|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-659 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 1276.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 1 MPEVYTVKVEEGRLATDGKPSVGPVYRSIYAKDGLLEVPSDFKSPWDFFRDSVKRNPNNNMLGRRQKTESKLGSYTWLTY 80
Cdd:PLN02861 1 MAETYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 81 QDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEKKI 160
Cdd:PLN02861 81 KEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 161 PSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKGVVI 240
Cdd:PLN02861 161 SSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 241 KNEAFMAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQELKPTIFCGVP 320
Cdd:PLN02861 241 TNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 321 RVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPQHKAAPLFDRLVFDKTKLALGGRVRILLSGAAPLPRHVE 400
Cdd:PLN02861 321 RVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 401 EFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESVPEMGYDALSNVPRGEICLRGNTLFSGYH 480
Cdd:PLN02861 401 EFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 481 KREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGNSFESFLVAVV 560
Cdd:PLN02861 481 KRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 561 VPERKAIEDWAKEHNLTDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIERDLITPTFKLKRPQL 640
Cdd:PLN02861 561 VPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQL 640
|
650
....*....|....*....
gi 356575070 641 LKYYKDHIDQLYKEAKGAM 659
Cdd:PLN02861 641 LKYYKDCIDQLYSEAKGGK 659
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
5-659 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 877.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 5 YTVKVEEGRLATDGKPSVGPVYRSIYAKDGLLEVPSDFKSPWDFFRDSVKRNPNNNMLGRRQKTESKLGSYTWLTYQDVY 84
Cdd:PLN02614 7 FIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPNPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 85 DAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEKKIPSVL 164
Cdd:PLN02614 87 DIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 165 SCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCFSWGEFLQLG-CLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNE 243
Cdd:PLN02614 167 KTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGeGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 244 AFMAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQELKPTIFCGVPRVF 323
Cdd:PLN02614 247 SIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 324 DRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPQHKAAPLFDRLVFDKTKLALGGRVRILLSGAAPLPRHVEEFM 403
Cdd:PLN02614 327 DRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 404 RVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESVPEMGYDALSNVPRGEICLRGNTLFSGYHKRE 483
Cdd:PLN02614 407 RVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKRE 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 484 DLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGNSFESFLVAVVVPE 563
Cdd:PLN02614 487 DLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPN 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 564 RKAIEDWAKEHNLTDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIERDLITPTFKLKRPQLLKY 643
Cdd:PLN02614 567 QQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKY 646
|
650
....*....|....*.
gi 356575070 644 YKDHIDQLYKEAKGAM 659
Cdd:PLN02614 647 YQSVIDEMYKTTNEKL 662
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
3-653 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 814.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 3 EVYTVKVEEGRLATDGKPSVGPVYRSIYAKDGLLEVPSDFKSPWDFFRDSVKRNPNNNMLGRRQKTESKLGSYTWLTYQD 82
Cdd:PLN02430 2 KSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 83 VYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEKKIPS 162
Cdd:PLN02430 82 VYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 163 VLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCFSWGEFLQLGcldWDLPSK----KKTDICTIMYTSGTTGDPKGV 238
Cdd:PLN02430 162 LLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMG---KENPSEtnppKPLDICTIMYTSGTSGDPKGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 239 VIKNEAFMAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQELKPTIFCG 318
Cdd:PLN02430 239 VLTHEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 319 VPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPQHKAAPLFDRLVFDKTKLALGGRVRILLSGAAPLPRH 398
Cdd:PLN02430 319 VPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 399 VEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESVPEMGYDALSNVPRGEICLRGNTLFSG 478
Cdd:PLN02430 399 IEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 479 YHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGNSFESFLVA 558
Cdd:PLN02430 479 YYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 559 VVVPERKAIEDWAKEHNLTDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIERDLITPTFKLKRP 638
Cdd:PLN02430 559 VVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRN 638
|
650
....*....|....*
gi 356575070 639 QLLKYYKDHIDQLYK 653
Cdd:PLN02430 639 NLLKYYQVEIDEMYR 653
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
73-653 |
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: 804.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEV 150
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 151 SIAFvqekkipsvlsclaqCSSNLKTivsfgsvsttqkkeaeghgascFSWGEFLQLGCLD-WDLPSKKKTDICTIMYTS 229
Cdd:cd05927 81 SIVF---------------CDAGVKV----------------------YSLEEFEKLGKKNkVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 230 GTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRVaGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQ 309
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNKI-NPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 310 ELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPQhkAAPLFDRLVFDKTKLALGGRVRILL 389
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVR--ASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 390 SGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSmTGTVGVPMTTIEARLESVPEMGYDALSNVPRGEIC 469
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDVPEMNYDAKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 470 LRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVY 548
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 549 GNSFESFLVAVVVPERKAIEDWAKEHNLTD-DFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIERD 627
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAASKGGGTgSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
570 580
....*....|....*....|....*.
gi 356575070 628 LITPTFKLKRPQLLKYYKDHIDQLYK 653
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1-654 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 642.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 1 MPEVYTVKVEEgRLaTDGKPSVgpvYRSIYA----KDGLLEVPsDFKSPWDFFRDSVKRNPNNNMLGRRQKTESKLGSYT 76
Cdd:PLN02736 4 HEQGYSVVLPE-KL-QTGKWNV---YRSARSplklVSRFPDHP-EIGTLHDNFVYAVETFRDYKYLGTRIRVDGTVGEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 77 WLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNscAVSY--VPLYDTLGPNAVEFIINHAEVSIAF 154
Cdd:PLN02736 78 WMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACS--AYSYvsVPLYDTLGPDAVKFIVNHAEVAAIF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 VQEKKIPSVLSCLAQCSSnLKTIVSFGSVSTTQKKEAEGHGASCFSWGEFLQLGCLDWDLPS-KKKTDICTIMYTSGTTG 233
Cdd:PLN02736 156 CVPQTLNTLLSCLSEIPS-VRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRpPKPEDVATICYTSGTTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 234 DPKGVVIKNEAFMAEVLSVDHIIMLtdrvaGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQELKP 313
Cdd:PLN02736 235 TPKGVVLTHGNLIANVAGSSLSTKF-----YPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 314 TIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPqhkAAPLFDRLVFDKTKLALGGRVRILLSGAA 393
Cdd:PLN02736 310 TIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKN---PSPMWDRLVFNKIKAKLGGRVRFMSSGAS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 394 PLPRHVEEFMRVTSGSTLSQGYGLTE-SCAGCFTAIGDvySMTGTVGVPMTTIEARLESVPEMGY-DALSNVPRGEICLR 471
Cdd:PLN02736 387 PLSPDVMEFLRICFGGRVLEGYGMTEtSCVISGMDEGD--NLSGHVGSPNPACEVKLVDVPEMNYtSEDQPYPRGEICVR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 472 GNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGN 550
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 551 SFESFLVAVVVPERKAIEDWAKEHNL-TDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIERDLI 629
Cdd:PLN02736 545 SLNSSLVAVVVVDPEVLKAWAASEGIkYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLL 624
|
650 660
....*....|....*....|....*
gi 356575070 630 TPTFKLKRPQLLKYYKDHIDQLYKE 654
Cdd:PLN02736 625 TPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
47-655 |
6.95e-177 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 516.19 E-value: 6.95e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNMLGRRqktesKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSC- 125
Cdd:COG1022 15 DLLRRRAARFPDRVALREK-----EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 126 AVSyVPLYDTLGPNAVEFIINHAEVSIAFVQ-EKKIPSVLSCLAQCSSnLKTIVSFgsvsttqKKEAEGHGASCFSWGEF 204
Cdd:COG1022 90 AVT-VPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELPS-LRHIVVL-------DPRGLRDDPRLLSLDEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 205 LQLGcLDWDLP--------SKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLA 276
Cdd:COG1022 161 LALG-REVADPaelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLG-----PGDRTLSFLPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 277 HVYDQIMETYCISKGSSIGFWQgDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYL 356
Cdd:COG1022 235 HVFERTVSYYALAAGATVAFAE-SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 357 EKGL----------PQHKaapLFDRLVFDKTKLALGGRVRILLSGAAPLPRHVEEFMRvTSGSTLSQGYGLTESCAG-CF 425
Cdd:COG1022 314 RARLagkspslllrLKHA---LADKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLTETSPViTV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 426 TAIGDVysMTGTVGVPMTTIEARLEsvpemgydalsnvPRGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQ 504
Cdd:COG1022 390 NRPGDN--RIGTVGPPLPGVEVKIA-------------EDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 505 SNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGNSfESFLVAVVVPERKAIEDWAKEHNLT-DDFKSL 583
Cdd:COG1022 455 EDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAEL 533
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356575070 584 CDNLKARKHI---LDELNStgqkhQLRGFELLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDHIDQLYKEA 655
Cdd:COG1022 534 AQDPEVRALIqeeVDRANA-----GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
73-637 |
4.58e-172 |
|
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: 500.59 E-value: 4.58e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSI 152
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 AFvqekkipsvlsclaqCSSnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskKKTDICTIMYTSGTT 232
Cdd:cd17639 81 IF---------------TDG---------------------------------------------KPDDLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 233 GDPKGVVIKNEAFMAEVLSVDHIImltDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFwqGDVRFLLE------ 306
Cdd:cd17639 101 GNPKGVMLTHGNLVAGIAGLGDRV---PELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgc 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 --DIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGlpqhKAAPLFDRLVFDKTKLALGGR 384
Cdd:cd17639 176 kgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEG----PGTPLLDELVFKKVRAALGGR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 VRILLSGAAPLPRHVEEFMRVTsGSTLSQGYGLTESCA-GCFTAIGDVYsmTGTVGVPMTTIEARLESVPEMGYDALSNV 463
Cdd:cd17639 252 LRYMLSGGAPLSADTQEFLNIV-LCPVIQGYGLTETCAgGTVQDPGDLE--TGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 464 PRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLI 542
Cdd:cd17639 329 PRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 543 ASIWVYGNSFESFLVAVVVPERKAIEDWAKEHNL-TDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNP 621
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 356575070 622 FDIERDLITPTFKLKR 637
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
73-640 |
2.44e-135 |
|
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: 404.28 E-value: 2.44e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSC-AVSyVPLYDTLGPNAVEFIINHAEVS 151
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIgAVP-VPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 152 IAFVQekkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskKKTDICTIMYTSGT 231
Cdd:cd05907 80 ALFVE-------------------------------------------------------------DPDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 232 TGDPKGVVIKNEAFMAEVLSVDHIIMltdrvAGEDDVYFSFLPLAHVYDQIM-ETYCISKGSSIGFWQgDVRFLLEDIQE 310
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLP-----ATEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFAS-SAETLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 311 LKPTIFCGVPRVFDRIYAGIKskvssagplqstlfqcaynyklkylekglpqHKAAPLFDRLVFDktkLALGGRVRILLS 390
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAIK-------------------------------VKAVPGLKRKLFD---LAVGGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 391 GAAPLPRHVEEFMRvTSGSTLSQGYGLTESCAGCFTAIGDVYSMtGTVGVPMTTIEARLesvpemgydalsnVPRGEICL 470
Cdd:cd05907 219 GGAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRI-GTVGKPLPGVEVRI-------------ADDGEILV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 471 RGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:cd05907 284 RGPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIG 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 550 NSfESFLVAVVVPERKAIEDWAKEHNLTD-DFKSLCDNLKARKHILDELNSTGQkhQLRGFELLKAIHLEPNPFDIERDL 628
Cdd:cd05907 364 DG-RPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGE 440
|
570
....*....|..
gi 356575070 629 ITPTFKLKRPQL 640
Cdd:cd05907 441 LTPTLKLKRPVI 452
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
39-652 |
4.31e-123 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 381.00 E-value: 4.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 39 PSDFKSPWD-------FFRDSVKRNPNNNMLGRRQ----KTESK----------LGSYTWLTYQDVYDAAMKMGSAIRSR 97
Cdd:PLN02387 47 PELVETPWEgattlaaLFEQSCKKYSDKRLLGTRKlisrEFETSsdgrkfeklhLGEYEWITYGQVFERVCNFASGLVAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 98 GVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEKKipsvLSCLAQCSSNLKTI 177
Cdd:PLN02387 127 GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQ----LKKLIDISSQLETV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 178 VSF------GSVSTTQKKEAEGHGASCFSWGEFL-QLGCLDWDLPSKkkTDICTIMYTSGTTGDPKGVVIKNEAFMAEVL 250
Cdd:PLN02387 203 KRViymddeGVDSDSSLSGSSNWTVSSFSEVEKLgKENPVDPDLPSP--NDIAVIMYTSGSTGLPKGVMMTHGNIVATVA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 251 SVDHIImltdRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFwqGDVRFLLE-----------DIQELKPTIFCGV 319
Cdd:PLN02387 281 GVMTVV----PKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 320 PRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEK------GLpqhkAAPLFDRLVFDKTKLALGGRVRILLSGAA 393
Cdd:PLN02387 355 PAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGswfgawGL----EKLLWDALVFKKIRAVLGGRIRFMLSGGA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 394 PLPRHVEEFMRVTSGSTLSQGYGLTESCAG-CFTAIGDvySMTGTVGVPMTTIEARLESVPEMGYDAL-SNVPRGEICLR 471
Cdd:PLN02387 431 PLSGDTQRFINICLGAPIGQGYGLTETCAGaTFSEWDD--TSVGRVGPPLPCCYVKLVSWEEGGYLISdKPMPRGEIVIG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 472 GNTLFSGYHKREDLTKEVM-VDG----WFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIW 546
Cdd:PLN02387 509 GPSVTLGYFKNQEKTDEVYkVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 547 VYGNSFESFLVAVVVPERKAIEDWAKEHNLT-DDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIE 625
Cdd:PLN02387 589 VHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPE 668
|
650 660
....*....|....*....|....*..
gi 356575070 626 RDLITPTFKLKRPQLLKYYKDHIDQLY 652
Cdd:PLN02387 669 SGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
76-654 |
1.64e-108 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 343.11 E-value: 1.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 76 TWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFV 155
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 156 QEKKIPSVLSCLAQCSSNLKTIVSFGSVSTTqkkeAEGHGASCFSWGEFLQLG-----CLDWDLPSKKKtDICTIMYTSG 230
Cdd:PTZ00216 200 NGKNVPNLLRLMKSGGMPNTTIIYLDSLPAS----VDTEGCRLVAWTDVVAKGhsagsHHPLNIPENND-DLALIMYTSG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 231 TTGDPKGVVIKNEAFMAEVLSVDHiiMLTDRVAG--EDDVYFSFLPLAHVYDQIMETYCISKGSSIGFwqGDVRFLLE-- 306
Cdd:PTZ00216 275 TTGDPKGVMHTHGSLTAGILALED--RLNDLIGPpeEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtf 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 -----DIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGlpqhKAAPLFDRLVFDKTKLAL 381
Cdd:PTZ00216 351 arphgDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEG----KDTPYWNEKVFSAPRAVL 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 382 GGRVRILLSGAAPLPRHVEEFMRVTSGsTLSQGYGLTES-CAGCFTAIGDVYsmTGTVGVPMTTIEARLESVPEMGY-DA 459
Cdd:PTZ00216 427 GGRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTETvCCGGIQRTGDLE--PNAVGQLLKGVEMKLLDTEEYKHtDT 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 LSnvPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQ 538
Cdd:PTZ00216 504 PE--PRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQ 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 539 CPLIA--SIWVYGNSFESFLVAVVVPERKAIEDWAKEHNLTDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELLKAIH 616
Cdd:PTZ00216 582 NELVVpnGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVR 661
|
570 580 590
....*....|....*....|....*....|....*...
gi 356575070 617 LEPNPFDIERDLITPTFKLKRPQLLKYYKDHIDQLYKE 654
Cdd:PTZ00216 662 VLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
49-522 |
3.47e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 333.13 E-value: 3.47e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 49 FRDSVKRNPNnnmlgrrqKTESKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVS 128
Cdd:pfam00501 1 LERQAARTPD--------KTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 129 YVPLYDTLGPNAVEFIINHAEVSIAFVQE-KKIPSVLSCLAQCSSNLKTIVSfgsvsttqkkEAEGHGASCFSWGEFLQL 207
Cdd:pfam00501 73 YVPLNPRLPAEELAYILEDSGAKVLITDDaLKLEELLEALGKLEVVKLVLVL----------DRDPVLKEEPLPEEAKPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 208 GCLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIImLTDRVAGEDDVYFSFLPLAHVYDQIMETYC 287
Cdd:pfam00501 143 DVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVR-PRGFGLGPDDRVLSTLPLFHDFGLSLGLLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 288 -ISKGSSIGFWQGDVRF----LLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynyklkyLEKGLPq 362
Cdd:pfam00501 222 pLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNML-----------------------------LEAGAP- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 363 hkaaplfdrlvfdktKLALGGRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAI--GDVYSMTGTVGV 440
Cdd:pfam00501 272 ---------------KRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLplDEDLRSLGSVGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 441 PMTTIEARLESVPEMGYDALSNVprGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIF 519
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPVPPGEP--GELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
...
gi 356575070 520 KLS 522
Cdd:pfam00501 415 KLG 417
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
73-644 |
6.46e-74 |
|
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: 246.61 E-value: 6.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSI 152
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 AFV--------QEKKIP-SVLSCLAQCSSNLKtivsfgsvsttqkkeaeghgasCF-SWGEFLQLGCLDWDLPSKKKTDI 222
Cdd:cd05932 82 LFVgklddwkaMAPGVPeGLISISLPPPSAAN----------------------CQyQWDDLIAQHPPLEERPTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 223 CTIMYTSGTTGDPKGVViknEAFMAEVLSVDHIIMLTDrvAGEDDVYFSFLPLAHVYDQI-METYCISKGSSIGFWQGDV 301
Cdd:cd05932 140 ATLIYTSGTTGQPKGVM---LTFGSFAWAAQAGIEHIG--TEENDRMLSYLPLAHVTERVfVEGGSLYGGVLVAFAESLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 302 RFLlEDIQELKPTIFCGVPRVFDRIYAGIKSKVssagPLQstlfqcaynyKLKYLEKglpqhkaAPLFDRLVFDKTKLAL 381
Cdd:cd05932 215 TFV-EDVQRARPTLFFSVPRLWTKFQQGVQDKI----PQQ----------KLNLLLK-------IPVVNSLVKRKVLKGL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 382 G-GRVRILLSGAAPLPRHVEEFMRvTSGSTLSQGYGLTESCAgcftaigdvYSM--------TGTVGVPMTTIEARLEsv 452
Cdd:cd05932 273 GlDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFA---------YSHlnypgrdkIGTVGNAGPGVEVRIS-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 453 pemgydalsnvPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVEN 531
Cdd:cd05932 341 -----------EDGEILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAP 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 532 IENKYLQCPLIASIWVYGNSFESFLVAVVVPERkaiedwAKEHNLTDDFKSLCDNLKArkhILDELNSTGQKHqlrgfEL 611
Cdd:cd05932 410 IENKLAEHDRVEMVCVIGSGLPAPLALVVLSEE------ARLRADAFARAELEASLRA---HLARVNSTLDSH-----EQ 475
|
570 580 590
....*....|....*....|....*....|...
gi 356575070 612 LKAIHLEPNPFDIERDLITPTFKLKRPQLLKYY 644
Cdd:cd05932 476 LAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
73-638 |
2.90e-72 |
|
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: 241.11 E-value: 2.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSI 152
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 AFVQEkkipsvlsclaqcSSNlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTT 232
Cdd:cd17640 81 LVVEN-------------DSD-----------------------------------------------DLATIIYTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 233 GDPKGVVIKNEAFMAEVlsvDHIIMLTDRVAGedDVYFSFLPLAHVYDQIMETYCISKGSSIGFwqGDVRFLLEDIQELK 312
Cdd:cd17640 101 GNPKGVMLTHANLLHQI---RSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 313 PTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCaynyklkylekglpqhkaaplfdrlvfdktkLALGGRVRILLSGA 392
Cdd:cd17640 174 PHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF-------------------------------FLSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 393 APLPRHVEEFMRVTsGSTLSQGYGLTE----SCAGCFTAIgdvysMTGTVGVPMTTIEARLesvpemgYDALSNVP---- 464
Cdd:cd17640 223 GALPPHVDTFFEAI-GIEVLNGYGLTEtspvVSARRLKCN-----VRGSVGRPLPGTEIKI-------VDPEGNVVlppg 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 465 -RGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLI 542
Cdd:cd17640 290 eKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 543 ASIWVYGNSfESFLVAVVVPERKAIEDWAKEHN--LTDDFKSLCDNLKARK----HILDELNStgqKHQLRGFELLKAIH 616
Cdd:cd17640 370 EQIMVVGQD-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKlyknEIKDEISN---RPGFKSFEQIAPFA 445
|
570 580
....*....|....*....|..
gi 356575070 617 LEPNPFdIERDLITPTFKLKRP 638
Cdd:cd17640 446 LLEEPF-IENGEMTQTMKIKRN 466
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
46-619 |
1.04e-69 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 233.93 E-value: 1.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 46 WDFFRDSVKRNPNNNML---GRRqktesklgsytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
Cdd:COG0318 2 ADLLRRAAARHPDRPALvfgGRR------------LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 123 NSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVqekkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswg 202
Cdd:COG0318 70 LRAGAVVVPLNPRLTAEELAYILEDSGARALVT----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 203 eflqlgcldwdlpskkktdiCTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDQI 282
Cdd:COG0318 103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT-----PGDVVLVALPLFHVFGLT 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 283 METY-CISKGSSI----GFwqgDVRFLLEDIQELKPTIFCGVPRVFDRiyagikskvssagplqstlfqcaynyklkyle 357
Cdd:COG0318 158 VGLLaPLLAGATLvllpRF---DPERVLELIERERVTVLFGVPTMLAR-------------------------------- 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 358 kglpqhkaapLFDRLVFDKTKLAlggRVRILLSGAAPLPRHV-EEFMRVTsGSTLSQGYGLTESCAGCFTAIGDV-YSMT 435
Cdd:COG0318 203 ----------LLRHPEFARYDLS---SLRLVVSGGAPLPPELlERFEERF-GVRIVEGYGLTETSPVVTVNPEDPgERRP 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 436 GTVGVPMTTIEARLesVPEMGYDalsnVPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKII 512
Cdd:COG0318 269 GSVGRPLPGVEVRI--VDEDGRE----LPPgevGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIV 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 513 DRKKNIFKLSqGEYIAVENIENKYLQCPLIASIWVYGNSFESF---LVAVVVP------ERKAIEDWAKEHnltddfksl 583
Cdd:COG0318 343 GRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWgerVVAFVVLrpgaelDAEELRAFLRER--------- 412
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 356575070 584 cdnLKARK-----HILDEL--NSTG--QKHQLRgfELLKAIHLEP 619
Cdd:COG0318 413 ---LARYKvprrvEFVDELprTASGkiDRRALR--ERYAAGALEA 452
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
73-652 |
1.19e-68 |
|
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: 234.94 E-value: 1.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIA-MEACNSCAVSyVPLYDTLGPNAVEFIINHAEVS 151
Cdd:cd05933 4 DKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAaVGAIFAGGIA-VGIYTTNSPEACQYVAETSEAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 152 IAFV----QEKKIPSVLSCLAQcssnLKTIVSFgsvsttqKKEAEGHGASCFSWGEFLQLGC------LDWDLPSKKKTD 221
Cdd:cd05933 83 ILVVenqkQLQKILQIQDKLPH----LKAIIQY-------KEPLKEKEPNLYSWDEFMELGRsipdeqLDAIISSQKPNQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 222 ICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRVAGEDDVyFSFLPLAHVYDQIMETY-CISKGSSIGFWQGD 300
Cdd:cd05933 152 CCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESV-VSYLPLSHIAAQILDIWlPIKVGGQVYFAQPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 VR--FLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAYN----YKLKYLEKGLPQHKAAPLFDRLVF 374
Cdd:cd05933 231 ALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGvgleTNLKLMGGESPSPLFYRLAKKLVF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 375 DKTKLALG-GRVRILLSGAAPLPRHVEEFMrvtsgstLS------QGYGLTEsCAGCFTAIGDVYSMTGTVGVPMTTIEA 447
Cdd:cd05933 311 KKVRKALGlDRCQKFFTGAAPISRETLEFF-------LSlnipimELYGMSE-TSGPHTISNPQAYRLLSCGKALPGCKT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 448 RLESVPEMGYdalsnvprGEICLRGNTLFSGYHKREDLTKE-VMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEY 526
Cdd:cd05933 383 KIHNPDADGI--------GEICFWGRHVFMGYLNMEDKTEEaIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 527 IAVENIENKY-LQCPLIASIWVYGNS--FESFLVAV---VVPERKAIEDwakehNLTDDFKSLCDNLKARKHILDEL--- 597
Cdd:cd05933 455 VPPVPIEDAVkKELPIISNAMLIGDKrkFLSMLLTLkceVNPETGEPLD-----ELTEEAIEFCRKLGSQATRVSEIagg 529
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356575070 598 -------------NSTGQKHQLRGFELLKAIHLePNPFDIERDLITPTFKLKRPQLLKYYKDHIDQLY 652
Cdd:cd05933 530 kdpkvyeaieegiKRVNKKAISNAQKIQKWVIL-EKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
69-637 |
1.06e-59 |
|
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: 209.97 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 69 ESKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHA 148
Cdd:cd17641 3 EKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 149 EVSIAFVQ-EKKIPSVLSCLAQCSSNLKTIV---------------SFGSVsttqkkEAEGHGASCFSWGEFLQLgcldw 212
Cdd:cd17641 83 GARVVIAEdEEQVDKLLEIADRIPSVRYVIYcdprgmrkyddprliSFEDV------VALGRALDRRDPGLYERE----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 213 dLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFM---AEVLSVDHIimltdrvaGEDDVYFSFLPLAHVYDQIMET-YCI 288
Cdd:cd17641 152 -VAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLghcAAYLAADPL--------GPGDEYVSVLPLPWIGEQMYSVgQAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 289 SKGSSIGFWQgDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQC-------AYNYKLKYLEKGLP 361
Cdd:cd17641 223 VCGFIVNFPE-EPETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELgmklglrALDRGKRGRPVSLW 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 362 QHKAAPLFDRLVFDKTKLALG-GRVRILLSGAAPLPRHVEEFMRVTsGSTLSQGYGLTESCAGCFT-AIGDVYSmtGTVG 439
Cdd:cd17641 302 LRLASWLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVhRDGDVDP--DTVG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 440 VPMTTIEARLESVpemgydalsnvprGEICLRGNTLFSGYHKREDLTKE-VMVDGWFHTGDIGEWQSNGAMKIIDRKKNI 518
Cdd:cd17641 379 VPFPGTEVRIDEV-------------GEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 519 FKLSQGEYIAVENIENKYLQCPLIASIWVYGNSFEsFLVAVVVPERKAIEDWAKEHNLT-DDFKSLCDNLKA----RKHI 593
Cdd:cd17641 446 GTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRP-YLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVyeliRKEV 524
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 356575070 594 LDELNSTGQKHQLRGFELLkaiHLEPNPFDIErdlITPTFKLKR 637
Cdd:cd17641 525 EKVNASLPEAQRIRRFLLL---YKELDADDGE---LTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
78-637 |
2.89e-57 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 200.75 E-value: 2.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd05914 88 ED-------------------------------------------------------------DVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLtdrvaGEDDVYFSFLPLAHVY----DQIMETYcisKGSSIGFWQGDVRFLLEDIQELKP 313
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEVVLL-----GKGDKILSILPLHHIYpltfTLLLPLL---NGAHVVFLDKIPSAKIIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 314 TIFCGVPR---VFDRIYAGIKSKVSSAGPLQstlfqcaynyKLkylekglpqhkAAPLFDR----LVFDKTKLALGGRVR 386
Cdd:cd05914 179 TPTLGVPVplvIEKIFKMDIIPKLTLKKFKF----------KL-----------AKKINNRkirkLAFKKVHEAFGGNIK 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 387 ILLSGAAPLPRHVEEFMRvTSGSTLSQGYGLTEsCAG--CFTAIGDVYSmtGTVGVPMTTIEARLESVPEMGYDalsnvp 464
Cdd:cd05914 238 EFVIGGAKINPDVEEFLR-TIGFPYTIGYGMTE-TAPiiSYSPPNRIRL--GSAGKVIDGVEVRIDSPDPATGE------ 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 465 rGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIA 543
Cdd:cd05914 308 -GEIIVRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVL 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 544 SIWVYGNSFESFLVAVVVPERkaieDWAKEHNLTDDFKSLCDNLkarkhiLDELNStgqkhQLRGFELLKAIHLEPNPFD 623
Cdd:cd05914 387 ESLVVVQEKKLVALAYIDPDF----LDVKALKQRNIIDAIKWEV------RDKVNQ-----KVPNYKKISKVKIVKEEFE 451
|
570
....*....|....
gi 356575070 624 ierdlITPTFKLKR 637
Cdd:cd05914 452 -----KTPKGKIKR 460
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
78-601 |
4.81e-57 |
|
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: 200.52 E-value: 4.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSNLKtIVSFGSvsttqkkEAEGHGASCFSWGEFLqlGCLDWDLPSKK---KTDICTIMYTSGTTGD 234
Cdd:cd05911 91 DGLEKVKEAAKELGPKDK-IIVLDD-------KPDGVLSIEDLLSPTL--GEEDEDLPPPLkdgKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNEAFMAEVLSVdhiIMLTDRVAGEDDVYFSFLPLAHVYdqimetyciskgssiGFWqgdvrFLLEdiqelkpT 314
Cdd:cd05911 161 PKGVCLSHRNLIANLSQV---QTFLYGNDGSNDVILGFLPLYHIY---------------GLF-----TTLA-------S 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 315 IFCGVPRVfdriyagIKSKVSSAgplqsTLFQCAYNYKLKYLekGLPQHKAAPLFDRLVFDKTKLAlggRVRILLSGAAP 394
Cdd:cd05911 211 LLNGATVI-------IMPKFDSE-----LFLDLIEKYKITFL--YLVPPIAAALAKSPLLDKYDLS---SLRVILSGGAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 395 LPRHVEEFM-RVTSGSTLSQGYGLTESCAGCFTAIGDVYSmTGTVGVPMTTIEARLesVPEMGYDALSNVPRGEICLRGN 473
Cdd:cd05911 274 LSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDK-PGSVGRLLPNVEAKI--VDDDGKDSLGPNEPGEICVRGP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 474 TLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIASIWVYG--- 549
Cdd:cd05911 351 QVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIGipd 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356575070 550 -NSFESfLVAVVVPER------KAIEDWAKEHNltDDFKslcdNLKARKHILDEL--NSTG 601
Cdd:cd05911 430 eVSGEL-PRAYVVRKPgeklteKEVKDYVAKKV--ASYK----QLRGGVVFVDEIpkSASG 483
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
79-607 |
5.46e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 195.79 E-value: 5.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEK 158
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 159 KIPSVLSCLAQCSSnLKTIVsfgsvsTTQKKEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKGV 238
Cdd:PRK06187 113 FVPLLAAILPQLPT-VRTVI------VEGDGPAAPLAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 239 VIKNEAFMAEVLSVDHIIMLTDrvageDDVYFSFLPLAHVYD---QIMETYCISKGSSIG-FwqgDVRFLLEDIQELKPT 314
Cdd:PRK06187 186 VLSHRNLFLHSLAVCAWLKLSR-----DDVYLVIVPMFHVHAwglPYLALMAGAKQVIPRrF---DPENLLDLIETERVT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 315 IFCGVPrvfdriyagikskvssagplqsTLFQcaynyklkylekGLPQHKAAPLFDrlvFdktklalgGRVRILLSGAAP 394
Cdd:PRK06187 258 FFFAVP----------------------TIWQ------------MLLKAPRAYFVD---F--------SSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 395 LPRH-VEEFMRVTsGSTLSQGYGLTESCaGCFTA------IGDVYSMTGTVGVPMTTIEARL-----ESVPEMGYDAlsn 462
Cdd:PRK06187 293 LPPAlLREFKEKF-GIDLVQGYGMTETS-PVVSVlppedqLPGQWTKRRSAGRPLPGVEARIvdddgDELPPDGGEV--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 463 vprGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYI-AVEnIENKYLQCPL 541
Cdd:PRK06187 368 ---GEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIyPRE-LEDALYGHPA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356575070 542 IASIWVYGNSFESF---LVAVVVPE------RKAIEDWAKEHnLTdDFKslcdnLKARKHILDEL--NSTG--QKHQLR 607
Cdd:PRK06187 443 VAEVAVIGVPDEKWgerPVAVVVLKpgatldAKELRAFLRGR-LA-KFK-----LPKRIAFVDELprTSVGkiLKRVLR 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
46-607 |
1.46e-53 |
|
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: 190.85 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 46 WDFFRDSVKRNPNNNML---GRrqktesklgsytWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
Cdd:cd05936 2 ADLLEEAARRFPDKTALifmGR------------KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 123 NSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVqekkipsvlsclaqcssnlktIVSFgsvsttqkkeaeghgASCFSWG 202
Cdd:cd05936 70 LKAGAVVVPLNPLYTPRELEHILNDSGAKALIV---------------------AVSF---------------TDLLAAG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 203 EFLQLGcldwdlPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRvagEDDVYFSFLPLAHVYDQ- 281
Cdd:cd05936 114 APLGER------VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLE---GDDVVLAALPLFHVFGLt 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 282 IMETYCISKGSSIGFWQgdvRF----LLEDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLfqcaYNYKLkyle 357
Cdd:cd05936 185 VALLLPLALGATIVLIP---RFrpigVLKEIRKHRVTIFPGVP----------------------TM----YIALL---- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 358 kglpqhkAAPLFDRLVFdktklalgGRVRILLSGAAPLPRHV-EEFMRVTsGSTLSQGYGLTESC-AGCFTAIGDVySMT 435
Cdd:cd05936 232 -------NAPEFKKRDF--------SSLRLCISGGAPLPVEVaERFEELT-GVPIVEGYGLTETSpVVAVNPLDGP-RKP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 436 GTVGVPMTTIEARLesvpemgYDALSN-VPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKI 511
Cdd:cd05936 295 GSIGIPLPGTEVKI-------VDDDGEeLPPgevGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFI 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 512 IDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVYG----NSFESfLVAVVVP------ERKAIEDWAKEHnLTddfk 581
Cdd:cd05936 368 VDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVVGvpdpYSGEA-VKAFVVLkegaslTEEEIIAFCREQ-LA---- 440
|
570 580 590
....*....|....*....|....*....|..
gi 356575070 582 slcdNLKARKHI--LDEL--NSTGQ--KHQLR 607
Cdd:cd05936 441 ----GYKVPRQVefRDELpkSAVGKilRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
221-574 |
1.88e-53 |
|
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: 186.72 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDQIMETYCISKGSSI----GF 296
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-----EGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 297 WQGDVrflLEDIQELKPTIFCGVPRVFDRiyagikskvssagplqstlfqcaynyklkylekglpqhkaapLFDRLVFDK 376
Cdd:cd04433 76 DPEAA---LELIEREKVTILLGVPTLLAR------------------------------------------LLKAPESAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 377 TKLAlggRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESC-AGCFTAIGDVYSMTGTVGVPMTTIEARLesVPEM 455
Cdd:cd04433 111 YDLS---SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgTVATGPPDDDARKPGSVGRPVPGVEVRI--VDPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 456 GYDALSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENK 535
Cdd:cd04433 186 GGELPPGEI-GELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAV 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 356575070 536 YLQCPLIASIWVYG---NSFESFLVAVVVPERKA--IEDWAKEH 574
Cdd:cd04433 264 LLGHPGVAEAAVVGvpdPEWGERVVAVVVLRPGAdlDAEELRAH 307
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
188-653 |
3.29e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 192.24 E-value: 3.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 188 KKEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSV-DHIIMLTDRVaged 266
Cdd:PTZ00342 272 KEKAKKLGISIILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLcKHSIFKKYNP---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 267 DVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQ 346
Cdd:PTZ00342 348 KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 347 CAYNYK--------LKYLEKglpqhkaapLFDrlVFDKTKLALGGRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLT 418
Cdd:PTZ00342 428 KILSLRksnnnggfSKFLEG---------ITH--ISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 419 ESCAGCFTAIGDVYSmTGTVGVPMT-TIEARLESVPEmgYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFH 496
Cdd:PTZ00342 497 ETTGPIFVQHADDNN-TESIGGPISpNTKYKVRTWET--YKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFK 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 497 TGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGNSFESFLVAVVVPERKAIEDWAKEHNL 576
Cdd:PTZ00342 574 TGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNM 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 577 -------TDDF-KSLCDNLKARKHILD----ELNSTGQKHQLRGFELLKAIHLEPNPFDIErDLITPTFKLKRPQLLKYY 644
Cdd:PTZ00342 654 lestginEKNYlEKLTDETINNNIYVDyvkgKMLEVYKKTNLNRYNIINDIYLTSKVWDTN-NYLTPTFKVKRFYVFKDY 732
|
....*....
gi 356575070 645 KDHIDQLYK 653
Cdd:PTZ00342 733 AFFIDQVKK 741
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
224-630 |
2.90e-50 |
|
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: 184.20 E-value: 2.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 224 TIMYTSGTTGDPKGvvikneAFMAEVLSVDhiiMLTDRVAGEDD-----VYFSFLPLAHVYDQIMETYCISKGSSIGFW- 297
Cdd:cd17632 227 LLIYTSGSTGTPKG------AMYTERLVAT---FWLKVSSIQDIrppasITLNFMPMSHIAGRISLYGTLARGGTAYFAa 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 298 QGDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKV---SSAGPLQSTLFQCAynyklkylekglpqhkAAPLFDRLvf 374
Cdd:cd17632 298 ASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELdrrSVAGADAETLAERV----------------KAELRERV-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 375 dktklaLGGRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTEscAGcftaigdVYSMTGTVGVPmTTIEARLESVPE 454
Cdd:cd17632 360 ------LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AG-------AVILDGVIVRP-PVLDYKLVDVPE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 455 MGYDAL-SNVPRGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSQGEYIAVENI 532
Cdd:cd17632 424 LGYFRTdRPHPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 533 ENKYLQCPLIASIWVYGNSFESFLVAVVVPerkaiedwakehnlTDDFKSLCDNLKARKHILDELNSTGQKHQLRGFELL 612
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNSERAYLLAVVVP--------------TQDALAGEDTARLRAALAESLQRIAREAGLQSYEIP 569
|
410
....*....|....*...
gi 356575070 613 KAIHLEPNPFDIERDLIT 630
Cdd:cd17632 570 RDFLIETEPFTIANGLLS 587
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
78-601 |
7.09e-49 |
|
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: 177.03 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEvsiafvqe 157
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkiPSVLsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcLDwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd17631 93 ---AKVL---------------------------------------------FD---------DLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVdhiimLTDRVAGEDDVYFSFLPLAHVydQIMETYCISkgssiGFWQG---------DVRFLLEDI 308
Cdd:cd17631 116 AMLTHRNLLWNAVNA-----LAALDLGPDDVLLVVAPLFHI--GGLGVFTLP-----TLLRGgtvvilrkfDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 309 QELKPTIFCGVPrvfdriyagikskvssagplqsTLFQcaynyklkylekGLPQHKAaplfdrlvFDKTKLAlggRVRIL 388
Cdd:cd17631 184 ERHRVTSFFLVP----------------------TMIQ------------ALLQHPR--------FATTDLS---SLRAV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 389 LSGAAPLPRHVEEFMRVTsGSTLSQGYGLTESCAG-CFTAIGDVYSMTGTVGVPMTTIEARLesVPEMGYDALSNVPrGE 467
Cdd:cd17631 219 IYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGvTFLSPEDHRRKLGSAGRPVFFVEVRI--VDPDGREVPPGEV-GE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 468 ICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQCPLIASIWV 547
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAV 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 548 YGNSFESF---LVAVVVPERKAiedwakehNLTDD--FKSLCDNL---KARKHIL--DEL--NSTG 601
Cdd:cd17631 374 IGVPDEKWgeaVVAVVVPRPGA--------ELDEDelIAHCRERLaryKIPKSVEfvDALprNATG 431
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
78-608 |
2.87e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 171.63 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLScLAQCSSNLKTIVSFgsvsttQKKEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKG 237
Cdd:PRK07656 111 LFLGVDYS-ATTRLPALEHVVIC------ETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVI------KNEAFMAEVLSVDhiimltdrvagEDDVYFSFLPLAHV--YDQIMETyCISKGSSI----GFwqgDVRFLL 305
Cdd:PRK07656 184 AMLthrqllSNAADWAEYLGLT-----------EGDRYLAANPFFHVfgYKAGVNA-PLMRGATIlplpVF---DPDEVF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 306 EDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLfqcaYNYKLkylekglpQHKAAplfdrlvfDKTKLAlggRV 385
Cdd:PRK07656 249 RLIETERITVLPGPP----------------------TM----YNSLL--------QHPDR--------SAEDLS---SL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 386 RILLSGAAPLPRHVEEFMRVTSG-STLSQGYGLTESC-AGCFTAIGD-VYSMTGTVGVPMTTIEARLesVPEMGYDALSN 462
Cdd:PRK07656 284 RLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASgVTTFNRLDDdRKTVAGTIGTAIAGVENKI--VNELGEEVPVG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 463 VPrGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQG--EYIAveNIENKYLQC 539
Cdd:PRK07656 362 EV-GELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGfnVYPA--EVEEVLYEH 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 540 PLIASIWVYGNSFESF---LVAVVVPERKA------IEDWAKEHnltddfkslCDNLKARKHI--LDEL--NSTGQ--KH 604
Cdd:PRK07656 438 PAVAEAAVIGVPDERLgevGKAYVVLKPGAelteeeLIAYCREH---------LAKYKVPRSIefLDELpkNATGKvlKR 508
|
....
gi 356575070 605 QLRG 608
Cdd:PRK07656 509 ALRE 512
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
47-574 |
5.71e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 157.47 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNML---GRRQktesklgsytwlTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC- 122
Cdd:PRK05605 36 DLYDNAVARFGDRPALdffGATT------------TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 123 --NSCAVSYVPLYDT---LGPnaveFIINHAEVSIAFvqeKKIPSVLSCLAQCSSnLKTIVSFG---------------S 182
Cdd:PRK05605 104 rlGAVVVEHNPLYTAhelEHP----FEDHGARVAIVW---DKVAPTVERLRRTTP-LETIVSVNmiaampllqrlalrlP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 183 VSTTQKKEAEGHGAS--CFSWGEFLQ---LGCLDW-DLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHII 256
Cdd:PRK05605 176 IPALRKARAALTGPApgTVPWETLVDaaiGGDGSDvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 257 mltDRVAGEDDVYFSFLPLAHVYDQimeTYCISKGSSIG-----FWQGDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIK 331
Cdd:PRK05605 256 ---PGLGDGPERVLAALPMFHAYGL---TLCLTLAVSIGgelvlLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 332 skvssagplqstlfqcaynyklkylEKGLPqhkaaplfdrlvfdktklaLGGrVRILLSGAAPLPRH-VEEFMRVTSGSt 410
Cdd:PRK05605 330 -------------------------ERGVD-------------------LSG-VRNAFSGAMALPVStVELWEKLTGGL- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 411 LSQGYGLTESCAgcfTAIGDVYSMT---GTVGVPMTTIEARLESvPEmgyDALSNVP---RGEICLRGNTLFSGYHKRED 484
Cdd:PRK05605 364 LVEGYGLTETSP---IIVGNPMSDDrrpGYVGVPFPDTEVRIVD-PE---DPDETMPdgeEGELLVRGPQVFKGYWNRPE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 485 LTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNI-----FKLSQGEyiavenIENKYLQCPLIASIWVYG----NSFESf 555
Cdd:PRK05605 437 ETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELiitggFNVYPAE------VEEVLREHPGVEDAAVVGlpreDGSEE- 509
|
570 580
....*....|....*....|....*
gi 356575070 556 LVAVVVPE------RKAIEDWAKEH 574
Cdd:PRK05605 510 VVAAVVLEpgaaldPEGLRAYCREH 534
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
79-549 |
6.20e-40 |
|
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: 151.68 E-value: 6.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFvqek 158
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 159 kipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkkTDICTIMYTSGTTGDPKGV 238
Cdd:cd05934 81 -------------------------------------------------------------VDPASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 239 VIKN-EAFMAEVLSVDHiimltdRVAGEDDVYFSFLPLAHVYDQIMETY-CISKGSSI---------GFWQgdvrflleD 307
Cdd:cd05934 100 VITHaNLTFAGYYSARR------FGLGEDDVYLTVLPLFHINAQAVSVLaALSVGATLvllprfsasRFWS--------D 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 308 IQELKPTIFCGVPRVFDRIYAGIKSkvssagplqstlfqcaynyklkylekglPQHKAAPLfdRLVFdktklalggrvri 387
Cdd:cd05934 166 VRRYGATVTNYLGAMLSYLLAQPPS----------------------------PDDRAHRL--RAAY------------- 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 388 llsGAAPLPRHVEEFMRvTSGSTLSQGYGLTESCAgCFTAIGDVYSMTGTVGVPMTTIEARLesVPEMGYDALSNVPrGE 467
Cdd:cd05934 203 ---GAPNPPELHEEFEE-RFGVRLLEGYGMTETIV-GVIGPRDEPRRPGSIGRPAPGYEVRI--VDDDGQELPAGEP-GE 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 468 ICLR---GNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQCPLIAS 544
Cdd:cd05934 275 LVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVRE 353
|
....*
gi 356575070 545 IWVYG 549
Cdd:cd05934 354 AAVVA 358
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
73-543 |
1.45e-36 |
|
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: 143.93 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC-NSCAVSYvPLYDTLGPNAVEFIINHAEVS 151
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVpGMGAVLH-TINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 152 IAFVQekkiPSVLSCLAQCSSNLKTIVSFgSVSTTQKKEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGT 231
Cdd:cd12119 100 VVFVD----RDFLPLLEAIAPRLPTVEHV-VVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 232 TGDPKGVVIKNEAFMAEVLSvdhiIMLTDRVA-GEDDVYFSFLPLAHVYdqimetyciSKGSS-IGFWQG---------- 299
Cdd:cd12119 175 TGNPKGVVYSHRSLVLHAMA----ALLTDGLGlSESDVVLPVVPMFHVN---------AWGLPyAAAMVGaklvlpgpyl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 300 DVRFLLEDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLFQcaynyklkylekGLPQHkaaplfdrlvFDKTKL 379
Cdd:cd12119 242 DPASLAELIEREGVTFAAGVP----------------------TVWQ------------GLLDH----------LEANGR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 380 ALGGRVRILLSGAAPLPRHVEEFMRvtSGSTLSQGYGLTESCA-GCFTAIGDV---------YSMTGTVGVPMTTIEARL 449
Cdd:cd12119 278 DLSSLRRVVIGGSAVPRSLIEAFEE--RGVRVIHAWGMTETSPlGTVARPPSEhsnlsedeqLALRAKQGRPVPGVELRI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 450 ESvPEMGYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAV 529
Cdd:cd12119 356 VD-DDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWISS 433
|
490
....*....|....
gi 356575070 530 ENIENKYLQCPLIA 543
Cdd:cd12119 434 VELENAIMAHPAVA 447
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
47-607 |
1.74e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 143.92 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNnnmlgrrqKTESKLGSYTWlTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCA 126
Cdd:PRK08316 15 DILRRSARRYPD--------KTALVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 127 VSYVPLYDTLGPNAVEFIINHAEVSIAFVQekkipSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGhgaSCFSWGEFLQ 206
Cdd:PRK08316 86 AVHVPVNFMLTGEELAYILDHSGARAFLVD-----PALAPTAEAALALLPVDTLILSLVLGGREAPG---GWLDFADWAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 207 LGCLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVdhIIMLTdrvAGEDDVYFSFLPLAHV--YDQIME 284
Cdd:PRK08316 158 AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSC--IVAGD---MSADDIPLHALPLYHCaqLDVFLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 285 TYCISKGSSIGFWQGDVRFLLEDIQELKPTIFCGVPRVFdrIyagikskvssagplqstlfqcaynyklkylekGLPQHk 364
Cdd:PRK08316 233 PYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVW--I--------------------------------SLLRH- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 365 aaPLFDRlvFDKTKLALGgrvrilLSGAAPLPRHV-EEFMRVTSGSTLSQGYGLTEsCAGCFTAIG--DVYSMTGTVGVP 441
Cdd:PRK08316 278 --PDFDT--RDLSSLRKG------YYGASIMPVEVlKELRERLPGLRFYNCYGQTE-IAPLATVLGpeEHLRRPGSAGRP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 442 MTTIEARLESvpemgyDALSNVPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNI 518
Cdd:PRK08316 347 VLNVETRVVD------DDGNDVAPgevGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDM 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 519 FKlSQGEYIAVENIENKYLQCPLIASIWVYGNSFESFL---VAVVVPERkaiedwakEHNLTDDfkSLCDNLKAR----- 590
Cdd:PRK08316 421 IK-TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIeavTAVVVPKA--------GATVTED--ELIAHCRARlagfk 489
|
570 580
....*....|....*....|....*
gi 356575070 591 --KHIL--DEL--NSTGQ--KHQLR 607
Cdd:PRK08316 490 vpKRVIfvDELprNPSGKilKRELR 514
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
79-574 |
3.16e-35 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 138.35 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQek 158
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 159 kipsvlSCLaqcSSNLKTIVSFGSVSTTQKKEAEghgascfswgeflqlgcLDWDLPSKKktdICTIMYTSGTTGDPKGV 238
Cdd:TIGR01923 79 ------SLL---EEKDFQADSLDRIEAAGRYETS-----------------LSASFNMDQ---IATLMFTSGTTGKPKAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 239 VIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRfLLEDIQELKPTIFCG 318
Cdd:TIGR01923 130 PHTFRNHYASAVGSKENLGFT-----EDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ-LLEMIANERVTHISL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 319 VPRVFDRiyagikskvssagplqstlfqcaynyklkYLEKGLPQHkaaplfdrlvfdktklalggRVRILLSGAAPLPRH 398
Cdd:TIGR01923 204 VPTQLNR-----------------------------LLDEGGHNE--------------------NLRKILLGGSAIPAP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 399 VEEfMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESVPEMGYdalsnvprGEICLRGNTLFSG 478
Cdd:TIGR01923 235 LIE-EAQQYGLPIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH--------GEIMVKGANLMKG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 479 YHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWV-------YGNS 551
Cdd:TIGR01923 306 YLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQV 384
|
490 500
....*....|....*....|...
gi 356575070 552 FESFLVAVVVPERKAIEDWAKEH 574
Cdd:TIGR01923 385 PVAYIVSESDISQAKLIAYLTEK 407
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
78-607 |
4.99e-35 |
|
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: 138.19 E-value: 4.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQD-VYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFvq 156
Cdd:cd05941 12 ITYADlVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 ekkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGDPK 236
Cdd:cd05941 90 ----------------------------------------------------------------DPALILYTSGTTGRPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVI--KNEAFMAEvlsvdhiiMLTDRVA-GEDDVYFSFLPLAHVYDqimetycISKGSSIGFWQG-DVRFL------LE 306
Cdd:cd05941 106 GVVLthANLAANVR--------ALVDAWRwTEDDVLLHVLPLHHVHG-------LVNALLCPLFAGaSVEFLpkfdpkEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 DIQELKP--TIFCGVPRVFDRiyagikskvssagplqstlfqcaynyklkyLEKGLPQHKAAPLFDRlvfdktKLALGgR 384
Cdd:cd05941 171 AISRLMPsiTVFMGVPTIYTR------------------------------LLQYYEAHFTDPQFAR------AAAAE-R 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 VRILLSGAAPLPRHV-EEFMRVTsGSTLSQGYGLTEScagcftaigdvySMT-----------GTVGVPMTTIEARLesV 452
Cdd:cd05941 214 LRLMVSGSAALPVPTlEEWEAIT-GHTLLERYGMTEI------------GMAlsnpldgerrpGTVGMPLPGVQARI--V 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 453 PEMGYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKK-NIFKlSQGEYIAVE 530
Cdd:cd05941 279 DEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSAL 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 531 NIENKYLQCPLIASIWVYGNSFESF---LVAVVVPErkaiedwAKEHNLT-DDFKSLCDNLKARK------HILDEL--N 598
Cdd:cd05941 358 EIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLR-------AGAAALSlEELKEWAKQRLAPYkrprrlILVDELprN 430
|
570
....*....|.
gi 356575070 599 STG--QKHQLR 607
Cdd:cd05941 431 AMGkvNKKELR 441
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
63-507 |
6.66e-34 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 136.78 E-value: 6.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 63 GRRQKT----ESKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSC-AVsYVPLYDTLG 137
Cdd:COG0365 21 GRGDKValiwEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIgAV-HSPVFPGFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 138 PNAVEFIINHAEVSIAFVQE------KKIPS---VLSCLAQCSSNLKTIVsfgsvstTQKKEAEGHGASCFSWGEFLQLG 208
Cdd:COG0365 100 AEALADRIEDAEAKVLITADgglrggKVIDLkekVDEALEELPSLEHVIV-------VGRTGADVPMEGDLDWDELLAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 209 CLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVL-SVDHIIMLTdrvagEDDVYFS--------------FL 273
Cdd:COG0365 173 SAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLDLK-----PGDVFWCtadigwatghsyivYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 274 PLAH-----VYDqimetyciskgSSIGFWQGDVrfLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqca 348
Cdd:COG0365 248 PLLNgatvvLYE-----------GRPDFPDPGR--LWELIEKYGVTVFFTAPTAIRAL---------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 349 ynykLKYLEKGLPQHkaaplfdrlvfDKTKLalggrvRILLSGAAPLPRHV-EEFMRVTsGSTLSQGYGLTESCaGCFTA 427
Cdd:COG0365 293 ----MKAGDEPLKKY-----------DLSSL------RLLGSAGEPLNPEVwEWWYEAV-GVPIVDGWGQTETG-GIFIS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 428 ---IGDVYSmtGTVGVPMTTIEARLesVPEMGYDALSNVPrGEICLRGN--TLFSGYHKREDLTKEVMVD---GWFHTGD 499
Cdd:COG0365 350 nlpGLPVKP--GSMGKPVPGYDVAV--VDEDGNPVPPGEE-GELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGD 424
|
....*...
gi 356575070 500 IGEWQSNG 507
Cdd:COG0365 425 GARRDEDG 432
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
72-606 |
1.37e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 131.91 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 72 LGSYTWLTYQDVYDAAMKMGSAIRSR-GVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEV 150
Cdd:PRK06839 22 ITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 151 SIAFVQEKkipsvlscLAQCSSNLKTIVSFGS-VSTTQKKEAEGHGAScfswgeflqlgcldwDLPSKKKTDICTIMYTS 229
Cdd:PRK06839 102 TVLFVEKT--------FQNMALSMQKVSYVQRvISITSLKEIEDRKID---------------NFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 230 GTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVydqimetyciskgSSIGFwqgdvrFLLediq 309
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLT-----MHDRSIVLLPLFHI-------------GGIGL------FAF---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 310 elkPTIFCG----VPRVFDriyagikskvssagPLQStlfqcaynykLKYLEK-------GLPQ-HKAapLFDRLVFDKT 377
Cdd:PRK06839 211 ---PTLFAGgviiVPRKFE--------------PTKA----------LSMIEKhkvtvvmGVPTiHQA--LINCSKFETT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 378 KLAlggRVRILLSGAAPLPrhvEEFMR--VTSGSTLSQGYGLTESCAGCFT-AIGDVYSMTGTVGVPMTTIEARLESvpe 454
Cdd:PRK06839 262 NLQ---SVRWFYNGGAPCP---EELMRefIDRGFLFGQGFGMTETSPTVFMlSEEDARRKVGSIGKPVLFCDYELID--- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 455 mgyDALSNVPRG---EICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVEN 531
Cdd:PRK06839 333 ---ENKNKVEVGevgELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 532 IENKYLQCPLIASIWVYGNSFESF---LVAVVVPERKA--IEDWAKEHNLTDDFKSlcdNLKARKHILDEL--NSTG--Q 602
Cdd:PRK06839 409 VEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVKKSSSvlIEKDVIEHCRLFLAKY---KIPKEIVFLKELpkNATGkiQ 485
|
....
gi 356575070 603 KHQL 606
Cdd:PRK06839 486 KAQL 489
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
78-608 |
2.55e-32 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 129.39 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVsiafvqe 157
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskKKTDICTIMYTSGTTGDPKG 237
Cdd:cd05912 75 ------------------------------------------------------------KLDDIATIMYTSGTTGKPKG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTDrvageDDVYFSFLPLAHV--YDQIMETycISKGSSIGFWQG-DVRFLLEDIQELKPT 314
Cdd:cd05912 95 VQQTFGNHWWSAIGSALNLGLTE-----DDNWLCALPLFHIsgLSILMRS--VIYGMTVYLVDKfDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 315 IFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKYLEKGLPQHkaaplfdrlvfdktklalggrVRILLSGAAP 394
Cdd:cd05912 168 IISVVPTMLQRL--------------------------LEILGEGYPNN---------------------LRCILLGGGP 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 395 LPRHVEEFMRvTSGSTLSQGYGLTESCAGCFTA-IGDVYSMTGTVGVPMTTIEARLE--SVPEMGYdalsnvprGEICLR 471
Cdd:cd05912 201 APKPLLEQCK-EKGIPVYQSYGMTETCSQIVTLsPEDALNKIGSAGKPLFPVELKIEddGQPPYEV--------GEILLK 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 472 GNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVYGNS 551
Cdd:cd05912 272 GPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVGIP 350
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 552 FESF---LVAVVVPERKAIEDwakehNLTDDFKSLCDNLKARKHI--LDEL--NSTG--QKHQLRG 608
Cdd:cd05912 351 DDKWgqvPVAFVVSERPISEE-----ELIAYCSEKLAKYKVPKKIyfVDELprTASGklLRHELKQ 411
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
78-520 |
1.03e-31 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 129.28 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSclaqcsSNLKTIVSfgsvsttqkKEAEGHGASCFSwgeflQLGCLDWDLPSK---KKTDICTIMYTSGTTGD 234
Cdd:cd05904 113 ELAEKLAS------LALPVVLL---------DSAEFDSLSFSD-----LLFEADEAEPPVvviKQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNEAFMAevlSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISK-GSSI----GFwqgDVRFLLEDIQ 309
Cdd:cd05904 173 SKGVMLTHRNLIA---MVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVvvmpRF---DLEELLAAIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 310 ELKPTIFCGVPRVfdrIYAGIKSKVSSAGPLQStlfqcaynyklkylekglpqhkaaplfdrlvfdktklalggrVRILL 389
Cdd:cd05904 247 RYKVTHLPVVPPI---VLALVKSPIVDKYDLSS------------------------------------------LRQIM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 390 SGAAPLPRHVEE-FMRVTSGSTLSQGYGLTESCAG---CFTAIGDV--YSMTGTVgVPMTtiEARLESvPEMGyDALSNV 463
Cdd:cd05904 282 SGAAPLGKELIEaFRAKFPNVDLGQGYGMTESTGVvamCFAPEKDRakYGSVGRL-VPNV--EAKIVD-PETG-ESLPPN 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 356575070 464 PRGEICLRGNTLFSGYHKREDLTKE-VMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFK 520
Cdd:cd05904 357 QTGELWIRGPSIMKGYLNNPEATAAtIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
76-532 |
4.84e-31 |
|
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: 127.03 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 76 TWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFV 155
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 156 QEKkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascFSWGEFLQLGCLDWD-LPSKKKTDICTIMYTSGTTGD 234
Cdd:cd12118 108 DRE----------------------------------------FEYEDLLAEGDPDFEwIPPADEWDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNE-AFMAevlSVDHIIMLTdrvAGEDDVYFSFLPLAHVydqimETYCIS------KGSSIGFWQGDVRFLLED 307
Cdd:cd12118 148 PKGVVYHHRgAYLN---ALANILEWE---MKQHPVYLWTLPMFHC-----NGWCFPwtvaavGGTNVCLRKVDAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 308 IQELKPTIFCGVPRVFDRIyagIKSKVSSAGPLQstlfqcaynyklkylekglpqhkaaplfdrlvfdktklalgGRVRI 387
Cdd:cd12118 217 IEKHKVTHFCGAPTVLNML---ANAPPSDARPLP-----------------------------------------HRVHV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 388 LLSGAAPlPRHVeeFMRVTS-GSTLSQGYGLTEScAGCFTA-----------IGDVYSMTGTVGVPMTTIEarlesvPEM 455
Cdd:cd12118 253 MTAGAPP-PAAV--LAKMEElGFDVTHVYGLTET-YGPATVcawkpewdelpTEERARLKARQGVRYVGLE------EVD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 456 GYDA--LSNVPR-----GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIA 528
Cdd:cd12118 323 VLDPetMKPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENIS 401
|
....*..
gi 356575070 529 ---VENI 532
Cdd:cd12118 402 sveVEGV 408
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
73-574 |
8.58e-31 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 126.66 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSI 152
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 AFVQEKkipSVLSCLAQCSSNLKTIVsfgsvsttqkkEAEGHGASCFSWGEFLQLGCLDWDLPSKKKT------DICTIM 226
Cdd:cd05926 90 VLTPKG---ELGPASRAASKLGLAIL-----------ELALDVGVLIRAPSAESLSNLLADKKNAKSEgvplpdDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 227 YTSGTTGDPKGVVIKNEAFMAEVlsvdHIIMLTDRVaGEDDVYFSFLPLAHVYDQI--METYCISKGSSI--------GF 296
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASA----TNITNTYKL-TPDDRTLVVMPLFHVHGLVasLLSTLAAGGSVVlpprfsasTF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 297 WQgdvrflleDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLFQcaynyklkYL---EKGLPQHKAAPLfdrlv 373
Cdd:cd05926 231 WP--------DVRDYNATWYTAVP----------------------TIHQ--------ILlnrPEPNPESPPPKL----- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 374 fdktklalggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTA--IGDVYSmTGTVGVPmTTIEARLes 451
Cdd:cd05926 268 ------------RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRK-PGSVGKP-VGVEVRI-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 452 VPEMGyDALSNVPRGEICLRGNTLFSGYHKREDLTKEV-MVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVE 530
Cdd:cd05926 332 LDEDG-EILPPGVVGEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPL 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 356575070 531 NIENKYLQCPLIASIWVYGNSFESF---LVAVVVPE------RKAIEDWAKEH 574
Cdd:cd05926 410 EVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLRegasvtEEELRAFCRKH 462
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
78-607 |
2.54e-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: 124.03 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivSFGSVSttqkkeaeghgascfswgeFLQLGcldwdlpskkkTDICTIMYTSGTTGDPKG 237
Cdd:cd05903 82 ---------------------RFRQFD-------------------PAAMP-----------DAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEvlsvdhIIMLTDRVA-GEDDVYFSFLPLAHVydqimetyciskgssIGFWQGdvrFLLediqelkPTIF 316
Cdd:cd05903 111 VMHSHNTLSAS------IRQYAERLGlGPGDVFLVASPMAHQ---------------TGFVYG---FTL-------PLLL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 317 cGVPRVFDRIYAGIKSKVSSAgplqstlfqcaynyklkylEKGLPQHKAAPLFdrlVFDKTKLALGG-----RVRILLSG 391
Cdd:cd05903 160 -GAPVVLQDIWDPDKALALMR-------------------EHGVTFMMGATPF---LTDLLNAVEEAgeplsRLRTFVCG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 392 AAPLPRHVEEFMRVTSGSTLSQGYGLTESCaGCFTAI--GDVYSMTGTVGVPMTTIEARLesVPEMGyDALSNVPRGEIC 469
Cdd:cd05903 217 GATVPRSLARRAAELLGAKVCSAYGSTECP-GAVTSItpAPEDRRLYTDGRPLPGVEIKV--VDDTG-ATLAPGVEGELL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 470 LRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356575070 550 NSFESF---LVAVVVPERKAiedwakehnlTDDFKSLCDNLKA----------RKHILDEL--NSTG--QKHQLR 607
Cdd:cd05903 372 LPDERLgerACAVVVTKSGA----------LLTFDELVAYLDRqgvakqywpeRLVHVDDLprTPSGkvQKFRLR 436
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
78-535 |
7.89e-30 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 123.60 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRsRGVNPGDRCGIYgsnCPEWIIAMEACNSCAVS-YVP--LYDTLGPNAVEFIINHAEV---- 150
Cdd:cd05909 8 LTYRKLLTGAIALARKLA-KMTKEGENVGVM---LPPSAGGALANFALALSgKVPvmLNYTAGLRELRACIKLAGIktvl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 151 -SIAFVQEKKIPSVLSCLAQCSsnlktIVSF----GSVSTTQKKEAEGHGASCFSWgEFLQLGCLDwdlpsKKKTDICTI 225
Cdd:cd05909 84 tSKQFIEKLKLHHLFDVEYDAR-----IVYLedlrAKISKADKCKAFLAGKFPPKW-LLRIFGVAP-----VQPDDPAVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 226 MYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYdqimetyciskGSSIGFW----QG-- 299
Cdd:cd05909 153 LFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPN-----PEDVVFGALPFFHSF-----------GLTGCLWlpllSGik 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 300 --------DVRFLLEDIQELKPTIFCGVPrVFDRIYAgikskvssagplqstlfqcayNYKLKYLEKGLpqhkaaplfdR 371
Cdd:cd05909 217 vvfhpnplDYKKIPELIYDKKATILLGTP-TFLRGYA---------------------RAAHPEDFSSL----------R 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 372 LVFdktklalggrvrillSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAgcftaigdVYSMT--------GTVGVPMT 443
Cdd:cd05909 265 LVV---------------AGAEKLKDTLRQEFQEKFGIRILEGYGTTECSP--------VISVNtpqspnkeGTVGRPLP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 444 TIEARLESVPemGYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSq 523
Cdd:cd05909 322 GMEVKIVSVE--THEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA- 398
|
490
....*....|..
gi 356575070 524 GEYIAVENIENK 535
Cdd:cd05909 399 GEMVSLEAIEDI 410
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
47-572 |
1.82e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 123.34 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNMLGRRQKTESklgsytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCA 126
Cdd:PRK12583 22 DAFDATVARFPDREALVVRHQALR-------YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 127 VSYVPLYDTLGPNAVEFIINHAEVS-------------IAFVQEKkIPSVLSCLAQCSSN-----LKTIVSFGsvsttqK 188
Cdd:PRK12583 95 AILVNINPAYRASELEYALGQSGVRwvicadafktsdyHAMLQEL-LPGLAEGQPGALACerlpeLRGVVSLA------P 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 189 KEAEGHGAscfsWGEFLQLG--CLDWDLPSKKKT----DICTIMYTSGTTGDPKGV------VIKNEAFMAEVLSVdhii 256
Cdd:PRK12583 168 APPPGFLA----WHELQARGetVSREALAERQASldrdDPINIQYTSGTTGFPKGAtlshhnILNNGYFVAESLGL---- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 257 mltdrvaGEDDVYFSFLPLAHVYDQIMETY-CISKGSSIGFWQG--DVRFLLEDIQELKPTIFCGVPRVFdriyagiksk 333
Cdd:PRK12583 240 -------TEHDRLCVPVPLYHCFGMVLANLgCMTVGACLVYPNEafDPLATLQAVEEERCTALYGVPTMF---------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 334 vssagplqstlfqcaynykLKYLEkglpqHkaaPLFDRlvFDKTKLALGgrvrilLSGAAPLPRHVeeFMRVTSGSTLSQ 413
Cdd:PRK12583 303 -------------------IAELD-----H---PQRGN--FDLSSLRTG------IMAGAPCPIEV--MRRVMDEMHMAE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 414 ---GYGLTESCAgcftaigdVYSMTGtvgvPMTTIEARLESV----P--EMGY-DALSN-VPRGEI---CLRGNTLFSGY 479
Cdd:PRK12583 346 vqiAYGMTETSP--------VSLQTT----AADDLERRVETVgrtqPhlEVKVvDPDGAtVPRGEIgelCTRGYSVMKGY 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 480 HKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVYGNSFESF--- 555
Cdd:PRK12583 414 WNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYgee 492
|
570 580
....*....|....*....|...
gi 356575070 556 LVAVVV--PERKAIE----DWAK 572
Cdd:PRK12583 493 IVAWVRlhPGHAASEeelrEFCK 515
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
78-518 |
1.57e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 120.52 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEA---CNSCAVSYVPLYDTlgpNAVEFIINHAEVSIAF 154
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGtllAGGIVVQTNPLYTE---RELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 VQEKKIPSVLSclAQCSSNLKTIV-----SFGSVSTT------QKKEA-------EGHgaSCFSWGEFLQLGCLDWDLPS 216
Cdd:PRK06710 127 CLDLVFPRVTN--VQSATKIEHVIvtriaDFLPFPKNllypfvQKKQSnlvvkvsESE--TIHLWNSVEKEVNTGVEVPC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 217 KKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHiiMLTDRVAGEDdVYFSFLPLAHVYDQ--IMETYCISKGSSI 294
Cdd:PRK06710 203 DPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ--WLYNCKEGEE-VVLGVLPFFHVYGMtaVMNLSIMQGYKMV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 295 GFWQGDVRFLLEDIQELKPTIFCGVPRVFDRIyagikskvssagpLQSTLFQcayNYKLKylekglpqhkaaplfdrlvf 374
Cdd:PRK06710 280 LIPKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-------------LNSPLLK---EYDIS-------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 375 dktklalggRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESVpE 454
Cdd:PRK06710 324 ---------SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL-E 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356575070 455 MGyDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNI 518
Cdd:PRK06710 394 TG-EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
78-607 |
1.59e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 119.68 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSclaqcssnlKTIVSFGSVSTTQKKEAEghgascfswgeFLQlgclDWDLpskkkTDICTIMYTSGTTGDPKG 237
Cdd:PRK03640 108 DFEAKLIP---------GISVKFAELMNGPKEEAE-----------IQE----EFDL-----DEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VV--IKNEaFMAEVLSVDHIiMLTdrvagEDDVYFSFLPLAHV-----------YDqiMETYCISKgssigFwqgDVRFL 304
Cdd:PRK03640 159 VIqtYGNH-WWSAVGSALNL-GLT-----EDDCWLAAVPIFHIsglsilmrsviYG--MRVVLVEK-----F---DAEKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 305 LEDIQELKPTIFCGVPRVFDRIYAgikskvssagplqstlfqcaynyklKYLEKGLPQHkaaplfdrlvfdktklalggr 384
Cdd:PRK03640 222 NKLLQTGGVTIISVVSTMLQRLLE-------------------------RLGEGTYPSS--------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 VRILLSGAAPLPRHVEEFMRvTSGSTLSQGYGLTESCAGCFTAIGDvYSMT--GTVGVPMTTIEARLESvpemgyDALSN 462
Cdd:PRK03640 256 FRCMLLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETASQIVTLSPE-DALTklGSAGKPLFPCELKIEK------DGVVV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 463 VPR--GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCP 540
Cdd:PRK03640 328 PPFeeGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 541 LIASIWVYGNSFE---SFLVAVVVPERKAIEdwakehnltDDFKSLC-DNLK-----ARKHILDEL--NSTG--QKHQLR 607
Cdd:PRK03640 407 GVAEAGVVGVPDDkwgQVPVAFVVKSGEVTE---------EELRHFCeEKLAkykvpKRFYFVEELprNASGklLRHELK 477
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
79-527 |
2.93e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 119.67 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEK 158
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 159 KIPSVLSCLAQCSsNLKTIVsfgsVSTTQKKEAEGHGASCFSWGEFLQLG--CLDWDLPsKKKTDICTIMYTSGTTGDPK 236
Cdd:PRK08162 125 FAEVAREALALLP-GPKPLV----IDVDDPEYPGGRFIGALDYEAFLASGdpDFAWTLP-ADEWDAIALNYTSGTTGNPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNE-AFMAEVLSVDHIIMltdrvaGEDDVYFSFLPLAHVydqimETYC------ISKGSSIGFWQGDVRFLLEDIQ 309
Cdd:PRK08162 199 GVVYHHRgAYLNALSNILAWGM------PKHPVYLWTLPMFHC-----NGWCfpwtvaARAGTNVCLRKVDPKLIFDLIR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 310 ELKPTIFCGVPRVfdriyagikskvssagplQSTLFQcaynyklkylekglpqhkaAPlfdrlvfDKTKLALGGRVRILL 389
Cdd:PRK08162 268 EHGVTHYCGAPIV------------------LSALIN-------------------AP-------AEWRAGIDHPVHAMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 390 SGAAPlPRHVEEFMRvTSGSTLSQGYGLTES------CA--GCFTA--IGDVYSMTGTVGVPMTTiearLESVPEMGYDA 459
Cdd:PRK08162 304 AGAAP-PAAVIAKME-EIGFDLTHVYGLTETygpatvCAwqPEWDAlpLDERAQLKARQGVRYPL----QEGVTVLDPDT 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356575070 460 LSNVPR-----GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYI 527
Cdd:PRK08162 378 MQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENI 449
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
78-607 |
2.15e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 116.80 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVqE 157
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT-E 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCfswGEFLQLGCLDWDLPSkkktdicTIMYTSGTTGDPKG 237
Cdd:PRK07786 122 AALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEA---GPAHAPVDIPNDSPA-------LIMYTSGTTGRPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSvdhiIMLTDRVAGEDDVYFSFLPLAHVydqimetycISKGSSIGFWQGDVRFLLEDIQELKPTifc 317
Cdd:PRK07786 192 AVLTHANLTGQAMT----CLRTNGADINSDVGFVGVPLFHI---------AGIGSMLPGLLLGAPTVIYPLGAFDPG--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 318 gvpRVFDRIYAgikSKVSSAG--PLQstlFQ--CAynyklkylekglpQHKAAPlfdrlvfdkTKLALggrvRILLSGAA 393
Cdd:PRK07786 256 ---QLLDVLEA---EKVTGIFlvPAQ---WQavCA-------------EQQARP---------RDLAL----RVLSWGAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 394 PLPRHVEEFMRVT-SGSTLSQGYGLTE-SCAGCFTAIGDVYSMTGTVGVPMTTIEARLESvpemgyDALSNVPRG---EI 468
Cdd:PRK07786 301 PASDTLLRQMAATfPEAQILAAFGQTEmSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVD------ENMNDVPVGevgEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 469 CLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVY 548
Cdd:PRK07786 375 VYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVI 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356575070 549 GNSFESF---LVAVVVPeRKAIEDWAKEHnlTDDFksLCDNLKARKH-----ILDEL--NSTGQ--KHQLR 607
Cdd:PRK07786 454 GRADEKWgevPVAVAAV-RNDDAALTLED--LAEF--LTDRLARYKHpkaleIVDALprNPAGKvlKTELR 519
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
78-574 |
2.04e-26 |
|
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: 112.57 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVqe 157
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvsttqkkeaeghGAScfswgeflqlgcLDwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd05935 80 -------------------------------------GSE------------LD---------DLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHV--YDQIMETYCISKGSSIGFWQGDVRFLLEDIQELKPTI 315
Cdd:cd05935 102 CMHTHFSAAANALQSAVWTGLT-----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 316 FCGVPRVFDRIYAGIKSKvssagplqstlfqcayNYKLKYLekglpqhkaaplfdrlvfdktklalggrvRILLSGAAPL 395
Cdd:cd05935 177 WTNIPTMLVDLLATPEFK----------------TRDLSSL-----------------------------KVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 396 PRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTgTVGVPMTTIEARLESvPEMGYDALSNVpRGEICLRGNTL 475
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQ-CLGIP*FGVDARVID-IETGRELPPNE-VGEIVVRGPQI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 476 FSGYHKREDLTKE--VMVDG--WFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQCPLIASIWVYG-- 549
Cdd:cd05935 289 FKGYWNRPEETEEsfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVISvp 367
|
490 500 510
....*....|....*....|....*....|....
gi 356575070 550 --NSFESFLVAVVV-PERKA------IEDWAKEH 574
Cdd:cd05935 368 deRVGEEVKAFIVLrPEYRGkvteedIIEWAREQ 401
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
221-592 |
9.64e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 111.89 E-value: 9.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGD 300
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 VRFLLEDIQELKPTIFCGVPRVfdriyagikskvssagplqSTLFQCAYNyklkylekglpqhkaAPLFDRLVFDKTKLA 380
Cdd:PRK08751 289 PRDMPGFVKELKKTRFTAFTGV-------------------NTLFNGLLN---------------TPGFDQIDFSSLKMT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 381 LGGrvrillsGAApLPRHVEEFMRVTSGSTLSQGYGLTE-SCAGCFTAIgDVYSMTGTVGVPMTTIEARLESvpemgyDA 459
Cdd:PRK08751 335 LGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTEtSPAACINPL-TLKEYNGSIGLPIPSTDACIKD------DA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 LSNVPRGEI---CLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENK 535
Cdd:PRK08751 400 GTVLAIGEIgelCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDV 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356575070 536 YLQCPLIASIwvygnsfesflVAVVVPERKAIED-----WAKEHNLT-DDFKSLC-DNLKARKH 592
Cdd:PRK08751 479 IAMMPGVLEV-----------AAVGVPDEKSGEIvkvviVKKDPALTaEDVKAHArANLTGYKQ 531
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
225-569 |
1.50e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 110.46 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 225 IMYTSGTTGDPKGVVIKNEAFMAevlSVDhiiMLTDrvAGE---DDVYFSFLPLAHVYDQIMETY-CISKGSSIgfwQGD 300
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAA---DLD---ALAE--AWQwtaDDVLVHGLPLFHVHGLVLGVLgPLRIGNRF---VHT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 VRFLLEDIQE---LKPTIFCGVPRVFDRIYAgiksKVSSAGplqstlfqcaynyklkylekglpqhkaaplfdrlvfdkt 377
Cdd:PRK07787 202 GRPTPEAYAQalsEGGTLYFGVPTVWSRIAA----DPEAAR--------------------------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 378 klALGGrVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFT-AIGDvySMTGTVGVPMTTIEARL--ESVPE 454
Cdd:PRK07787 239 --ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTrADGE--RRPGWVGLPLAGVETRLvdEDGGP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 455 MGYDALSnvpRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDR------KKNIFKLSQGEyi 527
Cdd:PRK07787 314 VPHDGET---VGELQVRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE-- 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 356575070 528 avenIENKYLQCPLIASIWVYGNSFESF---LVAVVVPERKAIED 569
Cdd:PRK07787 389 ----IETALLGHPGVREAAVVGVPDDDLgqrIVAYVVGADDVAAD 429
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-607 |
2.18e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 108.13 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 220 TDICTIMYTSGTTGDPKGV------VIKNEAFMAEVLSVdhiimltdrvaGEDDVYFSFLPLAHVYDQIMETY-CISKGS 292
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGAtlthhnIVNNGYFIGERLGL-----------TEQDRLCIPVPLFHCFGSVLGVLaCLTHGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 293 SI-----GFwqgDVRFLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynyklkylekgLPQHKaap 367
Cdd:cd05917 71 TMvfpspSF---DPLAVLEAIEKEKCTALHGVPTMFIAE---------------------------------LEHPD--- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 368 lfdrlvFDKTKLalgGRVRILLSGAAPLP----RHVEEFMRVTSgstLSQGYGLTESCAGCF-TAIGD-VYSMTGTVGVP 441
Cdd:cd05917 112 ------FDKFDL---SSLRTGIMAGAPCPpelmKRVIEVMNMKD---VTIAYGMTETSPVSTqTRTDDsIEKRVNTVGRI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 442 MTTIEARL-----ESVPEMGYdalsnvpRGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRK 515
Cdd:cd05917 180 MPHTEAKIvdpegGIVPPVGV-------PGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 516 KNIFkLSQGEYIAVENIENKYLQCPLIASIWVYGnsfesflvavvVPERKAIED---WAK---EHNLT-DDFKSLCD--- 585
Cdd:cd05917 253 KDMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG-----------VPDERYGEEvcaWIRlkeGAELTeEDIKAYCKgki 320
|
410 420
....*....|....*....|....*....
gi 356575070 586 -NLKARKHIL--DELNSTG----QKHQLR 607
Cdd:cd05917 321 aHYKVPRYVFfvDEFPLTVsgkiQKFKLR 349
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
79-507 |
5.17e-25 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 108.12 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSR-GVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGPNA-VEFIINHAEVSIAFVQ 156
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 EKkIPSVLSCLAQCssnlktivsFGSVSTTQKKEAEGHGAscfswgeflqlgcLDWDLPSKKKTDICTIMYTSGTTGDPK 236
Cdd:TIGR01733 80 SA-LASRLAGLVLP---------VILLDPLELAALDDAPA-------------PPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAEVLS-VDHIIMltdrvaGEDDVYFSFLPLAH---VYDQIM-----ETYCISKGSSIGFWQGDVRFLLEd 307
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWlARRYGL------DPDDRVLQFASLSFdasVEEIFGallagATLVVPPEDEERDDAALLAALIA- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 308 iqELKPTIFCGVPRVFDRIyagikskVSSAGPLQSTLfqcaynyklkylekglpqhkaaplfdRLVFdktklalggrvri 387
Cdd:TIGR01733 210 --EHPVTVLNLTPSLLALL-------AAALPPALASL--------------------------RLVI------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 388 lLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGC----FTAIGDVYSMTGTVGVPMTTIEARLESvpemgyDALSNV 463
Cdd:TIGR01733 242 -LGGEALTPALVDRWRARGPGARLINLYGPTETTVWStatlVDPDDAPRESPVPIGRPLANTRLYVLD------DDLRPV 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 464 PR---GEICLRGNTLFSGYHKREDLTKEVMVDGWF---------HTGDIGEWQSNG 507
Cdd:TIGR01733 315 PVgvvGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRTGDLVRYLPDG 370
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
78-520 |
9.48e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.53 E-value: 9.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIA-MEACNSCAVSYV--PLYdtlgpNAVEfIINHAEVSIAf 154
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAfLGASRRGAVTTTanPFY-----TPAE-IAKQAKASGA- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 vqekKIPSVLSCLAQCSSNLKTIVSFGSVSTtqkkeaEGHGASCFSWGEFLQLGclDWDLPSKK--KTDICTIMYTSGTT 232
Cdd:PLN02246 124 ----KLIITQSCYVDKLKGLAEDDGVTVVTI------DDPPEGCLHFSELTQAD--ENELPEVEisPDDVVALPYSSGTT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 233 GDPKGVVIKNEAFmaeVLSVdhiimlTDRVAGE--------DDVYFSFLPLAHVY--DQIMetYC-ISKGSSIGFWQgdv 301
Cdd:PLN02246 192 GLPKGVMLTHKGL---VTSV------AQQVDGEnpnlyfhsDDVILCVLPMFHIYslNSVL--LCgLRVGAAILIMP--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 302 RF----LLEDIQELKPTIFCGVPRVfdrIYAGIKSKVSSAGPLQStlfqcaynyklkylekglpqhkaaplfdrlvfdkt 377
Cdd:PLN02246 258 KFeigaLLELIQRHKVTIAPFVPPI---VLAIAKSPVVEKYDLSS----------------------------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 378 klalggrVRILLSGAAPLPRHVEE-FMRVTSGSTLSQGYGLTEScagcftaiGDVYSMT---------------GTVgvp 441
Cdd:PLN02246 300 -------IRMVLSGAAPLGKELEDaFRAKLPNAVLGQGYGMTEA--------GPVLAMClafakepfpvksgscGTV--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 442 mtTIEARLESV-PEMGYDALSNVPrGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIF 519
Cdd:PLN02246 362 --VRNAELKIVdPETGASLPRNQP-GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELI 438
|
.
gi 356575070 520 K 520
Cdd:PLN02246 439 K 439
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
78-562 |
3.51e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 106.99 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSNLKTIVSFGSVSTTQK--KEAEGHGASCFSwgeflqlgclDWDLPskkkTDICTIMYTSGTTGDP 235
Cdd:PRK06188 118 APFVERALALLARVPSLKHVLTLGPVPDGVDllAAAAKFGPAPLV----------AAALP----PDIAGLAYTGGTTGKP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 236 KGVVIKNEAfMAEVLSvdhiIMLTDRVAGEDDVYFSFLPLAH-----VYDQIMetycisKGSSI----GFWQGDVrflLE 306
Cdd:PRK06188 184 KGVMGTHRS-IATMAQ----IQLAEWEWPADPRFLMCTPLSHaggafFLPTLL------RGGTVivlaKFDPAEV---LR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 DIQELKPTIFCGVPRVfdrIYAGIKSKVSSAGPLQStlfqcaynyklkyLEkglpqhkaaplfdrlvfdktklalggrvr 386
Cdd:PRK06188 250 AIEEQRITATFLVPTM---IYALLDHPDLRTRDLSS-------------LE----------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 387 ILLSGAAPL-P-RHVEEFMRVtsGSTLSQGYGLTEsCAGCFTAIGDVYSMT------GTVGVPMTTIEARLESvpemgyD 458
Cdd:PRK06188 285 TVYYGASPMsPvRLAEAIERF--GPIFAQYYGQTE-APMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLD------E 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 459 ALSNVPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENK 535
Cdd:PRK06188 356 DGREVAQgevGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDV 434
|
490 500 510
....*....|....*....|....*....|
gi 356575070 536 YLQCPLIASIWVYGNSFESF---LVAVVVP 562
Cdd:PRK06188 435 LAEHPAVAQVAVIGVPDEKWgeaVTAVVVL 464
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
77-549 |
5.35e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.04 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 77 WlTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEvsiafvq 156
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 ekkiPSVLSCLAQCSSNLKTIVSFGSVSTtqkkEAEGHGAScfswgeflqlgcldwDLPSKKKTDICTIMYTSGTTGDPK 236
Cdd:PRK09088 95 ----PRLLLGDDAVAAGRTDVEDLAAFIA----SADALEPA---------------DTPSIPPERVSLILFTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAevlsVDHIIMLTDRVAGEDdvyfSFL---PLAHVYDQIMETY-CISKGSSI----GFWQGDVRFLLEDi 308
Cdd:PRK09088 152 GVMLSERNLQQ----TAHNFGVLGRVDAHS----SFLcdaPMFHIIGLITSVRpVLAVGGSIlvsnGFEPKRTLGRLGD- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 309 QELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynyklkylekglpqhKAAPLFDRlvfdktklALGGRVRIL 388
Cdd:PRK09088 223 PALGITHYFCVPQMAQAF-------------------------------------RAQPGFDA--------AALRHLTAL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 389 LSGAAPlprHVEEFMR--VTSGSTLSQGYGLTEScagcftaiGDVYSMT----------GTVGVPMTTIEARLesVPEMG 456
Cdd:PRK09088 258 FTGGAP---HAAEDILgwLDDGIPMVDGFGMSEA--------GTVFGMSvdcdvirakaGAAGIPTPTVQTRV--VDDQG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 457 YDALSNVPrGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENK 535
Cdd:PRK09088 325 NDCPAGVP-GELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAV 402
|
490
....*....|....
gi 356575070 536 YLQCPLIASIWVYG 549
Cdd:PRK09088 403 LADHPGIRECAVVG 416
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
79-549 |
7.30e-24 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 106.07 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQEK 158
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 159 KIPSVLScLAQCSSNLKTIVSFGSVSTTQKKEA-----EGHGASCFSWGEFLQlgcldwdlPS-KKKTDICTIMYTSGTT 232
Cdd:cd17642 126 GLQKVLN-VQKKLKIIKTIIILDSKEDYKGYQClytfiTQNLPPGFNEYDFKP--------PSfDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 233 GDPKGVVIKNEAFMAevlSVDHIImltDRVAG----EDDVYFSFLPLAHVYDQIME-TYCISKGSSIGFWQGDVRFLLED 307
Cdd:cd17642 197 GLPKGVQLTHKNIVA---RFSHAR---DPIFGnqiiPDTAILTVIPFHHGFGMFTTlGYLICGFRVVLMYKFEEELFLRS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 308 IQELKPTIFCGVPrvfdriyagikskvssagplqsTLFQCaynyklkylekgLPQHkaaPLFDRlvFDKTKLalggrvRI 387
Cdd:cd17642 271 LQDYKVQSALLVP----------------------TLFAF------------FAKS---TLVDK--YDLSNL------HE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 388 LLSGAAPLPRHVEEFMRVTSG-STLSQGYGLTESCAGCF-TAIGDVysMTGTVGVPMTTIEARLESvPEMGyDALSNVPR 465
Cdd:cd17642 306 IASGGAPLSKEVGEAVAKRFKlPGIRQGYGLTETTSAILiTPEGDD--KPGAVGKVVPFFYAKVVD-LDTG-KTLGPNER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 466 GEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIAS 544
Cdd:cd17642 382 GELCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFD 460
|
....*
gi 356575070 545 IWVYG 549
Cdd:cd17642 461 AGVAG 465
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
78-561 |
3.61e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 103.43 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 K-KIPSVLSClaqcssnlKTIVSFGSVSTTQKKEAEGHGASCfswgeflqlgcldwDLPSKKKTDICTIMYTSGTTGDPK 236
Cdd:PRK06145 108 EfDAIVALET--------PKIVIDAAAQADSRRLAQGGLEIP--------------PQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAEvlSVDHIIMLTdrvAGEDDVYFSFLPLAHVydqimeTYCISKGSSIgFWQGDvrfLLEDIQELKP-TI 315
Cdd:PRK06145 166 GVMHSYGNLHWK--SIDHVIALG---LTASERLLVVGPLYHV------GAFDLPGIAV-LWVGG---TLRIHREFDPeAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 316 FCGVPRvfDRIYAGIKSKVSSAGPLqstlfqcaynyklkylekglpqhkAAPLFDRLVFDKTKLALGGRVRillsgaAPL 395
Cdd:PRK06145 231 LAAIER--HRLTCAWMAPVMLSRVL------------------------TVPDRDRFDLDSLAWCIGGGEK------TPE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 396 PRhVEEFMRVTSGSTLSQGYGLTESCAG-CFTAIGDVYSMTGTVGVPMTTIEARLESvpEMGYDALSNVpRGEICLRGNT 474
Cdd:PRK06145 279 SR-IRDFTRVFTRARYIDAYGLTETCSGdTLMEAGREIEKIGSTGRALAHVEIRIAD--GAGRWLPPNM-KGEICMRGPK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 475 LFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVYG---NS 551
Cdd:PRK06145 355 VTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIGvhdDR 433
|
490
....*....|
gi 356575070 552 FESFLVAVVV 561
Cdd:PRK06145 434 WGERITAVVV 443
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
78-584 |
6.09e-23 |
|
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: 102.33 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGPNA-VEFIINHAEVSIAFVQ 156
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLIAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 EkkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkkTDICTIMYTSGTTGDPK 236
Cdd:cd05945 96 G--------------------------------------------------------------DDNAYIIFTSGSTGRPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAevlSVDHiiMLTDRVAGEDDVY-----FSF-LPLAHVYdqimetYCISKGSSIgfW------QGDVRFL 304
Cdd:cd05945 114 GVQISHDNLVS---FTNW--MLSDFPLGPGDVFlnqapFSFdLSVMDLY------PALASGATL--VpvprdaTADPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 305 LEDIQELKPTIFCGVPrvfdriyagikskvssagplqSTLFQCAynyklkyLEKGLPQHKAAPLfdRLVfdktklalggr 384
Cdd:cd05945 181 FRFLAEHGITVWVSTP---------------------SFAAMCL-------LSPTFTPESLPSL--RHF----------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 vriLLSGAaPLP-RHVEEFMRVTSGSTLSQGYGLTESCAGCfTAI---GDVYSMTGTV--GVPMTtiEARLESVPEMGyD 458
Cdd:cd05945 220 ---LFCGE-VLPhKTARALQQRFPDARIYNTYGPTEATVAV-TYIevtPEVLDGYDRLpiGYAKP--GAKLVILDEDG-R 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 459 ALSNVPRGEICLRGNTLFSGYHKREDLTKEV--MVDG--WFHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIEN 534
Cdd:cd05945 292 PVPPGEKGELVISGPSVSKGYLNNPEKTAAAffPDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEA 370
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 356575070 535 KYLQCPLIAS---IWVYGNSFESFLVAVVVPErKAIEDWakehnLTDDFKSLC 584
Cdd:cd05945 371 ALRQVPGVKEavvVPKYKGEKVTELIAFVVPK-PGAEAG-----LTKAIKAEL 417
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
76-568 |
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 356575070 76 TWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPL-YDTLGPNaVEFIINHAEVSIAF 154
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPInTALRGPQ-LEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 VQEKKIPSVLSCLAQCSSnLKTIVSFGSVSttqkkeaEGHGASCFSWGEFLQLGCLDwDLPSKKKTDICTIMYTSGTTGD 234
Cdd:PRK06155 124 VEAALLAALEAADPGDLP-LPAVWLLDAPA-------SVSVPAGWSTAPLPPLDAPA-PAAAVQPGDTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNEAF------MAEVLSVdhiimltdrvaGEDDVYFSFLPLAHV-----YDQIMETYCI----SKGSSIGFW-- 297
Cdd:PRK06155 195 SKGVCCPHAQFywwgrnSAEDLEI-----------GADDVLYTTLPLFHTnalnaFFQALLAGATyvlePRFSASGFWpa 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 298 ----QGDVRFLLediqelkptifcgvprvfdriyagikskvssaGPLQSTLfqcaynyklkylekgLPQHKAAPlfDRlv 373
Cdd:PRK06155 264 vrrhGATVTYLL--------------------------------GAMVSIL---------------LSQPARES--DR-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 374 fdktklalGGRVRILLSGAAPlPRHVEEFmRVTSGSTLSQGYGLTESCAGCFTAIGDvySMTGTVGVPMTTIEARLesVP 453
Cdd:PRK06155 293 --------AHRVRVALGPGVP-AALHAAF-RERFGVDLLDGYGSTETNFVIAVTHGS--QRPGSMGRLAPGFEARV--VD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 454 EMGYDALSNVPrGEICLRGNTLF---SGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVE 530
Cdd:PRK06155 359 EHDQELPDGEP-GELLLRADEPFafaTGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSF 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 356575070 531 NIENKYLQCPLIASIWVYGNSFE----SFLVAVVVPERKAIE 568
Cdd:PRK06155 437 EVEQVLLSHPAVAAAAVFPVPSElgedEVMAAVVLRDGTALE 478
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
75-607 |
1.47e-22 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 102.23 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 75 YTWLtyqDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAF 154
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 VQEKKIPSVLSCLAQCSSNLKT--------IVSFGSVSTTQKKEAEGHGAscFSWGEFLQLG--CLDWDLPSKKKTDIcT 224
Cdd:PLN02479 123 VDQEFFTLAEEALKILAEKKKSsfkpplliVIGDPTCDPKSLQYALGKGA--IEYEKFLETGdpEFAWKPPADEWQSI-A 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 225 IMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHV----YDQIMETYCiskGSSIGFWQGD 300
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMN-----EGAVYLWTLPMFHCngwcFTWTLAALC---GTNICLRQVT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 VRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKvssagplqstlfqcaynyklkylekglpqhkaaplfdrlvfdkTKLA 380
Cdd:PLN02479 272 AKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSE-------------------------------------------TILP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 381 LGGRVRILLSGAAPLPRHV----EEFMRVTSGSTLSQGYGLTESCAgcFTAIGDvysmtgtvGVPMTTiEARLESVPEMG 456
Cdd:PLN02479 309 LPRVVHVMTAGAAPPPSVLfamsEKGFRVTHTYGLSETYGPSTVCA--WKPEWD--------SLPPEE-QARLNARQGVR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 457 YDALSN-----------VPR-----GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFk 520
Cdd:PLN02479 378 YIGLEGldvvdtktmkpVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDII- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 521 LSQGEYIAVENIENKYLQCPLIASIWVYGNSFESF---LVAVVVPERKAieDWAKEHNLTDDFKSLC-DNLKA----RKH 592
Cdd:PLN02479 457 ISGGENISSLEVENVVYTHPAVLEASVVARPDERWgesPCAFVTLKPGV--DKSDEAALAEDIMKFCrERLPAywvpKSV 534
|
570
....*....|....*....
gi 356575070 593 ILDELNSTG----QKHQLR 607
Cdd:PLN02479 535 VFGPLPKTAtgkiQKHVLR 553
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
78-564 |
4.98e-22 |
|
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: 99.33 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAevsiafvqe 157
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssNLKTIVSfgsvsttqkkEAEghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd05972 72 ---------------GAKAIVT----------DAE----------------------------DPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLtdrvaGEDDVYFS--------------FLPLAHVYDQIMETYciskgssIGFwqgDVRF 303
Cdd:cd05972 99 VLHTHSYPLGHIPTAAYWLGL-----RPDDIHWNiadpgwakgawssfFGPWLLGATVFVYEG-------PRF---DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 304 LLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynyklkylekglpqhkAAPLFDRLVFdktklalgG 383
Cdd:cd05972 164 ILELLERYGVTSFCGPPTAYRML--------------------------------------IKQDLSSYKF--------S 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 RVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAgcftAIGDVYSMT---GTVGVPMTTIEARLesVPEMGYDAL 460
Cdd:cd05972 198 HLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL----TVGNFPDMPvkpGSMGRPTPGYDVAI--IDDDGRELP 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 461 SNVPrGEICLRGNT--LFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQ 538
Cdd:cd05972 272 PGEE-GDIAIKLPPpgLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLE 349
|
490 500
....*....|....*....|....*.
gi 356575070 539 CPLIAsiwvygnsfESFLVAVVVPER 564
Cdd:cd05972 350 HPAVA---------EAAVVGSPDPVR 366
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-607 |
1.88e-21 |
|
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: 98.21 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSNLKTIVSfgsvsttqkkeAEGHGASC-FSWGEFLqLGCLDWDLPSKK--KTDICTIMYTSGTTGD 234
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIV-----------SGGAGPEAgALLLAEL-VAAEAEQLKPAAthADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVV--IKNEAFMAEvLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDqimetycISKGSSIGFWQGDVRFLL------- 305
Cdd:cd05959 178 PKGVVhlHADIYWTAE-LYARNVLGIR-----EDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptpa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 306 ---EDIQELKPTIFCGVPrvfdRIYAGIkskvssagplqstlfqcaynyklkylekglpqhkaaplfdrLVFDKTKLALG 382
Cdd:cd05959 245 avfKRIRRYRPTVFFGVP----TLYAAM-----------------------------------------LAAPNLPSRDL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 383 GRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTEscAG---CFTAIGDVYsmTGTVGVPMTTIEARLesVPEMGYDA 459
Cdd:cd05959 280 SSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLhifLSNRPGRVR--YGTTGKPVPGYEVEL--RDEDGGDV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 LSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQC 539
Cdd:cd05959 354 ADGEP-GELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQH 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 540 PLIASIWVYGNSFESFL---VAVVVPERKAiedwAKEHNLTDDFKSLC-DNLKARKH-----ILDELNSTG----QKHQL 606
Cdd:cd05959 432 PAVLEAAVVGVEDEDGLtkpKAFVVLRPGY----EDSEALEEELKEFVkDRLAPYKYprwivFVDELPKTAtgkiQRFKL 507
|
.
gi 356575070 607 R 607
Cdd:cd05959 508 R 508
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
39-522 |
2.14e-21 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 98.55 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 39 PSDFKSPWDFFRDSVKRNPNNNMLGRRQKTesklgsytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIA 118
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPAFICMGKA---------ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 119 MEA---CNSCAVSYVPLYDtlgPNAVEFIINHAEVSIAFVQEKKIPSVLSCLAqcSSNLKTIV--SFGS----------- 182
Cdd:PRK07059 90 IAAvlrAGYVVVNVNPLYT---PRELEHQLKDSGAEAIVVLENFATTVQQVLA--KTAVKHVVvaSMGDllgfkghivnf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 183 VSTTQKKEAEGHG-ASCFSWGEFLQLGC-LDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTD 260
Cdd:PRK07059 165 VVRRVKKMVPAWSlPGHVRFNDALAEGArQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 261 RVAGEDDVYFSF--LPLAHVYdqiMETYCiskgSSIGFWQGDVRFLLED-------IQELKptifcgvprvfdriyagiK 331
Cdd:PRK07059 245 EKKPRPDQLNFVcaLPLYHIF---ALTVC----GLLGMRTGGRNILIPNprdipgfIKELK------------------K 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 332 SKVSSAgPLQSTLFQCAYNyklkylekglpqhkaAPLFDRLVFDKTKLALGGrvrillsGAApLPRHVEEFMRVTSGSTL 411
Cdd:PRK07059 300 YQVHIF-PAVNTLYNALLN---------------NPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 412 SQGYGLTES--CAGCFTAIGDVYsmTGTVGVPM--TTIEARLESVPEMgydALSNVprGEICLRGNTLFSGYHKREDLTK 487
Cdd:PRK07059 356 TEGYGLSETspVATCNPVDATEF--SGTIGLPLpsTEVSIRDDDGNDL---PLGEP--GEICIRGPQVMAGYWNRPDETA 428
|
490 500 510
....*....|....*....|....*....|....*.
gi 356575070 488 EVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLS 522
Cdd:PRK07059 429 KVMTaDGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
215-549 |
4.97e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.22 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 215 PSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYD-QIMETYCISKGSS 293
Cdd:PLN02574 193 PVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGlSLFVVGLLSLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 294 IGFWQG-DVRFLLEDIQELKPTIFCGVPRVfdrIYAGIKS-KVSSAGPLQStlfqcaynykLKYLEKGlpqhkAAPLFDR 371
Cdd:PLN02574 273 IVVMRRfDASDMVKVIDRFKVTHFPVVPPI---LMALTKKaKGVCGEVLKS----------LKQVSCG-----AAPLSGK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 372 LvfdktklalggrvrillsgaaplprhVEEFMRVTSGSTLSQGYGLTESCA----GCFTAIGDVYSmtgTVGVPMTTIEA 447
Cdd:PLN02574 335 F--------------------------IQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYS---SVGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 448 RlesVPEMGYDALsnVP---RGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLsQ 523
Cdd:PLN02574 386 K---VVDWSTGCL--LPpgnCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-K 459
|
330 340
....*....|....*....|....*.
gi 356575070 524 GEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:PLN02574 460 GFQIAPADLEAVLISHPEIIDAAVTA 485
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
47-607 |
7.03e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 96.80 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNML-----GRRqktesklgsYTWLTYQDVYDAamkMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEA 121
Cdd:PRK08315 20 QLLDRTAARYPDREALvyrdqGLR---------WTYREFNEEVDA---LAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 122 CNSCAVSYV---PLYDTlgpNAVEFIINHAEVS-------------IAFVQEKkIPSVLSCLA-QCSSN----LKTIVSF 180
Cdd:PRK08315 88 TAKIGAILVtinPAYRL---SELEYALNQSGCKaliaadgfkdsdyVAMLYEL-APELATCEPgQLQSArlpeLRRVIFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 181 GsvsttqkkeAEGHgASCFSWGEFLQLGC--LDWDLPSKKKT----DICTIMYTSGTTGDPKGV------VIKNEAFMAE 248
Cdd:PRK08315 164 G---------DEKH-PGMLNFDELLALGRavDDAELAARQATldpdDPINIQYTSGTTGFPKGAtlthrnILNNGYFIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 249 VLSvdhiimLTdrvagEDD-----VyfsflPLAHVYDQIMETY-CISKGSSI-----GFwqgDVRFLLEDIQELKPTIFC 317
Cdd:PRK08315 234 AMK------LT-----EEDrlcipV-----PLYHCFGMVLGNLaCVTHGATMvypgeGF---DPLATLAAVEEERCTALY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 318 GVPrvfdriyagikskvssagplqsTLFQCAYNyklkylekglpqHkaaPLFDRlvFDKTKLALGgrvriLLSGAaPLPr 397
Cdd:PRK08315 295 GVP----------------------TMFIAELD------------H---PDFAR--FDLSSLRTG-----IMAGS-PCP- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 398 hvEEFM-RVTSGSTLSQ---GYGLTESCAGCF-TAIGD-VYSMTGTVGVPMTTIEARLesV-PEMGYDalsnVPR---GE 467
Cdd:PRK08315 329 --IEVMkRVIDKMHMSEvtiAYGMTETSPVSTqTRTDDpLEKRVTTVGRALPHLEVKI--VdPETGET----VPRgeqGE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 468 ICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIW 546
Cdd:PRK08315 401 LCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQ 479
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356575070 547 VYGnsfesflvavvVPERKAIED---W--AKE-HNLT-DDFKSLCDNLKAR----KHI--LDE--LNSTG--QKHQLR 607
Cdd:PRK08315 480 VVG-----------VPDEKYGEEvcaWiiLRPgATLTeEDVRDFCRGKIAHykipRYIrfVDEfpMTVTGkiQKFKMR 546
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
221-607 |
7.05e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 96.66 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAevlsvdHIIMLTDRVA-GEDDVYFSFLPLAH----VYDQIMEtycISKGSSIg 295
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTLMA------NIVPYAERLGlGADDVILMASPMAHqtgfMYGLMMP---VMLGATA- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 296 fwqgdvrfLLEDIQElkptifcgVPRVFDRIYAGIKSKVSSAGPLQSTLfqcaynyklkyleKGLPQHKAAPLfdrlvfd 375
Cdd:PRK13295 268 --------VLQDIWD--------PARAAELIRTEGVTFTMASTPFLTDL-------------TRAVKESGRPV------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 376 ktklalgGRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTV-GVPMTTIEARLESvpe 454
Cdd:PRK13295 312 -------SSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTdGCPLPGVEVRVVD--- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 455 mgyDALSNVPRGEI---CLRGNTLFSGYHKREDLTKeVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVEN 531
Cdd:PRK13295 382 ---ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 532 IENKYLQCPLIASIWVYGNSFESF---LVAVVVPER------KAIEDWAKEHNLTDDFkslcdnLKARKHILDELNSTG- 601
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAYPDERLgerACAFVVPRPgqsldfEEMVEFLKAQKVAKQY------IPERLVVRDALPRTPs 530
|
....*....
gi 356575070 602 ---QKHQLR 607
Cdd:PRK13295 531 gkiQKFRLR 539
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
221-602 |
8.00e-21 |
|
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: 93.93 E-value: 8.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAevlSVDhiiMLTDRVA-GEDDVYFSFLPLAHVydqimetyciskgSSIGFWqg 299
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA---SAA---GLHSRLGfGGGDSWLLSLPLYHV-------------GGLAIL-- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 300 dVRFLLediqelkptifCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAynyklkyLEKGLPQHKAAPLFDRLvfdktkl 379
Cdd:cd17630 60 -VRSLL-----------AGAELVLLERNQALAEDLAPPGVTHVSLVPTQ-------LQRLLDSGQGPAALKSL------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 380 alggrvRILLSGAAPLPRHVEEFMRvTSGSTLSQGYGLTE----SCAGCFTAIGDvysmtGTVGVPMTTIEARLesvpem 455
Cdd:cd17630 114 ------RAVLLGGAPIPPELLERAA-DRGIPLYTTYGMTEtasqVATKRPDGFGR-----GGVGVLLPGRELRI------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 456 gydalsnVPRGEICLRGNTLFSGYHKReDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENK 535
Cdd:cd17630 176 -------VEDGEIWVGGASLAMGYLRG-QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356575070 536 YLQCPLIASIWVYGNSFESF---LVAVVVPERKAIEDwakehNLTDDFKSLCDNLKARKHI--LDELNSTGQ 602
Cdd:cd17630 247 LAAHPAVRDAFVVGVPDEELgqrPVAVIVGRGPADPA-----ELRAWLKDKLARFKLPKRIypVPELPRTGG 313
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
69-549 |
1.60e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.52 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 69 ESKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHA 148
Cdd:PRK08008 29 ESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 149 EVSIAFVQEKKIPSVLSCLAQCSSNLKTIVsfgsVSTTQKKEAEGhgASCFSWGEFLQLGCLDwDLPSKKKTDICTIMYT 228
Cdd:PRK08008 109 QASLLVTSAQFYPMYRQIQQEDATPLRHIC----LTRVALPADDG--VSSFTQLKAQQPATLC-YAPPLSTDDTAEILFT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 229 SGTTGDPKGVVIKneafmaevlsvdHIIMltdRVAG----------EDDVYFSFLPLAHVYDQI---METYC-------I 288
Cdd:PRK08008 182 SGTTSRPKGVVIT------------HYNL---RFAGyysawqcalrDDDVYLTVMPAFHIDCQCtaaMAAFSagatfvlL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 289 SKGSSIGFWQgdvrflleDIQELKPTIFCGVPRVFdriyagikskvssagplqSTLFqcaynyklkyLEKGLPQHKAAPL 368
Cdd:PRK08008 247 EKYSARAFWG--------QVCKYRATITECIPMMI------------------RTLM----------VQPPSANDRQHCL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 369 FDRLVF----DKTKLALGGR--VRILLSgaaplprhveefmrvtsgstlsqgYGLTESCAGcftAIGDvysmtgtvgvpM 442
Cdd:PRK08008 291 REVMFYlnlsDQEKDAFEERfgVRLLTS------------------------YGMTETIVG---IIGD-----------R 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 443 TTIEARLESV--PEMGYDA---------LSNVPRGEICLRG---NTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNG 507
Cdd:PRK08008 333 PGDKRRWPSIgrPGFCYEAeirddhnrpLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEG 412
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 356575070 508 AMKIIDRKKNIFKLSqGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:PRK08008 413 FFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
48-549 |
2.66e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 94.72 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 48 FFRDSVKRNPNNNMLGRRQKTesklgsYTWLTYQDVYDAamkMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAV 127
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRS------WTWREIDARVDA---LAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 128 SYVPLYDTLGPNAVEFIINHAEVSiAFVQEKKIPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEA---EGHGAScfswgef 204
Cdd:PRK07470 83 VWVPTNFRQTPDEVAYLAEASGAR-AMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEAlvaRHLGAR------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 205 LQLGCLDWDLPskkktdiCTIMYTSGTTGDPKGVVIKNEAfMAEVLSvDHiimLTDRVAG--EDDVYFSFLPLAHvydqi 282
Cdd:PRK07470 155 VANAAVDHDDP-------CWFFFTSGTTGRPKAAVLTHGQ-MAFVIT-NH---LADLMPGttEQDASLVVAPLSH----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 283 metyciskGSSIgfwqgdvrFLLEDIQELKPTIFCGVPRvFD--RIYAGI-KSKVSsagplqsTLFQCAYNYKLkylekg 359
Cdd:PRK07470 218 --------GAGI--------HQLCQVARGAATVLLPSER-FDpaEVWALVeRHRVT-------NLFTVPTILKM------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 360 LPQHKAAplfDRlvFDKTKLalggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTEsCAGCFT----AIGDVYSMT 435
Cdd:PRK07470 268 LVEHPAV---DR--YDHSSL------RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE-VTGNITvlppALHDAEDGP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 436 ----GTVGVPMTTIEARLESvpemgyDALSNVP---RGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGA 508
Cdd:PRK07470 336 dariGTCGFERTGMEVQIQD------DEGRELPpgeTGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGF 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 356575070 509 MKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:PRK07470 410 LYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
78-522 |
3.06e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 94.72 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSsnLKTI--VSFGSVSTTQKK-----EAEGHGASCFSWGEFLQL--GC-LDWDLPSKKKTDICTIMY 227
Cdd:PRK06178 139 QLAPVVEQVRAETS--LRHVivTSLADVLPAEPTlplpdSLRAPRLAAAGAIDLLPAlrACtAPVPLPPPALDALAALNY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 228 TSGTTGDPKGVvIKNEAFMAEVLSVDHIIMLtdrVAGEDDVYFSFLPLahvydqimetyciskgssigFW-QGdvrfllE 306
Cdd:PRK06178 217 TGGTTGMPKGC-EHTQRDMVYTAAAAYAVAV---VGGEDSVFLSFLPE--------------------FWiAG------E 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 DIQELKPtIFCGVPRVF------DRIYAGIKS-KVSS-AGPLQStlfqcaynyklkYLEkgLPQHKAAPLFD-------R 371
Cdd:PRK06178 267 NFGLLFP-LFSGATLVLlarwdaVAFMAAVERyRVTRtVMLVDN------------AVE--LMDHPRFAEYDlsslrqvR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 372 LV-FDKtKLALGGRVRillsgaaplprhveefMRVTSGSTLSQG-YGLTES-CAGCFTAiG------DVYSMTGTVGVPM 442
Cdd:PRK06178 332 VVsFVK-KLNPDYRQR----------------WRALTGSVLAEAaWGMTEThTCDTFTA-GfqdddfDLLSQPVFVGLPV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 443 TTIEARLESvpemgYDALSNVP---RGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIF 519
Cdd:PRK06178 394 PGTEFKICD-----FETGELLPlgaEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEML 468
|
...
gi 356575070 520 KLS 522
Cdd:PRK06178 469 KVN 471
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
78-574 |
6.24e-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: 93.42 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KkipsvlscLAQCSSNLKTIVSFGSVSTTQKKEAEGHGAScfswgeflqlgcldwdlpskkKTDICTIMYTSGTTGDPKG 237
Cdd:cd12117 103 S--------LAGRAGGLEVAVVIDEALDAGPAGNPAVPVS---------------------PDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIImltdrvAGEDDVyfsFLPLahvydqimetyciskgSSIGFwqgDVrFLLEdiqelkptifc 317
Cdd:cd12117 154 VAVTHRGVVRLVKNTNYVT------LGPDDR---VLQT----------------SPLAF---DA-STFE----------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 318 gvprVFDRIYAGIKSKVSSAGPLQSTLFqcaynyklkyLEKGLPQHKA------APLFDRLVfDKTKLALGGrVRILLSG 391
Cdd:cd12117 194 ----IWGALLNGARLVLAPKGTLLDPDA----------LGALIAEEGVtvlwltAALFNQLA-DEDPECFAG-LRELLTG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 392 --AAPlPRHVEEFMRVTSGSTLSQGYGLTES--CAGCFtAIGDVYSMTGTV--GVPMTTIEARLesVPEMGYDALSNVPr 465
Cdd:cd12117 258 geVVS-PPHVRRVLAACPGLRLVNGYGPTENttFTTSH-VVTELDEVAGSIpiGRPIANTRVYV--LDEDGRPVPPGVP- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 466 GEICLRGNTLFSGYHKREDLTKEVMV-----DG--WFHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQ 538
Cdd:cd12117 333 GELYVGGDGLALGYLNRPALTAERFVadpfgPGerLYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRA 411
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 356575070 539 CPLIASIWVY---GNSFESFLVAVVVPERK----AIEDWAKEH 574
Cdd:cd12117 412 HPGVREAVVVvreDAGGDKRLVAYVVAEGAldaaELRAFLRER 454
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
43-655 |
7.98e-20 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 94.54 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 43 KSPWDFFRDSVKRNPNNNMLGrrQKTESklGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
Cdd:PTZ00297 427 RSLGEMWERSVTRHSTFRCLG--QTSES--GESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVAC 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 123 NSCAVSYVPLYDTlgPNAVEFIINHAEVSIAFVQEKKIPSVLSCLaqcSSNLKTIVSFGS-VSTTQKKEAEGHGASCFSW 201
Cdd:PTZ00297 503 ALYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCR---SRKLETVVYTHSfYDEDDHAVARDLNITLIPY 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 202 GEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKneafmaeVLSVDHIIMLTD------------RVAGEDDVY 269
Cdd:PTZ00297 578 EFVEQKGRLCPVPLKEHVTTDTVFTYVVDNTTSASGDGLA-------VVRVTHADVLRDistlvmtgvlpsSFKKHLMVH 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 270 FSflPLAHVYDQIMETYCISKGSSIGfwQGDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLQSTLFQCAY 349
Cdd:PTZ00297 651 FT--PFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAF 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 350 NYKLKYLEKglpQHKAAPLFDRLVFDKTKLALGGRVRILlsgaaplprhveefmrVTSGSTLSQGYGLTESCAGCFTAIG 429
Cdd:PTZ00297 727 QLRSRLINI---HRRDSSLLRFIFFRATQELLGGCVEKI----------------VLCVSEESTSFSLLEHISVCYVPCL 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 430 DVYSMTGTVGV------PMTTIEARLESvpemgYDALSNvprgeiclrGNTLFSGYHKREDLTKevmvdgwfHTGDI-GE 502
Cdd:PTZ00297 788 REVFFLPSEGVfcvdgtPAPSLQVDLEP-----FDEPSD---------GAGIGQLVLAKKGEPR--------RTLPIaAQ 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 503 WQSNGAMKIIDRKKNIFKLSQGEYIAVENIENKYLQCPLIASIWVYGNSFESfLVAVVVPERKAIE-DWAKEHNLTD-DF 580
Cdd:PTZ00297 846 WKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGEgGG 924
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 581 KSLCDNLK-----ARKHILDELNSTGQKHQLRGFELLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDHIDQLYKEA 655
Cdd:PTZ00297 925 PARQLGWTelvayASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDV 1004
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
78-607 |
8.81e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.02 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEvsiafvqe 157
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAE-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkiPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGAscfswgeFLQLGCldwDLPSKKKT------DICTIMYTSGT 231
Cdd:PRK07514 101 ---PALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGS-------LLEAAA---AAPDDFETvprgadDLAAILYTSGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 232 TGDPKGVVI--KNEAFMAEVLsVDHIimltdRVaGEDDVYFSFLPLAHVYDQIMETYCI-SKGSSIGFWQgdvRFLLEDI 308
Cdd:PRK07514 168 TGRSKGAMLshGNLLSNALTL-VDYW-----RF-TPDDVLIHALPIFHTHGLFVATNVAlLAGASMIFLP---KFDPDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 309 QELKP--TIFCGVPRVFDRIyagikskvssagpLQStlfqcaynyklkylekglpqhkaaPLFDRlvfdktklALGGRVR 386
Cdd:PRK07514 238 LALMPraTVMMGVPTFYTRL-------------LQE------------------------PRLTR--------EAAAHMR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 387 ILLSGAAPL--PRHVEEFMRvtSGSTLSQGYGLTESCagcftaigdvysMT-----------GTVGVPMTTIEARLESvP 453
Cdd:PRK07514 273 LFISGSAPLlaETHREFQER--TGHAILERYGMTETN------------MNtsnpydgerraGTVGFPLPGVSLRVTD-P 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 454 EMGYDalsnVPRGEIC---LRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAV 529
Cdd:PRK07514 338 ETGAE----LPPGEIGmieVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGKDLI-ISGGYNVYP 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 530 ENIENKYLQCPLIASIWVYGNSFESF---LVAVVVPERKAIEDwakEHNLTDDFKSLCDNLKARK--HILDEL--NSTG- 601
Cdd:PRK07514 413 KEVEGEIDELPGVVESAVIGVPHPDFgegVTAVVVPKPGAALD---EAAILAALKGRLARFKQPKrvFFVDELprNTMGk 489
|
....*..
gi 356575070 602 -QKHQLR 607
Cdd:PRK07514 490 vQKNLLR 496
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
215-522 |
8.93e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.19 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 215 PSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHII--MLTDrvaGEDDVYFSfLPLAHVYDQIMEtyC---IS 289
Cdd:PRK08974 201 PELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYgpLLHP---GKELVVTA-LPLYHIFALTVN--CllfIE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 290 KGSsigfwqgdvRFLL----EDI----QELKPTIFCGVPRVfdriyagikskvssagplqSTLFQCAYNyklkylekglp 361
Cdd:PRK08974 275 LGG---------QNLLitnpRDIpgfvKELKKYPFTAITGV-------------------NTLFNALLN----------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 362 qhkaAPLFDRLVFDKTKLALGGrvrillsgAAPLPRHVEEFMRVTSGSTLSQGYGLTEsCAGCFTAIG-DVYSMTGTVGV 440
Cdd:PRK08974 316 ----NEEFQELDFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTE-CSPLVSVNPyDLDYYSGSIGL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 441 PMTTIEARLesVPEMGYDaLSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFK 520
Cdd:PRK08974 383 PVPSTEIKL--VDDDGNE-VPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMIL 459
|
..
gi 356575070 521 LS 522
Cdd:PRK08974 460 VS 461
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
78-607 |
1.17e-19 |
|
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: 92.14 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVqe 157
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvsttqkkEAEghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd05919 89 --------------------------------SAD----------------------------DIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VV--IKNEAFMAEVLSVDHI-IMLTDRVAGEDDVYFSF-------LPLAhvydqimetyciSKGSSIGF--WQGDVRfLL 305
Cdd:cd05919 109 VMhaHRDPLLFADAMAREALgLTPGDRVFSSAKMFFGYglgnslwFPLA------------VGASAVLNpgWPTAER-VL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 306 EDIQELKPTIFCGVPRVFDRIyagIKSKVSSAGPLQStlfqcaynyklkylekglpqhkaaplfdrlvfdktklalggrV 385
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANL---LDSCAGSPDALRS------------------------------------------L 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 386 RILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMtGTVGVPMTTIEARLesVPEMGYDALSNVPr 465
Cdd:cd05919 211 RLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRL-GSTGRPVPGYEIRL--VDEEGHTIPPGEE- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 466 GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQCPLIASI 545
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEA 365
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356575070 546 WVYGNSFESFLV---AVVVPERKAIEDWAKEHNLTDdfkSLCDNLKARK-----HILDEL--NSTG--QKHQLR 607
Cdd:cd05919 366 AVVAVPESTGLSrltAFVVLKSPAAPQESLARDIHR---HLLERLSAHKvprriAFVDELprTATGklQRFKLR 436
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
47-542 |
1.68e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.50 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNMLGRRQKTesklgSYTwltYQDVYDAAMKMGSAIRSRGVNPGDRCGIygsNCPEW----IIAMEAC 122
Cdd:PRK06087 27 DYWQQTARAMPDKIAVVDNHGA-----SYT---YSALDHAASRLANWLLAKGIEPGDRVAF---QLPGWceftIIYLACL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 123 NSCAVSyVPLYDTLGPNAVEFIIN--HAEVSIAFVQEKKI---PSVLSCLAQCSSnLKTIVSFgsvsttqKKEAEGHgaS 197
Cdd:PRK06087 96 KVGAVS-VPLLPSWREAELVWVLNkcQAKMFFAPTLFKQTrpvDLILPLQNQLPQ-LQQIVGV-------DKLAPAT--S 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 198 CFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAH 277
Cdd:PRK06087 165 SLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-----WQDVFMMPAPLGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 278 vydqimetyciskgsSIGFWQGdvrfllediqeLKPTIFCGVPRVFDRIYagiKSKvssagplqstlfQCAynyKLKYLE 357
Cdd:PRK06087 240 ---------------ATGFLHG-----------VTAPFLIGARSVLLDIF---TPD------------ACL---ALLEQQ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 358 KGLPQHKAAP-LFDRLVF---DKTKLAlggRVRILLSGAAPLP----RHVEEFmrvtsGSTLSQGYGLTESCAGCFTAIG 429
Cdd:PRK06087 276 RCTCMLGATPfIYDLLNLlekQPADLS---ALRFFLCGGTTIPkkvaRECQQR-----GIKLLSVYGSTESSPHAVVNLD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 430 DVYSMTG-TVGVPMTTIEARLESvpemgyDALSNVPRG---EICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQ 504
Cdd:PRK06087 348 DPLSRFMhTDGYAAAGVEIKVVD------EARKTLPPGcegEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMD 421
|
490 500 510
....*....|....*....|....*....|....*...
gi 356575070 505 SNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLI 542
Cdd:PRK06087 422 EAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKI 458
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-574 |
2.21e-19 |
|
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: 91.44 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkkTDICTIMYTSGTTGDPKG 237
Cdd:cd05930 93 --------------------------------------------------------------DDLAYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVyDQIMETYC-ISKGSSI----GFWQGDVRFLLEDIQELK 312
Cdd:cd05930 111 VMVEHRGLVNLLLWMQEAYPLT-----PGDRVLQFTSFSFD-VSVWEIFGaLLAGATLvvlpEEVRKDPEALADLLAEEG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 313 PTIFCGVPRVFdriyagikskvssagplqSTLFQCAYNYKLKYLekglpqhkaaplfdRLVFdktklalggrvrilLSGA 392
Cdd:cd05930 185 ITVLHLTPSLL------------------RLLLQELELAALPSL--------------RLVL--------------VGGE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 393 APLPRHVEEFMRVTSGSTLSQGYGLTESCAGC-FTAIGDVYSMTGTV--GVPMTTIEAR-----LESVPEmgydalsNVP 464
Cdd:cd05930 219 ALPPDLVRRWRELLPGARLVNLYGPTEATVDAtYYRVPPDDEEDGRVpiGRPIPNTRVYvldenLRPVPP-------GVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 465 rGEICLRGNTLFSGYHKREDLTKEVMVDGWFH-------TGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYL 537
Cdd:cd05930 292 -GELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALL 369
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 356575070 538 QCPLIAS---IWVYGNSFESFLVAVVVPERK------AIEDWAKEH 574
Cdd:cd05930 370 AHPGVREaavVAREDGDGEKRLVAYVVPDEGgeldeeELRAHLAER 415
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
77-566 |
3.65e-19 |
|
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: 90.81 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 77 WLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGPNA-VEFIINHAEVSIAFV 155
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 156 QEkKIPSVLSClaqcssnlktivsfgSVSTTQKKEAEGHGASCFSWGEflqlgcldwDLPSkkktDICTIMYTSGTTGDP 235
Cdd:cd12116 91 DD-ALPDRLPA---------------GLPVLLLALAAAAAAPAAPRTP---------VSPD----DLAYVIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 236 KGVVIKNEAF------MAEVLSV---DHIIMLTDrVAGEDDVYFSFLPL---AHVYDQIMETyciskgssigfwQGDVRF 303
Cdd:cd12116 142 KGVVVSHRNLvnflhsMRERLGLgpgDRLLAVTT-YAFDISLLELLLPLlagARVVIAPRET------------QRDPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 304 LLEDIQELKPTIfcgvprvfdriyagikskvssagpLQSTlfqcaynyklkylekglpqhkaaPLFDRLVFDKTKLALGG 383
Cdd:cd12116 209 LARLIEAHSITV------------------------MQAT-----------------------PATWRMLLDAGWQGRAG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 rVRILLSGAApLPRHVEEFMRVTSGStLSQGYGLTE----SCAGCFT-AIGDVysmtgTVGVPM--TTI---EARLESVP 453
Cdd:cd12116 242 -LTALCGGEA-LPPDLAARLLSRVGS-LWNLYGPTEttiwSTAARVTaAAGPI-----PIGRPLanTQVyvlDAALRPVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 454 EmgydalsNVPrGEICLRGNTLFSGYHKREDLTKEVMVDG--------WFHTGDIGEWQSNGAMKIIDRKKNIFKLsQGE 525
Cdd:cd12116 314 P-------GVP-GELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI-RGH 384
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 356575070 526 YIAVENIENKYLQCPLI--ASIWVYGNSFESFLVAVVVPERKA 566
Cdd:cd12116 385 RIELGEIEAALAAHPGVaqAAVVVREDGGDRRLVAYVVLKAGA 427
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
73-516 |
4.33e-19 |
|
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: 91.19 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACnsCAVSYVPLydTLGPNAVEFIINHAEvsi 152
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC--VLAGFVPA--PLTVPPTYDEPNARL--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 afvqeKKIPSVLSCLAQCssnlKTIVSFGSVSTTQKKEAE-GHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGT 231
Cdd:cd05906 108 -----RKLRHIWQLLGSP----VVLTDAELVAEFAGLETLsGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 232 TGDPKGVVIKNEAFMAEVLSVdhiimLTDRVAGEDDVYFSFLPLAHVydqimetyciskGSSIGFWQGDVRFLLEDIQEL 311
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGK-----IQHNGLTPQDVFLNWVPLDHV------------GGLVELHLRAVYLGCQQVHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 312 KPTIFCGVPRVFDRIYagiKSKVS-SAGPlqstlfQCAYNYKLKYLEKGLPQHkaaplFDRlvfdktklalgGRVRILLS 390
Cdd:cd05906 242 TEEILADPLRWLDLID---RYRVTiTWAP------NFAFALLNDLLEEIEDGT-----WDL-----------SSLRYLVN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 391 GAAPLPRHV-EEFMRVTSGSTLSQ-----GYGLTESCAGCFTAIGDVYSMTGT------VGVPMTTIEARLesVPEMGyD 458
Cdd:cd05906 297 AGEAVVAKTiRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSFPTYDHSQalefvsLGRPIPGVSMRI--VDDEG-Q 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 356575070 459 ALSNVPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGeWQSNGAMKIIDRKK 516
Cdd:cd05906 374 LLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
221-540 |
5.91e-19 |
|
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: 88.86 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLsvdhIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCI--SKGSSIGFWQ 298
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPD----ILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLihGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 299 GDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVssagplqstlfqcAYNYKLKYLEKGlpqhkaaplfdrlvfdktk 378
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSAN-------------ATVPSLRLIGYG------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 379 lalggrvrillsGAAPLPRHVEeFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESVPEMgyd 458
Cdd:cd17635 126 ------------GSRAIAADVR-FIEATGLTNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGI--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 459 ALSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQ 538
Cdd:cd17635 190 AGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEG 268
|
..
gi 356575070 539 CP 540
Cdd:cd17635 269 VS 270
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
221-549 |
6.06e-19 |
|
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: 88.33 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHvydqimeTYCISKGSSIGFWQG- 299
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT-----EDDRYLIINPFFH-------TFGYKAGIVACLLTGa 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 300 --------DVRFLLEDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLFQcaynyklkylekglpqhkaaPLFDR 371
Cdd:cd17638 69 tvvpvavfDVDAILEAIERERITVLPGPP----------------------TLFQ--------------------SLLDH 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 372 LVFDKTKLAlggRVRILLSGAAPLPRHVEEFMRVTSG-STLSQGYGLTESCAGCFTAIGD-VYSMTGTVGVPMTTIEARL 449
Cdd:cd17638 107 PGRKKFDLS---SLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVATMCRPGDdAETVATTCGRACPGFEVRI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 450 ESvpemgydalsnvpRGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIA 528
Cdd:cd17638 184 AD-------------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVY 249
|
330 340
....*....|....*....|.
gi 356575070 529 VENIENKYLQCPLIASIWVYG 549
Cdd:cd17638 250 PAEVEGALAEHPGVAQVAVIG 270
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
77-501 |
1.50e-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: 89.61 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 77 WLTYQDVYDAAMKMGSAIRSRGvNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVE---FIINHAEVSIA 153
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAErlaAILADAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 154 FVQEkkipSVLSCLAQCSSNLKTIVSFGSVSTTQKkeAEGHGAscfswgeflqlgclDWDLPSKKKTDICTIMYTSGTTG 233
Cdd:cd05931 103 LTTA----AALAAVRAFAASRPAAGTPRLLVVDLL--PDTSAA--------------DWPPPSPDPDDIAYLQYTSGSTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 234 DPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHvyDqiMetyciskgssigfwqGDVRFLLediqelkP 313
Cdd:cd05931 163 TPKGVVVTHRNLLANVRQIRRAYGLD-----PGDVVVSWLPLYH--D--M---------------GLIGGLL-------T 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 314 TIFCGVPRVFdriyagikskVSSAGPLQSTLFQcaynykLKYLEKGLPQHKAAPLFD-RLVFDKTK------LALgGRVR 386
Cdd:cd05931 212 PLYSGGPSVL----------MSPAAFLRRPLRW------LRLISRYRATISAAPNFAyDLCVRRVRdedlegLDL-SSWR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 387 ILLSGAAPL-PRHVEEFMRVTSG-----STLSQGYGLTESCagCFTAIGDVYSMTGTVGVPMTTIEARLESVPE------ 454
Cdd:cd05931 275 VALNGAEPVrPATLRRFAEAFAPfgfrpEAFRPSYGLAEAT--LFVSGGPPGTGPVVLRVDRDALAGRAVAVAAddpaar 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356575070 455 ----MGY----------DALSNVPR-----GEICLRGNTLFSGYHKREDLTKEVMV-------DGWFHTGDIG 501
Cdd:cd05931 353 elvsCGRplpdqevrivDPETGRELpdgevGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLG 425
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
196-547 |
5.74e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 87.73 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 196 ASCFSWGEFLQLG--CLD-WDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVdhIIMLTDRVAGEDdVYFSF 272
Cdd:PLN02330 157 EGAVNWKELLEAAdrAGDtSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS--LFSVGPEMIGQV-VTLGL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 273 LPLAHVYDqIMETYCIS---KGSSIGFWQGDVRFLLEdiqelkptifcgvprvfdriyAGIKSKVSSAGPLQSTLFQCAY 349
Cdd:PLN02330 234 IPFFHIYG-ITGICCATlrnKGKVVVMSRFELRTFLN---------------------ALITQEVSFAPIVPPIILNLVK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 350 NyklkylekglpqhkaaPLFDRlvFDKTKLALggrvRILLSGAAPL-PRHVEEFMRVTSGSTLSQGYGLTEScaGCFTAI 428
Cdd:PLN02330 292 N----------------PIVEE--FDLSKLKL----QAIMTAAAPLaPELLTAFEAKFPGVQVQEAYGLTEH--SCITLT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 429 -GDVYSMTG-----TVGVPMTTIEARLESvPEMGYDALSNVPrGEICLRGNTLFSGYH-KREDLTKEVMVDGWFHTGDIG 501
Cdd:PLN02330 348 hGDPEKGHGiakknSVGFILPNLEVKFID-PDTGRSLPKNTP-GELCVRSQCVMQGYYnNKEETDRTIDEDGWLHTGDIG 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 356575070 502 EWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIASIWV 547
Cdd:PLN02330 426 YIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
78-569 |
7.25e-18 |
|
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: 87.14 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSnLKTIVSFGSVSTTQKKEAeghGASCFSWGEFLQLGclDWDLPSKK-KTDICTIMYTSGTTGDPK 236
Cdd:TIGR03098 106 ERLDLLHPALPGCHD-LRTLIIVGDPAHASEGHP---GEEPASWPKLLALG--DADPPHPViDSDMAAILYTSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQG-DVRFLLEDIQELKPTI 315
Cdd:TIGR03098 180 GVVLSHRNLVAGAQSVATYLENR-----PDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYlLPRDVLKALEKHGITG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 316 FCGVPrvfdriyagikskvssagplqstlfqcaynyklkylekglpqhkaaPLFDRLVFDKTKLALGGRVRILLSGAAPL 395
Cdd:TIGR03098 255 LAAVP----------------------------------------------PLWAQLAQLDWPESAAPSLRYLTNSGGAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 396 PRHVEEFMR-VTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLesVPEMGYDALSNVPrGEICLRGNT 474
Cdd:TIGR03098 289 PRATLSRLRsFLPNARLFLMYGLTEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLV--LREDGSECAPGEE-GELVHRGAL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 475 LFSGYHKREDLTK----------------EVMVdgWfhTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQ 538
Cdd:TIGR03098 366 VAMGYWNDPEKTAerfrplppfpgelhlpELAV--W--SGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYA 440
|
490 500 510
....*....|....*....|....*....|....
gi 356575070 539 CPLIASIWVYGNSFESF---LVAVVVPERKAIED 569
Cdd:TIGR03098 441 TGLVAEAVAFGVPDPTLgqaIVLVVTPPGGEELD 474
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
221-522 |
9.20e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.13 E-value: 9.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHiiMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGD 300
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRA--LMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 VRFLLEDIQELKPTIFCGvprvfdriYAGIkskvssagplqSTLFQCAYNYklkylEKglpqhkaaplFDRLVFDKTKLA 380
Cdd:PRK05677 286 PRDLPAMVKELGKWKFSG--------FVGL-----------NTLFVALCNN-----EA----------FRKLDFSALKLT 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 381 LGGRVRILLSGAaplprhvEEFMRVTsGSTLSQGYGLTE-SCAGCFTAIGDVysMTGTVGVPMTTIEARLESvpemgyDA 459
Cdd:PRK05677 332 LSGGMALQLATA-------ERWKEVT-GCAICEGYGMTEtSPVVSVNPSQAI--QVGTIGIPVPSTLCKVID------DD 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356575070 460 LSNVPRGEI---CLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLS 522
Cdd:PRK05677 396 GNELPLGEVgelCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS 462
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
76-538 |
1.30e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.61 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 76 TWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFV 155
Cdd:PLN03102 38 TRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 156 Q---EKKIPSVLSCLAQCSSNLKTIVSF-GSVSTTQKKEAEGHGASCF-SWGE-----FLQLGCLdwdlpsKKKTDICTI 225
Cdd:PLN03102 118 DrsfEPLAREVLHLLSSEDSNLNLPVIFiHEIDFPKRPSSEELDYECLiQRGEptpslVARMFRI------QDEHDPISL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 226 MYTSGTTGDPKGVVIKNEAFMAEVLSVdhIIMLTdrvAGEDDVYFSFLPLAHVYDQIMeTYCISK--GSSIGFWQGDVRF 303
Cdd:PLN03102 192 NYTSGTTADPKGVVISHRGAYLSTLSA--IIGWE---MGTCPVYLWTLPMFHCNGWTF-TWGTAArgGTSVCMRHVTAPE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 304 LLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSsagplqstlfqcaynyklkylekglpqHKAAPlfdrlvfdktklalgg 383
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS---------------------------PRSGP---------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 rVRILLSGAAPLPRHVEEFMRVtsGSTLSQGYGLTESCAGC-FTAIGDVYS---------MTGTVGVPMTTiearLESVP 453
Cdd:PLN03102 303 -VHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVlFCEWQDEWNrlpenqqmeLKARQGVSILG----LADVD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 454 EMGYDALSNVPR-----GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIA 528
Cdd:PLN03102 376 VKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENIS 454
|
490
....*....|...
gi 356575070 529 ---VENIENKYLQ 538
Cdd:PLN03102 455 sveVENVLYKYPK 467
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
78-574 |
1.50e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 86.17 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSR-GVNPGDRCGIYGSNCPEWIIAMEAC-NSCAVsYVPLYDTLGPNAVEFIINHAEVSIAFV 155
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAIlRANAV-VVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 156 QEKKIPSVlsclAQCSSNL---KTIV-------------SFGSVSTTQKKEAEGHGASCFSWGEFLQLGcldwDLPSKKK 219
Cdd:PRK08314 115 GSELAPKV----APAVGNLrlrHVIVaqysdylpaepeiAVPAWLRAEPPLQALAPGGVVAWKEALAAG----LAPPPHT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 220 T---DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVydqimetyciskgssIGF 296
Cdd:PRK08314 187 AgpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST-----PESVVLAVLPLFHV---------------TGM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 297 WQGdvrfllediqeLKPTIFCG-----VPRvFDRiyagikskvSSAGPL----QSTLFQCAYNYKLKYLekglpqhkAAP 367
Cdd:PRK08314 247 VHS-----------MNAPIYAGatvvlMPR-WDR---------EAAARLieryRVTHWTNIPTMVVDFL--------ASP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 368 LFDRlvFDKTKLA-LGGrvrillsGAAPLPRHVEEFMRVTSGSTLSQGYGLTEScagcftaigdvysMTGTVGVPMTtiE 446
Cdd:PRK08314 298 GLAE--RDLSSLRyIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTET-------------MAQTHSNPPD--R 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 447 ARLE--SVPEMGYDA-------LSNVPR---GEICLRGNTLFSGYHKREDLTKEVMV--DG--WFHTGDIGEWQSNGAMK 510
Cdd:PRK08314 354 PKLQclGIPTFGVDArvidpetLEELPPgevGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 511 IIDRKKNI-----FKLSQGEyiaVENIENKY---LQCPLIASIWVY-GNSFEsflvAVVV--PERKA------IEDWAKE 573
Cdd:PRK08314 434 ITDRLKRMinasgFKVWPAE---VENLLYKHpaiQEACVIATPDPRrGETVK----AVVVlrPEARGktteeeIIAWARE 506
|
.
gi 356575070 574 H 574
Cdd:PRK08314 507 H 507
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
78-516 |
1.79e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 86.16 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTY----QDVYDAAmkmgSAIRSRGVNPGDRCGIYGSNCPEWIIAM---EACN-SCAVSyvPLydtLGPNAVEFIINHAE 149
Cdd:PRK07529 59 WTYaellADVTRTA----NLLHSLGVGPGDVVAFLLPNLPETHFALwggEAAGiANPIN--PL---LEPEQIAELLRAAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 150 VSI-----AFVQEKKIPSVLSCLAQCSsNLKTIVSFGS-------VSTTQKKEAEGHGASCFSWGEFL--QLGCLDWDLP 215
Cdd:PRK07529 130 AKVlvtlgPFPGTDIWQKVAEVLAALP-ELRTVVEVDLarylpgpKRLAVPLIRRKAHARILDFDAELarQPGDRLFSGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 216 SKKKTDICTIMYTSGTTGDPKGVVIK--NEAFMAEVLSvdhiiMLTDrvAGEDDVYFSFLPLAHV---YDQIMETycISK 290
Cdd:PRK07529 209 PIGPDDVAAYFHTGGTTGMPKLAQHThgNEVANAWLGA-----LLLG--LGPGDTVFCGLPLFHVnalLVTGLAP--LAR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 291 GSSIGF-----WQGD--VRFLLEDIQELKPTIFCGVPRVfdriYAGiKSKVSSAGPLQSTLfqcaynyklkylekglpqh 363
Cdd:PRK07529 280 GAHVVLatpqgYRGPgvIANFWKIVERYRINFLSGVPTV----YAA-LLQVPVDGHDISSL------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 364 kaaplfdrlvfdktklalggrvRILLSGAAPLPRHV-EEFMRVTsGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPM 442
Cdd:PRK07529 336 ----------------------RYALCGAAPLPVEVfRRFEAAT-GVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 443 TTIEARLESVPEMGyDALSNVPR---GEICLRGNTLFSGY---HKREDLTKEvmvDGWFHTGDIGEWQSNGAMKIIDRKK 516
Cdd:PRK07529 393 PYQRVRVVILDDAG-RYLRDCAVdevGVLCIAGPNVFSGYleaAHNKGLWLE---DGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
212-514 |
1.54e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 83.82 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 212 WDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHvydqimetyciSKG 291
Cdd:PRK08633 774 LYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLR-----NDDVILSSLPFFH-----------SFG 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 292 SSIGFW----QG----------DVRFLLEDIQELKPTIFCGVPrVFDRIYAgiKSKvssagplqstlfqcaynyklkyle 357
Cdd:PRK08633 838 LTVTLWlpllEGikvvyhpdptDALGIAKLVAKHRATILLGTP-TFLRLYL--RNK------------------------ 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 358 kglpqhKAAPL-FDRLvfdktklalggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTE-----SCAGCFTAIGDV 431
Cdd:PRK08633 891 ------KLHPLmFASL-------------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATEtspvaSVNLPDVLAADF 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 432 YSMT----GTVGVPMTTIEARLesV-PEmgydALSNVPRGE---ICLRGNTLFSGYHKREDLTKEVMVD----GWFHTGD 499
Cdd:PRK08633 952 KRQTgskeGSVGMPLPGVAVRI--VdPE----TFEELPPGEdglILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGD 1025
|
330
....*....|....*
gi 356575070 500 IGEWQSNGAMKIIDR 514
Cdd:PRK08633 1026 KGHLDEDGFLTITDR 1040
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
78-549 |
1.89e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.91 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSR-GVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQ 156
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 EKKIPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHgASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPK 236
Cdd:PRK05620 119 PRLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEG-IKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAEVLSvdhiIMLTDRVAGEDDVyfSFL---PLAHVydqimetycISKGSSIGFWQGdvrfllediqelkp 313
Cdd:PRK05620 198 GVVYSHRSLYLQSLS----LRTTDSLAVTHGE--SFLccvPIYHV---------LSWGVPLAAFMS-------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 314 tifcGVPRVF---DRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPQhkaaplfdrlvfdktKLALggrvRILLS 390
Cdd:PRK05620 249 ----GTPLVFpgpDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPE---------------RMSL----QEIYV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 391 GAAPLPRHVEEFMRVTSGSTLSQGYGLTEScagcftaigdvySMTGTVGVPMTTI--EARLESVPEMGY----------- 457
Cdd:PRK05620 306 GGSAVPPILIKAWEERYGVDVVHVWGMTET------------SPVGTVARPPSGVsgEARWAYRVSQGRfpasleyrivn 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 458 --DALSNVPR--GEICLRGNTLFSGY-----------------HKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKK 516
Cdd:PRK05620 374 dgQVMESTDRneGEIQVRGNWVTASYyhspteegggaastfrgEDVEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRAR 453
|
490 500 510
....*....|....*....|....*....|...
gi 356575070 517 NIFKlSQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:PRK05620 454 DVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
221-640 |
2.29e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 82.54 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSvdhiimltdRVA----GEDDVYFSFLPLAHV--YDQIMeTYCISKGSSI 294
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVQSLA---------KIAivgyGEDDVYLHTAPLCHIggLSSAL-AMLMVGACHV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 295 GFWQGDVRFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGplqstlFQCaynyklkylekglpqhkaaplfdrlvf 374
Cdd:PLN02860 243 LLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKV------FPS--------------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 375 dktklalggrVRILLSGAAPLP-RHVEEFMRVTSGSTLSQGYGLTESCAG-CFTAIGDVYSMTGTVGVPmTTIEARLESV 452
Cdd:PLN02860 290 ----------VRKILNGGGSLSsRLLPDAKKLFPNAKLFSAYGMTEACSSlTFMTLHDPTLESPKQTLQ-TVNQTKSSSV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 453 P--------------EMGYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKN 517
Cdd:PLN02860 359 HqpqgvcvgkpaphvELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKAGNLWLIGRSND 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 518 IFKlSQGEYIAVENIENKYLQCPLIASIWVYGNSfESFLVAVVVPERKAIEDWAKEHNLTDDFKslcdnlKARKHILDEL 597
Cdd:PLN02860 439 RIK-TGGENVYPEEVEAVLSQHPGVASVVVVGVP-DSRLTEMVVACVRLRDGWIWSDNEKENAK------KNLTLSSETL 510
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 356575070 598 NSTGQKHQLRGFELLKAIHLEPNPFDierdlITPTFKLKRPQL 640
Cdd:PLN02860 511 RHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
92-542 |
4.00e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 81.33 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 92 SAIRSRGVNPGDRCGIYGSNCPEWI-----IAMEACNSCAVsYVPLYDTLGPNAVEFIINHAEVSIAFVQEKKIPSVLSC 166
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTYIelsfaVAYAGGRLGLV-FVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 167 LAQCSSNlktivsfGSVSTTQKKEAEGHGASCFswgeflqlgcldwdlPSKKKtDICTIMYTSGTTGDPKGVVIKNEAFM 246
Cdd:cd05922 87 LPASPDP-------GTVLDADGIRAARASAPAH---------------EVSHE-DLALLLYTSGSTGSPKLVRLSHQNLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 247 AEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDQIMETYCISKGSSI----------GFWqgdvrfllEDIQELKPTIF 316
Cdd:cd05922 144 ANARSIAEYLGIT-----ADDRALTVLPLSYDYGLSVLNTHLLRGATLvltndgvlddAFW--------EDLREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 317 CGVPrvfdriyagikskvssagplqsTLFQcaynyklkylekglpqhkaapLFDRLVFDKTKLAlggRVRILLSGAAPLP 396
Cdd:cd05922 211 AGVP----------------------STYA---------------------MLTRLGFDPAKLP---SLRYLTQAGGRLP 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 397 RH-VEEFMRVTSGSTLSQGYGLTESCAGCFTAIGD-VYSMTGTVGVPMTtiEARLESVPEMGYDALSNVPrGEICLRGNT 474
Cdd:cd05922 245 QEtIARLRELLPGAQVYVMYGQTEATRRMTYLPPErILEKPGSIGLAIP--GGEFEILDDDGTPTPPGEP-GEIVHRGPN 321
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356575070 475 LFSGYHKRE-DLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQCPLI 542
Cdd:cd05922 322 VMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGLI 389
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
68-549 |
4.75e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 81.72 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 68 TESKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPE----WIIAMEACNSCAVsyvpLYDTLGPNAVEF 143
Cdd:PRK06018 30 TRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRhleaWYGIMGIGAICHT----VNPRLFPEQIAW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 144 IINHAEVSIAFVQEKKIPsVLSCLAQCSSNLKTIVSFGSVS----TTQK---------KEAEGHgascFSWGEFlqlgcl 210
Cdd:PRK06018 106 IINHAEDRVVITDLTFVP-ILEKIADKLPSVERYVVLTDAAhmpqTTLKnavayeewiAEADGD----FAWKTF------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 211 dwdlpskKKTDICTIMYTSGTTGDPKGVVIKNEAfmaevlSVDHIIMLTDRVA---GEDDVYFSFLPLAHVYDQIMETYC 287
Cdd:PRK06018 175 -------DENTAAGMCYTSGTTGDPKGVLYSHRS------NVLHALMANNGDAlgtSAADTMLPVVPLFHANSWGIAFSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 288 ISKGSSIGF--WQGDVRFLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKYLEkglpqhka 365
Cdd:PRK06018 242 PSMGTKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVWLML--------------------------LQYME-------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 366 aplfdrlvfdKTKLALGGRVRILLSGAApLPRH-VEEFmrVTSGSTLSQGYGLTEScagcftaigdvySMTGTVGV---P 441
Cdd:PRK06018 288 ----------KEGLKLPHLKMVVCGGSA-MPRSmIKAF--EDMGVEVRHAWGMTEM------------SPLGTLAAlkpP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 442 M--TTIEARLESVPEMGY-----------DALSNVPR-----GEICLRGNTLFSGYHKREDltKEVMVDGWFHTGDIGEW 503
Cdd:PRK06018 343 FskLPGDARLDVLQKQGYppfgvemkitdDAGKELPWdgktfGRLKVRGPAVAAAYYRVDG--EILDDDGFFDTGDVATI 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 356575070 504 QSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:PRK06018 421 DAYGYMRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
221-594 |
8.51e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 80.64 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVdHIIMLTDRVAGE------DDVYFSFLPLAHVYDQIMETYCISKGSSI 294
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQV-RACLSQLGPDGQplmkegQEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 295 GFWQGDVRFLLEDIQELKptifcgvprvfdriyagiKSKVSSAGPLqSTLFQCAYNYklkylekglpqhkaaPLFDRLVF 374
Cdd:PRK12492 287 NVLITNPRDIPGFIKELG------------------KWRFSALLGL-NTLFVALMDH---------------PGFKDLDF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 375 DKTKLALGGrvrillsGAAPLPRHVEEFMRVTsGSTLSQGYGLTE-SCAGCFTAIGDVySMTGTVGVPMTTieARLESVP 453
Cdd:PRK12492 333 SALKLTNSG-------GTALVKATAERWEQLT-GCTIVEGYGLTEtSPVASTNPYGEL-ARLGTVGIPVPG--TALKVID 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 454 EMGyDALSNVPRGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENI 532
Cdd:PRK12492 402 DDG-NELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFNVYPNEI 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356575070 533 ENKYLQCPLIASIWVYGnsfesflvavvVPERKAIED-----WAKEHNLT-DDFKSLC-DNL---KARKHIL 594
Cdd:PRK12492 480 EDVVMAHPKVANCAAIG-----------VPDERSGEAvklfvVARDPGLSvEELKAYCkENFtgyKVPKHIV 540
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
78-563 |
6.12e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 77.82 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINH--AEVSIAFV 155
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDsgARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 156 -----QEKKIPSVLSCLaqCSSNLKTIVSFGSVSTTQKKEAEGHgascFSWGEFLQLGCLdWDLPSKKKTDicTIMYTSG 230
Cdd:PRK12406 92 dllhgLASALPAGVTVL--SVPTPPEIAAAYRISPALLTPPAGA----IDWEGWLAQQEP-YDGPPVPQPQ--SMIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 231 TTGDPKGVviKNEAFMAEVLSvdhiimltdrvAGEDDVyfsflplAHVYDQIMETYCISKG-------SSIGFWQGDV-- 301
Cdd:PRK12406 163 TTGHPKGV--RRAAPTPEQAA-----------AAEQMR-------ALIYGLKPGIRALLTGplyhsapNAYGLRAGRLgg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 302 ------RF----LLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKylekgLPQHKaaplfdR 371
Cdd:PRK12406 223 vlvlqpRFdpeeLLQLIERHRITHMHMVPTMFIRL--------------------------LK-----LPEEV------R 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 372 LVFDKTKLalggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPmtTIEARLES 451
Cdd:PRK12406 266 AKYDVSSL------RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPGTVGKA--APGAELRF 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 452 VPEMGydalSNVPRGEIC-----LRGNTLFSgYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEY 526
Cdd:PRK12406 338 VDEDG----RPLPQGEIGeiysrIAGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVN 411
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 356575070 527 IAVENIENKYLQCPLIASIWVYGNSFESF---LVAVVVPE 563
Cdd:PRK12406 412 IYPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEPQ 451
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
225-549 |
3.10e-14 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 74.23 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 225 IMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHVYDQIMETYCISKG-SSIGFWQGDVRF 303
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLT-----EADVYLNMLPLFHIAGLNLALATFHAGgANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 304 LLEDIQELKPTIFCGVPrvfdriyagikskvssagPLQSTLFQCAynyklkylekglpqhkaaplfdrlvfDKTKLALGG 383
Cdd:cd17637 80 ALELIEEEKVTLMGSFP------------------PILSNLLDAA--------------------------EKSGVDLSS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 rvrilLSGAAPL--PRHVEEFMRVTsGSTLSQGYGLTEscAGCFTAIGDVYSMTGTVG--VPMTTIEArlesVPEMGYDa 459
Cdd:cd17637 116 -----LRHVLGLdaPETIQRFEETT-GATFWSLYGQTE--TSGLVTLSPYRERPGSAGrpGPLVRVRI----VDDNDRP- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 lsnVPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRK--KNIFKlSQGEYIAVENIEN 534
Cdd:cd17637 183 ---VPAgetGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEK 258
|
330
....*....|....*
gi 356575070 535 KYLQCPLIASIWVYG 549
Cdd:cd17637 259 VILEHPAIAEVCVIG 273
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
78-564 |
4.65e-14 |
|
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: 75.24 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPsvlsclAQCSSNLKTIVSFGSVSTtqkkeaeGHGASCfSWGEFLQLgcldwdlPSKKKTDICTIMYTSGTTGDPKG 237
Cdd:cd05923 109 DAQV------MDAIFQSGVRVLALSDLV-------GLGEPE-SAGPLIED-------PPREPEQPAFVFYTSGTTGLPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTdrvAGEDDVYFSFLPLAHVydqimetyciskgssIGFWQGDVRFLLEDiqelkpTIFC 317
Cdd:cd05923 168 AVIPQRAAESRVLFMSTQAGLR---HGRHNVVLGLMPLYHV---------------IGFFAVLVAALALD------GTYV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 318 gVPRVFDRIYAgikskvssagplqstlfqcaynykLKYLEK-------GLPQHkaaplFDRLV----FDKTKLAlggRVR 386
Cdd:cd05923 224 -VVEEFDPADA------------------------LKLIEQervtslfATPTH-----LDALAaaaeFAGLKLS---SLR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 387 ILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTEScagcFTAIGDVYSMTGTVGVPMTTIEARLESVPEMGYDALSNVPRG 466
Cdd:cd05923 271 HVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA----MNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 467 EIC--LRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIAS 544
Cdd:cd05923 347 ELIvaAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTE 425
|
490 500
....*....|....*....|...
gi 356575070 545 IWVYGNSFESF---LVAVVVPER 564
Cdd:cd05923 426 VVVIGVADERWgqsVTACVVPRE 448
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-574 |
6.57e-14 |
|
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: 73.67 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVVIK--NEAFMAEVLSVDHIImltdrvaGEDDVYFSFLPLAHV---YDQIMETycISKGSSIG 295
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHThsNEVYNAWMLALNSLF-------DPDDVLLCGLPLFHVngsVVTLLTP--LASGAHVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 296 F-----WQGDVRF--LLEDIQELKPTIFCGVPRVFdriyagikskvssagplqSTLFQCAYNYKLKYLekglpqhkaapl 368
Cdd:cd05944 74 LagpagYRNPGLFdnFWKLVERYRITSLSTVPTVY------------------AALLQVPVNADISSL------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 369 fdrlvfdktklalggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEAR 448
Cdd:cd05944 124 -----------------RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVR 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 449 LESVpemgyDALSNVPR-------GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkL 521
Cdd:cd05944 187 IKVL-----DGVGRLLRdcapdevGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-I 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356575070 522 SQGEYIAVENIENKYLQCPLIASIWVYG--NSFESFL-VAVV--VP----ERKAIEDWAKEH 574
Cdd:cd05944 261 RGGHNIDPALIEEALLRHPAVAFAGAVGqpDAHAGELpVAYVqlKPgavvEEEELLAWARDH 322
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
78-507 |
6.94e-14 |
|
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: 75.66 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMeacnsCAV-----SYVPLyDTLGPNA-VEFIINHAEVS 151
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVAL-----LAVlkagaAYVPL-DPAYPAErLAYMLEDAGAR 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 152 IAFVQEkkipSVLSCLAqcssnlktivsfgsvsttqkkeaeGHGASCFSWGEFLQLGCLDWDLPSK-KKTDICTIMYTSG 230
Cdd:COG1020 576 LVLTQS----ALAARLP------------------------ELGVPVLALDALALAAEPATNPPVPvTPDDLAYVIYTSG 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 231 TTGDPKGVVIKNEAF------MAEVLSVDHiimlTDRVAGeddvyFS-----------FLPLA-----HVYDQImetyci 288
Cdd:COG1020 628 STGRPKGVMVEHRALvnllawMQRRYGLGP----GDRVLQ-----FAslsfdasvweiFGALLsgatlVLAPPE------ 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 289 skgssigfWQGDVRFLLEDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLFQcaynyklkylekGLPQHKAAPL 368
Cdd:COG1020 693 --------ARRDPAALAELLARHRVTVLNLTP----------------------SLLR------------ALLDAAPEAL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 369 fdrlvfdktklalgGRVR-ILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGC-FTAIGDVYSMTGTV--GVPM-- 442
Cdd:COG1020 731 --------------PSLRlVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDStYYEVTPPDADGGSVpiGRPIan 796
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 443 TTIE---ARLESVPEmgydalsNVPrGEICLRGNTLFSGYHKREDLTKEVMVDG--------WFHTGDIGEWQSNG 507
Cdd:COG1020 797 TRVYvldAHLQPVPV-------GVP-GELYIGGAGLARGYLNRPELTAERFVADpfgfpgarLYRTGDLARWLPDG 864
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
78-549 |
2.00e-13 |
|
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: 72.92 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvSTTQKKEAEghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd05969 81 --------------------------ELYERTDPE----------------------------DPTLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTDrvageDDVYFS--------------FLPLAHvydqimetyciskGSSIGFWQG--DV 301
Cdd:cd05969 107 VLHVHDAMIFYYFTGKYVLDLHP-----DDIYWCtadpgwvtgtvygiWAPWLN-------------GVTNVVYEGrfDA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 302 RFLLEDIQELKPTIFCGVPRVFDRIyagiksKVSSAGPLQStlfqcaynYKLKYLekglpqhkaaplfdrlvfdktklal 381
Cdd:cd05969 169 ESWYGIIERVKVTVWYTAPTAIRML------MKEGDELARK--------YDLSSL------------------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 382 ggrvRILLSGAAPL-PRHVEEFMRVTsGSTLSQGYGLTESCAgcfTAIGDVYSM---TGTVGVPMTTIEARLesVPEMGy 457
Cdd:cd05969 210 ----RFIHSVGEPLnPEAIRWGMEVF-GVPIHDTWWQTETGS---IMIANYPCMpikPGSMGKPLPGVKAAV--VDENG- 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 458 DALSNVPRGEICLRGN--TLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENK 535
Cdd:cd05969 279 NELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESA 357
|
490
....*....|....
gi 356575070 536 YLQCPLIASIWVYG 549
Cdd:cd05969 358 LMEHPAVAEAGVIG 371
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
69-563 |
3.45e-13 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 71.96 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 69 ESKLGSytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLydtlgpnavefiinha 148
Cdd:cd17653 17 ESLGGS---LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 149 evsiafvqEKKIPSVlsclaqcssNLKTIVSfgsvsTTQKKeaeghgascfswgeFLqlgcldwdLPSKKKTDICTIMYT 228
Cdd:cd17653 78 --------DAKLPSA---------RIQAILR-----TSGAT--------------LL--------LTTDSPDDLAYIIFT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 229 SGTTGDPKGVVIKNEAFMAEVLSVDHIIMLT--DRVAgeddvyfsflplahvydQIMetyciskgsSIGFWqgdvrflle 306
Cdd:cd17653 114 SGSTGIPKGVMVPHRGVLNYVSQPPARLDVGpgSRVA-----------------QVL---------SIAFD--------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 diqelkptifCGVPRVFDRI-YAGIKSKVSSAGPLQSTLFQCAYnyklkylekgLPqhkAAPLF----DRLVFDKTKlal 381
Cdd:cd17653 159 ----------ACIGEIFSTLcNGGTLVLADPSDPFAHVARTVDA----------LM---STPSIlstlSPQDFPNLK--- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 382 ggrvRILLSGAAPLPRHVEEFmrvTSGSTLSQGYGLTESCAGCFTA---IGDVYSMTGTV-GVPMTTIEARLESVPEMgy 457
Cdd:cd17653 213 ----TIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTECTISSTMTellPGQPVTIGKPIpNSTCYILDADLQPVPEG-- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 458 dalsnvPRGEICLRGNTLFSGYHKREDLTKEVMV-----DGW--FHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVE 530
Cdd:cd17653 284 ------VVGEICISGVQVARGYLGNPALTASKFVpdpfwPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLE 356
|
490 500 510
....*....|....*....|....*....|....*.
gi 356575070 531 NIENK-YLQCPLI--ASIWVYGNsfesFLVAVVVPE 563
Cdd:cd17653 357 EIEEVvLQSQPEVtqAAAIVVNG----RLVAFVTPE 388
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
78-574 |
4.91e-13 |
|
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: 71.98 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGP-NAVEFIINHAEVSIAFVQ 156
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPeERIQYILEDSGADILLTQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 EKkipsvlscLAQCSSNLKTIVSFGSvSTTQKKEAEghgascfswgeflqlgcldwDL-PSKKKTDICTIMYTSGTTGDP 235
Cdd:cd17655 102 SH--------LQPPIAFIGLIDLLDE-DTIYHEESE--------------------NLePVSKSDDLAYVIYTSGSTGKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 236 KGVVIKNEAFMAEVLSVDHIIMLT--DRVAgeddvyfsflplahvydQImetyciskgSSIGFwqgDVrflleDIQELKP 313
Cdd:cd17655 153 KGVMIEHRGVVNLVEWANKVIYQGehLRVA-----------------LF---------ASISF---DA-----SVTEIFA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 314 TIFCGvprvfDRIYAGIKSKVSSAGPLQSTLFQcaynYKLKyLEKGLPQHKAaplfdrlVFDKTKLALGGRVRILLSGAA 393
Cdd:cd17655 199 SLLSG-----NTLYIVRKETVLDGQALTQYIRQ----NRIT-IIDLTPAHLK-------LLDAADDSEGLSLKHLIVGGE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 394 PLPRHVEE--FMRVTSGSTLSQGYGLTESCAGCftAIGDVYSMTGT-----VGVP-----MTTIEARLESVPEmgydals 461
Cdd:cd17655 262 ALSTELAKkiIELFGTNPTITNAYGPTETTVDA--SIYQYEPETDQqvsvpIGKPlgntrIYILDQYGRPQPV------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 462 NVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWF-------HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIEN 534
Cdd:cd17655 333 GVA-GELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEA 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 356575070 535 KYLQCPLI---ASIWVYGNSFESFLVAVVVPER----KAIEDWAKEH 574
Cdd:cd17655 411 RLLQHPDIkeaVVIARKDEQGQNYLCAYIVSEKelpvAQLREFLARE 457
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
78-566 |
1.08e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 71.07 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQ- 156
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDa 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 157 ----EKKIPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGAScfswgeflqlgcldwDLPSKKKTDICTIMYTSGTT 232
Cdd:PRK05852 124 dgphDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPAT---------------STPEGLRPDDAMIMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 233 GDPKGVVIKNEAFMAEVLSVDHIIMLTDRvagedDVYFSFLPLAHVYDQI--METYCISKG----------SSIGFWqgd 300
Cdd:PRK05852 189 GLPKMVPWTHANIASSVRAIITGYRLSPR-----DATVAVMPLYHGHGLIaaLLATLASGGavllpargrfSAHTFW--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 vrfllEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPlqstlfqcaynyklkylekglpqhkaAPLfdrlvfdktkla 380
Cdd:PRK05852 261 -----DDIKAVGATWYTAVPTIHQILLERAATEPSGRKP--------------------------AAL------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 381 lggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFT----AIGDVYSMTGTVGVPMTTIEARLESVpemG 456
Cdd:PRK05852 298 -----RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTtqieGIGQTENPVVSTGLVGRSTGAQIRIV---G 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 457 YDALSNVPR--GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIEN 534
Cdd:PRK05852 370 SDGLPLPAGavGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEG 448
|
490 500 510
....*....|....*....|....*....|....*
gi 356575070 535 KYLQCPLIASIWVYGNSFESF---LVAVVVPERKA 566
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESA 483
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
79-534 |
1.25e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.51 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACN-SCAVSYVpLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSgSGAVCHT-INPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCssnlKTIVSFGSVSTTQKKEAEGHGASCF-SWGEfLQLGCLDWdlPSKKKTDICTIMYTSGTTGDPK 236
Cdd:PRK07008 120 TFLPLVDALAPQC----PNVKGWVAMTDAAHLPAGSTPLLCYeTLVG-AQDGDYDW--PRFDENQASSLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFM--AEVLSVDHIIMLTDRvagedDVYFSFLPLAHVYDQIMETYCISKGSSIGFwQG---DVRFLLEDIQEL 311
Cdd:PRK07008 193 GALYSHRSTVlhAYGAALPDAMGLSAR-----DAVLPVVPMFHVNAWGLPYSAPLTGAKLVL-PGpdlDGKSLYELIEAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 312 KPTIFCGVPRVfdriYAGIKSKVSSAGPLQSTLfqcaynyklkylekglpqhkaaplfdrlvfdktklalggrVRILLSG 391
Cdd:PRK07008 267 RVTFSAGVPTV----WLGLLNHMREAGLRFSTL----------------------------------------RRTVIGG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 392 AAPLPRHVEEFMRVTsGSTLSQGYGLTEscagcFTAIGDVYSMT------------------GTV--GVPMTTIEARLES 451
Cdd:PRK07008 303 SACPPAMIRTFEDEY-GVEVIHAWGMTE-----MSPLGTLCKLKwkhsqlpldeqrkllekqGRViyGVDMKIVGDDGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 452 VPEMGydalsnVPRGEICLRGNTLFSGYHKREDltkEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVEN 531
Cdd:PRK07008 377 LPWDG------KAFGDLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSID 446
|
...
gi 356575070 532 IEN 534
Cdd:PRK07008 447 IEN 449
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
79-607 |
1.37e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 70.20 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVN-PGDRCGIYGSNCPEWI---IAMEACNSCAVSYVPLydtLGPNAVEFIINHAEVSIAF 154
Cdd:cd05958 12 TYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVacwFGIQKAGAIAVATMPL---LRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 VQEKkipsvlsclaqcssnlktivsfgsVSTTQkkeaeghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGD 234
Cdd:cd05958 89 CAHA------------------------LTASD---------------------------------DICILAFTSGTTGA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVV--IKNEAFMAEVLSVdHIIMLTdrvagEDDVYFSFLPLAHVYDQ-IMETYCISKGSS-IGFWQGDVRFLLEDIQE 310
Cdd:cd05958 112 PKATMhfHRDPLASADRYAV-NVLRLR-----EDDRFVGSPPLAFTFGLgGVLLFPFGVGASgVLLEEATPDLLLSAIAR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 311 LKPTIFCGVPRVfdriYAGIKSKVSSAGPLQSTLFQCaynyklkylekglpqhkaaplfdrlvfdktklalggrvrilLS 390
Cdd:cd05958 186 YKPTVLFTAPTA----YRAMLAHPDAAGPDLSSLRKC-----------------------------------------VS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 391 GAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDvYSMTGTVGVPMTTIEARLesVPEMGYDalsnVPRGEI-- 468
Cdd:cd05958 221 AGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPG-DARPGATGKPVPGYEAKV--VDDEGNP----VPDGTIgr 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 469 -CLRGNTlfsGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQCPLIASIW 546
Cdd:cd05958 294 lAVRGPT---GCRYLADKRQRTYVqGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECA 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 547 VYGNSFESFLV---AVVVPERKAIEDWAKEHNLTDDFKSLCDNLKARKHI--LDEL--NSTG--QKHQLR 607
Cdd:cd05958 370 VVGHPDESRGVvvkAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIefVTELprTATGklQRFALR 439
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
36-549 |
2.34e-12 |
|
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: 69.83 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 36 LEVPSDFKSPWDFFRDSVKRNPNNN-MLGRRQKTESKLGSYTWLTYQdvydaAMKMGSAIRSRGVNPGDRCGIYGSNCPE 114
Cdd:cd05970 10 INVPENFNFAYDVVDAMAKEYPDKLaLVWCDDAGEERIFTFAELADY-----SDKTANFFKAMGIGKGDTVMLTLKRRYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 115 WIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVS-IAFVQEKKIPSVL-SCLAQCSSNLKTIVSFGSVsttqkkeAE 192
Cdd:cd05970 85 FWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKmIVAIAEDNIPEEIeKAAPECPSKPKLVWVGDPV-------PE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 193 GhgascfsWGEFLQL---GCLDWDLP----SKKKTDICTIMYTSGTTGDPKgvvikneafMAEVlsvDHIIMLTDRVAG- 264
Cdd:cd05970 158 G-------WIDFRKLiknASPDFERPtansYPCGEDILLVYFSSGTTGMPK---------MVEH---DFTYPLGHIVTAk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 265 ------EDDVYFSFLPLA-------HVYDQIMetycisKGSSIGFWQGDvRF----LLEDIQELKPTIFCGVPRVFDRIy 327
Cdd:cd05970 219 ywqnvrEGGLHLTVADTGwgkavwgKIYGQWI------AGAAVFVYDYD-KFdpkaLLEKLSKYGVTTFCAPPTIYRFL- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 328 agIKSKVSsagplqstlfqcayNYKLKYLEKGLpqhkaaplfdrlvfdktklalggrvrillSGAAPLPRHVEEFMRVTS 407
Cdd:cd05970 291 --IREDLS--------------RYDLSSLRYCT-----------------------------TAGEALNPEVFNTFKEKT 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 408 GSTLSQGYGLTEscagCFTAIGDVYSMT---GTVGVPMttiearlesvPEMGYDAL----SNVP---RGEICLRGNT--- 474
Cdd:cd05970 326 GIKLMEGFGQTE----TTLTIATFPWMEpkpGSMGKPA----------PGYEIDLIdregRSCEageEGEIVIRTSKgkp 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356575070 475 --LFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:cd05970 392 vgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
73-562 |
2.72e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 69.72 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIIN------ 146
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDdsgara 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 147 ----HAEVSIAFVQEKKIPSVLSCL-AQCSSNLKTIVSFGSVSTtqkkeaeghgascfswgeflqlGCLDWDLPSKKKTD 221
Cdd:PRK13391 100 litsAAKLDVARALLKQCPGVRHRLvLDGDGELEGFVGYAEAVA----------------------GLPATPIADESLGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 222 icTIMYTSGTTGDPKGVVIK-NEAFMAEVLSVDHIIMLTDRVaGEDDVYFSFLPLAHVYDQIMETYCISKG-SSIGFWQG 299
Cdd:PRK13391 158 --DMLYSSGTTGRPKGIKRPlPEQPPDTPLPLTAFLQRLWGF-RSDMVYLSPAPLYHSAPQRAVMLVIRLGgTVIVMEHF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 300 DVRFLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKylekgLPQHKaaplfdRLVFDKTKL 379
Cdd:PRK13391 235 DAEQYLALIEEYGVTHTQLVPTMFSRM--------------------------LK-----LPEEV------RDKYDLSSL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 380 alggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIearLESVPEMGYDA 459
Cdd:PRK13391 278 ------EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGD---LHILDDDGAEL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 LSNVPrGEICLRGNTLFSgYHKREDLTKEVMVD--GWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYL 537
Cdd:PRK13391 349 PPGEP-GTIWFEGGRPFE-YLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLI 425
|
490 500
....*....|....*....|....*...
gi 356575070 538 QCPLIASIWVYGNSFESF---LVAVVVP 562
Cdd:PRK13391 426 THPKVADAAVFGVPNEDLgeeVKAVVQP 453
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
221-529 |
4.71e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 69.14 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKGVV------IKNEAFMAEVLSVDHIimltdrvagEDDVYFSFLPLAHVYdqimetyciskGSSI 294
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAVInthrmlCANQQMLAQTFPFLAE---------EPPVLVDWLPWNHTF-----------GGNH 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 295 GFwqGDV-----------------RF--LLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKY 355
Cdd:PRK08180 270 NL--GIVlynggtlyiddgkptpgGFdeTLRNLREISPTVYFNVPKGWEML--------------------------VPA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 356 LEK--GLpqhkAAPLFdrlvfdktklalgGRVRILLSGAAPLPRHV-EEFMRVTSGST-----LSQGYGLTEScAGCFTA 427
Cdd:PRK08180 322 LERdaAL----RRRFF-------------SRLKLLFYAGAALSQDVwDRLDRVAEATCgerirMMTGLGMTET-APSATF 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 428 IGDVYSMTGTVGVPMTTIEARLesVPEMGydalsnvpRGEICLRGNTLFSGYHKREDLTKEVMVD-GWFHTGDigewqsn 506
Cdd:PRK08180 384 TTGPLSRAGNIGLPAPGCEVKL--VPVGG--------KLEVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGD------- 446
|
330 340 350
....*....|....*....|....*....|....*
gi 356575070 507 gAMKIID------------RKKNIFKLSQGEYIAV 529
Cdd:PRK08180 447 -AVRFVDpadperglmfdgRIAEDFKLSSGTWVSV 480
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
78-571 |
1.06e-11 |
|
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: 67.49 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQe 157
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkKTDICTIMYTSGTTGDPKG 237
Cdd:cd17650 92 -------------------------------------------------------------PEDLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEafmaevlSVDHIIMLTDRVAGEDDVYFSFLPLAHV-YDQIMETYCIS--KGSSIGFWQGDVRF----LLEDIQE 310
Cdd:cd17650 111 VMVEHR-------NVAHAAHAWRREYELDSFPVRLLQMASFsFDVFAGDFARSllNGGTLVICPDEVKLdpaaLYDLILK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 311 LKPTIFCGVPRVfdriyagikskvssAGPLqstlfqcaynykLKYLEKglpqHKAAPLFDRLVfdktklalggrvrILLS 390
Cdd:cd17650 184 SRITLMESTPAL--------------IRPV------------MAYVYR----NGLDLSAMRLL-------------IVGS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 391 GAAPLPRHVEEFMRVTSGSTLSQGYGLTESC--AGCF--TAIGDVYSMTGTVGVP-----MTTIEARLESVPEMGYdals 461
Cdd:cd17650 221 DGCKAQDFKTLAARFGQGMRIINSYGVTEATidSTYYeeGRDPLGDSANVPIGRPlpntaMYVLDERLQPQPVGVA---- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 462 nvprGEICLRGNTLFSGYHKREDLTKEVMVDGWF-------HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIEN 534
Cdd:cd17650 297 ----GELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIES 371
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 356575070 535 KYLQCPLIASIWV---YGNSFESFLVAVVVPERKAieDWA 571
Cdd:cd17650 372 QLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTA 409
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
216-533 |
3.59e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 66.27 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 216 SKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRvagedDVYFSFLPLAHVYdqimetyciskGSSIG 295
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPN-----DRFMSALPLFHSF-----------GLTVG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 296 FwqgdvrfllediqeLKPtIFCGVpRVFdriyagikskvssagplqstLFQCAYNYKLkylekgLPQhkaaplfdrLVFD 375
Cdd:PRK08043 425 L--------------FTP-LLTGA-EVF--------------------LYPSPLHYRI------VPE---------LVYD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 376 K-------TKLALG-----------GRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTEsCAGCFTAIGDVYSMTGT 437
Cdd:PRK08043 454 RnctvlfgTSTFLGnyarfanpydfARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGT 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 438 VGVPMTTIEARLESVP--EMGydalsnvprGEICLRGNTLFSGYHKRE----------DLTKEVMVDGWFHTGDIGEWQS 505
Cdd:PRK08043 533 VGRILPGMDARLLSVPgiEQG---------GRLQLKGPNIMNGYLRVEkpgvlevptaENARGEMERGWYDTGDIVRFDE 603
|
330 340
....*....|....*....|....*...
gi 356575070 506 NGAMKIIDRKKNIFKLSqGEYIAVENIE 533
Cdd:PRK08043 604 QGFVQIQGRAKRFAKIA-GEMVSLEMVE 630
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
78-562 |
6.67e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.92 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSNLKTIVSFGSvsttqkkEAEGHGascfSWGEFLQlGCLDWDLPSKkkTDICTIMYTSGTTGDPKG 237
Cdd:PRK08276 92 ALADTAAELAAELPAGVPLLLVVAG-------PVPGFR----SYEEALA-AQPDTPIADE--TAGADMLYSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 vvIKNEAF---MAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAH----VYDQ----------IMETYciskgssigfwqgD 300
Cdd:PRK08276 158 --IKRPLPgldPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHtaplRFGMsalalggtvvVMEKF-------------D 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 301 VRFLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKylekgLPQHKaaplfdRLVFDKTKLa 380
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRM--------------------------LK-----LPEEV------RARYDVSSL- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 381 lggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTtieARLESVPEMGydal 460
Cdd:PRK08276 265 -----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDWLAHPGSVGKAVL---GEVRILDEDG---- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 461 SNVPRGEICL----RGNTLFSgYHKREDLTKEVMVD-GWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENK 535
Cdd:PRK08276 333 NELPPGEIGTvyfeMDGYPFE-YHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVNIYPQEIENL 410
|
490 500 510
....*....|....*....|....*....|
gi 356575070 536 YLQCPLIASIWVYGNSFESF---LVAVVVP 562
Cdd:PRK08276 411 LVTHPKVADVAVFGVPDEEMgerVKAVVQP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
78-566 |
7.78e-11 |
|
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: 64.98 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlSCLAQCSSNLKTIVSFGSVSTTqkkeaeghgascfswgeflqlgcldWDLPSKKK---TDICTIMYTSGTTGD 234
Cdd:cd12114 93 -------PDAQLDVAVFDVLILDLDALAA-------------------------PAPPPPVDvapDDLAYVIFTSGSTGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNEAFMAEVLSVdhiimlTDRVA-GEDDVYFSFLPLAH---VYDqIMETycISKGSSIGF----WQGDVRFLLE 306
Cdd:cd12114 141 PKGVMISHRAALNTILDI------NRRFAvGPDDRVLALSSLSFdlsVYD-IFGA--LSAGATLVLpdeaRRRDPAHWAE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 DIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqCAYnyklkylekgLPQHKAAPLFDRLVF---DKTKLALGG 383
Cdd:cd12114 212 LIERHGVTLWNSVPALLEML--------------------LDV----------LEAAQALLPSLRLVLlsgDWIPLDLPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 RVRILLSGAAPlprhveefmrvtsgstLSQGyGLTEscagcfTAIGDVYSMTGTV---------GVPMTTIEARLesVPE 454
Cdd:cd12114 262 RLRALAPDARL----------------ISLG-GATE------ASIWSIYHPIDEVppdwrsipyGRPLANQRYRV--LDP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 455 MGYDALSNVPrGEICLRGNTLFSGYHKREDLTKEVMVD-----GWFHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAV 529
Cdd:cd12114 317 RGRDCPDWVP-GELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIEL 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 356575070 530 ENIENKYLQCPLI--ASIWVYGNSFESFLVAVVVPERKA 566
Cdd:cd12114 395 GEIEAALQAHPGVarAVVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
78-569 |
7.85e-11 |
|
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: 64.67 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGPnavefiinhAEvSIAFVQE 157
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL-DPAYP---------AE-RLAFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLscLAQcssnlkTIVSFGSvsttqkkEAEGHGASCFSWGEFLQLGCLDWDLPsKKKTDICTIMYTSGTTGDPKG 237
Cdd:cd17651 90 DAGPVLV--LTH------PALAGEL-------AVELVAVTLLDQPGAAAGADAEPDPA-LDADDLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEafmaevlsvdhiiMLTDRVAGEDdVYFSFLPLAHVydqimetyciSKGSSIGFwqgDVRFllediQELKPTIFC 317
Cdd:cd17651 154 VVMPHR-------------SLANLVAWQA-RASSLGPGART----------LQFAGLGF---DVSV-----QEIFSTLCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 318 GVPRVFDRiyagikskvSSAGPLQSTLfqcaynykLKYLEKGLPQHKAAP--LFDRLVFDKTKL-ALGGRVRILLSGAAP 394
Cdd:cd17651 202 GATLVLPP---------EEVRTDPPAL--------AAWLDEQRISRVFLPtvALRALAEHGRPLgVRLAALRYLLTGGEQ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 395 LPRH--VEEFMRVTSGSTLSQGYGLTES---CAGCFTAIGDVYSMTGTVGVPMTTIE-----ARLESVPemgydalSNVP 464
Cdd:cd17651 265 LVLTedLREFCAGLPGLRLHNHYGPTEThvvTALSLPGDPAAWPAPPPIGRPIDNTRvyvldAALRPVP-------PGVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 465 rGEICLRGNTLFSGYHKREDLTKEVMVDGWF-------HTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYL 537
Cdd:cd17651 338 -GELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALA 415
|
490 500 510
....*....|....*....|....*....|....*
gi 356575070 538 QCPLIASIWVYG---NSFESFLVAVVVPERKAIED 569
Cdd:cd17651 416 RHPGVREAVVLAredRPGEKRLVAYVVGDPEAPVD 450
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
414-542 |
8.02e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 64.51 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 414 GYGLTES----CAgcftaigDVYSMTGTVGVPMTTIEARLESvpemgydalsnvprGEICLRGNTLFSGYHKREDLTKEV 489
Cdd:PRK09029 270 GYGLTEMastvCA-------KRADGLAGVGSPLPGREVKLVD--------------GEIWLRGASLALGYWRQGQLVPLV 328
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 356575070 490 MVDGWFHTGDIGEWQsNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLI 542
Cdd:PRK09029 329 NDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLV 379
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
79-549 |
8.72e-11 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 64.38 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 79 TYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIA-MEACNSCAVSyVPLYDTLGPNAVEFIINHAEVSiafvqe 157
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAhIAILRSGAIA-VPLFALFGPEALEYRLSNSGAS------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlgCLDWDLPSkkktDICTIMYTSGTTGDPKG 237
Cdd:cd05971 81 ---------------------------------------------------ALVTDGSD----DPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTDRvagEDDVYFSFLPLAhvydqimetyciskgssigfWQGDvrflLEDIqeLKPTIFC 317
Cdd:cd05971 106 ALHAHRVLLGHLPGVQFPFNLFPR---DGDLYWTPADWA--------------------WIGG----LLDV--LLPSLYF 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 318 GVPRV------FD--RIYAGIKSKVSSAGPLQSTLfqcaynykLKYLEKGLPQHKAAPLfdrlvfdktklalggRVRILL 389
Cdd:cd05971 157 GVPVLahrmtkFDpkAALDLMSRYGVTTAFLPPTA--------LKMMRQQGEQLKHAQV---------------KLRAIA 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 390 SGAAPLPRHVEEFMRVTSGSTLSQGYGLTE------SCAGCFTAigdvysMTGTVGVPMTTIEARLESvpemgyDALSNV 463
Cdd:cd05971 214 TGGESLGEELLGWAREQFGVEVNEFYGQTEcnlvigNCSALFPI------KPGSMGKPIPGHRVAIVD------DNGTPL 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 464 P---RGEICLR--GNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQ 538
Cdd:cd05971 282 PpgeVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLK 360
|
490
....*....|.
gi 356575070 539 CPLIASIWVYG 549
Cdd:cd05971 361 HPAVLMAAVVG 371
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
217-572 |
9.98e-11 |
|
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: 64.43 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 217 KKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAHvydqimetyciskgsSIGF 296
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK-----TKDRILSWMPLTH---------------DMGL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 297 WQGDVRFLLEDIQE-LKPTifcgvpRVFDR-----IYAGIKSKVSSAgplqstlfqCAYNYKLKYLEKGLPQHKAAPlfd 370
Cdd:cd05908 163 IAFHLAPLIAGMNQyLMPT------RLFIRrpilwLKKASEHKATIV---------SSPNFGYKYFLKTLKPEKAND--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 371 rlvFDKTKlalggrVRILLSGAAP-LPRHVEEFMRVTSGSTLSQG-----YGLTESCAGC---------FTAIGDVYSMT 435
Cdd:cd05908 225 ---WDLSS------IRMILNGAEPiDYELCHEFLDHMSKYGLKRNailpvYGLAEASVGAslpkaqspfKTITLGRRHVT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 436 GTVGVPMTT-IEARLESVPEMGYdALSN------------VPR---GEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTG 498
Cdd:cd05908 296 HGEPEPEVDkKDSECLTFVEVGK-PIDEtdiricdednkiLPDgyiGHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 499 DIGeWQSNGAMKIIDRKKN-IFKLSQGEY------IAVENIEnkyLQCPLIASIWVYGNSFESFLVAVVVPERKAIEDWA 571
Cdd:cd05908 375 DLG-FIRNGRLVITGREKDiIFVNGQNVYphdierIAEELEG---VELGRVVACGVNNSNTRNEEIFCFIEHRKSEDDFY 450
|
.
gi 356575070 572 K 572
Cdd:cd05908 451 P 451
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
74-245 |
1.34e-10 |
|
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: 64.52 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 74 SYTWlTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSI- 152
Cdd:cd17634 82 SRTI-SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLl 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 ----AFVQEKKIPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYT 228
Cdd:cd17634 161 itadGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYT 240
|
170
....*....|....*..
gi 356575070 229 SGTTGDPKGVVIKNEAF 245
Cdd:cd17634 241 SGTTGKPKGVLHTTGGY 257
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
78-239 |
1.90e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 63.75 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC-NSCAVS------YVP-----LYDTLGPNAVefiI 145
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAfKARAVPvnvnyrYVEdelryLLDDSDAVAL---V 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 146 NHAEVSiafvqekkiPSVLSCLAQCsSNLKTIVSFGSVSTtqkkEAEGHGAscFSWGEFLQLGCLDWDLPSKKKTDIcTI 225
Cdd:PRK07798 106 YEREFA---------PRVAEVLPRL-PKLRTLVVVEDGSG----NDLLPGA--VDYEDALAAGSPERDFGERSPDDL-YL 168
|
170
....*....|....
gi 356575070 226 MYTSGTTGDPKGVV 239
Cdd:PRK07798 169 LYTGGTTGMPKGVM 182
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
72-602 |
2.24e-10 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 63.62 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 72 LGSytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVS 151
Cdd:PRK13382 66 LGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 152 IAFVQEKKIPSVLSCLAQCSSNLKtIVSFGSVSTTQKKEA--EGHGascfswGEFLQlgcldwdlPSKKKTDicTIMYTS 229
Cdd:PRK13382 143 TVIYDEEFSATVDRALADCPQATR-IVAWTDEDHDLTVEVliAAHA------GQRPE--------PTGRKGR--VILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 230 GTTGDPKGVViKNEAFMAEVLSVdhiIMltDRVA--GEDDVYFSfLPLAHV--YDQIMetYCISKGSSI----GFwqgDV 301
Cdd:PRK13382 206 GTTGTPKGAR-RSGPGGIGTLKA---IL--DRTPwrAEEPTVIV-APMFHAwgFSQLV--LAASLACTIvtrrRF---DP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 302 RFLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynyklkyLEkgLPqhkaAPLFDRLVFDKTKLAL 381
Cdd:PRK13382 274 EATLDLIDRHRATGLAVVPVMFDRI-----------------------------MD--LP----AEVRNRYSGRSLRFAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 382 GgrvrillSGAAPLPRHVEEFMRvTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLESvpemgyDALS 461
Cdd:PRK13382 319 A-------SGSRMRPDVVIAFMD-QFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILD------QDFR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 462 NVPRGE---ICLRGNTLFSGYHKREdlTKEVMvDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQ 538
Cdd:PRK13382 385 EVPTGEvgtIFVRNDTQFDGYTSGS--TKDFH-DGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLAT 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 539 CPLIASIWVYGNSFESF---LVAVVVPERKA--IEDWAKEH---NLTddfkslcdNLKARKHI--LDEL--NSTGQ 602
Cdd:PRK13382 461 HPDVAEAAVIGVDDEQYgqrLAAFVVLKPGAsaTPETLKQHvrdNLA--------NYKVPRDIvvLDELprGATGK 528
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
47-239 |
2.66e-10 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 63.44 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSvKRNPNNNMLGRRQKTE------SKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAME 120
Cdd:cd05943 63 RWFPGA-RLNYAENLLRHADADDpaaiyaAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAML 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 121 AC-------NSCAVSYVP--LYDTLGP---------NAVEF---IINHAEVsIAFVQeKKIPSvlsclaqcssnLKTIVS 179
Cdd:cd05943 142 ATasigaiwSSCSPDFGVpgVLDRFGQiepkvlfavDAYTYngkRHDVREK-VAELV-KGLPS-----------LLAVVV 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356575070 180 FGSVSTTQKKEAeGHGASCFSWGEFL---QLGCLDWD-LPSKkktDICTIMYTSGTTGDPKGVV 239
Cdd:cd05943 209 VPYTVAAGQPDL-SKIAKALTLEDFLatgAAGELEFEpLPFD---HPLYILYSSGTTGLPKCIV 268
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
73-568 |
4.22e-10 |
|
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: 62.83 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 73 GSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWII----AMEA-CNSCAVSyvPLYDTLGPNAVEF--II 145
Cdd:cd05921 21 GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALmalaAMYAgVPAAPVS--PAYSLMSQDLAKLkhLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 146 NHAEVSIAFVQEKkipsvlsclAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCF-SWGEFLQLGCLDWDLPSKKKTDICT 224
Cdd:cd05921 99 ELLKPGLVFAQDA---------APFARALAAIFPLGTPLVVSRNAVAGRGAISFaELAATPPTAAVDAAFAAVGPDTVAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 225 IMYTSGTTGDPKGvVIKNEAFMAEVlsvdhIIMLTD---RVAGEDDVYFSFLPLAHVYdqimetyciskGSSIGF----W 297
Cdd:cd05921 170 FLFTSGSTGLPKA-VINTQRMLCAN-----QAMLEQtypFFGEEPPVLVDWLPWNHTF-----------GGNHNFnlvlY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 298 QGDVRFL-------------LEDIQELKPTIFCGVPRVFDRIYAGIKSKVSsagpLQSTLFQcaynyKLKYLE---KGLP 361
Cdd:cd05921 233 NGGTLYIddgkpmpggfeetLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFFK-----RLKLMFyagAGLS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 362 QHkaapLFDRLvfdkTKLALggrvrillsgaaplpRHVEEFMRVTSgstlsqGYGLTEScAGCFTAIGDVYSMTGTVGVP 441
Cdd:cd05921 304 QD----VWDRL----QALAV---------------ATVGERIPMMA------GLGATET-APTATFTHWPTERSGLIGLP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 442 MTTIEARLesVPEMGydalsnvpRGEICLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDigewqsngAMKIID------- 513
Cdd:cd05921 354 APGTELKL--VPSGG--------KYEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGD--------AAKLADpddpakg 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356575070 514 -----RKKNIFKLSQGEYIAVENIENKY-LQC-PLIASIWVYGNSFEsFLVAVVVPERKAIE 568
Cdd:cd05921 416 lvfdgRVAEDFKLASGTWVSVGPLRARAvAACaPLVHDAVVAGEDRA-EVGALVFPDLLACR 476
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
414-563 |
5.27e-10 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 61.55 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 414 GYGLTEsCAG--CFTAIGDvySMTGTVGVPMTTIEARLesVPEMGYDalsnVPRG---EICLRGNTLFSGYHKREDLTKE 488
Cdd:cd17636 142 GYGQTE-VMGlaTFAALGG--GAIGGAGRPSPLVQVRI--LDEDGRE----VPDGevgEIVARGPTVMAGYWNRPEVNAR 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356575070 489 VMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQCPLIASIWVYG---NSFESFLVAVVVPE 563
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAAVIGvpdPRWAQSVKAIVVLK 289
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
49-563 |
7.14e-10 |
|
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: 61.68 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 49 FRDSVKRNPNN-NMLGRRQKtesklgsytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAV 127
Cdd:cd17644 6 FEEQVERTPDAvAVVFEDQQ----------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 128 SYVPLYDTLGPNAVEFIINHAEVSIAFVQekkiPSVLSClaqcssnlktivsfgsvsttqkkeaeghgascfswgeflql 207
Cdd:cd17644 76 AYVPLDPNYPQERLTYILEDAQISVLLTQ----PENLAY----------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 208 gcldwdlpskkktdictIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDRvageddvyfsflplahvyDQIMETyc 287
Cdd:cd17644 111 -----------------VIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS------------------DRVLQF-- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 288 iskgSSIGFwqgDVrflleDIQELKPTIFCGVPRVF--DRIYAGIKSKVSSAGPLQSTLFQCAYNYKLKYLEKGLPQHKA 365
Cdd:cd17644 154 ----ASIAF---DV-----AAEEIYVTLLSGATLVLrpEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTID 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 366 APLFDRLVfdktklalggrvriLLSGAAPLPRHVEEFMRVTSGS-TLSQGYGLTESC--AGCF--TAIGDVYSMTGTVGV 440
Cdd:cd17644 222 LPSSLRLV--------------IVGGEAVQPELVRQWQKNVGNFiQLINVYGPTEATiaATVCrlTQLTERNITSVPIGR 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 441 PMTTIEA-----RLESVPemgydalSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWFH---------TGDIGEWQSN 506
Cdd:cd17644 288 PIANTQVyildeNLQPVP-------VGVP-GELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPD 359
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 507 GAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIASIWVYGNSFES---FLVAVVVPE 563
Cdd:cd17644 360 GNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVPH 418
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
78-239 |
7.18e-10 |
|
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: 62.12 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQE 157
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 ------KKI---PSVLSCLAQCSSNLKTIVSFGSvsttqKKEAEGHGASCFSWGEFLQLGclDWDLPSKKKTDICTIMYT 228
Cdd:cd05968 172 gftrrgREVnlkEEADKACAQCPTVEKVVVVRHL-----GNDFTPAKGRDLSYDEEKETA--GDGAERTESEDPLMIIYT 244
|
170
....*....|.
gi 356575070 229 SGTTGDPKGVV 239
Cdd:cd05968 245 SGTTGKPKGTV 255
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
78-533 |
7.53e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.95 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEF---IINHAEVSIAf 154
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERfcqITDPAAALVA- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 vQEKKIPSvlsclAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCFSWGEflqlgcldwdlPSKKKTDICTIMYTSGTTGD 234
Cdd:PRK05857 121 -PGSKMAS-----SAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGN-----------ADQGSEDPLAMIFTSGTTGE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNEAFMA--EVLSVDHIIMLtDRVAGEddVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVRFLLEDIQELK 312
Cdd:PRK05857 184 PKAVLLANRTFFAvpDILQKEGLNWV-TWVVGE--TTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 313 PTIFCGVPRVFDRIYAGIKSKVSSAGPLqstlfqcaynyklkylekglpqhkaaplfdRLvfdktkLALGGRVRIllsgA 392
Cdd:PRK05857 261 VATTCLVPTLLSKLVSELKSANATVPSL------------------------------RL------VGYGGSRAI----A 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 393 APLpRHVEefmrvTSGSTLSQGYGLTEScaGCfTAI---GDVYSMT----GTVGVPMTTIEARLEsvPEMG-----YDAL 460
Cdd:PRK05857 301 ADV-RFIE-----ATGVRTAQVYGLSET--GC-TALclpTDDGSIVkieaGAVGRPYPGVDVYLA--ATDGigptaPGAG 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356575070 461 SNVPRGEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIE 533
Cdd:PRK05857 370 PSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVD 441
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
216-534 |
9.88e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.37 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 216 SKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAevlsvDHIIMLTDRVAGEDDVYFSFLPLAHVYD-QIMETYCISKGSSI 294
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLA-----NQRACLKFFSPKEDDVMMSFLPPFHAYGfNSCTLFPLLSGVPV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 295 GFWQGDV--RFLLEDIQELKPTIFCGVPRVFDRIYAGIKSKVSSAGPLqstlfqcaynyklkylekglpqhkaaplfdRL 372
Cdd:PRK06334 254 VFAYNPLypKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSL------------------------------RF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 373 VfdktklALGGRV--RILLSGAAPLPRHVeefmrvtsgsTLSQGYGLTEsCAGCFTaIGDVYS--MTGTVGVPMTTIEAR 448
Cdd:PRK06334 304 V------VIGGDAfkDSLYQEALKTFPHI----------QLRQGYGTTE-CSPVIT-INTVNSpkHESCVGMPIRGMDVL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 449 LesVPEMGYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDG--WFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEY 526
Cdd:PRK06334 366 I--VSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEM 442
|
....*...
gi 356575070 527 IAVENIEN 534
Cdd:PRK06334 443 VSLEALES 450
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
214-565 |
1.32e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 61.52 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 214 LPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVdhiimlTDRV-AGEDDVYFSFLPLAHvydqimetyciskgs 292
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQV------AARIdFSPEDKVFNALPVFH--------------- 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 293 SIGFWQGDVRFLLEDIqelkPTIFCGVPR----VFDRIYAgikskvSSAGPLQST-LFQCAYNyklkylekglpqhKAAP 367
Cdd:PRK06814 846 SFGLTGGLVLPLLSGV----KVFLYPSPLhyriIPELIYD------TNATILFGTdTFLNGYA-------------RYAH 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 368 LFD----RLVFdktklalggrvrillSGAAPL---PRHV--EEFmrvtsGSTLSQGYGLTEsCAGCFTAIGDVYSMTGTV 438
Cdd:PRK06814 903 PYDfrslRYVF---------------AGAEKVkeeTRQTwmEKF-----GIRILEGYGVTE-TAPVIALNTPMHNKAGTV 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 439 GVPMTTIEARLESVP--EMGydalsnvprGEICLRGNTLFSGYHKREDL-TKEVMVDGWFHTGDIGEWQSNGAMKIIDRK 515
Cdd:PRK06814 962 GRLLPGIEYRLEPVPgiDEG---------GRLFVRGPNVMLGYLRAENPgVLEPPADGWYDTGDIVTIDEEGFITIKGRA 1032
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 356575070 516 KNIFKLSqGEYIAVENIENkylqcpLIASIWVYGNSfesflVAVVVP-ERK 565
Cdd:PRK06814 1033 KRFAKIA-GEMISLAAVEE------LAAELWPDALH-----AAVSIPdARK 1071
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
78-574 |
1.80e-09 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 60.40 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDtlgpnavefiINHAEVSIAFVQE 157
Cdd:cd17643 13 LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPI-D----------PAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLsclaqcssnlktivsfgsVSTTQkkeaeghgascfswgeflqlgcldwdlpskkktDICTIMYTSGTTGDPKG 237
Cdd:cd17643 82 DSGPSLL------------------LTDPD---------------------------------DLAYVIYTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNeafmAEVLSvdhIIMLTDRVAG--EDDVY---------FS----FLPLAHVYDQIMETYCISKgSSIGFWQgdvr 302
Cdd:cd17643 111 VVVSH----ANVLA---LFAATQRWFGfnEDDVWtlfhsyafdFSvweiWGALLHGGRLVVVPYEVAR-SPEDFAR---- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 303 fLLEDiqeLKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKYLEKGLPQHKAAplfdRLVFdktklaLG 382
Cdd:cd17643 179 -LLRD---EGVTVLNQTPSAFYQL--------------------------VEAADRDGRDPLAL----RYVI------FG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 383 GRvRILLSGAAPLPRHVEEfmrvtSGSTLSQGYGLTESCAgcFTAIGDVySMTGTVGVPMTTIEARLesvPEMGYDALSN 462
Cdd:cd17643 219 GE-ALEAAMLRPWAGRFGL-----DRPQLVNMYGITETTV--HVTFRPL-DAADLPAAAASPIGRPL---PGLRVYVLDA 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 463 ----VPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWF--------HTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYI 527
Cdd:cd17643 287 dgrpVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmyRTGDLARRLPDGELEYLGRADEQVKIR-GFRI 365
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 528 AVENIENKYLQCPLIASIWVYGNSFE---SFLVAVVVPE------RKAIEDWAKEH 574
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEpgdTRLVAYVVADdgaaadIAELRALLKEL 421
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
47-277 |
1.85e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 60.66 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNML--GRRQktesklgsytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNS 124
Cdd:PRK08279 41 DVFEEAAARHPDRPALlfEDQS-----------ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 125 CAVsyvplydtlgpnaVEFIINHAEV------SIAFVQEKKI---PSVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGhg 195
Cdd:PRK08279 110 LGA-------------VVALLNTQQRgavlahSLNLVDAKHLivgEELVEAFEEARADLARPPRLWVAGGDTLDDPEG-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 196 ascfsWGEFLQL--GCLDWDLPSKKKT---DICTIMYTSGTTGDPKGVVIKNEAFMaevLSVDHIIMLTDrvAGEDDVYF 270
Cdd:PRK08279 175 -----YEDLAAAaaGAPTTNPASRSGVtakDTAFYIYTSGTTGLPKAAVMSHMRWL---KAMGGFGGLLR--LTPDDVLY 244
|
....*..
gi 356575070 271 SFLPLAH 277
Cdd:PRK08279 245 CCLPLYH 251
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
78-564 |
3.47e-09 |
|
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: 59.60 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGPNAvefiinhaevSIAFVQE 157
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL-DPGYPAD----------RLAYMLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLsclaqcssnlktivsFGSVSTTQKKEAEGHGASCFSWGeFLQLGCLDWDLPSKKKTDICTImYTSGTTGDPKG 237
Cdd:cd17646 93 DAGPAVV---------------LTTADLAARLPAGGDVALLGDEA-LAAPPATPPLVPPRPDNLAYVI-YTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLT--DRVA-----GED-DVYFSFLPLAHvydqimetyciskGSSI------GfwQGDVRF 303
Cdd:cd17646 156 VMVTHAGIVNRLLWMQDEYPLGpgDRVLqktplSFDvSVWELFWPLVA-------------GARLvvarpgG--HRDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 304 LLEDIQELKPTIFCGVP---RVFdriyagikskVSSAGPLQstlfqcaynyklkylekglpqhkAAPLfdRLVFdktkla 380
Cdd:cd17646 221 LAALIREHGVTTCHFVPsmlRVF----------LAEPAAGS-----------------------CASL--RRVF------ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 381 lggrvrilLSGAAPLPRHVEEFMRVTsGSTLSQGYGLTEscagcfTAIGDVY------SMTGTV--GVPM--TTI---EA 447
Cdd:cd17646 260 --------CSGEALPPELAARFLALP-GAELHNLYGPTE------AAIDVTHwpvrgpAETPSVpiGRPVpnTRLyvlDD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 448 RLESVPemgydalSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWF-------HTGDIGEWQSNGAMKIIDRKKNIFK 520
Cdd:cd17646 325 ALRPVP-------VGVP-GELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVK 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 356575070 521 LsQGEYIAVENIENKYLQCPLIASIWVY---GNSFESFLVAVVVPER 564
Cdd:cd17646 397 I-RGFRVEPGEIEAALAAHPAVTHAVVVaraAPAGAARLVGYVVPAA 442
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-641 |
4.37e-09 |
|
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: 59.31 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 225 IMYTSGTTGDPKGvvIKnEAFMAEVLSVDHIIMLTDRVA-GEDDVYFSFLPLAHVYDQIMETYCISKG-SSIGFWQGDVR 302
Cdd:cd05929 130 MLYSGGTTGRPKG--IK-RGLPGGPPDNDTLMAAALGFGpGADSVYLSPAPLYHAAPFRWSMTALFMGgTLVLMEKFDPE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 303 FLLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKylekgLPQHKaaplfdRLVFDKTKLalg 382
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRL--------------------------LK-----LPEAV------RNAYDLSSL--- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 383 grvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPmttIEARLESVPEMGYDALSN 462
Cdd:cd05929 247 ---KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSVGRA---VLGKVHILDEDGNEVPPG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 463 VPrGEICLRGNTLFSgYHKREDLTKE-VMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPL 541
Cdd:cd05929 321 EI-GEVYFANGPGFE-YTNDPEKTAAaRNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 542 IASIWVYGNSFESF---LVAVVVPerkaiedwakeHNLTDDFKSLCDNLKArkHILDELNStgQKHqlrgfellkaihle 618
Cdd:cd05929 398 VLDAAVVGVPDEELgqrVHAVVQP-----------APGADAGTALAEELIA--FLRDRLSR--YKC-------------- 448
|
410 420
....*....|....*....|....
gi 356575070 619 PNPFDIERDLI-TPTFKLKRPQLL 641
Cdd:cd05929 449 PRSIEFVAELPrDDTGKLYRRLLR 472
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
78-518 |
1.02e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.09 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAfvqe 157
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGMLA---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlSCLAQCSSNLKTIVSFGSVSTTQKKEAEGhgascFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSGTTGDPKG 237
Cdd:PRK09192 126 -------SAQPAAIITPDELLPWVNEATHGNPLLHV-----LSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTdrvaGEDDVYFSFLPLAHvyDqiMetyciskgssigfwqGDVRFLLEDIQ-----ELK 312
Cdd:PRK09192 194 VIITHRALMANLRAISHDGLKV----RPGDRCVSWLPFYH--D--M---------------GLVGFLLTPVAtqlsvDYL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 313 PTifcgvpRVFDRiyagikskvssaGPLQStlfqcaynykLKYLEKGLPQHKAAPLFD-----RLVFDKTKLALG-GRVR 386
Cdd:PRK09192 251 PT------RDFAR------------RPLQW----------LDLISRNRGTISYSPPFGyelcaRRVNSKDLAELDlSCWR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 387 ILLSGAAPLPRHV-----EEFMRVT-SGSTLSQGYGLTESC-AGCFTAIG--------DVYSMTGT-VGVPMTTIEARLE 450
Cdd:PRK09192 303 VAGIGADMIRPDVlhqfaEAFAPAGfDDKAFMPSYGLAEATlAVSFSPLGsgivveevDRDRLEYQgKAVAPGAETRRVR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 451 S-------VPEMGY----DALSNVPR---GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGeWQSNGAMKIIDRKK 516
Cdd:PRK09192 383 TfvncgkaLPGHEIeirnEAGMPLPErvvGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
..
gi 356575070 517 NI 518
Cdd:PRK09192 462 DL 463
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
365-543 |
1.17e-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: 57.58 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 365 AAPLFDRLVFDKTKLALGGRVRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSmTGTVGVPMTT 444
Cdd:cd05974 182 APPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVK-AGSMGRPLPG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 445 IEARLesvpemgYDALSN-VPRGEICL-----RGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNI 518
Cdd:cd05974 261 YRVAL-------LDPDGApATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDV 333
|
170 180
....*....|....*....|....*.
gi 356575070 519 FKLSqgEY-IAVENIENKYLQCPLIA 543
Cdd:cd05974 334 FKSS--DYrISPFELESVLIEHPAVA 357
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
78-271 |
1.34e-08 |
|
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: 58.10 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAE----VSIA 153
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKpkliVTAS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 154 F-------VQEKKIPSVLSCLAQCSSNlKTIVsfgsVSTTQKKEAEGHGASCFSWGEFLQlGCLDWDLPSKKKTDICTIM 226
Cdd:cd05967 163 CgiepgkvVPYKPLLDKALELSGHKPH-HVLV----LNRPQVPADLTKPGRDLDWSELLA-KAEPVDCVPVAATDPLYIL 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356575070 227 YTSGTTGDPKGVVIKNEAFM-AEVLSVDHIIMLtdrvaGEDDVYFS 271
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHAvALNWSMRNIYGI-----KPGDVWWA 277
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-574 |
1.74e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDTLGPnavefiinhaEVSIAFVQE 157
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL-DPEYP----------AERLAYMLE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLscLAQCSSNLKTIVSFGsvsttqkkeaeghgascfswgefLQLGCLD---------WDLPSKKKTD---ICTI 225
Cdd:PRK12316 606 DSGVQLL--LSQSHLGRKLPLAAG-----------------------VQVLDLDrpaawlegySEENPGTELNpenLAYV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 226 MYTSGTTGDPKGVVIKNEA------FMAEVLSVDhiimLTDRVAGEDDVYFS------FLPLAhvydqimetyciSKGSS 293
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHRAlsnrlcWMQQAYGLG----VGDTVLQKTPFSFDvsvwefFWPLM------------SGARL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 294 IGFWQGDVRflleDIQELKPTIfcGVPRVfdriyagikskvssagplqSTLfqcaynyklkyleKGLPQHKAAPLFDRLV 373
Cdd:PRK12316 725 VVAAPGDHR----DPAKLVELI--NREGV-------------------DTL-------------HFVPSMLQAFLQDEDV 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 374 FDKTKLAlggrvRILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAG--CFTAIGDVySMTGTVGVPMTTIEARLes 451
Cdd:PRK12316 767 ASCTSLR-----RIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDvtHWTCVEEG-GDSVPIGRPIANLACYI-- 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 452 vpemgYDA-LSNVP---RGEICLRGNTLFSGYHKREDLTKEVMV-----DG--WFHTGDIGEWQSNGAMKIIDRKKNIFK 520
Cdd:PRK12316 839 -----LDAnLEPVPvgvLGELYLAGRGLARGYHGRPGLTAERFVpspfvAGerMYRTGDLARYRADGVIEYAGRIDHQVK 913
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 521 LsQGEYIAVENIENKYLQCPLIASIWVYGNSFESfLVAVVVPE------RKAIEDWAKEH 574
Cdd:PRK12316 914 L-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
221-561 |
1.83e-08 |
|
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: 56.64 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 221 DICTIMYTSGTTGDPKgVVIKNEAFMAEVLSVDHIIMLTDRvageDDVYFSFLPLAH---VYDQIMETYciSKGSSIGFW 297
Cdd:cd17633 1 NPFYIGFTSGTTGLPK-AYYRSERSWIESFVCNEDLFNISG----EDAILAPGPLSHslfLYGAISALY--LGGTFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 298 QGDVRFLLEDIQELKPTIFCGVPrvfdriyagikskvssagplqsTLFQCAYNYklkylekGLPQHKaaplfdrlvfdkt 377
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYLVP----------------------TMLQALART-------LEPESK------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 378 klalggrVRILLSGAAPLPRHVEE-FMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSmTGTVGVPMTTIEARLEsvpemg 456
Cdd:cd17633 112 -------IKSIFSSGQKLFESTKKkLKNIFPKANLIEFYGTSELSFITYNFNQESRP-PNSVGRPFPNVEIEIR------ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 457 ydALSNVPRGEICLRGNTLFSGYhkreDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKY 536
Cdd:cd17633 178 --NADGGEIGKIFVKSEMVFSGY----VRGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVL 250
|
330 340
....*....|....*....|....*...
gi 356575070 537 LQCPLIASIWVYGNSFESF---LVAVVV 561
Cdd:cd17633 251 KAIPGIEEAIVVGIPDARFgeiAVALYS 278
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
76-549 |
2.40e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 57.06 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 76 TWlTYQDVYDAAMKMGSAIRS-RGVNPGDRCGIYGSNCPEWIIAMEAcnscavsyvplYDTLGpnAVEFIINHAEVSIAF 154
Cdd:cd05937 5 TW-TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLG-----------LWSIG--AAPAFINYNLSGDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 155 VQEKKIpsvlsclaqcsSNLKTIVSfgsvsttqkkeaeghgascfswgeflqlgclDWDlpskkktDICTIMYTSGTTGD 234
Cdd:cd05937 71 IHCLKL-----------SGSRFVIV-------------------------------DPD-------DPAILIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 235 PKGVVIKNEAFMAEVLSVDHIIMLTDrvageDDVYFSFLPLAHVYDQIMET-YCISKGSSIG---------FWQgdvrfl 304
Cdd:cd05937 102 PKAAAISWRRTLVTSNLLSHDLNLKN-----GDRTYTCMPLYHGTAAFLGAcNCLMSGGTLAlsrkfsasqFWK------ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 305 leDIQELKPTIFCGVPRVFDRIYAGIKSKVSsagplQSTLFQCAYNYKLKylekglPQhkaapLFDRLvfdktklalggR 384
Cdd:cd05937 171 --DVRDSGATIIQYVGELCRYLLSTPPSPYD-----RDHKVRVAWGNGLR------PD-----IWERF-----------R 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 VRILLSgaaplprHVEEFMRVTSGStlsqgYGLTESCAGCFTAigdvysmtGTVGVPMTTIEARLESV-------PEMGY 457
Cdd:cd05937 222 ERFNVP-------EIGEFYAATEGV-----FALTNHNVGDFGA--------GAIGHHGLIRRWKFENQvvlvkmdPETDD 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 458 DALSN-------VPR---GEICLRGN----TLFSGYHKREDLTKEVMV-------DGWFHTGDIGEWQSNGAMKIIDRKK 516
Cdd:cd05937 282 PIRDPktgfcvrAPVgepGEMLGRVPfknrEAFQGYLHNEDATESKLVrdvfrkgDIYFRTGDLLRQDADGRWYFLDRLG 361
|
490 500 510
....*....|....*....|....*....|...
gi 356575070 517 NIFKLsQGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:cd05937 362 DTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
47-660 |
4.13e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.21 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPNNNMLGRRqktESKLGSYTWLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCA 126
Cdd:PRK12582 53 HLLAKWAAEAPDRPWLAQR---EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 127 VSYVP-----------------LYDTLGPNAVefiinhaevsiaFVQEkkipsvlscLAQCSSNLKTIVSFGSVSTTQKK 189
Cdd:PRK12582 130 VPAAPvspayslmshdhaklkhLFDLVKPRVV------------FAQS---------GAPFARALAALDLLDVTVVHVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 190 EAEGHGASCFSwgeflqlgcldwDLPSKKKTD-------------ICTIMYTSGTTGDPKGVvIKNEAFMAEVLSVdhII 256
Cdd:PRK12582 189 PGEGIASIAFA------------DLAATPPTAavaaaiaaitpdtVAKYLFTSGSTGMPKAV-INTQRMMCANIAM--QE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 257 MLTDRVA-GEDDVYFSFLPLAHvydqIMetyciskGSSIGF----WQGDVRFL-------------LEDIQELKPTIFCG 318
Cdd:PRK12582 254 QLRPREPdPPPPVSLDWMPWNH----TM-------GGNANFngllWGGGTLYIddgkplpgmfeetIRNLREISPTVYGN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 319 VPrvfdriyagikskvssagplqstlfqCAYNYKLKYLEKGlpqhkaaPLFDRLVFDktklalggRVRILLSGAAPLPRH 398
Cdd:PRK12582 323 VP--------------------------AGYAMLAEAMEKD-------DALRRSFFK--------NLRLMAYGGATLSDD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 399 VEEFMRVTSGST------LSQGYGLTEScAGCFTAIGDVYSMTGTVGVPMTTIEARLesvpemgydalsnVPRG---EIC 469
Cdd:PRK12582 362 LYERMQALAVRTtghripFYTGYGATET-APTTTGTHWDTERVGLIGLPLPGVELKL-------------APVGdkyEVR 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 470 LRGNTLFSGYHKREDLTKEVM-VDGWFHTGDigewqsngAMKIID------------RKKNIFKLSQGEYIAVENIENKY 536
Cdd:PRK12582 428 VKGPNVTPGYHKDPELTAAAFdEEGFYRLGD--------AARFVDpddpekglifdgRVAEDFKLSTGTWVSVGTLRPDA 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 537 LQC--PLIASIWVYGNSfESFLVAVVVPERKAIEDWAKEHNLTDD----FKSLCDNLKARkhiLDELNSTGQKHQLRgfe 610
Cdd:PRK12582 500 VAAcsPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPDAAPEdvvkHPAVLAILREG---LSAHNAEAGGSSSR--- 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 356575070 611 lLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDHIDQLYKEAKGAMV 660
Cdd:PRK12582 573 -IARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYAEPPGPDV 621
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
78-590 |
7.93e-08 |
|
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: 55.24 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMeacnsCAV-----SYVPLyDTLGPNA-VEFIInhaevs 151
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAM-----LAVlkaggAFVPL-DPSHPLQrLQEIL------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 152 iafvQEKKIPSVLsclaqCSSnlktivsfgsvsttqkkeaeghgascfswgeflqlgcldwdlPSkkktDICTIMYTSGT 231
Cdd:cd05918 93 ----QDTGAKVVL-----TSS------------------------------------------PS----DAAYVIFTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 232 TGDPKGVVIKNEAFMAEVLSVDHIIMLTDrvagEDDVY-FSflplAHVYD-QIMETYCI-SKGSSIgfwqgdvrflledi 308
Cdd:cd05918 118 TGKPKGVVIEHRALSTSALAHGRALGLTS----ESRVLqFA----SYTFDvSILEIFTTlAAGGCL-------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 309 qelkptifCgVPRVFDRI----YAGIKSKVSSAGpLQSTLfqcaynyklkylekglpqhkAAPLFDRLVFDKTKLALGGR 384
Cdd:cd05918 176 --------C-IPSEEDRLndlaGFINRLRVTWAF-LTPSV--------------------ARLLDPEDVPSLRTLVLGGE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 vrillsgaAPLPRHVEEFmrvTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTtieARLESVPEMGYDALsnVP 464
Cdd:cd05918 226 --------ALTQSDVDTW---ADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLG---ATCWVVDPDNHDRL--VP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 465 R---GEICLRGNTLFSGYHKREDLTKEVMVDG--W------------FHTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYI 527
Cdd:cd05918 290 IgavGELLIEGPILARGYLNDPEKTAAAFIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKI-RGQRV 368
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356575070 528 AVENIENKYLQCPLIAS------IWVYGNSFESFLVAVVVP---ERKAIEDWAKEHNLTDDFKSLCDNLKAR 590
Cdd:cd05918 369 ELGEIEHHLRQSLPGAKevvvevVKPKDGSSSPQLVAFVVLdgsSSGSGDGDSLFLEPSDEFRALVAELRSK 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
210-565 |
1.04e-07 |
|
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: 54.79 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 210 LDWDLPSKKKT----------DICTIMYTSGTTGDPKGVVIKNEAfMAEVLSVDHIIMLTDRvagEDDVY-FSFLPLAHV 278
Cdd:cd17656 108 LEDPSISQEDTsnidyinnsdDLLYIIYTSGTTGKPKGVQLEHKN-MVNLLHFEREKTNINF---SDKVLqFATCSFDVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 279 YDQIMETYCisKGssigfwqGDVRFLLEDIQelkptifcgvpRVFDRIYAGIKSKvssagPLQSTLFQCAYnYKLKYLEK 358
Cdd:cd17656 184 YQEIFSTLL--SG-------GTLYIIREETK-----------RDVEQLFDLVKRH-----NIEVVFLPVAF-LKFIFSER 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 359 GLpqhkAAPLFDRLvfdKTKLALGGRVRIllsgAAPLprhVEEFMRvtSGSTLSQGYGLTEScagcftaigDVysmtgtv 438
Cdd:cd17656 238 EF----INRFPTCV---KHIITAGEQLVI----TNEF---KEMLHE--HNVHLHNHYGPSET---------HV------- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 439 gVPMTTI--EARLESVPEMGyDALSNV------------PRG---EICLRGNTLFSGYHKREDLTKEVMVDGWF------ 495
Cdd:cd17656 286 -VTTYTInpEAEIPELPPIG-KPISNTwiyildqeqqlqPQGivgELYISGASVARGYLNRQELTAEKFFPDPFdpnerm 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356575070 496 -HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLI--ASIWVYGNSF-ESFLVAVVVPERK 565
Cdd:cd17656 364 yRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVseAVVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
220-549 |
2.22e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 53.92 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 220 TDICTIMYTSGTTGDPKGVVIKNE--AFMAevlsvdhiIMLTDRVA-GEDDVYFSFLPLAHVyDQIMETYC--ISKGSSI 294
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRkvASAG--------VMLAQRFGlGPDDVCYVSMPLFHS-NAVMAGWAvaLAAGASI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 295 GFWQgdvRF----LLEDIqelkptifcgvpRVFDRIYAGIKSKvssagPLQstlfqcaynYKLKYLEKglPQHKAAPLfd 370
Cdd:PRK07867 223 ALRR---KFsasgFLPDV------------RRYGATYANYVGK-----PLS---------YVLATPER--PDDADNPL-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 371 RLVFdktklalggrvrillsGAAPLPRHVEEFMRvTSGSTLSQGYGLTEscagcftaiGDVySMTGTVGVPMTTIEARLE 450
Cdd:PRK07867 270 RIVY----------------GNEGAPGDIARFAR-RFGCVVVDGFGSTE---------GGV-AITRTPDTPPGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 451 SVPEMGYDALSNVPRGEIC----------------LRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDR 514
Cdd:PRK07867 323 GVAIVDPDTGTECPPAEDAdgrllnadeaigelvnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGR 402
|
330 340 350
....*....|....*....|....*....|....*
gi 356575070 515 KKNIFKLSqGEYIAVENIENKYLQCPLIASIWVYG 549
Cdd:PRK07867 403 LGDWMRVD-GENLGTAPIERILLRYPDATEVAVYA 436
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
49-573 |
2.39e-07 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 53.71 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 49 FRDSVKRNPNNNMLGRRQKTesklgsytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVS 128
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQS---------LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 129 YVPLYDTLGPNAVEFIINHAEVSIAFVQEKkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflqlg 208
Cdd:cd17645 75 YVPIDPDYPGERIAYMLADSSAKILLTNPD-------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 209 cldwdlpskkktDICTIMYTSGTTGDPKGVVIKNEAFMAevLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDqiMETYcI 288
Cdd:cd17645 105 ------------DLAYVIYTSGSTGLPKGVMIEHHNLVN--LCEWHRPYFGVTPADKSLVYASFSFDASAWE--IFPH-L 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 289 SKGSSIGFWQGDVRFlleDIQELKptifcgvpRVFDRiyAGIKskvssagplqstlfqcaynykLKYLEKGLPQHkaapl 368
Cdd:cd17645 168 TAGAALHVVPSERRL---DLDALN--------DYFNQ--EGIT---------------------ISFLPTGAAEQ----- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 369 FDRLvfDKTKLalggrvRILLSGAAPLPRHVEEfmrvtsGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEAR 448
Cdd:cd17645 209 FMQL--DNQSL------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVY 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 449 LESvpemgyDALSNVP---RGEICLRGNTLFSGYHKREDLTKEVMV-------DGWFHTGDIGEWQSNGAMKIIDRKKNI 518
Cdd:cd17645 275 ILD------EALQLQPigvAGELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356575070 519 FKLsQGEYIAVENIENKYLQCPLI---ASIWVYGNSFESFLVAVVVPERK----AIEDWAKE 573
Cdd:cd17645 349 VKI-RGYRIEPGEIEPFLMNHPLIelaAVLAKEDADGRKYLVAYVTAPEEipheELREWLKN 409
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
220-569 |
3.82e-07 |
|
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: 53.17 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 220 TDICTIMYTSGTTGDPKGVvikneafMAEVLSVDHIIM-LTDRVAGEDDVYFSFLPLA-HVYDQIMETYCISKGSsigfw 297
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGV-------LVEHGSVVNLRTsLSERYFGRDNGDEAVLFFSnYVFDFFVEQMTLALLN----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 298 qGDVRFLLEDIQELKPtifcgvprvfDRIYAGI-KSKVS--SAGPLQSTLFQcaynyklkylekglpqhkaaplFDRLvf 374
Cdd:cd17648 162 -GQKLVVPPDEMRFDP----------DRFYAYInREKVTylSGTPSVLQQYD----------------------LARL-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 375 dkTKLAlggrvRILLSGAAPLPRHVEEfMRVTSGSTLSQGYGLTESCAgcfTAIGDVYS----MTGTVGVPMTTIEARLE 450
Cdd:cd17648 207 --PHLK-----RVDAAGEEFTAPVFEK-LRSRFAGLIINAYGPTETTV---TNHKRFFPgdqrFDKSLGRPVRNTKCYVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 451 SvpemgyDALSNVP---RGEICLRGNTLFSGYHKREDLTKEVMVDGWFH---------------TGDIGEWQSNGAMKII 512
Cdd:cd17648 276 N------DAMKRVPvgaVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargrnarlykTGDLVRWLPSGELEYL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356575070 513 DRKKNIFKLsQGEYIAVENIENKYLQCPLI---ASIWVYGNSF-----ESFLVAVVVPERKAIED 569
Cdd:cd17648 350 GRNDFQVKI-RGQRIEPGEVEAALASYPGVrecAVVAKEDASQaqsriQKYLVGYYLPEPGHVPE 413
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
78-269 |
8.99e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.20 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC--NSCAVSyvPLYDTLGPNAVEFIINHAEVSI--- 152
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGAlkNGAIVG--PLFEAFMEEAVRDRLEDSEAKVlit 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 --AFVQEKKIPSVlsclaqcsSNLKTIVSFGsvsttqkkEAEGHGASCFSWGEFLQLGCLDWDLPSKKKTDICTIMYTSG 230
Cdd:PRK04319 152 tpALLERKPADDL--------PSLKHVLLVG--------EDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSG 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356575070 231 TTGDPKGVVIKNEAfmaevlsvdhiiMLTDRVAG-------EDDVY 269
Cdd:PRK04319 216 STGKPKGVLHVHNA------------MLQHYQTGkyvldlhEDDVY 249
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
47-564 |
9.56e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 51.55 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 47 DFFRDSVKRNPnnnmlgRRQKTESKLGSytwLTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCA 126
Cdd:cd12115 3 DLVEAQAARTP------DAIALVCGDES---LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 127 VSYVPLYDTLGPNAVEFIINHAEVSIAFVQekkipsvlsclaqcssnlktivsfgsvsttqkkeaeghgascfswgeflq 206
Cdd:cd12115 74 AAYVPLDPAYPPERLRFILEDAQARLVLTD-------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 207 lgcldwdlpskkKTDICTIMYTSGTTGDPKGVVIKN-----------EAFMAEVLSVdhiIMLTDRVAGEDDVYFSFLPL 275
Cdd:cd12115 104 ------------PDDLAYVIYTSGSTGRPKGVAIEHrnaaaflqwaaAAFSAEELAG---VLASTSICFDLSVFELFGPL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 276 AHvydqimetyciskGSSIgfwqgdvrFLLEDIQELkptifcgvprvfdriyagikskVSSAGPLQSTLFQCAYNYKLKY 355
Cdd:cd12115 169 AT-------------GGKV--------VLADNVLAL----------------------PDLPAAAEVTLINTVPSAAAEL 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 356 LEKGlpqhkaaplfdrlvfdktklALGGRVRIL-LSGaAPLPRH-VEEFMRVTSGSTLSQGYGLTESCA-GCFTAIGDVY 432
Cdd:cd12115 206 LRHD--------------------ALPASVRVVnLAG-EPLPRDlVQRLYARLQVERVVNLYGPSEDTTySTVAPVPPGA 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 433 SMTGTVGVPM--TTIE---ARLESVPemgydalSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWFH-------TGDI 500
Cdd:cd12115 265 SGEVSIGRPLanTQAYvldRALQPVP-------LGVP-GELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDL 336
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356575070 501 GEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLI--ASIWVYGNSF-ESFLVAVVVPER 564
Cdd:cd12115 337 VRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVreAVVVAIGDAAgERRLVAYIVAEP 402
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
225-561 |
1.74e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 51.28 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 225 IMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTDrvagEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQGDVrfl 304
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKD----IPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGI--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 305 lediqeLKPTifcgvpRVFDRIYAGI-KSKVSSAGPLQSTlfqcaynykLKYLEKGLPQHKAAplfdrlvfdKTKLALGG 383
Cdd:PTZ00237 332 ------IKNK------HIEDDLWNTIeKHKVTHTLTLPKT---------IRYLIKTDPEATII---------RSKYDLSN 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 RVRILLSGAA---PLPRHVEEFMRVTSgstlSQGYGLTESCAG---CFTAIGDVYSmtgTVGVPMTTIEARLESvpEMGY 457
Cdd:PTZ00237 382 LKEIWCGGEVieeSIPEYIENKLKIKS----SRGYGQTEIGITylyCYGHINIPYN---ATGVPSIFIKPSILS--EDGK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 458 DALSNvPRGEICLR---GNTLFSGYHKREDLTKEVMVD--GWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENI 532
Cdd:PTZ00237 453 ELNVN-EIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKIS-GNKVQLNTI 530
|
330 340 350
....*....|....*....|....*....|..
gi 356575070 533 ENKYLQCPLI---ASIWVYGNSFESFLVAVVV 561
Cdd:PTZ00237 531 ETSILKHPLVlecCSIGIYDPDCYNVPIGLLV 562
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-534 |
2.50e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.54 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 218 KKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVlsvDHIIMLTDRVAGEDDVYfSFLPLAhVYDQIME-TYCISKGSSIGF 296
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQI---DALRQLYGIRPGEVDLA-TFPLFA-LFGPALGlTSVIPDMDPTRP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 297 WQGDVRFLLEDIQELKPTIFCGVPRVFDRIYAgikskvssagplqstlfQCAYNyklkylEKGLPQhkaaplfdrlvfdk 376
Cdd:cd05910 158 ARADPQKLVGAIRQYGVSIVFGSPALLERVAR-----------------YCAQH------GITLPS-------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 377 tklalggrVRILLSGAAPLPRHVEEFMR--VTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGT---------VGVPMTTI 445
Cdd:cd05910 201 --------LRRVLSAGAPVPIALAARLRkmLSDEAEILTPYGATEALPVSSIGSRELLATTTAatsggagtcVGRPIPGV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 446 EARL-----ESVPEMGYD-ALSNVPRGEICLRGNTLFSGYHKREDLTKEVMVDG-----WFHTGDIGEWQSNGAMKIIDR 514
Cdd:cd05910 273 RVRIieiddEPIAEWDDTlELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGR 352
|
330 340
....*....|....*....|..
gi 356575070 515 KKNIFKLSQGEY--IAVENIEN 534
Cdd:cd05910 353 KAHRVITTGGTLytEPVERVFN 374
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
78-574 |
3.40e-06 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 49.94 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDtlgPNavefiinHAEVSIAFVQE 157
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPL-D---PA-------YPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLscLAQcSSNLKTIVsfgsvsttqkkeaeghgascfswgeflqlgcldwdlpskkktdictimYTSGTTGDPKG 237
Cdd:cd17652 82 DARPALL--LTT-PDNLAYVI------------------------------------------------YTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNE---AFMAEvlsvdhiimLTDRVA-GEDDVYFSFlplahvydqimetyciskgSSIGFwqgDVRFLlediqELKP 313
Cdd:cd17652 111 VVVTHRglaNLAAA---------QIAAFDvGPGSRVLQF-------------------ASPSF---DASVW-----ELLM 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 314 TIFCG-----VPRvfDRIYAGikskvssaGPLQSTLFQCAYNYKLkylekgLPQHKAAPLFDRlvfdktklALGGRVRIL 388
Cdd:cd17652 155 ALLAGatlvlAPA--EELLPG--------EPLADLLREHRITHVT------LPPAALAALPPD--------DLPDLRTLV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 389 LSGAAPLPRHVEefmRVTSGSTLSQGYGLTES--CA---GCFTAIGDVysmtgTVGVPMT-----TIEARLESVPemgyd 458
Cdd:cd17652 211 VAGEACPAELVD---RWAPGRRMINAYGPTETtvCAtmaGPLPGGGVP-----PIGRPVPgtrvyVLDARLRPVP----- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 459 alSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWF--------HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVE 530
Cdd:cd17652 278 --PGVP-GELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmyRTGDLARWRADGQLEFLGRADDQVKI-RGFRIELG 353
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 356575070 531 NIENKYLQCPLI--ASIWVYGN-SFESFLVAVVVPE------RKAIEDWAKEH 574
Cdd:cd17652 354 EVEAALTEHPGVaeAVVVVRDDrPGDKRLVAYVVPApgaaptAAELRAHLAER 406
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-566 |
3.41e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSIAFVQe 157
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ- 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 kkipsvlsclaqcsSNLKTIVSFGSVSTTQKKEAEGHGAScfswgeflqlgcldwDLPSKKKTD-ICTIMYTSGTTGDPK 236
Cdd:PRK12316 3162 --------------SHLRLPLAQGVQVLDLDRGDENYAEA---------------NPAIRTMPEnLAYVIYTSGSTGKPK 3212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 237 GVVIKNEAFMAEVLSVDHIIMLTDRVAGEDDVYFSFLPLAHVYDQIMETYCISKGSSIGFWQgDVRFLLEDIQElkptif 316
Cdd:PRK12316 3213 GVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWR-DPALLVELINS------ 3285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 317 cgvprvfdriyagikskvssagplqstlfqcaynyklkyleKGLPQHKAAPLFDRLVFDKTKLALGGRVRILLSGAAPLP 396
Cdd:PRK12316 3286 -----------------------------------------EGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALP 3324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 397 rhVEEFMRVTSGSTLSQGYGLTESCAGCFT-AIGDVYSMTGTVGVPMTTIEARLESvpemgyDALSNVPRG---EICLRG 472
Cdd:PRK12316 3325 --ADLQQQVFAGLPLYNLYGPTEATITVTHwQCVEEGKDAVPIGRPIANRACYILD------GSLEPVPVGalgELYLGG 3396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 473 NTLFSGYHKREDLTKEVMVDGWF-------HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIASI 545
Cdd:PRK12316 3397 EGLARGYHNRPGLTAERFVPDPFvpgerlyRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREA 3475
|
490 500
....*....|....*....|.
gi 356575070 546 WVYGNSFESfLVAVVVPERKA 566
Cdd:PRK12316 3476 VVLAVDGRQ-LVAYVVPEDEA 3495
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
386-560 |
3.62e-06 |
|
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: 50.14 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 386 RILLSGAAPLPRHVeeFMRVTS--GSTLSQGYGLTEscaG--CFTAIGD-VYSMTGTVGVPMTTI-EARLesVPEMGYDa 459
Cdd:COG1021 303 RVLQVGGAKLSPEL--ARRVRPalGCTLQQVFGMAE---GlvNYTRLDDpEEVILTTQGRPISPDdEVRI--VDEDGNP- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 lsnVPRGEI---CLRGNTLFSGYHKREDLTKEVM-VDGWFHTGDIGEWQSNGAMKIIDRKKNifklsQ----GEYIAVEN 531
Cdd:COG1021 375 ---VPPGEVgelLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEKIAAEE 446
|
170 180
....*....|....*....|....*....
gi 356575070 532 IENKYLQCPLIASiwvygnsfesflVAVV 560
Cdd:COG1021 447 VENLLLAHPAVHD------------AAVV 463
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
78-277 |
3.86e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.55 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVnPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDtlgpnavefiinhAEVSIAFVQE 157
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP-------------PESARRHHQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KkipsVLSCLAQCSSNLKTIVSFGSVSTTQKKEAEGHGAScfswgEFLQLGCLD------WDLPSKKKTDICTIMYTSGT 231
Cdd:PRK05691 107 R----LLSIIADAEPRLLLTVADLRDSLLQMEELAAANAP-----ELLCVDTLDpalaeaWQEPALQPDDIAFLQYTSGS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356575070 232 TGDPKGV------VIKNEAFMAEVLSVDhiimltdrvAGEDDVYFSFLPLAH 277
Cdd:PRK05691 178 TALPKGVqvshgnLVANEQLIRHGFGID---------LNPDDVIVSWLPLYH 220
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
385-561 |
7.62e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 48.84 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 385 VRILLSGAAPL-PRHVEEFMRvTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPMTTIEARLesvpeMGYDALSNV 463
Cdd:PRK13383 294 LRVVMSSGDRLdPTLGQRFMD-TYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRI-----LDRNNRPVG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 464 PR--GEICLRGNTLFSGYhkrEDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPL 541
Cdd:PRK13383 368 PRvtGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPA 443
|
170 180
....*....|....*....|...
gi 356575070 542 IASIWVYGNSFESF---LVAVVV 561
Cdd:PRK13383 444 VADNAVIGVPDERFghrLAAFVV 466
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
389-563 |
8.33e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 48.50 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 389 LSGAAPLPRHVEEfMRVTSGSTLSQGYGLTESCAGCftaigdVYSmtgtvGVPMTTIEARLESvpemgydalsnvprGEI 468
Cdd:PRK07824 157 LVGGGPAPAPVLD-AAAAAGINVVRTYGMSETSGGC------VYD-----GVPLDGVRVRVED--------------GRI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 469 CLRGNTLFSGYhkREDLTKEVMVD-GWFHTGDIGEWQSnGAMKIIDRKKNIFKlSQGEYIAVENIENKYLQCPLIASIWV 547
Cdd:PRK07824 211 ALGGPTLAKGY--RNPVDPDPFAEpGWFRTDDLGALDD-GVLTVLGRADDAIS-TGGLTVLPQVVEAALATHPAVADCAV 286
|
170
....*....|....*....
gi 356575070 548 YGNSFESF---LVAVVVPE 563
Cdd:PRK07824 287 FGLPDDRLgqrVVAAVVGD 305
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
78-122 |
1.02e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 48.60 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC 143
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
386-568 |
1.41e-05 |
|
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: 48.09 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 386 RILLSGAAPLPRHVEEFMRVTSGSTLSQGYGLTESCAgCFTAIGDVYS-MTGTVGVPMTTI-EARLesVPEMGYDalsnV 463
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL-NYTRLDDPDEvIIHTQGRPMSPDdEIRV--VDEEGNP----V 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 464 PRGEI---CLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQC 539
Cdd:cd05920 331 PPGEEgelLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRH 409
|
170 180 190
....*....|....*....|....*....|...
gi 356575070 540 PLIASIWVYGNSfESFL----VAVVVPERKAIE 568
Cdd:cd05920 410 PAVHDAAVVAMP-DELLgersCAFVVLRDPPPS 441
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
228-519 |
1.57e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.84 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 228 TSGTTGDPKGVVIKNEAFMAEVLSV-DHIimltdRVAGEDDVYFSFLPLAHvyDQIMETYCISKGSSIGFWQGdvrflle 306
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLnARV-----GLDAATDVGCSWLPLYH--DMGLAFLLTAALAGAPLWLA------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 307 diqelkPTifcgvpRVFdriyagikskvsSAGPLQStlfqcaynykLKYLEKGLPQHKAAPLFDRLVFDK-----TKLAL 381
Cdd:PRK05851 226 ------PT------TAF------------SASPFRW----------LSWLSDSRATLTAAPNFAYNLIGKyarrvSDVDL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 382 GgRVRILLSGAAPLprHVEEFMRVT--------SGSTLSQGYGLTES-CA------GCFTAIGDVYSMTGT-------VG 439
Cdd:PRK05851 272 G-ALRVALNGGEPV--DCDGFERFAtamapfgfDAGAAAPSYGLAEStCAvtvpvpGIGLRVDEVTTDDGSgarrhavLG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 440 VPMTTIEARLESvpemGYDALSNVPR--GEICLRGNTLFSGYHKREDLTKevmvDGWFHTGDIGeWQSNGAMKIIDRKK- 516
Cdd:PRK05851 349 NPIPGMEVRISP----GDGAAGVAGReiGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLG-YLVDGGLVVCGRAKe 419
|
330
....*....|
gi 356575070 517 -------NIF 519
Cdd:PRK05851 420 litvagrNIF 429
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
78-239 |
2.30e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.48 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC-------NSCAVSYvplydtlGPNAVefiinhaev 150
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATaslgaiwSSCSPDF-------GVQGV--------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 151 sIA-FVQEKkiPSVLSC----------------LAQCSSNLKTIVSFGSVSTTQKKEAEGHGASCFSWGEFLQLGC---- 209
Cdd:PRK03584 179 -LDrFGQIE--PKVLIAvdgyryggkafdrrakVAELRAALPSLEHVVVVPYLGPAAAAAALPGALLWEDFLAPAEaael 255
|
170 180 190
....*....|....*....|....*....|....
gi 356575070 210 ----LDWDLPskkktdiCTIMYTSGTTGDPKGVV 239
Cdd:PRK03584 256 efepVPFDHP-------LWILYSSGTTGLPKCIV 282
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
78-610 |
3.80e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 46.84 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVpLYDTlGPNAVEFiinhAEVSI----- 152
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARII-LLNT-GFSGPQL----AEVAAregvk 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 AFVQEKKIPSVLSCLAQCSSNLKTIVsfGSVSTTQKKEAEghgascfsWGEFLQL--GCLDWDLPSKKKTDICTIMyTSG 230
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRAWG--GNPDDDEPSGST--------DETLDDLiaGSSTAPLPKPPKPGGIVIL-TSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 231 TTGDPKGVVIKneafmaEVLSVDHIIMLTDRV---AGEddVYFSFLPLAHVYDQIMETYCISKGSSIGFWQgdvRF---- 303
Cdd:PRK07788 218 TTGTPKGAPRP------EPSPLAPLAGLLSRVpfrAGE--TTLLPAPMFHATGWAHLTLAMALGSTVVLRR---RFdpea 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 304 LLEDIQELKPTIFCGVPRVFDRIyagikskvssagplqstlfqcaynykLKYLEKGLPQHKAAPLfdRLVFdktklalgg 383
Cdd:PRK07788 287 TLEDIAKHKATALVVVPVMLSRI--------------------------LDLGPEVLAKYDTSSL--KIIF--------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 384 rvrilLSGAAPLPRHVEEFMRvTSGSTLSQGYGLTEsCAgcFTAIG---DVYSMTGTVGVPMTTIEARLesvpemgYDAL 460
Cdd:PRK07788 330 -----VSGSALSPELATRALE-AFGPVLYNLYGSTE-VA--FATIAtpeDLAEAPGTVGRPPKGVTVKI-------LDEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 461 SN-VPRGE---ICLRGNTLFSGY-HKRedlTKEvMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENK 535
Cdd:PRK07788 394 GNeVPRGVvgrIFVGNGFPFEGYtDGR---DKQ-IIDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 536 YLQCPLIASIWVYGNSFESF---LVAVVVPER------KAIEDWAKehnltddfkslcDNLkARKHI------LDEL--N 598
Cdd:PRK07788 469 LAGHPDVVEAAVIGVDDEEFgqrLRAFVVKAPgaaldeDAIKDYVR------------DNL-ARYKVprdvvfLDELprN 535
|
570
....*....|....
gi 356575070 599 STGQ--KHQLRGFE 610
Cdd:PRK07788 536 PTGKvlKRELREMD 549
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
78-239 |
1.27e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 45.24 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLYDTLGPNAVEFIINHAEVSI----- 152
Cdd:cd05966 85 ITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLvitad 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 153 -AFVQEKKIP---SVLSCLAQCSSNLKTIVsfgsvsttqkkeAEGHGASCfSWGEFLQlgcLDWDLPSKKKTDICT---- 224
Cdd:cd05966 165 gGYRGGKVIPlkeIVDEALEKCPSVEKVLV------------VKRTGGEV-PMTEGRD---LWWHDLMAKQSPECEpewm 228
|
170 180
....*....|....*....|..
gi 356575070 225 -------IMYTSGTTGDPKGVV 239
Cdd:cd05966 229 dsedplfILYTSGSTGKPKGVV 250
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
396-549 |
1.28e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.02 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 396 PRHVEEFMRvTSGSTLSQGYGLTEScAGCFT--------AIGdvysmTGTVGV----PMTTIE---ARLEsvpEMGydAL 460
Cdd:PRK13388 277 PRDIAEFSR-RFGCQVEDGYGSSEG-AVIVVrepgtppgSIG-----RGAPGVaiynPETLTEcavARFD---AHG--AL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 461 SNVPR--GEIC-LRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYL 537
Cdd:PRK13388 345 LNADEaiGELVnTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVD-GENLSAAPIERILL 423
|
170
....*....|..
gi 356575070 538 QCPLIASIWVYG 549
Cdd:PRK13388 424 RHPAINRVAVYA 435
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
439-607 |
2.53e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 43.96 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 439 GVPMTTiEARLESVPEMGYDALSNVPRGEICLRGNTLFSGYHKREDLTKEVMV-DGWFHTGDIGEWQSNGAMKIIDRKKN 517
Cdd:PRK06164 352 GRPASP-EARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGD 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 518 IFKLSqGEYIAVENIENKYLQCPLIASIWVYGNSFESFLVAV--VVPERKAIED------WAKEHnlTDDFKslcdnLKA 589
Cdd:PRK06164 431 SLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVafVIPTDGASPDeaglmaACREA--LAGFK-----VPA 502
|
170 180
....*....|....*....|....*
gi 356575070 590 RKHILDELNSTG-------QKHQLR 607
Cdd:PRK06164 503 RVQVVEAFPVTEsangakiQKHRLR 527
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
468-588 |
4.51e-04 |
|
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: 43.19 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 468 ICLRGNTLFSGYHKREDLTK-EVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFKLSqGEYIAVENIENKYLQCPLIASIW 546
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKEAA 441
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 356575070 547 VYGNSFESF---LVAVVvperKAIEDWAKEHNLTDDFKSLCDNLK 588
Cdd:cd05915 442 VVAIPHPKWqerPLAVV----VPRGEKPTPEELNEHLLKAGFAKW 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-563 |
5.00e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 43.79 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSCAVSYVPLyDtlgpnavefiINHAEVSIAFVQE 157
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-D----------PNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 158 KKIPSVLSCLAQCSSNLKTIVSFGSVSTTQKKEaeghgascfsWGEFLQLGcldwDLPSKKKTDICTIMYTSGTTGDPKG 237
Cdd:PRK12316 2098 DSGAALLLTQRHLLERLPLPAGVARLPLDRDAE----------WADYPDTA----PAVQLAGENLAYVIYTSGSTGLPKG 2163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 238 VVIKNEAFMAEVLSVDHIIMLTDrvageDDVYFSFLPLAhvYDQIMETYciskgssigFWQ--GDVRFLLEDIQELKPti 315
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSP-----ADCELQFMSFS--FDGAHEQW---------FHPllNGARVLIRDDELWDP-- 2225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 316 fcgvprvfDRIYAGIKSKVSSAGplqstLFQCAYNYKLKYLEkglpQHKAAPLfdrlvfdktklalggRVRILLSGAAPL 395
Cdd:PRK12316 2226 --------EQLYDEMERHGVTIL-----DFPPVYLQQLAEHA----ERDGRPP---------------AVRVYCFGGEAV 2273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 396 PRH-VEEFMRVTSGSTLSQGYGLTESCAGCFTAIGDVYSMTGTVGVPM-TTIEARLESVPEMGYDALSNVPRGEICLRGN 473
Cdd:PRK12316 2274 PAAsLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIgRALGNRRAYILDADLNLLAPGMAGELYLGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 474 TLFSGYHKREDLTKEVMVDGWF--------HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIASI 545
Cdd:PRK12316 2354 GLARGYLNRPGLTAERFVPDPFsasgerlyRTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREA 2432
|
490 500
....*....|....*....|
gi 356575070 546 WVYGNSFES--FLVAVVVPE 563
Cdd:PRK12316 2433 VVVAQDGASgkQLVAYVVPD 2452
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
78-122 |
9.60e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 42.24 E-value: 9.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 356575070 78 LTYQDVYDAAMKMGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
Cdd:PRK10524 85 YTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLAC 129
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
386-563 |
1.22e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.34 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 386 RILLSGAApLPRH-VEEFMRVTsGSTLSQGYGLTESCAGC--FTAIGDVYSMTGTVGVP---------MTTIEARLESVP 453
Cdd:PRK10252 721 QVFCSGEA-LPADlCREWQQLT-GAPLHNLYGPTEAAVDVswYPAFGEELAAVRGSSVPigypvwntgLRILDARMRPVP 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 454 emgydalSNVPrGEICLRGNTLFSGYHKREDLTKEVMVDGWF-------HTGDIGEWQSNGAMKIIDRKKNIFKLsQGEY 526
Cdd:PRK10252 799 -------PGVA-GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQR 869
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356575070 527 IAVENIENKYLQCPLIASIWVYGNSF---------ESFLVAVVVPE 563
Cdd:PRK10252 870 IELGEIDRAMQALPDVEQAVTHACVInqaaatggdARQLVGYLVSQ 915
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
466-549 |
1.55e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 41.69 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 466 GEICLRGNTLFSGYHKREDLTKEVMVDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYLQCPLIASI 545
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEI 412
|
....
gi 356575070 546 WVYG 549
Cdd:PRK07638 413 VVIG 416
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
212-277 |
1.84e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.25 E-value: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 212 WDLPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFMAEVLSVDHIIMLTdrvagEDDVYFSFLPLAH 277
Cdd:PRK07769 172 WVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQ-----EGDRGVSWLPFFH 232
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
460-562 |
2.08e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 41.13 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 460 LSNVPRGEICLRGNTLFSGY--HKREDltkevmvDGWFHTGDIGEWQSNGAMKIIDRKKNIFkLSQGEYIAVENIENKYL 537
Cdd:PRK07445 296 IPANQTGNITIQAQSLALGYypQILDS-------QGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAIL 367
|
90 100
....*....|....*....|....*...
gi 356575070 538 QCPLIASIWVYG---NSFESFLVAVVVP 562
Cdd:PRK07445 368 ATGLVQDVCVLGlpdPHWGEVVTAIYVP 395
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
363-543 |
3.08e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.92 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 363 HKAAPLFdRLVFDKTKLALGGRVRILLSGAAPLPRHV-EEFMRVTSGSTLSQGYGLTEscagcfTAIGDVY-------SM 434
Cdd:PRK05691 1369 HFVPPLL-QLFIDEPLAAACTSLRRLFSGGEALPAELrNRVLQRLPQVQLHNRYGPTE------TAINVTHwqcqaedGE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 435 TGTVGVPMTTIEARLESvpemgyDALSNVPRG---EICLRGNTLFSGYHKREDLTKEVMV------DG--WFHTGDIGEW 503
Cdd:PRK05691 1442 RSPIGRPLGNVLCRVLD------AELNLLPPGvagELCIGGAGLARGYLGRPALTAERFVpdplgeDGarLYRTGDRARW 1515
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 356575070 504 QSNGAMKIIDRKKNIFKLsQGEYIAVENIENKYLQCPLIA 543
Cdd:PRK05691 1516 NADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLAQPGVA 1554
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
214-294 |
7.06e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 39.33 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356575070 214 LPSKKKTDICTIMYTSGTTGDPKGVVIKNEAFmaevLSVDHIIMLTDRVAGEDDVYFSfLPLAHVYDQIMET-YCISKGS 292
Cdd:cd05939 98 QDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRY----YRIAAGAYYAFGMRPEDVVYDC-LPLYHSAGGIMGVgQALLHGS 172
|
..
gi 356575070 293 SI 294
Cdd:cd05939 173 TV 174
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
220-294 |
8.49e-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: 39.20 E-value: 8.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356575070 220 TDICTIMYTSGTTGDPKGVVIKNEafmaEVLSVDHIIMLtdRVAGEDDVYFSFLPLAHVYDQIMETY-CISKGSSI 294
Cdd:cd05938 144 KSPALYIYTSGTTGLPKAARISHL----RVLQCSGFLSL--CGVTADDVIYITLPLYHSSGFLLGIGgCIELGATC 213
|
|
| |
