*....|....*....|...
gi 226491570 490 LTNEAIVDGWFHTGDIGEMTPDG 512
Cdd:PRK07867 373 ADAERMRGGVYWSGDLAYRDADG 395
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-530 |
5.03e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.60 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVA----MQACNGYslvcVPLYDTLGAGAVDYIIDHAEIDVVF 158
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVAllavLKAGGAY----VPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 IQDKKIKEILSPncKSAKRLkalvAFTSATteqnkeadqigikmyAWDDFlkvGKDNPRQPCPPQasDICTVMYTSGTSG 238
Cdd:PRK12316 2106 TQRHLLERLPLP--AGVARL----PLDRDA---------------EWADY---PDTAPAVQLAGE--NLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHESHAMYVKGVdlfmdQFDDKMTTDDVFLSFLPLAhiLDRMIEEYF--FHKGASI---GYYHGDLNALRDDI 313
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAA-----GERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGARVlirDDELWDPEQLYDEM 2232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 314 VELKPTLLVGVPrVYeriyegiLKAIAEL-------RPLRRVIFNAlynrklasmkagyshkTASPFAdmlAFRKVKARL 386
Cdd:PRK12316 2233 ERHGVTILDFPP-VY-------LQQLAEHaerdgrpPAVRVYCFGG----------------EAVPAA---SLRLAWEAL 2285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 387 GGrlrllisggaplsneieefmrvttcAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVP-ATYTEIRLEEVPEMGYNPL 465
Cdd:PRK12316 2286 RP-------------------------VYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPiGRALGNRRAYILDADLNLL 2340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 466 GVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWF--------HTGDIGEMTPDGILKVIDR-----KKNIFKLSQGE 530
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlyRTGDLARYRADGVVEYLGRidhqvKIRGFRIELGE 2418
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-519 |
7.44e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK12316 4578 TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSH 4657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeiLSPNCKSAKRLKALVaftsatTEQNKEadqigikmyaWDDFlkvGKDNPRQPCPPQasDICTVMYTSGTSGQPKG 242
Cdd:PRK12316 4658 -----LLQRLPIPDGLASLA------LDRDED----------WEGF---PAHDPAVRLHPD--NLAYVIYTSGSTGRPKG 4711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHES-----HAMyvkgvdlfmdQFDDKMTTDDVFLSFLPLAhiLDRMIEEYF--FHKGASI-----GYYhgDLNALR 310
Cdd:PRK12316 4712 VAVSHGSlvnhlHAT----------GERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGASVvirddSLW--DPERLY 4777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 311 DDIVELKPTLLVGVPRVYERIYEGiLKAIAELRPLRRVIFNAlynrklasmkagyshktaspfadmlafrkvKARLGGRL 390
Cdd:PRK12316 4778 AEIHEHRVTVLVFPPVYLQQLAEH-AERDGEPPSLRVYCFGG------------------------------EAVAQASY 4826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 391 RLLISGGAPlsneieefmrvttcAYFIQGYGLTETL--------GPSTVCYIDDMALVGSAGVPATYteirleeVPEMGY 462
Cdd:PRK12316 4827 DLAWRALKP--------------VYLFNGYGPTETTvtvllwkaRDGDACGAAYMPIGTPLGNRSGY-------VLDGQL 4885
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 463 NPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWF--------HTGDIGEMTPDGILKVIDR 519
Cdd:PRK12316 4886 NPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlyRTGDLARYRADGVIDYLGR 4950
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
83-567 |
1.10e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 67.60 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDK 162
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYERE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 ---KIKEILSpnckSAKRLKALVAFTSATTEqnkEADQIGIkmyAWDDFLKVGkDNPRQPCPPQASDIcTVMYTSGTSGQ 239
Cdd:PRK07798 110 fapRVAEVLP----RLPKLRTLVVVEDGSGN---DLLPGAV---DYEDALAAG-SPERDFGERSPDDL-YLLYTGGTTGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHEshamyvkgvDLFMDQFD--DKMTTDDV--------------FLSFLPLAHildrmieeyFFHKGASIGYYH 303
Cdd:PRK07798 178 PKGVMWRQE---------DIFRVLLGgrDFATGEPIedeeelakraaagpGMRRFPAPP---------LMHGAGQWAAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 304 GDLN----ALRDDiVELKPtllvgvprvyeriyEGILKAIAELRPLRRVIFNALYNRklasmkagyshktasPFADmlAF 379
Cdd:PRK07798 240 ALFSgqtvVLLPD-VRFDA--------------DEVWRTIEREKVNVITIVGDAMAR---------------PLLD--AL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 380 RKVKARLGGRLRLLISGGAPLSNEI-EEFMRVTTCAYFIQGYGLTETlGpstvcyiddmalVGSAGVPATYTEIRLEEVP 458
Cdd:PRK07798 288 EARGPYDLSSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSET-G------------FGGSGTVAKGAVHTGGPRF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 459 EMG---------YNPL--GVPSRGEICIRGkSLFAGYYKSPELTNEA--IVDG--WFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:PRK07798 355 TIGprtvvldedGNPVepGSGEIGWIARRG-HIPLGYYKDPEKTAETfpTIDGvrYAIPGDRARVEADGTITLLGRGSVC 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 226491570 524 FKlSQGEYVAVEYLEKVYGFPPLVEDIWVYG---DSFRSSLVAVVNP 567
Cdd:PRK07798 434 IN-TGGEKVFPEEVEEALKAHPDVADALVVGvpdERWGQEVVAVVQL 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
223-572 |
1.99e-11 |
|
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: 66.80 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDdkMTTDDVFLSFlpLAHILDRMIEEYFFhkgasigyy 302
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRA---LSTSALAHGRALG--LTSESRVLQF--ASYTFDVSILEIFT--------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 hgdlnalrddivelkpTLLVG----VPRVYERIyEGILKAIAElrplrrvifnalynrklasMKAGYSHKTASpFADMLA 378
Cdd:cd05918 168 ----------------TLAAGgclcIPSEEDRL-NDLAGFINR-------------------LRVTWAFLTPS-VARLLD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 379 FRKVKarlggRLRLLISGGAPLSNE-IEEFM-RVTTcayfIQGYGLTE-TLGpSTVCYIDDMALVGSAGVPAT------- 448
Cdd:cd05918 211 PEDVP-----SLRTLVLGGEALTQSdVDTWAdRVRL----INAYGPAEcTIA-ATVSPVVPSTDPRNIGRPLGatcwvvd 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 449 -YTEIRLEevpemgynPLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDG--W------------FHTGDIGEMTPDGI 513
Cdd:cd05918 281 pDNHDRLV--------PIGAV--GELLIEGPILARGYLNDPEKTAAAFIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGS 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226491570 514 LKVIDRKKNIFKLsQG---EYVAVEYleKVYGFPPLVED-----IWVYGDSFRSSLVAVVNPHQENT 572
Cdd:cd05918 351 LEYVGRKDTQVKI-RGqrvELGEIEH--HLRQSLPGAKEvvvevVKPKDGSSSPQLVAFVVLDGSSS 414
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
83-519 |
7.22e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.03 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDY---IIDHAEIdvvfi 159
Cdd:PRK05857 43 RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERfcqITDPAAA----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 qdkkikeILSPNCK-SAKRLKALVAFTSATTeqnkeadqIGIKMYAWDDFLKVGKDNPRQPCPPQASDICTVMYTSGTSG 238
Cdd:PRK05857 118 -------LVAPGSKmASSAVPEALHSIPVIA--------VDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLTHES-----HAMYVKGVDlFMDQFDDKMTtddvfLSFLPLAHILDRM-IEEYFFHKGASI-GYYHGD-----L 306
Cdd:PRK05857 183 EPKAVLLANRTffavpDILQKEGLN-WVTWVVGETT-----YSPLPATHIGGLWwILTCLMHGGLCVtGGENTTslleiL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 307 NALRDDIVELKPTLLVgvprvyeriyegilKAIAELRplrrvifnalynrklasmkagySHKTASPfadmlafrkvkarl 386
Cdd:PRK05857 257 TTNAVATTCLVPTLLS--------------KLVSELK----------------------SANATVP-------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 387 ggRLRLLISGGaplSNEIEEFMRVTTCA--YFIQGYGLTETlGPSTVCYIDDMALV-----GSAGVPATYTEIRLEevPE 459
Cdd:PRK05857 287 --SLRLVGYGG---SRAIAADVRFIEATgvRTAQVYGLSET-GCTALCLPTDDGSIvkieaGAVGRPYPGVDVYLA--AT 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226491570 460 MGYNPL---GVPSR--GEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDR 519
Cdd:PRK05857 359 DGIGPTapgAGPSAsfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGR 423
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
223-526 |
1.42e-10 |
|
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: 63.81 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLTHESHAmyvkgvDLFMDQFDD-KMTTDDVFLSFlplahildrmieeyffhkgASIGY 301
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLA------NLAAAQIAAfDVGPGSRVLQF-------------------ASPSF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 302 yhgdlnalrdD--IVELKPTLLVG-----VPRvyERIYEGilKAIAELRPLRRVIFNALYNRKLASMkagyshktasPFA 374
Cdd:cd17652 146 ----------DasVWELLMALLAGatlvlAPA--EELLPG--EPLADLLREHRITHVTLPPAALAAL----------PPD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 375 DMLAfrkvkarlggrLRLLISGGAPLSNEIEEfmRVTTCAYFIQGYGLTETlgpsTVCYIDDMALVGSA----GVPATYT 450
Cdd:cd17652 202 DLPD-----------LRTLVVAGEACPAELVD--RWAPGRRMINAYGPTET----TVCATMAGPLPGGGvppiGRPVPGT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 451 EI-----RLEEVPemgynpLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWF--------HTGDIGEMTPDGILKVI 517
Cdd:cd17652 265 RVyvldaRLRPVP------PGVP--GELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmyRTGDLARWRADGQLEFL 336
|
....*....
gi 226491570 518 DRKKNIFKL 526
Cdd:cd17652 337 GRADDQVKI 345
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
216-537 |
1.65e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.60 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 216 PRQP-CPPQASDICTVMYTSGTSGQPKGVMLTHE----SHAMYVKGVDLfmdqfddkmTTDDVFLSFLPLahildrmiee 290
Cdd:PRK06814 783 PLVYfCNRDPDDPAVILFTSGSEGTPKGVVLSHRnllaNRAQVAARIDF---------SPEDKVFNALPV---------- 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 291 yfFHkgaSIGYYHGDLNALRDDIvelkPTLLVGVPRVYERIYEGILKAIAElrplrrVIFNAlynrklASMKAGYShKTA 370
Cdd:PRK06814 844 --FH---SFGLTGGLVLPLLSGV----KVFLYPSPLHYRIIPELIYDTNAT------ILFGT------DTFLNGYA-RYA 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 371 SPFaDmlaFRkvkarlggRLRLLISGGAPLSNE-----IEEF-MRVttcayfIQGYGLTETlGPSTVCYIDDMALVGSAG 444
Cdd:PRK06814 902 HPY-D---FR--------SLRYVFAGAEKVKEEtrqtwMEKFgIRI------LEGYGVTET-APVIALNTPMHNKAGTVG 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 445 VPATYTEIRLEEVPemgynplGVPSRGEICIRGKSLFAGYYKS--PELTnEAIVDGWFHTGDIGEMTPDGILKVIDRKKN 522
Cdd:PRK06814 963 RLLPGIEYRLEPVP-------GIDEGGRLFVRGPNVMLGYLRAenPGVL-EPPADGWYDTGDIVTIDEEGFITIKGRAKR 1034
|
330
....*....|....*...
gi 226491570 523 IFKLSqGEYV---AVEYL 537
Cdd:PRK06814 1035 FAKIA-GEMIslaAVEEL 1051
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
83-549 |
2.47e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.41 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACN--GYSLVcvpLYDT-LGAGAVDYIIDHAEIDVVFI 159
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGkvGARII---LLNTgFSGPQLAEVAAREGVKALVY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 qDKKIKEILSPNCKSAKRLKALVAFTSATTEQNKEADQIgikmyawDDFLKVGKDNPrQPCPPQASDIctVMYTSGTSGQ 239
Cdd:PRK07788 153 -DDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETL-------DDLIAGSSTAP-LPKPPKPGGI--VILTSGTTGT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 240 PKGVMLTHEShamyvkgvdlfmdqfddkmttddvflSFLPLAHILDRM---------IEEYFFHkgaSIGYYHGDLN-AL 309
Cdd:PRK07788 222 PKGAPRPEPS--------------------------PLAPLAGLLSRVpfragettlLPAPMFH---ATGWAHLTLAmAL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 310 R---------------DDIVELKPTLLVGVPRVYERiyegILKAIAELRPlrrvifnalyNRKLASmkagyshktaspfa 374
Cdd:PRK07788 273 GstvvlrrrfdpeatlEDIAKHKATALVVVPVMLSR----ILDLGPEVLA----------KYDTSS-------------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 375 dmlafrkvkarlggrLRLLISGGAPLSNEIEEfmrvttcayfiqgyGLTETLGP-------ST---VCYIDDMALV---- 440
Cdd:PRK07788 325 ---------------LKIIFVSGSALSPELAT--------------RALEAFGPvlynlygSTevaFATIATPEDLaeap 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 441 GSAGVPATYTEIRL-----EEVPEmgynplGVPsrGEICIRGKSLFAGYYKSPeltNEAIVDGWFHTGDIGEMTPDGILK 515
Cdd:PRK07788 376 GTVGRPPKGVTVKIldengNEVPR------GVV--GRIFVGNGFPFEGYTDGR---DKQIIDGLLSSGDVGYFDEDGLLF 444
|
490 500 510
....*....|....*....|....*....|....
gi 226491570 516 VIDRKKNIFkLSQGEYVaveylekvygFPPLVED 549
Cdd:PRK07788 445 VDGRDDDMI-VSGGENV----------FPAEVED 467
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
83-274 |
2.58e-10 |
|
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: 63.35 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAC-----------NGYSlvcvplYDTLGAGAVDyiidh 151
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACarigavhsvvfAGFS------AESLADRIND----- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 152 AEIDVVF----------------IQDKKIKEILSP-NCKSAKRLKALVAFTSatteqnkeadqiGIKMYaWDDFLKvgkd 214
Cdd:cd05966 155 AQCKLVItadggyrggkviplkeIVDEALEKCPSVeKVLVVKRTGGEVPMTE------------GRDLW-WHDLMA---- 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 215 NPRQPCPPQ---ASDICTVMYTSGTSGQPKGVMltHeSHAMYVKGVDLFMDQ-FDDKMttDDVF 274
Cdd:cd05966 218 KQSPECEPEwmdSEDPLFILYTSGSTGKPKGVV--H-TTGGYLLYAATTFKYvFDYHP--DDIY 276
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
216-523 |
2.74e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.09 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 216 PRQPCPPQASDICTVMYTSGTSGQPKGVMLTHES-----HAMYVKGvdlfmdQFDdkmTTDDVFLSFLPLahildrmiee 290
Cdd:PRK07768 143 PIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNlyanaEAMFVAA------EFD---VETDVMVSWLPL---------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 291 yfFHKGASIGY-----YHGDlnalrdDIVELKPTLLVGVPRVYERIyegilkaIAELRplrrvifnalynrklASMkagy 365
Cdd:PRK07768 204 --FHDMGMVGFltvpmYFGA------ELVKVTPMDFLRDPLLWAEL-------ISKYR---------------GTM---- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 366 shkTASP-FA-DMLAFRKVKARLGGR-----LRLLISGGAPLSNE-IEEF--------MRVTTcayFIQGYGLTE-TLGP 428
Cdd:PRK07768 250 ---TAAPnFAyALLARRLRRQAKPGAfdlssLRFALNGAEPIDPAdVEDLldagarfgLRPEA---ILPAYGMAEaTLAV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 429 S--------TVCYID-DMALVGSAGVPATYTEIR-----------LEE--VPEMGyNPLGVPSRGEICIRGKSLFAGYYK 486
Cdd:PRK07768 324 SfspcgaglVVDEVDaDLLAALRRAVPATKGNTRrlatlgpplpgLEVrvVDEDG-QVLPPRGVGVIELRGESVTPGYLT 402
|
330 340 350
....*....|....*....|....*....|....*....
gi 226491570 487 --SPELTNEAivDGWFHTGDIGEMTPDGILKVIDRKKNI 523
Cdd:PRK07768 403 mdGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-572 |
5.99e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQdk 162
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ-- 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilsPNCKSAKRLKALVAFTSATTEQNKEAdqigikmyawddflkvgkdNPRQPCPPQasDICTVMYTSGTSGQPKG 242
Cdd:PRK12316 3162 -------SHLRLPLAQGVQVLDLDRGDENYAEA-------------------NPAIRTMPE--NLAYVIYTSGSTGKPKG 3213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAhiLDRMIEEYFfhkgasigyyhgdlnalrddivelkPTLLV 322
Cdd:PRK12316 3214 VGIRHSALSNHLCWMQQAYG-----LGVGDRVLQFTTFS--FDVFVEELF-------------------------WPLMS 3261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 323 GVPRVyeriyegilkaiaeLRPLRRVIFNALYNRKLASMKAGYSHKTASPFADMLAfrKVKARLGGRLRLLISGGAPLSN 402
Cdd:PRK12316 3262 GARVV--------------LAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE--EEDAHRCTSLKRIVCGGEALPA 3325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 403 EIEEfmRVTTCAYFIQGYGLTETLGPSTVCYI-DDMALVGSAGVPATYTEIRLEEVpemGYNPLGVPSRGEICIRGKSLF 481
Cdd:PRK12316 3326 DLQQ--QVFAGLPLYNLYGPTEATITVTHWQCvEEGKDAVPIGRPIANRACYILDG---SLEPVPVGALGELYLGGEGLA 3400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 482 AGYYKSPELTNEAIVDGWF-------HTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:PRK12316 3401 RGYHNRPGLTAERFVPDPFvpgerlyRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLA 3479
|
490
....*....|....*...
gi 226491570 555 DSFRsSLVAVVNPHQENT 572
Cdd:PRK12316 3480 VDGR-QLVAYVVPEDEAG 3496
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
223-519 |
6.04e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.87 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLTHESHAMYVKgvdlFMDQFDDkMTTDDVFLSFLPLAhiLDRMIEEYFfhkgasigyy 302
Cdd:PRK12467 3235 MGENLAYVIYTSGSTGKPKGVGVRHGALANHLC----WIAEAYE-LDANDRVLLFMSFS--FDGAQERFL---------- 3297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 hgdlnalrddivelkPTLLVGVPRVyerIYEGILKAIAELRplrrvifnALYNRKLASMkagySHKTASPFADMLAFRKV 382
Cdd:PRK12467 3298 ---------------WTLICGGCLV---VRDNDLWDPEELW--------QAIHAHRISI----ACFPPAYLQQFAEDAGG 3347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 383 KArlGGRLRLLISGGAPLS-NEIEEFMRVTTCAYFIQGYGLTETLGPSTVcyiddMALVGSAGVPATYTEI------RLE 455
Cdd:PRK12467 3348 AD--CASLDIYVFGGEAVPpAAFEQVKRKLKPRGLTNGYGPTEAVVTVTL-----WKCGGDAVCEAPYAPIgrpvagRSI 3420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226491570 456 EVPEMGYNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFH--------TGDIGEMTPDGILKVIDR 519
Cdd:PRK12467 3421 YVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyrTGDLARYRADGVIEYLGR 3492
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
223-570 |
7.25e-10 |
|
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: 61.80 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDdkMTTDDVFLSFlplahildrmieeyffhkgASIGYy 302
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHN---LVNLCEWHRPYFG--VTPADKSLVY-------------------ASFSF- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 hgDLNALrddivELKPTLLVGVPrvyeriyegiLKAIAELRPLRRVIFNALYNRKlasmkagysHKTASPFADMLAfRKV 382
Cdd:cd17645 157 --DASAW-----EIFPHLTAGAA----------LHVVPSERRLDLDALNDYFNQE---------GITISFLPTGAA-EQF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 383 KARLGGRLRLLISGGAPLSNEIEEFMRVttcayfIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIR-LEEvpEMG 461
Cdd:cd17645 210 MQLDNQSLRVLLTGGDKLKKIERKGYKL------VNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYiLDE--ALQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 462 YNPLGVPsrGEICIRGKSLFAGYYKSPELTNEAIV-------DGWFHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAV 534
Cdd:cd17645 282 LQPIGVA--GELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEP 358
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 226491570 535 EYLEKVYGFPPLVEDIWVY----GDSfRSSLVAVVNPHQE 570
Cdd:cd17645 359 GEIEPFLMNHPLIELAAVLakedADG-RKYLVAYVTAPEE 397
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
83-526 |
9.93e-10 |
|
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: 61.18 E-value: 9.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQdk 162
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksakrlkalvaftsatteqnkeadqigikmyawddflkvgkdnprqpcppqASDICTVMYTSGTSGQPKG 242
Cdd:cd12115 104 -------------------------------------------------------------PDDLAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMyvkgvdlFMDQFDDKMTTDD---------------VFLSFLPLAHildrmieeyffhkGASIGYYHGDLn 307
Cdd:cd12115 123 VAIEHRNAAA-------FLQWAAAAFSAEElagvlastsicfdlsVFELFGPLAT-------------GGKVVLADNVL- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 308 ALRDDIVELKPTLLVGVPrvyeriyegilKAIAELrplrrvifnalynrklasmkagyshktaspfadmLAFRKVKARLg 387
Cdd:cd12115 182 ALPDLPAAAEVTLINTVP-----------SAAAEL----------------------------------LRHDALPASV- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 388 grlRLLISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVG-SAGVPATYTEI-----RLEEVPem 460
Cdd:cd12115 216 ---RVVNLAGEPLPRDlVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEvSIGRPLANTQAyvldrALQPVP-- 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226491570 461 gynpLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWFH-------TGDIGEMTPDGILKVIDRKKNIFKL 526
Cdd:cd12115 291 ----LGVP--GELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQVKV 357
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
83-570 |
1.23e-09 |
|
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: 60.95 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQdk 162
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 kikeilspncksaKRLKALVAFTSATTeqnkeadqigikMYAWDDFLKVGKDNPRQPCppQASDICTVMYTSGTSGQPKG 242
Cdd:cd17656 93 -------------RHLKSKLSFNKSTI------------LLEDPSISQEDTSNIDYIN--NSDDLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 243 VMLTHESHAMYVKgvdlFMDQFDDKMTTDDVfLSFLPLAhiLDRMIEEYF--FHKGASIgyYHGDLNALRD-----DIVE 315
Cdd:cd17656 146 VQLEHKNMVNLLH----FEREKTNINFSDKV-LQFATCS--FDVCYQEIFstLLSGGTL--YIIREETKRDveqlfDLVK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 316 LKPTLLVGVPRVYeriyegiLKAIAELRPLrrvifnalynrklasmkagyshktASPFADMLafrkvkarlggrlRLLIS 395
Cdd:cd17656 217 RHNIEVVFLPVAF-------LKFIFSEREF------------------------INRFPTCV-------------KHIIT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 396 GGAPL--SNEIEEFMRVTTCAYFiQGYGLTET--LGPSTVCYIDDMALVGSAGVPATYTEIRLEEvPEMGYNPLGVPsrG 471
Cdd:cd17656 253 AGEQLviTNEFKEMLHEHNVHLH-NHYGPSEThvVTTYTINPEAEIPELPPIGKPISNTWIYILD-QEQQLQPQGIV--G 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 472 EICIRGKSLFAGYYKSPELTNEAIVDGWF-------HTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVEYLEKVYGFP 544
Cdd:cd17656 329 ELYISGASVARGYLNRQELTAEKFFPDPFdpnermyRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNH 407
|
490 500
....*....|....*....|....*....
gi 226491570 545 PLVED--IWVYGDSFRSS-LVAVVNPHQE 570
Cdd:cd17656 408 PGVSEavVLDKADDKGEKyLCAYFVMEQE 436
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
83-246 |
2.08e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 60.54 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAC-----------NGYSlvcvplydtlgAGAV-DYIID 150
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACarigavhsvvfGGFS-----------AEALaDRIID 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 151 hAEIDVVFIQD------KKI--KEI----LSpNCKSAKrlKALVA-FTSATTEQNKEADqigikmYAWDDFLKVGKDNpr 217
Cdd:PRK00174 169 -AGAKLVITADegvrggKPIplKANvdeaLA-NCPSVE--KVIVVrRTGGDVDWVEGRD------LWWHELVAGASDE-- 236
|
170 180 190
....*....|....*....|....*....|..
gi 226491570 218 qpCPPQ---ASDICTVMYTSGTSGQPKGVMLT 246
Cdd:PRK00174 237 --CEPEpmdAEDPLFILYTSGSTGKPKGVLHT 266
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
83-567 |
2.27e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 60.16 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACN--GYSLVcvpLYDTLGAG-AVDYIIDHAEIDVVFI 159
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANriGADIL---LLNTSFAGpALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 160 qDKKIKEILS---PNCKSAKRLkalVAFTSATTEQNKEAdqigikmyawddfLKVGKDNPRQPCPPQASDicTVMYTSGT 236
Cdd:PRK13382 147 -DEEFSATVDralADCPQATRI---VAWTDEDHDLTVEV-------------LIAAHAGQRPEPTGRKGR--VILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 237 SGQPKGVMLTHESHAMYVKGVdlfmdqfddkmttddvfLSFLPLAHILDRMIEEYFFHK-GASigyyhgdlnalrddivE 315
Cdd:PRK13382 208 TGTPKGARRSGPGGIGTLKAI-----------------LDRTPWRAEEPTVIVAPMFHAwGFS----------------Q 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 316 LKPTLLVGVPRVYERIY--EGILKAIAELRPLRRVIFNALYNRKlasmkagyshktaspfadMLAFRKVKARLGGR-LRL 392
Cdd:PRK13382 255 LVLAASLACTIVTRRRFdpEATLDLIDRHRATGLAVVPVMFDRI------------------MDLPAEVRNRYSGRsLRF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 393 LISGGAPLSNEI-EEFM-RVTTCAYfiQGYGLTETLGPSTVCYIDDMALVGSAGVPATYTEIRLEEvPEMGYNPLGvpSR 470
Cdd:PRK13382 317 AAASGSRMRPDVvIAFMdQFGDVIY--NNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILD-QDFREVPTG--EV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 471 GEICIRGKSLFAGYYKSpelTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDI 550
Cdd:PRK13382 392 GTIFVRNDTQFDGYTSG---STKDFHDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDVAEA 467
|
490 500
....*....|....*....|
gi 226491570 551 WVYG---DSFRSSLVAVVNP 567
Cdd:PRK13382 468 AVIGvddEQYGQRLAAFVVL 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-530 |
2.44e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.95 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPL---Y--DTLGagavdYIIDHAEIDVV 157
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLdpeYprERLA-----YMIEDSGIELL 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 158 FIQDKKIKEILSPNcksakRLKALVAftsatteqnkeaDQIGIKMYAWDDflkvgkDNPRQPCPPQasDICTVMYTSGTS 237
Cdd:PRK12467 1676 LTQSHLQARLPLPD-----GLRSLVL------------DQEDDWLEGYSD------SNPAVNLAPQ--NLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 238 GQPKGVMLTHesHAMyVKGVDLFMDQFDdkMTTDDVFLSFLPLAhiLDRMIEEYFFH--KGASI----GYYHGDLNALRD 311
Cdd:PRK12467 1731 GRPKGAGNRH--GAL-VNRLCATQEAYQ--LSAADVVLQFTSFA--FDVSVWELFWPliNGARLviapPGAHRDPEQLIQ 1803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 312 DIVELKPTLLVGVPRVYERIYEgILKAIAELRPLRRVIFNAlynrklasmkagyshkTASPFAdmlAFRKVKARLGGRlr 391
Cdd:PRK12467 1804 LIERQQVTTLHFVPSMLQQLLQ-MDEQVEHPLSLRRVVCGG----------------EALEVE---ALRPWLERLPDT-- 1861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 392 llisggaplsneieefmrvttcaYFIQGYGLTETLGPSTVCYIDDMALVGSAGVP--------ATYteirleeVPEMGYN 463
Cdd:PRK12467 1862 -----------------------GLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPigqpianlSTY-------ILDASLN 1911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 464 PLGVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWF--------HTGDIGEMTPDGILKV---IDRKKNI--FKLSQGE 530
Cdd:PRK12467 1912 PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlyRTGDLARYRADGVIEYlgrIDHQVKIrgFRIELGE 1991
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
84-523 |
4.21e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 84 YKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGAGAVDYIIDHAEidvVFIQDKK 163
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLR---GMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 164 IKEILSPncksakrlKALVAFTSATTEQNKeadqiGIKMYAWDDFlkvgKDNPRQPC---PPQASDICTVMYTSGTSGQP 240
Cdd:PRK09192 129 PAAIITP--------DELLPWVNEATHGNP-----LLHVLSHAWF----KALPEADValpRPTPDDIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 241 KGVMLTHES-----HAMYVKGVdlfmdqfddKMTTDDVFLSFLPlahildrmieeyFFHKGASIGYYhgdLNALRDDI-V 314
Cdd:PRK09192 192 RGVIITHRAlmanlRAISHDGL---------KVRPGDRCVSWLP------------FYHDMGLVGFL---LTPVATQLsV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 315 ELKPTllvgvpRVYERiyegilkaiaelRPLrrvIFNALYNRKLASMkaGYShktaSPFA-DMLAFRKVKARLGG----R 389
Cdd:PRK09192 248 DYLPT------RDFAR------------RPL---QWLDLISRNRGTI--SYS----PPFGyELCARRVNSKDLAEldlsC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LRLLISGGAPLSNEI-EEFMRVTTCA-----YFIQGYGLTE-TLGPS-----------TV---CYIDDMALVGSAGVPAT 448
Cdd:PRK09192 301 WRVAGIGADMIRPDVlHQFAEAFAPAgfddkAFMPSYGLAEaTLAVSfsplgsgivveEVdrdRLEYQGKAVAPGAETRR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 449 YTEIRL--EEVPEMGY---NPLG--VPSR--GEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTpDGILKVIDR 519
Cdd:PRK09192 381 VRTFVNcgKALPGHEIeirNEAGmpLPERvvGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGR 459
|
....
gi 226491570 520 KKNI 523
Cdd:PRK09192 460 AKDL 463
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
216-540 |
6.27e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.34 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 216 PRQP-CPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLahildrmieeyfFH 294
Cdd:PRK08043 355 PRLAqVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIAD-----FTPNDRFMSALPL------------FH 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 295 K-GASIGYyhgdlnalrddiveLKPtLLVGVpRVYerIYEGilkaiaelrPLR-RVIFNALYNRKL-----ASMKAGYSH 367
Cdd:PRK08043 418 SfGLTVGL--------------FTP-LLTGA-EVF--LYPS---------PLHyRIVPELVYDRNCtvlfgTSTFLGNYA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 368 KTASPFaDMlafrkvkarlgGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETlGPSTVCYIDDMALVGSAGVPA 447
Cdd:PRK08043 471 RFANPY-DF-----------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEC-APVVSINVPMAAKPGTVGRIL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 448 TYTEIRLEEVPemgynplGVPSRGEICIRGKSLFAGYYK--------SPELTNEA--IVDGWFHTGDIGEMTPDGILKVI 517
Cdd:PRK08043 538 PGMDARLLSVP-------GIEQGGRLQLKGPNIMNGYLRvekpgvleVPTAENARgeMERGWYDTGDIVRFDEQGFVQIQ 610
|
330 340
....*....|....*....|...
gi 226491570 518 DRKKNIFKLSqGEYVAVEYLEKV 540
Cdd:PRK08043 611 GRAKRFAKIA-GEMVSLEMVEQL 632
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
83-247 |
5.91e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 55.96 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNgySL-----VCVPLYdtlGAGAVdyiIDH-AEID- 155
Cdd:PRK03584 116 SWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATA--SLgaiwsSCSPDF---GVQGV---LDRfGQIEp 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 156 VVFI-----------QDK--KIKEIlspnCKSAKRLKALVAFTSATTEQNKEADqigIKMYAWDDFLKVGKDNPRQPCPP 222
Cdd:PRK03584 188 KVLIavdgyryggkaFDRraKVAEL----RAALPSLEHVVVVPYLGPAAAAAAL---PGALLWEDFLAPAEAAELEFEPV 260
|
170 180 190
....*....|....*....|....*....|..
gi 226491570 223 QASDICTVMYTSGTSGQPK-------GVMLTH 247
Cdd:PRK03584 261 PFDHPLWILYSSGTTGLPKcivhghgGILLEH 292
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
384-527 |
9.18e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 54.88 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 384 ARLGGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETlgpstVCYIDD----MALVGSAGVPATYTEIRLeevpe 459
Cdd:cd05974 196 ASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET-----TALVGNspgqPVKAGSMGRPLPGYRVAL----- 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226491570 460 mgYNPLGVPSR-GEICI-----RGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLS 527
Cdd:cd05974 266 --LDPDGAPATeGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
390-539 |
1.65e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 54.23 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 LRLLISGGAPLSNEIEEfmRVTT---CAyFIQGYGLTETLgpstVCYI----DDMALVGSAGVPATYT-EIRLeeVPEMG 461
Cdd:PRK10946 302 LKLLQVGGARLSETLAR--RIPAelgCQ-LQQVFGMAEGL----VNYTrlddSDERIFTTQGRPMSPDdEVWV--ADADG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 462 yNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI-VDGWFHTGDIGEMTPDGILKVIDRKKNifklsQ----GEYVAVEY 536
Cdd:PRK10946 373 -NPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEE 446
|
...
gi 226491570 537 LEK 539
Cdd:PRK10946 447 IEN 449
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
388-524 |
1.74e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 388 GRLRLLISGGAPLsnEIEEFMRVTTC-AYF-------IQGYGLTETL------GPSTVCYIDDMALVGSA--------GV 445
Cdd:PRK05851 272 GALRVALNGGEPV--DCDGFERFATAmAPFgfdagaaAPSYGLAESTcavtvpVPGIGLRVDEVTTDDGSgarrhavlGN 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 446 PATYTEIRLEEvpemGYNPLGVPSR--GEICIRGKSLFAGYYKSPELTNeaivDGWFHTGDIGEMTpDGILKVIDRKK-- 521
Cdd:PRK05851 350 PIPGMEVRISP----GDGAAGVAGReiGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLGYLV-DGGLVVCGRAKel 420
|
....*....
gi 226491570 522 ------NIF 524
Cdd:PRK05851 421 itvagrNIF 429
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
230-530 |
3.28e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 230 VMYTSGTSGQPKGVMLTHESHAMYVKGVdlfMDQFDdkMTTDDVFLSFLplahildrmieeyffhkgaSIGYyhgDLNAL 309
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAV---IERFG--MRADDCELHFY-------------------SINF---DAASE 2390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 310 RddiveLKPTLLVGVPRVYERIYEGILKAIAELRPLRRVifNALynrklasmkaGYSHKTASPFADMLAFRkvkarlGGR 389
Cdd:PRK05691 2391 R-----LLVPLLCGARVVLRAQGQWGAEEICQLIREQQV--SIL----------GFTPSYGSQLAQWLAGQ------GEQ 2447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 390 L--RLLISGGAPLSNE-IEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVP---------ATYTEIRLEEV 457
Cdd:PRK05691 2448 LpvRMCITGGEALTGEhLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVPigrvvgarvAYILDADLALV 2527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 458 PEMGynplgvpsRGEICIRGKSLFAGYYKSPELTNEAIV------DG--WFHTGDIGEMTPDGILKVIDR-----KKNIF 524
Cdd:PRK05691 2528 PQGA--------TGELYVGGAGLAQGYHDRPGLTAERFVadpfaaDGgrLYRTGDLVRLRADGLVEYVGRidhqvKIRGF 2599
|
....*.
gi 226491570 525 KLSQGE 530
Cdd:PRK05691 2600 RIELGE 2605
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
59-529 |
3.52e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 53.24 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 59 KYADNRMLGWRPfkdgvPGPYLWK----------SYKEIYDEVLQAGSAL-QKLGVQPGSRVGIYGANCPQWIVAMQACN 127
Cdd:cd05928 14 QWADKEKAGKRP-----PNPALWWvngkgdevkwSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 128 GYSLVCVPLYDTLGAGAVDYIIDHAEIDVVFIQDKKIKEI--LSPNCKSAKrLKALVAFTSatteqnkeadqigikMYAW 205
Cdd:cd05928 89 RTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVdsVASECPSLK-TKLLVSEKS---------------RDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 206 DDFLK-VGKDNPRQPCPPQAS-DICTVMYTSGTSGQPKgvMLTHeSHAMYvkGVDLFMD-QFDDKMTTDDVFLSFLPLAH 282
Cdd:cd05928 153 LNFKElLNEASTEHHCVETGSqEPMAIYFTSGTTGSPK--MAEH-SHSSL--GLGLKVNgRYWLDLTASDIMWNTSDTGW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 283 ILDrMIEEYF--FHKGASIGYYH---GDLNALRDDIVELKPTLLVGVPRVYeRIyegilkaiaelrplrrvifnaLYNRK 357
Cdd:cd05928 228 IKS-AWSSLFepWIQGACVFVHHlprFDPLVILKTLSSYPITTFCGAPTVY-RM---------------------LVQQD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 358 LASMKagyshktaspfadmlaFRkvkarlggRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLgpsTVCYI-DD 436
Cdd:cd05928 285 LSSYK----------------FP--------SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG---LICANfKG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 437 MALV-GSAGVPATYTEIRLeeVPEMGyNPLGVPSRGEICIRGK-----SLFAGYYKSPELTNEAIVDGWFHTGDIGEMTP 510
Cdd:cd05928 338 MKIKpGSMGKASPPYDVQI--IDDNG-NVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDE 414
|
490
....*....|....*....
gi 226491570 511 DGILKVIDRKKNIFkLSQG 529
Cdd:cd05928 415 DGYFWFMGRADDVI-NSSG 432
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
208-567 |
3.97e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 52.74 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 208 FLKVGKDNPRQ---------PCPPQASDICTVMYTSGTSGQPKGVMLTheSHAMYVKGvdlfmDQFDDKMTTDDVFLSFL 278
Cdd:PRK07824 9 LLPVPAQDERRaallrdalrVGEPIDDDVALVVATSGTTGTPKGAMLT--AAALTASA-----DATHDRLGGPGQWLLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 279 PLAHIldrmieeyffhKGASIgyyhgdlnALRDDIVELKPTLLvGVPRVYEriYEGILKAIAELRPLRRvifnalynrkl 358
Cdd:PRK07824 82 PAHHI-----------AGLQV--------LVRSVIAGSEPVEL-DVSAGFD--PTALPRAVAELGGGRR----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 359 asmkagYSHKTASPFADMLAFRKVKARLGGRLRLLIsGGAPLSNEIEE------FMRVTTcayfiqgYGLTETLGPstvC 432
Cdd:PRK07824 129 ------YTSLVPMQLAKALDDPAATAALAELDAVLV-GGGPAPAPVLDaaaaagINVVRT-------YGMSETSGG---C 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 433 YIDdmalvgsaGVPATYTEIRLEEvpemgynplgvpsrGEICIRGKSLFAGYYKSPEltNEAIVD-GWFHTGDIGEMTpD 511
Cdd:PRK07824 192 VYD--------GVPLDGVRVRVED--------------GRIALGGPTLAKGYRNPVD--PDPFAEpGWFRTDDLGALD-D 246
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 512 GILKVIDRKKNIFKlSQGEYVAVEYLEKVYGFPPLVEDIWVYG---DSFRSSLVAVVNP 567
Cdd:PRK07824 247 GVLTVLGRADDAIS-TGGLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVG 304
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
83-514 |
5.38e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.59 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACN----GYslvcVPLYDTLGAGAVDYIIDHAEIDVVF 158
Cdd:PRK04813 29 TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVkaghAY----IPVDVSSPAERIEMIIEVAKPSLII 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 iqdkkikeilspncksakrlkalvaftsATTEQNKEADqiGIKMYAWDDFlkvgKDNPRQPCPPQAS------DICTVMY 232
Cdd:PRK04813 105 ----------------------------ATEELPLEIL--GIPVITLDEL----KDIFATGNPYDFDhavkgdDNYYIIF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 233 TSGTSGQPKGVMLTHEShamyvkgvdlfMDQFDDKMTTD------DVFLSFLPlahildrmieeYFFhkgasigyyhgDL 306
Cdd:PRK04813 151 TSGTTGKPKGVQISHDN-----------LVSFTNWMLEDfalpegPQFLNQAP-----------YSF-----------DL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 307 NalrddIVELKPTLLVGvprvyeriyeGILKAIAelrplRRVI--FNALYNRkLASMKAGYSHKTASpFADM-LAFRKVK 383
Cdd:PRK04813 198 S-----VMDLYPTLASG----------GTLVALP-----KDMTanFKQLFET-LPQLPINVWVSTPS-FADMcLLDPSFN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 384 ARLGGRLRLLISGGAPLSNEIEE--FMRVTTcAYFIQGYGLTETLGPSTVCYIDDMALVGSAGVPATYT--EIRLEEVPE 459
Cdd:PRK04813 256 EEHLPNLTHFLFCGEELPHKTAKklLERFPS-ATIYNTYGPTEATVAVTSIEITDEMLDQYKRLPIGYAkpDSPLLIIDE 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 460 MGyNPLGVPSRGEICIRGKSLFAGYYKSPELTNEAI--VDGW--FHTGDIGEMtPDGIL 514
Cdd:PRK04813 335 EG-TKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYL-EDGLL 391
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
223-523 |
5.89e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.25 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLtheSHAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLAHILdrmieeyffhkgasigyy 302
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQV---SHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDM------------------ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 hGDLNALrddiveLKPtLLVGVPRVyeriyegiLKAIAEL--RPLRRVifnalynrKLASMKAGyshkTASPFADmLAFR 380
Cdd:PRK05691 223 -GLIGGL------LQP-IFSGVPCV--------LMSPAYFleRPLRWL--------EAISEYGG----TISGGPD-FAYR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 381 KVKARLG---------GRLRLLISGGAPL-SNEIEEFM-RVTTCAY----FIQGYGLTE-TL---------GPSTVcYID 435
Cdd:PRK05691 274 LCSERVSesalerldlSRWRVAYSGSEPIrQDSLERFAeKFAACGFdpdsFFASYGLAEaTLfvsggrrgqGIPAL-ELD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 436 DMALVGSAGVPATYTEIRLEEVPEMGYNPLGV-PSR---------GEICIRGKSLFAGYYKSPELTNEAIV--DG--WFH 501
Cdd:PRK05691 353 AEALARNRAEPGTGSVLMSCGRSQPGHAVLIVdPQSlevlgdnrvGEIWASGPSIAHGYWRNPEASAKTFVehDGrtWLR 432
|
330 340
....*....|....*....|..
gi 226491570 502 TGDIGEMTpDGILKVIDRKKNI 523
Cdd:PRK05691 433 TGDLGFLR-DGELFVTGRLKDM 453
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
78-538 |
6.17e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 52.82 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 78 PYLWKS----YKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVCVPLYDTLGagaVDYIIDHAE 153
Cdd:PTZ00237 85 PYLKKTikltYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYS---VKSLIDRIE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 154 IdvvfIQDKKI---------KEI--LSPNCKSAKRL---KALVAFTSATTEQNKEADQIGIK-------MYAWDDFLKVG 212
Cdd:PTZ00237 162 T----ITPKLIittnygilnDEIitFTPNLKEAIELstfKPSNVITLFRNDITSESDLKKIEtiptipnTLSWYDEIKKI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 213 KDNPRQP----CPPQASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDQFDDKMTtddvflsflplahildrmi 288
Cdd:PTZ00237 238 KENNQSPfyeyVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTV------------------- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 289 eeYFFHkgASIGY--YHGDLNALrddivelkptLLVGVPRVyerIYE-GILKAIAELRPLRRVIFNALYNRKLASMKAGY 365
Cdd:PTZ00237 299 --VFSH--SSIGWvsFHGFLYGS----------LSLGNTFV---MFEgGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 366 SHKTASPFADMLafrKVKARLgGRLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGPSTVCYIDDMALVGSAGV 445
Cdd:PTZ00237 362 YLIKTDPEATII---RSKYDL-SNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGV 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 446 PATYTE--IRLEEVPEMGYNPLgvpsrGEICIR---GKSLFAGYYKSPELTNEAIVD--GWFHTGDIGEMTPDGILKVID 518
Cdd:PTZ00237 438 PSIFIKpsILSEDGKELNVNEI-----GEVAFKlpmPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVS 512
|
490 500
....*....|....*....|
gi 226491570 519 RKKNIFKLSqGEYVAVEYLE 538
Cdd:PTZ00237 513 RSDDQIKIS-GNKVQLNTIE 531
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-567 |
1.22e-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: 51.31 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 222 PQASDICTVMYTSGTSGQPKGVMLTHeshAMYVKGVDLFMDQFDdkMTTDDVFLSFLPLAHILD------RMIEEYFFHK 295
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRH---GTFAAQIDALRQLYG--IRPGEVDLATFPLFALFGpalgltSVIPDMDPTR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 296 GASIgyyhgDLNALRDDIVELKPTLLVGVPRVYERIYEGILKAIAELRPLRRVIfnalynrklasmKAGyshktaSPfad 375
Cdd:cd05910 157 PARA-----DPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVL------------SAG------AP--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 376 mlafrkVKARLGGRLRLLISGGAPlsneieefmrvttcayFIQGYGLTETLgpsTVCYIDDMAL---------------V 440
Cdd:cd05910 211 ------VPIALAARLRKMLSDEAE----------------ILTPYGATEAL---PVSSIGSRELlatttaatsggagtcV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 441 GS--AGVPATYTEIRLEEVPEMGyNPLGVPSR--GEICIRGKSLFAGYYKSPELTNEAIVDG-----WFHTGDIGEMTPD 511
Cdd:cd05910 266 GRpiPGVRVRIIEIDDEPIAEWD-DTLELPRGeiGEITVTGPTVTPTYVNRPVATALAKIDDnsegfWHRMGDLGYLDDE 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 226491570 512 GILKVIDRKKNIFKLSQGEYVAvEYLEKVYGFPPLVEdiwvygdsfRSSLVAVVNP 567
Cdd:cd05910 345 GRLWFCGRKAHRVITTGGTLYT-EPVERVFNTHPGVR---------RSALVGVGKP 390
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
403-554 |
1.93e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.80 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 403 EIEEFMRVTTCAYFiQGYGLTETLGPSTVcyiDDMALVGSAGVPATYTEI----RLEEVPEMGYNPLGV-----PSRGEI 473
Cdd:PRK13388 279 DIAEFSRRFGCQVE-DGYGSSEGAVIVVR---EPGTPPGSIGRGAPGVAIynpeTLTECAVARFDAHGAllnadEAIGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 474 CIR-GKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFKLSqGEYVAVEYLEKVYGFPPLVEDIWV 552
Cdd:PRK13388 355 VNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRVAV 433
|
..
gi 226491570 553 YG 554
Cdd:PRK13388 434 YA 435
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
83-554 |
3.09e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 50.04 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAcngyslvcvplydTLGAGAVdyiidhaeidVVFIQDK 162
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLG-------------LVKIGAV----------AALINYN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEIL--SPNCKSAKrlkALVAftsatteqnkeadqigikmyawddflkvgkdnprqpcppqasDICTVMYTSGTSGQP 240
Cdd:cd05940 62 LRGESLahCLNVSSAK---HLVV------------------------------------------DAALYIYTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 241 KGVMLTHEShamYVKGVDLFMDQFddKMTTDDVFLSFLPLahildrmieeyfFHKGASIGYYHGDLN-----ALR----- 310
Cdd:cd05940 97 KAAIISHRR---AWRGGAFFAGSG--GALPSDVLYTCLPL------------YHSTALIVGWSACLAsgatlVIRkkfsa 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 311 ----DDIVELKPTLLVgvprvyeriYegilkaIAELrplrrvifnalyNRKLASMKAGYSHKTaspfadmlafRKVKARL 386
Cdd:cd05940 160 snfwDDIRKYQATIFQ---------Y------IGEL------------CRYLLNQPPKPTERK----------HKVRMIF 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 387 GGRLRLLISG------GAPlsnEIEEFMRVTTCAY-FIQGYGLTETLG--PSTVCYIDDMALVG---SAGVPATYTEIRL 454
Cdd:cd05940 203 GNGLRPDIWEefkerfGVP---RIAEFYAATEGNSgFINFFGKPGAIGrnPSLLRKVAPLALVKydlESGEPIRDAEGRC 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 455 EEVPemgynplgvpsRGE----IC-IRGKSLFAGYYKSPElTNEAIV-------DGWFHTGDIGEMTPDGILKVIDRKKN 522
Cdd:cd05940 280 IKVP-----------RGEpgllISrINPLEPFDGYTDPAA-TEKKILrdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
490 500 510
....*....|....*....|....*....|..
gi 226491570 523 IFKLsQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:cd05940 348 TFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
83-247 |
8.30e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 49.27 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQAcngyslvcvplydTLGAGAVDYIIDHAEidvvfiQDK 162
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA-------------IVEAGAAWLPLDTGY------PDD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 163 KIKEILSpnckSAKrlKALVAFTSAttEQNKEADQIGIKMYAWDDFLKVGKDNPRQPcpPQASDICTVMYTSGTSGQPKG 242
Cdd:PRK10252 546 RLKMMLE----DAR--PSLLITTAD--QLPRFADVPDLTSLCYNAPLAPQGAAPLQL--SQPHHTAYIIFTSGSTGRPKG 615
|
....*
gi 226491570 243 VMLTH 247
Cdd:PRK10252 616 VMVGQ 620
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
223-519 |
8.59e-06 |
|
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: 48.84 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 223 QASDICTVMYTSGTSGQPKGVMLTHESHAMYVKGVDLFMDqFDDkmttDDVFLSFLPLAhiLDRMIEEYFfhkGAsigYY 302
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFG-FNE----DDVWTLFHSYA--FDFSVWEIW---GA---LL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 303 HGdlnalrddivelkpTLLVGVPRvyeriyeGILKAIAELRPL---RRV-IFNalynrklasmkagyshKTASPFADMLA 378
Cdd:cd17643 158 HG--------------GRLVVVPY-------EVARSPEDFARLlrdEGVtVLN----------------QTPSAFYQLVE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 379 FRKVKARLGGRLRLLISGGAPLsneieEFMRV--------TTCAYFIQGYGLTETLGPSTVCYIDDMALVGSA----GVP 446
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEAL-----EAAMLrpwagrfgLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAaspiGRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 447 ATYTEIRLeevpeMGYN----PLGVPsrGEICIRGKSLFAGYYKSPELTNEAIVDGWF--------HTGDIGEMTPDGIL 514
Cdd:cd17643 276 LPGLRVYV-----LDADgrpvPPGVV--GELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmyRTGDLARRLPDGEL 348
|
....*
gi 226491570 515 KVIDR 519
Cdd:cd17643 349 EYLGR 353
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-554 |
1.00e-05 |
|
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: 48.17 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 226 DICTVMYTSGTSGQPKGVMLTHESH-AMYVKGVDLFmdqfddKMTTDDVFLSFLPLAHILDRMIEEYFFHKGAS-IGYYH 303
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWiESFVCNEDLF------NISGEDAILAPGPLSHSLFLYGAISALYLGGTfIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 304 GDLNALRDDIVELKPTLLVGVPRVYE---RIYEGILKAiaelrplrRVIFnalynrklasmkagyshkTASPFADMLAFR 380
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQalaRTLEPESKI--------KSIF------------------SSGQKLFESTKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 381 KVKArlggrlrllisgGAPLSNEIEefmrvttcayFiqgYGLTETLGPSTVCYiDDMALVGSAGVPATYTEIRLEEVPEM 460
Cdd:cd17633 129 KLKN------------IFPKANLIE----------F---YGTSELSFITYNFN-QESRPPNSVGRPFPNVEIEIRNADGG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 461 GYnplgvpsrGEICIRGKSLFAGYYKSPELTNeaivDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKV 540
Cdd:cd17633 183 EI--------GKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESV 249
|
330
....*....|....
gi 226491570 541 YGFPPLVEDIWVYG 554
Cdd:cd17633 250 LKAIPGIEEAIVVG 263
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
97-282 |
1.52e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.95 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 97 ALQKLGVQPGSRVGIYGANCPQWIVAMQACN--GyslVCVPLYDTLGAGAVdyiIDHAeIDVV----FIQDkkikEILSP 170
Cdd:PRK08279 78 WAAARGVGKGDVVALLMENRPEYLAAWLGLAklG---AVVALLNTQQRGAV---LAHS-LNLVdakhLIVG----EELVE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 171 NCKSAK-RLKALVAFTSATTEQNKEADqigikmyAWDDFLKVG----KDNPRQPCPPQASDICTVMYTSGTSGQPKGVML 245
Cdd:PRK08279 147 AFEEARaDLARPPRLWVAGGDTLDDPE-------GYEDLAAAAagapTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVM 219
|
170 180 190
....*....|....*....|....*....|....*..
gi 226491570 246 THESHAMYVKGVDLFMDqfddkMTTDDVFLSFLPLAH 282
Cdd:PRK08279 220 SHMRWLKAMGGFGGLLR-----LTPDDVLYCCLPLYH 251
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
83-243 |
2.28e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 47.64 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACN--G--YSLVcvplYDTLGAGAVDYIIDHAEIDVVF 158
Cdd:PRK10524 86 TFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACAriGaiHSVV----FGGFASHSLAARIDDAKPVLIV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 IQD------KKI--KEILSPNCKSAKRLKALVAFTS---ATTEQNKEADQigikmyawdDF--LKVGKDNPRQPCP-PQA 224
Cdd:PRK10524 162 SADagsrggKVVpyKPLLDEAIALAQHKPRHVLLVDrglAPMARVAGRDV---------DYatLRAQHLGARVPVEwLES 232
|
170
....*....|....*....
gi 226491570 225 SDICTVMYTSGTSGQPKGV 243
Cdd:PRK10524 233 NEPSYILYTSGTTGKPKGV 251
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
420-554 |
3.41e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 46.91 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 420 YGLTETlgPSTVCYID-DMALVG--SAGVPATYTEIRLEEvpemgynplgvPSRGEICIRGKSLFAGYYksPELTNEAIV 496
Cdd:PRK07445 261 YGMTET--ASQIATLKpDDFLAGnnSSGQVLPHAQITIPA-----------NQTGNITIQAQSLALGYY--PQILDSQGI 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 497 dgwFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:PRK07445 326 ---FETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLG 379
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
214-521 |
3.96e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.86 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 214 DNPRQPC--PPQASDICTVMYTSGTSGQPKGVMLTHES-HAMYVKGVDLFMDQFDDKMTTDDVFLSFLPLahildrmiee 290
Cdd:PRK05850 147 DSPRGSDarPRDLPSTAYLQYTSGSTRTPAGVMVSHRNvIANFEQLMSDYFGDTGGVPPPDTTVVSWLPF---------- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 291 yffhkgasigyYHgDLNAlrddIVELKPTLLVGVPRVyeriyegILKAIAEL-RPLRRVifnalynRKLASMKAGYShkt 369
Cdd:PRK05850 217 -----------YH-DMGL----VLGVCAPILGGCPAV-------LTSPVAFLqRPARWM-------QLLASNPHAFS--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 370 ASP-FADMLAFRKVK----ARLG-GRLRLLISGG-----APLSNEIEEFMRVTTCAYFIQ-GYGLTE-TL--------GP 428
Cdd:PRK05850 264 AAPnFAFELAVRKTSdddmAGLDlGGVLGIISGServhpATLKRFADRFAPFNLRETAIRpSYGLAEaTVyvatrepgQP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 429 STVCYIDDMAL-VGSA--------------GVPATYTeIRLEEVPEMGYNPLGVPsrGEICIRGKSLFAGYYKSPELTNE 493
Cdd:PRK05850 344 PESVRFDYEKLsAGHAkrcetgggtplvsyGSPRSPT-VRIVDPDTCIECPAGTV--GEIWVHGDNVAAGYWQKPEETER 420
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 226491570 494 ----AIVD---G-----WFHTGDIGEMTpDGILKVIDRKK 521
Cdd:PRK05850 421 tfgaTLVDpspGtpegpWLRTGDLGFIS-EGELFIVGRIK 459
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
225-520 |
7.52e-05 |
|
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: 45.85 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 225 SDICTVMYTSGTSGQPKGVMLTHEShamYVKGVDLFMDQFDDKMTTDDVFLSFlpLAHILDRMIEEYFF-----HKGASI 299
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGVLVEHGS---VVNLRTSLSERYFGRDNGDEAVLFF--SNYVFDFFVEQMTLallngQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 300 -GYYHGDLNALRDDIVELKPTLLVGVPRVYERIyegilkAIAELRPLRRVIFnalynrklasmkAGYSHKTAspfadmlA 378
Cdd:cd17648 169 pDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY------DLARLPHLKRVDA------------AGEEFTAP-------V 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 379 FRKVKARLGGRLrllisggaplsneieefmrvttcayfIQGYGLTETLGPSTVCYID-----DMALvgSAGVPATYTEI- 452
Cdd:cd17648 224 FEKLRSRFAGLI--------------------------INAYGPTETTVTNHKRFFPgdqrfDKSL--GRPVRNTKCYVl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 453 --RLEEVPemgynplgVPSRGEICIRGKSLFAGYYKSPELTNEAIVDGWFH---------------TGDIGEMTPDGILK 515
Cdd:cd17648 276 ndAMKRVP--------VGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargrnarlykTGDLVRWLPSGELE 347
|
....*
gi 226491570 516 VIDRK 520
Cdd:cd17648 348 YLGRN 352
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
230-519 |
7.80e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 230 VMYTSGTSGQPKGVMLTHESHAMYVKgvdlFMdQFDDKMTTDDVFLSFLPLAhiLDRMIEEYFFhkgasigyyhgdlnal 309
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAALAERLQ----WM-QATYALDDSDVLMQKAPIS--FDVSVWECFW---------------- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 310 rddivelkpTLLVGVPRVyeriyegiLKAIAELRPLRRVIfnALYNRKlasmkagysHKTASPFADMLAFRKVKARLGG- 388
Cdd:PRK05691 1335 ---------PLITGCRLV--------LAGPGEHRDPQRIA--ELVQQY---------GVTTLHFVPPLLQLFIDEPLAAa 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 389 --RLRLLISGGAPLSNEIEEfmRVTTCAYFIQ---GYGLTETLGPST--VCYIDDmALVGSAGVPATYTEIRLEEvPEMG 461
Cdd:PRK05691 1387 ctSLRRLFSGGEALPAELRN--RVLQRLPQVQlhnRYGPTETAINVThwQCQAED-GERSPIGRPLGNVLCRVLD-AELN 1462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226491570 462 YNPLGVPsrGEICIRGKSLFAGYYKSPELTNEAIV------DG--WFHTGDIGEMTPDGILKVIDR 519
Cdd:PRK05691 1463 LLPPGVA--GELCIGGAGLARGYLGRPALTAERFVpdplgeDGarLYRTGDRARWNADGALEYLGR 1526
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
471-569 |
1.04e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.16 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 471 GEICIRGKSLFAGYYKSPELTNEAIVDGWFHTGDIGEMTPDGILKVIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDI 550
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEI 412
|
90 100
....*....|....*....|..
gi 226491570 551 WVYG--DSFRSSL-VAVVNPHQ 569
Cdd:PRK07638 413 VVIGvpDSYWGEKpVAIIKGSA 434
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
83-554 |
1.54e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 44.73 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 83 SYKEIYDEVLQAGSALQK-LGVQPGSRVGIYGANCPQWIVAMQACngYSLVCVPL---YDTLGAGAVdyiidhaeidvvf 158
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGL--WSIGAAPAfinYNLSGDPLI------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 159 iqdkkikeilspNCKSAKRLKALVAftsatteqnkeadqigikmyawDDflkvgkdnprqpcppqaSDICTVMYTSGTSG 238
Cdd:cd05937 72 ------------HCLKLSGSRFVIV----------------------DP-----------------DDPAILIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 239 QPKGVMLtheSHAMYVKGVDLFMDQFDdkMTTDDVFLSFLPL----AHILDRMieeYFFHKGASIGYYHG-DLNALRDDI 313
Cdd:cd05937 101 LPKAAAI---SWRRTLVTSNLLSHDLN--LKNGDRTYTCMPLyhgtAAFLGAC---NCLMSGGTLALSRKfSASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 314 VELKPTLLVgvprvyeriYEGilkaiaelrPLRRVIFNAlynrklasmkagyshkTASPFADMlafRKVKARLGGRLRLL 393
Cdd:cd05937 173 RDSGATIIQ---------YVG---------ELCRYLLST----------------PPSPYDRD---HKVRVAWGNGLRPD 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 394 ISG------GAPlsnEIEEFmrvttcayfiqgYGLTETLGPSTVCYIDDMALvGSAGVPATYTEIRLEEV---------- 457
Cdd:cd05937 216 IWErfrerfNVP---EIGEF------------YAATEGVFALTNHNVGDFGA-GAIGHHGLIRRWKFENQvvlvkmdpet 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 458 ------PEMGY---NPLGVPsrGEICIR----GKSLFAGYYKSPELTNEAIV-------DGWFHTGDIGEMTPDGILKVI 517
Cdd:cd05937 280 ddpirdPKTGFcvrAPVGEP--GEMLGRvpfkNREAFQGYLHNEDATESKLVrdvfrkgDIYFRTGDLLRQDADGRWYFL 357
|
490 500 510
....*....|....*....|....*....|....*..
gi 226491570 518 DRKKNIFKLsQGEYVAVEYLEKVYGFPPLVEDIWVYG 554
Cdd:cd05937 358 DRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
204-570 |
1.81e-04 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 44.68 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 204 AWDDFLKVGKDNPRQPCPPQA--SDIctvMYTSGTSGQPKGVMLTHESHAMYVKgvDLFMDQFDDKMTTDDVFLSFLPLA 281
Cdd:cd05929 105 GLEDYEAAEGGSPETPIEDEAagWKM---LYSGGTTGRPKGIKRGLPGGPPDND--TLMAAALGFGPGADSVYLSPAPLY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 282 HildrmieeyffhkGASIGYYHGdlnalrddivelkpTLLVGVPRVYERIY--EGILKAIAELRPLRRVIFNALYNRKLA 359
Cdd:cd05929 180 H-------------AAPFRWSMT--------------ALFMGGTLVLMEKFdpEEFLRLIERYRVTFAQFVPTMFVRLLK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 360 SMKA-GYSHKTASpfadmlafrkvkarlggrLRLLISGGAPLSNEIEEFMRVTTCAYFIQGYGLTETLGpSTVCYIDD-M 437
Cdd:cd05929 233 LPEAvRNAYDLSS------------------LKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQG-LTIINGEEwL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 438 ALVGSAGVPAtytEIRLEEVPEMGYN-PLGVPsrGEICIRGKSLFAgYYKSPELTNEAIV-DGWFHTGDIGEMTPDGILK 515
Cdd:cd05929 294 THPGSVGRAV---LGKVHILDEDGNEvPPGEI--GEVYFANGPGFE-YTNDPEKTAAARNeGGWSTLGDVGYLDEDGYLY 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 226491570 516 VIDRKKNIFkLSQGEYVAVEYLEKVYGFPPLVEDIWVYG---DSFRSSLVAVVNPHQE 570
Cdd:cd05929 368 LTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQPAPG 424
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
61-274 |
4.05e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 43.73 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 61 ADNRMLGWRPFKDGVPGPYlwkSYKEIYDEVLQAGSALQKLGVQPGSRVGIYGANCPQWIVAMQACNGYSLVcvplYDTL 140
Cdd:PLN02654 103 GDKIAIYWEGNEPGFDASL---TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAV----HSVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 141 GAGAvdyiidHAEIDVVFIQDKKIKEILSpnCKSAKR------LKALVafTSATTEQNKEADQIGI--------KMYAWD 206
Cdd:PLN02654 176 FAGF------SAESLAQRIVDCKPKVVIT--CNAVKRgpktinLKDIV--DAALDESAKNGVSVGIcltyenqlAMKRED 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226491570 207 DFLKVGKDNPRQPCPPQASDICTV-----------MYTSGTSGQPKGVMltHESHAMYVKGVDLFMDQFDDKMTtdDVF 274
Cdd:PLN02654 246 TKWQEGRDVWWQDVVPNYPTKCEVewvdaedplflLYTSGSTGKPKGVL--HTTGGYMVYTATTFKYAFDYKPT--DVY 320
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
475-554 |
4.17e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 40.35 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226491570 475 IRGKSLFAGYYKSPELTNEAIV-------DGWFHTGDIGEMTPDGILKVIDRKKNIFKLsQGEYVAVEYLEKVYGFPPLV 547
Cdd:cd05938 356 ITQQSPFLGYAGDKEQTEKKLLrdvfkkgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRW-KGENVATTEVADVLGLLDFL 434
|
....*..
gi 226491570 548 EDIWVYG 554
Cdd:cd05938 435 QEVNVYG 441
|
|
| |
