|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1-660 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 1423.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 1 MKSFAAKAEEGVKGIDGKPSVGPVYRNLLSEKGFPPIDSEITTAWDIFSKSVEKFPDNNMLGWRRIVDEKVGPYMWKTYK 80
Cdd:PLN02430 1 MKSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 81 EVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIK 160
Cdd:PLN02430 81 EVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 161 GLLEPDCKCAKRLKAIVSFTNVSDELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVL 240
Cdd:PLN02430 161 ELLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 241 THQAVATFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKPTYLAGVP 320
Cdd:PLN02430 241 THEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 321 RVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGYSHSKASPMADFIAFRKIRDKLGGRIRLLVSGGAPLSPEIE 400
Cdd:PLN02430 321 RVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 401 EFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAEMGYDPLGENPAGEICIRGQCMFSGYY 480
Cdd:PLN02430 401 EFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 481 KNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSMLVAVV 560
Cdd:PLN02430 481 KNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 561 VPNPETINRWAKDLGFTKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNL 640
Cdd:PLN02430 561 VPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNL 640
|
650 660
....*....|....*....|
gi 2065806855 641 LKYYQVQIDEMYRKLASKKI 660
Cdd:PLN02430 641 LKYYQVEIDEMYRKLAEKRI 660
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
72-653 |
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: 843.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAE--PGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEI 149
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 150 DFVFVQDtkikgllepdckcakrlkaivsftnvsdelshkaseiGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTS 229
Cdd:cd05927 81 SIVFCDA-------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 230 GTSGDPKGVVLTHQAVATFVVGMDIFMDQFeDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQ 309
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEIL-NKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 310 ELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGysHSKASPMADFIAFRKIRDKLGGRIRLLV 389
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSG--VVRASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 390 SGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCmLGTVGIPAVYNEIRLEEVAEMGYDPLGENPAGEIC 469
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDVPEMNYDAKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 470 IRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVY 548
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 549 GDSFKSMLVAVVVPNPETINRWAKD-LGFTKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKPFDVERD 627
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAASkGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
570 580
....*....|....*....|....*.
gi 2065806855 628 LVTATLKNRRNNLLKYYQVQIDEMYR 653
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
2-658 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 757.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 2 KSFAAKAEEGVKGIDGKPSVGPVYRNLLSEKGFP-PIDSeITTAWDIFSKSVEKFPDNNMLGWRRIVDEKVGPYMWKTYK 80
Cdd:PLN02614 5 KKFIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPnPIEG-MDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 81 EVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIK 160
Cdd:PLN02614 84 EVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 161 GLLEPDCKCAKRLKAIVSFTNVSDELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVL 240
Cdd:PLN02614 164 ELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 241 THQAVATFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKPTYLAGVP 320
Cdd:PLN02614 244 SNESIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 321 RVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGYSHSKASPMADFIAFRKIRDKLGGRIRLLVSGGAPLSPEIE 400
Cdd:PLN02614 324 RVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 401 EFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAEMGYDPLGENPAGEICIRGQCMFSGYY 480
Cdd:PLN02614 404 SFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTLFSGYY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 481 KNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSMLVAVV 560
Cdd:PLN02614 484 KREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 561 VPNPETINRWAKDLGFTKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNL 640
Cdd:PLN02614 564 NPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQL 643
|
650
....*....|....*...
gi 2065806855 641 LKYYQVQIDEMYRKLASK 658
Cdd:PLN02614 644 LKYYQSVIDEMYKTTNEK 661
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-653 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 756.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 1 MKSFAAKAEEGVKGIDGKPSVGPVYRNLLSEKGFPPIDSEITTAWDIFSKSVEKFPDNNMLGWRRIVDEKVGPYMWKTYK 80
Cdd:PLN02861 2 AETYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 81 EVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIK 160
Cdd:PLN02861 82 EVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKIS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 161 GLLEPDCKCAKRLKAIVSFTNVSDELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAfNICTIMYTSGTSGDPKGVVL 240
Cdd:PLN02861 162 SILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKT-DICTIMYTSGTTGEPKGVIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 241 THQAVATFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKPTYLAGVP 320
Cdd:PLN02861 241 TNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 321 RVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGYSHSKASPMADFIAFRKIRDKLGGRIRLLVSGGAPLSPEIE 400
Cdd:PLN02861 321 RVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 401 EFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAEMGYDPLGENPAGEICIRGQCMFSGYY 480
Cdd:PLN02861 401 EFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 481 KNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSMLVAVV 560
Cdd:PLN02861 481 KRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 561 VPNPETINRWAKDLGFTKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNL 640
Cdd:PLN02861 561 VPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQL 640
|
650
....*....|...
gi 2065806855 641 LKYYQVQIDEMYR 653
Cdd:PLN02861 641 LKYYKDCIDQLYS 653
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
24-656 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 580.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 24 VYRNLLSE----KGFPPIDsEITTAWDIFSKSVEKFPDNNMLGWRRIVDEKVGPYMWKTYKEVYEEVLQIGSALRAVGAE 99
Cdd:PLN02736 23 VYRSARSPlklvSRFPDHP-EIGTLHDNFVYAVETFRDYKYLGTRIRVDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 100 PGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIKGLLE--PDCKCakrLKAIV 177
Cdd:PLN02736 102 KGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSclSEIPS---VRLIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 178 SFTNVSDELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMD 257
Cdd:PLN02736 179 VVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 258 QFEdkmthDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQEL 337
Cdd:PLN02736 259 FYP-----SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKES 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 338 NPRRRLIFNALYKHKLAWMNRGYShskASPMADFIAFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGL 417
Cdd:PLN02736 334 GGLKERLFNAAYNAKKQALENGKN---PSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 418 TET---LGGTALGfpDEMCmlGTVGIPAVYNEIRLEEVAEMGY----DPLgenPAGEICIRGQCMFSGYYKNPELTEEVI 490
Cdd:PLN02736 411 TETscvISGMDEG--DNLS--GHVGSPNPACEVKLVDVPEMNYtsedQPY---PRGEICVRGPIIFKGYYKDEVQTREVI 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 491 -KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSMLVAVVVPNPETINR 569
Cdd:PLN02736 484 dEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 570 WAKDLGF-TKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNLLKYYQVQI 648
Cdd:PLN02736 564 WAASEGIkYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAI 643
|
....*...
gi 2065806855 649 DEMYRKLA 656
Cdd:PLN02736 644 SDMYAELA 651
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
39-654 |
6.54e-171 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 501.17 E-value: 6.54e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 39 SEITTAWDIFSKSVEKFPDNNMLGWRRivdekVGPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAM 118
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKE-----DGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 119 EACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIKGLLEPDCKCAKRLKAIVSFtnvsDElshKASEIGVKTY 198
Cdd:COG1022 83 LAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVL----DP---RGLRDDPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 199 SWLDFLHMGREKPEET------NPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSF 272
Cdd:COG1022 156 SLDELLALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-----LGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 273 LPLAHILDRMNEEYFFRKGASVgYYHGDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHK 352
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATV-AFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 353 LAWMNRGYSHSKASPM-------ADFIAFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLR---VTcccfVVQGYGLTETLG 422
Cdd:COG1022 310 RRYARARLAGKSPSLLlrlkhalADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRalgIP----VLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 423 GTALGFPDEMcMLGTVGIPAVYNEIRLeevaemgydplGENpaGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIG 501
Cdd:COG1022 386 VITVNRPGDN-RIGTVGPPLPGVEVKI-----------AED--GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 502 EILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSfKSMLVAVVVPNPETINRWAKDLGFT-KPF 580
Cdd:COG1022 452 ELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSY 530
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065806855 581 EELCSFPELKEHIISELkstAEKNK-LRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNLLKYYQVQIDEMYRK 654
Cdd:COG1022 531 AELAQDPEVRALIQEEV---DRANAgLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
72-640 |
2.41e-166 |
|
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: 485.95 E-value: 2.41e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYivehaeidf 151
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIH--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 vfvqdtkikGLLEPDCKcakrlkAIvsFTNvsdelshkaseigvktyswldflhmgrEKPEEtnppkafnICTIMYTSGT 231
Cdd:cd17639 72 ---------SLNETECS------AI--FTD---------------------------GKPDD--------LACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTHQAVATFVVGMDIFMDQFedkMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYyhGDLNVLRD----- 306
Cdd:cd17639 100 TGNPKGVMLTHGNLVAGIAGLGDRVPEL---LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 307 ---DIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGYShskaSPMADFIAFRKIRDKLGG 383
Cdd:cd17639 175 ckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG----TPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 384 RIRLLVSGGAPLSPEIEEFLRVTCCCfVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLEEVAEMGYDPLGEN 463
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIVLCP-VIQGYGLTETCAGGTVQDPGDL-ETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 464 PAGEICIRGQCMFSGYYKNPELTEEVIK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVV 542
Cdd:cd17639 329 PRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 543 QDIWVYGDSFKSMLVAVVVPNPETINRWAKDLGF-TKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKP 621
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*....
gi 2065806855 622 FDVERDLVTATLKNRRNNL 640
Cdd:cd17639 489 WTPENGLVTAAQKLKRKEI 507
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
72-638 |
3.22e-127 |
|
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: 383.48 E-value: 3.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDF 151
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 VFVqdtkikgllepdckcakrlkaivsftnvsdelshkaseigvktyswldflhmgrEKPEETnppkafniCTIMYTSGT 231
Cdd:cd05907 81 LFV------------------------------------------------------EDPDDL--------ATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHILDRMNEEYF-FRKGASVGYYHGDlNVLRDDIQE 310
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLP-----ATEGDRHLSFLPLAHVFERRAGLYVpLLAGARIYFASSA-ETLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 311 LKPTYLAGVPRVFERIHEGI-QKALQELnprRRLIFnalykhKLAwmnrgyshskaspmadfiafrkirdkLGGRIRLLV 389
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAIkVKAVPGL---KRKLF------DLA--------------------------VGGRLRFAA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 390 SGGAPLSPEIEEFLRvTCCCFVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLeevaemgydplgeNPAGEIC 469
Cdd:cd05907 218 SGGAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDN-RIGTVGKPLPGVEVRI-------------ADDGEIL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 470 IRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVY 548
Cdd:cd05907 283 VRGPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVI 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 549 GDSfKSMLVAVVVPNPETINRWAKDLG-FTKPFEELCSFPELKEHIISELKSTAEknKLRKFEYIKAVAVETKPFDVERD 627
Cdd:cd05907 363 GDG-RPFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENG 439
|
570
....*....|.
gi 2065806855 628 LVTATLKNRRN 638
Cdd:cd05907 440 ELTPTLKLKRP 450
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
41-652 |
1.57e-122 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 379.85 E-value: 1.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 41 ITTAWDIFSKSVEKFPDNNMLGWRRIVD------------EKV--GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGI 106
Cdd:PLN02387 57 ATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfEKLhlGEYEWITYGQVFERVCNFASGLVALGHNKEERVAI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 107 YGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIKGL--LEPDCKCAKRLKAIVSFTNVSD 184
Cdd:PLN02387 137 FADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLidISSQLETVKRVIYMDDEGVDSD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 185 ELSHKASEIGVKTYSwlDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTH-QAVATFVVGMDIFmdqfeDKM 263
Cdd:PLN02387 217 SSLSGSSNWTVSSFS--EVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHgNIVATVAGVMTVV-----PKL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 264 THDDVYLSFLPLAHILDRMNEEYFFRKGASVGYyhGDLNVLRD-----------DIQELKPTYLAGVPRVFERIHEGIQK 332
Cdd:PLN02387 290 GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 333 ALQELNPRRRLIFNALYKHKLAWMNRGYSHSKASPMA--DFIAFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCF 410
Cdd:PLN02387 368 KVDAKGGLAKKLFDIAYKRRLAAIEGSWFGAWGLEKLlwDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAP 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 411 VVQGYGLTETLGGTALGFPDEMCmLGTVGIPAVYNEIRLEEVAEMGY----DPLgenPAGEICIRGQCMFSGYYKNPELT 486
Cdd:PLN02387 448 IGQGYGLTETCAGATFSEWDDTS-VGRVGPPLPCCYVKLVSWEEGGYlisdKPM---PRGEIVIGGPSVTLGYFKNQEKT 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 487 EEVIKDG-----WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSMLVAVVV 561
Cdd:PLN02387 524 DEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVV 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 562 PNPETINRWAKDLGFT-KPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNL 640
Cdd:PLN02387 604 PSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQI 683
|
650
....*....|..
gi 2065806855 641 LKYYQVQIDEMY 652
Cdd:PLN02387 684 RKKFKDDLKKLY 695
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
48-522 |
6.66e-120 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 363.56 E-value: 6.66e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 48 FSKSVEKFPDnnmlgwRRIVDekVGPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLI 127
Cdd:pfam00501 1 LERQAARTPD------KTALE--VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 128 CVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIkglLEPDCKCAKRLKAIVSfTNVSDELSHKASEIGVKTYSWLDflhmg 207
Cdd:pfam00501 73 YVPLNPRLPAEELAYILEDSGAKVLITDDALK---LEELLEALGKLEVVKL-VLVLDRDPVLKEEPLPEEAKPAD----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 208 rEKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIfMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYF 287
Cdd:pfam00501 144 -VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKR-VRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 288 -FRKGASVGYYHG----DLNVLRDDIQELKPTYLAGVPRVFERIhegiqkaLQELNPRRRlifnalykhklawmnrgysh 362
Cdd:pfam00501 222 pLLAGATVVLPPGfpalDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRA-------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 363 skaspmadfiafrkirdkLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDE--MCMLGTVGI 440
Cdd:pfam00501 275 ------------------LLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDedLRSLGSVGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 441 PAVYNEIRLEEVAEMGYDPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIK-DGWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPVPPGE--PGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
...
gi 2065806855 520 KLS 522
Cdd:pfam00501 415 KLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
74-654 |
3.36e-111 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 350.43 E-value: 3.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 74 YMwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:PTZ00216 121 YI--TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQDTKIKGLLepdckcakRLKAIVSFTNVS----DELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFN---ICTIM 226
Cdd:PTZ00216 199 CNGKNVPNLL--------RLMKSGGMPNTTiiylDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPENnddLALIM 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 227 YTSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYyhGDLNVLRD 306
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 307 -------DIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGyshsKASPMADFIAFRKIRD 379
Cdd:PTZ00216 349 tfarphgDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEG----KDTPYWNEKVFSAPRA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 380 KLGGRIRLLVSGGAPLSPEIEEFLRVtccCF--VVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLEEVAEMGY 457
Cdd:PTZ00216 425 VLGGRVRAMLSGGGPLSAATQEFVNV---VFgmVIQGWGLTETVCCGGIQRTGDL-EPNAVGQLLKGVEMKLLDTEEYKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 458 DPLGEnPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIF 536
Cdd:PTZ00216 501 TDTPE-PRGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALY 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 537 GQNSVVQD--IWVYGDSFKSMLVAVVVPNPETINRWAKDLGFTKPFEELCSFPELKEHIISELKSTAEKNKLRKFEYIKA 614
Cdd:PTZ00216 580 GQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRH 659
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2065806855 615 VAVETKPFDVERDLVTATLKNRRNNLLKYYQVQIDEMYRK 654
Cdd:PTZ00216 660 VRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
72-638 |
2.42e-82 |
|
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: 267.69 E-value: 2.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEAcaahtlicvplydTLGSGAVD---------- 141
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQG-------------IMALGAVDvvrgsdssve 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 142 ---YIVEHAEIDFVFVQdtkikgllepdckcakrlkaivsftnvsdelshkaseigvktyswldflhmgrekpeetNPPK 218
Cdd:cd17640 68 ellYILNHSESVALVVE-----------------------------------------------------------NDSD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 219 afNICTIMYTSGTSGDPKGVVLTHqavATFVVGMDIFMDQFEDKMThdDVYLSFLPLAHILDRMNEEYFFRKGASVGYyh 298
Cdd:cd17640 89 --DLATIIYTSGTTGNPKGVMLTH---ANLLHQIRSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAY-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 299 GDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALykhklawmnrgyshskaspmadfiafrkir 378
Cdd:cd17640 160 TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF------------------------------ 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 379 dKLGGRIRLLVSGGAPLSPEIEEFLRVTCCcFVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLeeVAEMGYD 458
Cdd:cd17640 210 -LSGGIFKFGISGGGALPPHVDTFFEAIGI-EVLNGYGLTETSPVVSARRLKCN-VRGSVGRPLPGTEIKI--VDPEGNV 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 459 PLGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFG 537
Cdd:cd17640 285 VLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALM 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 538 QNSVVQDIWVYGDSFKSmLVAVVVPNPETINRWAKDLGFTKPFEE---LCSFPELKEHIISELKSTAEKNKLRKFEYIKA 614
Cdd:cd17640 365 RSPFIEQIMVVGQDQKR-LGALIVPNFEELEKWAKESGVKLANDRsqlLASKKVLKLYKNEIKDEISNRPGFKSFEQIAP 443
|
570 580
....*....|....*....|....
gi 2065806855 615 VAVETKPFdVERDLVTATLKNRRN 638
Cdd:cd17640 444 FALLEEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
78-644 |
1.52e-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: 248.15 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVqdt 157
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikGLLEpDCKCAKrlkaivsfTNVSDELSHKAS---EIGVKTYSWLDFLHMGREKpEETNPPKAFNICTIMYTSGTSGD 234
Cdd:cd05932 85 ---GKLD-DWKAMA--------PGVPEGLISISLpppSAANCQYQWDDLIAQHPPL-EERPTRFPEQLATLIYTSGTTGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 235 PKGVVLTHQAVA-TFVVGMDIFMDQFEDKMthddvyLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKP 313
Cdd:cd05932 152 PKGVMLTFGSFAwAAQAGIEHIGTEENDRM------LSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 314 TYLAGVPRVFERIHEGIQKALqelnPRRRLifNALYKhklawmnrgyshskaSPMADFIAFRKIRDKLG-GRIRLLVSGG 392
Cdd:cd05932 226 TLFFSVPRLWTKFQQGVQDKI----PQQKL--NLLLK---------------IPVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 393 APLSPEIEEFLRvTCCCFVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLEEvaemgydplgenpAGEICIRG 472
Cdd:cd05932 285 APVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRD-KIGTVGNAGPGVEVRISE-------------DGEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 473 QCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDS 551
Cdd:cd05932 350 PALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 552 FkSMLVAVVVPNpETINRWAkDLGFTKPFEElcsfpELKEHIiselkstAEKNK-LRKFEYIKAVAVETKPFDVERDLVT 630
Cdd:cd05932 430 L-PAPLALVVLS-EEARLRA-DAFARAELEA-----SLRAHL-------ARVNStLDSHEQLAGIVVVKDPWSIDNGILT 494
|
570
....*....|....
gi 2065806855 631 ATLKNRRNNLLKYY 644
Cdd:cd05932 495 PTLKIKRNVLEKAY 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
45-564 |
1.07e-72 |
|
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: 241.64 E-value: 1.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 45 WDIFSKSVEKFPDNNML--GWRRIvdekvgpymwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACA 122
Cdd:COG0318 2 ADLLRRAAARHPDRPALvfGGRRL-----------TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 123 AHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVqdtkikgllepdckcakrlkaivsftnvsdelshkaseigvktyswld 202
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 203 flhmgrekpeetnppkafniCTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHI---L 279
Cdd:COG0318 103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG-----LTPGDVVLVALPLFHVfglT 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 280 DRMNeeYFFRKGASVgYYHGDLNVLR--DDIQELKPTYLAGVPRVFERIhegiqkaLQELNPRRRlifnalykhklawmn 357
Cdd:COG0318 158 VGLL--APLLAGATL-VLLPRFDPERvlELIERERVTVLFGVPTMLARL-------LRHPEFARY--------------- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 358 rgyshskaspmaDFiafrkirdklgGRIRLLVSGGAPLSPE-IEEFLRVTCCCFVvQGYGLTETLGGTALGFPDEM-CML 435
Cdd:COG0318 213 ------------DL-----------SSLRLVVSGGAPLPPElLERFEERFGVRIV-EGYGLTETSPVVTVNPEDPGeRRP 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 436 GTVGIPAVYNEIRLeeVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDR 514
Cdd:COG0318 269 GSVGRPLPGVEVRI--VDEDGRElPPGE--VGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGR 344
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2065806855 515 KKNLIKLSqGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP 564
Cdd:COG0318 345 KKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVVGvpdEKWGERVVAFVVLRP 396
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
78-652 |
2.82e-72 |
|
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: 244.57 E-value: 2.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIA-MEACAAHTlICVPLYDTLGSGAVDYIVEHAEIDFVFVQD 156
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAaVGAIFAGG-IAVGIYTTNSPEACQYVAETSEANILVVEN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 TK-------IKGLLepdckcaKRLKAIVSFtnvSDELSHKasEIGVktYSWLDFLHMGREKPEET-----NPPKAFNICT 224
Cdd:cd05933 89 QKqlqkilqIQDKL-------PHLKAIIQY---KEPLKEK--EPNL--YSWDEFMELGRSIPDEQldaiiSSQKPNQCCT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVaTFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFfrkGASVG--YYHGDLN 302
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNI-TWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWL---PIKVGgqVYFAQPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 303 VLR----DDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIF----NALYKHKLAWMNRGYSHSKASPMADFIAF 374
Cdd:cd05933 231 ALKgtlvKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLMGGESPSPLFYRLAKKLVF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 375 RKIRDKLG-GRIRLLVSGGAPLSPEIEEFlrvtcccF------VVQGYGLTETLGGTALGFPDEMcMLGTVG--IPAVYN 445
Cdd:cd05933 311 KKVRKALGlDRCQKFFTGAAPISRETLEF-------FlslnipIMELYGMSETSGPHTISNPQAY-RLLSCGkaLPGCKT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 446 EIRLEEvaemgydplgENPAGEICIRGQCMFSGYYKNPELTEEVIK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQG 524
Cdd:cd05933 383 KIHNPD----------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITAGG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 525 EYVALEHLENIFGQN-SVVQDIWVYGDS--FKSMLVAV---VVP---------NPETINrWAKDLGFTKP-FEELCSFPE 588
Cdd:cd05933 453 ENVPPVPIEDAVKKElPIISNAMLIGDKrkFLSMLLTLkceVNPetgepldelTEEAIE-FCRKLGSQATrVSEIAGGKD 531
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 589 LK-----EHIISEL--KSTAEKNKLRKFeyikavAVETKPFDVERDLVTATLKNRRNNLLKYYQVQIDEMY 652
Cdd:cd05933 532 PKvyeaiEEGIKRVnkKAISNAQKIQKW------VILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
75-637 |
7.28e-65 |
|
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: 224.22 E-value: 7.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 75 MWK--TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMeaCAAHTLICVPL--YDTLGSGAVDYIVEHAEID 150
Cdd:cd17641 8 IWQefTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAE--LAAQAIGALSLgiYQDSMAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 151 FVFVQDT-KIKGLLEpdckCAKRLKAiVSFTNVSDELshkaseiGVKTY--SWL----DFLHMGREKP--------EETN 215
Cdd:cd17641 86 VVIAEDEeQVDKLLE----IADRIPS-VRYVIYCDPR-------GMRKYddPRLisfeDVVALGRALDrrdpglyeREVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 216 PPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFmdqfeDKMTHDDVYLSFLPLAHILDRMneeYFFRKGASVG 295
Cdd:cd17641 154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAA-----DPLGPGDEYVSVLPLPWIGEQM---YSVGQALVCG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 296 Y---YHGDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGYSHSK-------A 365
Cdd:cd17641 226 FivnFPEEPETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPvslwlrlA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 366 SPMADFIAFRKIRDKLG-GRIRLLVSGGAPLSPEIEEFLR---VTcccfVVQGYGLTETLGGTALgFPDEMCMLGTVGIP 441
Cdd:cd17641 306 SWLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHaigVP----LKQLYGQTELAGAYTV-HRDGDVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 442 AVYNEIRLEEVaemgydplgenpaGEICIRGQCMFSGYYKNPELT-EEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIK 520
Cdd:cd17641 381 FPGTEVRIDEV-------------GEILVRSPGVFVGYYKNPEATaEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 521 LSQGEYVALEHLENIFGQNSVVQDIWVYGDSfKSMLVAVVVPNPETINRWAKD--LGFTKpFEELCSFPELKEHIISEL- 597
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQrgIAFTT-YTDLASRPEVYELIRKEVe 525
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2065806855 598 ---KSTAEKNKLRKFeyikavAVETKPFDVERDLVTATLKNRR 637
Cdd:cd17641 526 kvnASLPEAQRIRRF------LLLYKELDADDGELTRTRKVRR 562
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
78-573 |
5.35e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 220.44 E-value: 5.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVqDT 157
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV-DS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEPdckcAKRLKAIVSFTNVSDELSHKASEIGVKTYS-WLDflhmgrEKPEeTNPPKAFN---ICTIMYTSGTSG 233
Cdd:PRK06187 112 EFVPLLAA----ILPQLPTVRTVIVEGDGPAAPLAPEVGEYEeLLA------AASD-TFDFPDIDendAAAMLYTSGTTG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 234 DPKGVVLTHQAVATFVVGMDIFMdqfedKMTHDDVYLSFLPLAHIldrmneeyffrkGAS-VGY---YHG---------D 300
Cdd:PRK06187 181 HPKGVVLSHRNLFLHSLAVCAWL-----KLSRDDVYLVIVPMFHV------------HAWgLPYlalMAGakqviprrfD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 301 LNVLRDDIQELKPTYLAGVPRvferihegiqkalqelnprrrlIFNALYKHKLAwmnrgyshskasPMADFiafrkirdk 380
Cdd:PRK06187 244 PENLLDLIETERVTFFFAVPT----------------------IWQMLLKAPRA------------YFVDF--------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 381 lgGRIRLLVSGGAPLSPE-IEEFLRVTCCCFvVQGYGLTETLG-GTALGFPDEMC----MLGTVGIPAVYNEIRL--EEV 452
Cdd:PRK06187 281 --SSLRLVIYGGAALPPAlLREFKEKFGIDL-VQGYGMTETSPvVSVLPPEDQLPgqwtKRRSAGRPLPGVEARIvdDDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 453 AEMgydPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYV-ALEh 531
Cdd:PRK06187 358 DEL---PPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIyPRE- 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 532 LENIFGQNSVVQDIWVYG---DSFKSMLVAVVVP------NPETINRWAKD 573
Cdd:PRK06187 433 LEDALYGHPAVAEVAVIGvpdEKWGERPVAVVVLkpgatlDAKELRAFLRG 483
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
45-573 |
6.73e-62 |
|
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: 213.19 E-value: 6.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 45 WDIFSKSVEKFPDNNMLgwrrIVDEKvgpymWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAH 124
Cdd:cd05936 2 ADLLEEAARRFPDKTAL----IFMGR-----KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 125 TLICVPLYDTLGSGAVDYIVEhaeidfvfvqdtkikgllepDCKCakrlKAIVSFTnvsdelshkaseigvktySWLDFL 204
Cdd:cd05936 73 GAVVVPLNPLYTPRELEHILN--------------------DSGA----KALIVAV------------------SFTDLL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 205 HMGrEKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMdqfEDKMTHDDVYLSFLPLAHILDR--- 281
Cdd:cd05936 111 AAG-APLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL---EDLLEGDDVVLAALPLFHVFGLtva 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 282 MNeeYFFRKGASVGYYHG--DLNVLrDDIQELKPTYLAGVPRvferihegiqkalqelnprrrlIFNALYKHKlawmnrg 359
Cdd:cd05936 187 LL--LPLALGATIVLIPRfrPIGVL-KEIRKHRVTIFPGVPT----------------------MYIALLNAP------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 360 yshskaspmadfiAFRKIRDKlggRIRLLVSGGAPLSPEI-EEFLRVTcCCFVVQGYGLTETLGGTALGFPDEMCMLGTV 438
Cdd:cd05936 235 -------------EFKKRDFS---SLRLCISGGAPLPVEVaERFEELT-GVPIVEGYGLTETSPVVAVNPLDGPRKPGSI 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 439 GIP--AVYNEIRLEEVAEMgydPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKK 516
Cdd:cd05936 298 GIPlpGTEVKIVDDDGEEL---PPGE--VGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKK 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 517 NLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP------ETINRWAKD 573
Cdd:cd05936 373 DMI-IVGGFNVYPREVEEVLYEHPAVAEAAVVGvpdPYSGEAVKAFVVLKEgaslteEEIIAFCRE 437
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
78-565 |
5.56e-60 |
|
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: 208.07 E-value: 5.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDt 157
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaivsftnvsdelshkaseigvktyswldflhmgrekPEETnppkafniCTIMYTSGTSGDPKG 237
Cdd:cd05914 88 -----------------------------------------------------EDDV--------ALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFmdqfeDKMTHDDVYLSFLPLAHILDRMNEE-YFFRKGASVgYYHGDL-NVLRDDIQELKPTY 315
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEV-----VLLGKGDKILSILPLHHIYPLTFTLlLPLLNGAHV-VFLDKIpSAKIIALAFAQVTP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 316 LAGVPRVFERIHEGIqKALQELNPRRRLIFnALYKHKLawmNRGYSHskaspmadfIAFRKIRDKLGGRIRLLVSGGAPL 395
Cdd:cd05914 181 TLGVPVPLVIEKIFK-MDIIPKLTLKKFKF-KLAKKIN---NRKIRK---------LAFKKVHEAFGGNIKEFVIGGAKI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 396 SPEIEEFLRVTCCCFVvQGYGLTETlGGTALGFPDEMCMLGTVGIPAVYNEIRLeevaemgYDPLGENPAGEICIRGQCM 475
Cdd:cd05914 247 NPDVEEFLRTIGFPYT-IGYGMTET-APIISYSPPNRIRLGSAGKVIDGVEVRI-------DSPDPATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 476 FSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEHLENIFGQNSVVQDIWVYGDSFKs 554
Cdd:cd05914 318 MKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK- 396
|
490
....*....|.
gi 2065806855 555 mLVAVVVPNPE 565
Cdd:cd05914 397 -LVALAYIDPD 406
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
224-631 |
6.05e-59 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 208.46 E-value: 6.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 224 TIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFEDKmthdDVYLSFLPLAHILDRMNEEYFFRKGAsVGYYHG--DL 301
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPA----SITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDM 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 302 NVLRDDIQELKPTYLAGVPRVFERIHegiQKALQELNPRrrlifnalykhklawmnrgyshSKASPMADFIAFR---KIR 378
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLF---QRYQAELDRR----------------------SVAGADAETLAERvkaELR 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 379 DK-LGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETlGGTALgfpdemcmLGTVGIPAVYnEIRLEEVAEMGY 457
Cdd:cd17632 357 ERvLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEA-GAVIL--------DGVIVRPPVL-DYKLVDVPELGY 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 458 ----DPlgeNPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDI-GEILPNGvLKIIDRKKNLIKLSQGEYVALEH 531
Cdd:cd17632 427 frtdRP---HPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVAR 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 532 LENIFGQNSVVQDIWVYGDSFKSMLVAVVVPNPETINRwakdlgftKPFEELcsFPELKEhiisELKSTAEKNKLRKFEY 611
Cdd:cd17632 503 LEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAG--------EDTARL--RAALAE----SLQRIAREAGLQSYEI 568
|
410 420
....*....|....*....|
gi 2065806855 612 IKAVAVETKPFDVERDLVTA 631
Cdd:cd17632 569 PRDFLIETEPFTIANGLLSG 588
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-587 |
6.25e-58 |
|
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: 198.66 E-value: 6.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 222 ICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDifmdqFEDKMTHDDVYLSFLPLAHIldrmneeyffrkGASVGY----Y 297
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALA-----ASGGLTEGDVFLSTLPLFHI------------GGLFGLlgalL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 298 HGDLNVLRDD---------IQELKPTYLAGVPRVFERIhegiqkaLQELNPRrrlifnalykhklawmnrGYSHSkaspm 368
Cdd:cd04433 65 AGGTVVLLPKfdpeaalelIEREKVTILLGVPTLLARL-------LKAPESA------------------GYDLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 369 adfiafrkirdklggRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDE-MCMLGTVGIPAVYNEI 447
Cdd:cd04433 115 ---------------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDdARKPGSVGRPVPGVEV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 448 RLeeVAEMGyDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYV 527
Cdd:cd04433 180 RI--VDPDG-GELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENV 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065806855 528 ALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP------ETINRWAKD-LGFTKP---FEELCSFP 587
Cdd:cd04433 256 YPAEVEAVLLGHPGVAEAAVVGvpdPEWGERVVAVVVLRPgadldaEELRAHVRErLAPYKVprrVVFVDALP 328
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
136-658 |
1.66e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 196.09 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 136 GSGAVDYIVEHAEIDFVFVQDTKIKGLLEPDCKCAKRLKaivsftnvsdELSHKASEIGVktySWLDFLHMGREKPEE-- 213
Cdd:PTZ00342 231 NNGNKNNKEEQKGNDLSNELEDISLGPLEYDKEKLEKIK----------DLKEKAKKLGI---SIILFDDMTKNKTTNyk 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 214 -TNPPKAFnICTIMYTSGTSGDPKGVVLTHQAVATFVVGM---DIFmdqfedKMTHDDVYLSFLPLAHILDRMNEEYFFR 289
Cdd:PTZ00342 298 iQNEDPDF-ITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLckhSIF------KKYNPKTHLSYLPISHIYERVIAYLSFM 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 290 KGASVGYYHGDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHKLAWMNRGYShskaspma 369
Cdd:PTZ00342 371 LGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFS-------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 370 DFI-----AFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETlGGTALGFPDEMCMLGTVGIPAVY 444
Cdd:PTZ00342 443 KFLegithISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTET-TGPIFVQHADDNNTESIGGPISP 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 445 N---EIRLEEVaemgYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIK 520
Cdd:PTZ00342 522 NtkyKVRTWET----YKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 521 LSQGEYVALEHLENIFGQNSVVQDIWVYGDSfkSMlvavvvPNPETINRWAKDLGFTkpfeelcsfpELKEHIISELKST 600
Cdd:PTZ00342 598 LSQGEYIETDMLNNLYSQISFINFCVVYGDD--SM------DGPLAIISVDKYLLFK----------CLKDDNMLESTGI 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 601 AEKNKLRKF-----------EYIKAVAVET-------------------KPFDVERDLvTATLKNRRNNLLKYYQVQIDE 650
Cdd:PTZ00342 660 NEKNYLEKLtdetinnniyvDYVKGKMLEVykktnlnryniindiyltsKVWDTNNYL-TPTFKVKRFYVFKDYAFFIDQ 738
|
....*...
gi 2065806855 651 MYRKLASK 658
Cdd:PTZ00342 739 VKKIYKNK 746
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
78-564 |
6.51e-51 |
|
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: 183.95 E-value: 6.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEpDCKCAKRLKAIVSFTnvsdelSHKASEIGVKTyswLDFLHMGREKPEETNPPK--AFNICTIMYTSGTSGDP 235
Cdd:cd05911 92 GLEKVKE-AAKELGPKDKIIVLD------DKPDGVLSIED---LLSPTLGEEDEDLPPPLKdgKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHqavATFVVGMDIFMDQFEDKMTHDDVYLSFLPLAH------------------ILDRMNEEYFFrkgasvgyy 297
Cdd:cd05911 162 KGVCLSH---RNLIANLSQVQTFLYGNDGSNDVILGFLPLYHiyglfttlasllngatviIMPKFDSELFL--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 298 hgdlnvlrDDIQELKPTYLAGVPRvferihegiqkalqelnprrrlIFNALYKHklawmnrgyshskasPMADFIAFRKI 377
Cdd:cd05911 230 --------DLIEKYKITFLYLVPP----------------------IAAALAKS---------------PLLDKYDLSSL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 378 RDklggrirlLVSGGAPLSPEIEEFL-RVTCCCFVVQGYGLTETlGGTALGFPDEMCMLGTVGIPAVYNEIRLeeVAEMG 456
Cdd:cd05911 265 RV--------ILSGGAPLSKELQELLaKRFPNATIKQGYGMTET-GGILTVNPDGDDKPGSVGRLLPNVEAKI--VDDDG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 457 YDPLGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENI 535
Cdd:cd05911 334 KDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
490 500 510
....*....|....*....|....*....|..
gi 2065806855 536 FGQNSVVQDIWVYG--DSFKSML-VAVVVPNP 564
Cdd:cd05911 413 LLEHPGVADAAVIGipDEVSGELpRAYVVRKP 444
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
78-564 |
2.21e-48 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 175.49 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFvqdt 157
Cdd:cd17631 22 TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaivsftnvsDELshkaseigvktyswldflhmgrekpeetnppkafniCTIMYTSGTSGDPKG 237
Cdd:cd17631 98 --------------------------DDL------------------------------------ALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVV--GMDIFMDQfedkmthDDVYLSFLPLAHI--LDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKP 313
Cdd:cd17631 116 AMLTHRNLLWNAVnaLAALDLGP-------DDVLLVVAPLFHIggLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 314 TYLAGVPrvferihegiqkalqelnprrrLIFNALYKHKLAwmnRGYSHSkaspmadfiafrkirdklggRIRLLVSGGA 393
Cdd:cd17631 189 TSFFLVP----------------------TMIQALLQHPRF---ATTDLS--------------------SLRAVIYGGA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 394 PLSPEIEEFLRVTCCCFVvQGYGLTETLGG-TALGFPDEMCMLGTVGIPAVYNEIRLeeVAEMGyDPLGENPAGEICIRG 472
Cdd:cd17631 224 PMPERLLRALQARGVKFV-QGYGMTETSPGvTFLSPEDHRRKLGSAGRPVFFVEVRI--VDPDG-REVPPGEVGEIVVRG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 473 QCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYG--- 549
Cdd:cd17631 300 PHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIGvpd 378
|
490
....*....|....*
gi 2065806855 550 DSFKSMLVAVVVPNP 564
Cdd:cd17631 379 EKWGEAVVAVVVPRP 393
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
78-519 |
2.38e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 174.71 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAmeACAAHTL--ICVPLYDTLGSGAVDYIVEHAEIDFVFVQ 155
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIA--ALGALKAgaVVVPLNTRYTADEAAYILARGDAKALFVL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 DtkikGLLEPDCKCAKRLKAIVSFTNVSDElshKASEIGVKTYSWLDFLHMGrEKPEETNPPKAFNICTIMYTSGTSGDP 235
Cdd:PRK07656 110 G----LFLGVDYSATTRLPALEHVVICETE---EDDPHTEKMKTFTDFLAAG-DPAERAPEVDPDDVADILFTSGTTGRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHQAVatfvvgmdifMDQFED-----KMTHDDVYLSFLPLAHIldrmneeyF---------FRKGASVgYYHGDL 301
Cdd:PRK07656 182 KGAMLTHRQL----------LSNAADwaeylGLTEGDRYLAANPFFHV--------FgykagvnapLMRGATI-LPLPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 302 NVLR--DDIQELKPTYLAGVPRvferihegiqkalqelnprrrlIFNALYKHklawmnrgyshskasPMADFIAFRKIRd 379
Cdd:PRK07656 243 DPDEvfRLIETERITVLPGPPT----------------------MYNSLLQH---------------PDRSAEDLSSLR- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 380 klggrirLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTETLGGTALGFPDE--MCMLGTVGIPAVYNEIRLeeVAEMG 456
Cdd:PRK07656 285 -------LAVTGAASMPVAlLERFESELGVDIVLTGYGLSEASGVTTFNRLDDdrKTVAGTIGTAIAGVENKI--VNELG 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065806855 457 yDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIK-DGWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:PRK07656 356 -EEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
212-520 |
6.81e-41 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 156.24 E-value: 6.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 212 EETNPPKAF----NICTIMYTSGTSGDPKGVVLTHQavaTFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHIldrmneeYF 287
Cdd:cd05904 146 DEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHR---NLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHI-------YG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 288 F--------RKGASV----GYyhgDLNVLRDDIQELKPTYLAGVPrvferihegiqkalqelnPrrrlIFNALYKHKLAw 355
Cdd:cd05904 216 LssfalgllRLGATVvvmpRF---DLEELLAAIERYKVTHLPVVP------------------P----IVLALVKSPIV- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 356 mnRGYSHSKaspmadfiafrkirdklggrIRLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEM-- 432
Cdd:cd05904 270 --DKYDLSS--------------------LRQIMSGAAPLGKElIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKdr 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 433 CMLGTVGipavyneiRLEEVAEMGY-DP-----LGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILP 505
Cdd:cd05904 328 AKYGSVG--------RLVPNVEAKIvDPetgesLPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDE 399
|
330
....*....|....*
gi 2065806855 506 NGVLKIIDRKKNLIK 520
Cdd:cd05904 400 DGYLFIVDRLKELIK 414
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-566 |
2.19e-39 |
|
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: 150.13 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVqdt 157
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaivsftnvsdelshkaseigvktyswldflhmgrekpeetnppkafNICTIMYTSGTSGDPKG 237
Cdd:cd05934 82 ---------------------------------------------------------------DPASILYTSGTTGPPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHIldrmNEEYFfrkGASVGYYHGDLNVLR---------DDI 308
Cdd:cd05934 99 VVITHANLTFAGYYSARRFG-----LGEDDVYLTVLPLFHI----NAQAV---SVLAALSVGATLVLLprfsasrfwSDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 309 QELKPTYLAGVPRVFERIHEgiqkalQELNPRRRlifnalykhklawmnrgyshskaspmadfiafrkirdklGGRIRLl 388
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLA------QPPSPDDR---------------------------------------AHRLRA- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 389 VSGGAPLSPEIEEFlrvtCCCF---VVQGYGLTETLGGTAlGFPDEMCMLGTVGIPAVYNEIRLeeVAEMGYD-PLGEnp 464
Cdd:cd05934 201 AYGAPNPPELHEEF----EERFgvrLLEGYGMTETIVGVI-GPRDEPRRPGSIGRPAPGYEVRI--VDDDGQElPAGE-- 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 465 AGEICIR---GQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSV 541
Cdd:cd05934 272 PGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPA 350
|
490 500
....*....|....*....|....*....
gi 2065806855 542 VQDIWVYG--DSFK--SMLVAVVVPNPET 566
Cdd:cd05934 351 VREAAVVAvpDEVGedEVKAVVVLRPGET 379
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
46-565 |
1.60e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 149.70 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 46 DIFSKSVEKFPDNNMLGWRRIVdekvgpymWkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHT 125
Cdd:PRK08316 15 DILRRSARRYPDKTALVFGDRS--------W-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 126 LICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTkikglLEPDCKCAKRLKAIVSFTnVSDELSHKASEIGvktysWLDFLH 205
Cdd:PRK08316 86 AVHVPVNFMLTGEELAYILDHSGARAFLVDPA-----LAPTAEAALALLPVDTLI-LSLVLGGREAPGG-----WLDFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 206 MGreKPEETNPPKAF----NICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHI--L 279
Cdd:PRK08316 155 WA--EAGSVAEPDVEladdDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD-----MSADDIPLHALPLYHCaqL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 280 DRMNEEYFfrkgasvgyYHGDLNVLRDdiqelKPTylagVPRVFERIHEGiqKALQELNP-------RRRLIFNalyKHK 352
Cdd:PRK08316 228 DVFLGPYL---------YVGATNVILD-----APD----PELILRTIEAE--RITSFFAPptvwislLRHPDFD---TRD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 353 LAWMNRGYshSKASPMADFIaFRKIRDKLGGrirllvsggaplspeieefLRVTCCcfvvqgYGLTEtLG--GTALGFPD 430
Cdd:PRK08316 285 LSSLRKGY--YGASIMPVEV-LKELRERLPG-------------------LRFYNC------YGQTE-IAplATVLGPEE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 431 EMCMLGTVGIPAVYNEIRLeeVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVL 509
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRV--VDDDGNDvAPGE--VGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYI 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 510 KIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPE 565
Cdd:PRK08316 412 TVVDRKKDMIK-TGGENVASREVEEALYTHPAVAEVAVIGlpdPKWIEAVTAVVVPKAG 469
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-535 |
3.46e-38 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 148.55 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEAcaahtlicVPlydtlGSGAV-------------DYIV 144
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYA--------VP-----GMGAVlhtinprlfpeqiAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 145 EHAEIDFVFVqDTKIKGLLEPDCKCAKRLKAIVSFTNVSDElshkASEIGVKTYSWLDFLhmGREKPEETNPPKAFN-IC 223
Cdd:cd12119 94 NHAEDRVVFV-DRDFLPLLEAIAPRLPTVEHVVVMTDDAAM----PEPAGVGVLAYEELL--AAESPEYDWPDFDENtAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 224 TIMYTSGTSGDPKGVVLTHQAVA--TFVVGMDIFMDqfedkMTHDDVYLSFLPLAHIldrmNEEYFFRKGASVG------ 295
Cdd:cd12119 167 AICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLG-----LSESDVVLPVVPMFHV----NAWGLPYAAAMVGaklvlp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 296 --YYHGDlnVLRDDIQELKPTYLAGVPRVferihegiqkaLQELnprrrlifnalykhkLAWMNRGYSHSKAspmadfia 373
Cdd:cd12119 238 gpYLDPA--SLAELIEREGVTFAAGVPTV-----------WQGL---------------LDHLEANGRDLSS-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 374 frkirdklggrIRLLVSGGAPLSPE-IEEFLR--VTcccfVVQGYGLTETLG-GTALGFPDEMCMLG---------TVGI 440
Cdd:cd12119 282 -----------LRRVVIGGSAVPRSlIEAFEErgVR----VIHAWGMTETSPlGTVARPPSEHSNLSedeqlalraKQGR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 441 PAVYNEIRL--EEVAEMGYDplGENpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNL 518
Cdd:cd12119 347 PVPGVELRIvdDDGRELPWD--GKA-VGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDV 423
|
490
....*....|....*..
gi 2065806855 519 IKlSQGEYVALEHLENI 535
Cdd:cd12119 424 IK-SGGEWISSVELENA 439
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
37-573 |
6.38e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 148.61 E-value: 6.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 37 IDSEITTAWDIFSKSVEKFPDNNMLgwrrivdEKVGPYMwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWII 116
Cdd:PRK05605 27 LDYGDTTLVDLYDNAVARFGDRPAL-------DFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 117 AMEACaahtlicvplydtLGSGAVdyIVEH------AEIDFVF---------VQDtKIKGLLE--PDckcAKRLKAIVSF 179
Cdd:PRK05605 98 AFYAV-------------LRLGAV--VVEHnplytaHELEHPFedhgarvaiVWD-KVAPTVErlRR---TTPLETIVSV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 180 TNVS---------------------DELSHKASEigvkTYSWLDFLH--MGREKPEETNP-PKAFNICTIMYTSGTSGDP 235
Cdd:PRK05605 159 NMIAampllqrlalrlpipalrkarAALTGPAPG----TVPWETLVDaaIGGDGSDVSHPrPTPDDVALILYTSGTTGKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHQAVATFVVGMDIFMDQFEDKmthDDVYLSFLPLAHIldrmneeYFFRKGASVGYYHG---------DLNVLRD 306
Cdd:PRK05605 235 KGAQLTHRNLFANAAQGKAWVPGLGDG---PERVLAALPMFHA-------YGLTLCLTLAVSIGgelvllpapDIDLILD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 307 DIQELKPTYLAGVPRVFERIHEGIQKalqelnprrrlifnalykhklawmnRGYShskaspmadfiafrkirdkLGGrIR 386
Cdd:PRK05605 305 AMKKHPPTWLPGVPPLYEKIAEAAEE-------------------------RGVD-------------------LSG-VR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 387 LLVSGGAPLSPEI-EEFLRVTCCcFVVQGYGLTETlGGTALGFP-DEMCMLGTVGIPAVYNEIRLEEVAEMGYD-PLGEn 463
Cdd:PRK05605 340 NAFSGAMALPVSTvELWEKLTGG-LLVEGYGLTET-SPIIVGNPmSDDRRPGYVGVPFPDTEVRIVDPEDPDETmPDGE- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 464 pAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQ 543
Cdd:PRK05605 417 -EGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVE 494
|
570 580 590
....*....|....*....|....*....|....*....
gi 2065806855 544 DIWVYG---DSFKSMLVAVVVPN------PETINRWAKD 573
Cdd:PRK05605 495 DAAVVGlprEDGSEEVVAAVVLEpgaaldPEGLRAYCRE 533
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
221-589 |
1.96e-37 |
|
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: 145.13 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHQAVATFVvgmDIFMDQFEdkMTHDDVYLSFLPLAHILDRMNEEYF-FRKGASVgYYHG 299
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANV---RALVDAWR--WTEDDVLLHVLPLHHVHGLVNALLCpLFAGASV-EFLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 300 DLNVLRDDIQELKP--TYLAGVPRVFERihegiqkalqelnprrrLIfnalykhklawmnrgyshskASPMADFIAFRKI 377
Cdd:cd05941 164 KFDPKEVAISRLMPsiTVFMGVPTIYTR-----------------LL--------------------QYYEAHFTDPQFA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 378 RDKLGGRIRLLVSGGAPLSPEI-EEFLRVTCCcFVVQGYGLTETlgGTALGFP-DEMCMLGTVGIPAVYNEIRLeeVAEM 455
Cdd:cd05941 207 RAAAAERLRLMVSGSAALPVPTlEEWEAITGH-TLLERYGMTEI--GMALSNPlDGERRPGTVGMPLPGVQARI--VDEE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 456 GYDPLGENPAGEICIRGQCMFSGYYKNPELT-EEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV-ALEHLE 533
Cdd:cd05941 282 TGEPLPRGEVGEIQVRGPSVFKEYWNKPEATkEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVsALEIER 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065806855 534 NIFGQNSvVQDIWVYG---DSFKSMLVAVVVPNPETIN-------RWAKD-LGFTKPFEELCSFPEL 589
Cdd:cd05941 362 VLLAHPG-VSECAVIGvpdPDWGERVVAVVVLRAGAAAlsleelkEWAKQrLAPYKRPRRLILVDEL 427
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
78-564 |
3.84e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 145.39 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALR-AVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQD 156
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 TKIKGLLEPDCKCAkrLKAIVSFTNVSDELSHKASeigvktyswldflhmGREKPEETNPpkaFNICtimYTSGTSGDPK 236
Cdd:PRK06839 109 TFQNMALSMQKVSY--VQRVISITSLKEIEDRKID---------------NFVEKNESAS---FIIC---YTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHI--LDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKPT 314
Cdd:PRK06839 166 GAVLTQENMFWNALNNTFAID-----LTMHDRSIVLLPLFHIggIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 315 YLAGVPRVFERIHEGIQKALQELNprrrlifnalykhklawmnrgyshskaspmadfiafrkirdklggRIRLLVSGGAP 394
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETTNLQ---------------------------------------------SVRWFYNGGAP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 LSPE-IEEF----LRVTcccfvvQGYGLTETLGGT-ALGFPDEMCMLGTVGIPAVYNEIRLeeVAEMGYD-PLGEnpAGE 467
Cdd:PRK06839 276 CPEElMREFidrgFLFG------QGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYEL--IDENKNKvEVGE--VGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 468 ICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWV 547
Cdd:PRK06839 346 LLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAV 424
|
490 500
....*....|....*....|
gi 2065806855 548 YG---DSFKSMLVAVVVPNP 564
Cdd:PRK06839 425 VGrqhVKWGEIPIAFIVKKS 444
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
78-573 |
9.29e-37 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 142.97 E-value: 9.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVqdt 157
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllePDCKCAKRLKAIvsftNVSDELSHKASEIGVKTYSWLDflhmgrekpeetnppkafNICTIMYTSGTSGDPKG 237
Cdd:TIGR01923 78 -------DSLLEEKDFQAD----SLDRIEAAGRYETSLSASFNMD------------------QIATLMFTSGTTGKPKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFMdqfedKMTHDDVYLSFLPLAHIldrMNEEYFFR---KGASVgYYHGDLNVLRDDIQELKPT 314
Cdd:TIGR01923 129 VPHTFRNHYASAVGSKENL-----GFTEDDNWLLSLPLYHI---SGLSILFRwliEGATL-RIVDKFNQLLEMIANERVT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 315 YLAGVPRVFERIhegiqkaLQELNPRRRLifnalykhklawmnrgyshskaspmadfiafrkirdklggriRLLVSGGAP 394
Cdd:TIGR01923 200 HISLVPTQLNRL-------LDEGGHNENL------------------------------------------RKILLGGSA 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 LS-PEIEEflrvtCCCF---VVQGYGLTETlGGTALGFPDEMCM-LGTVGIPAVYNEIRLEEVAEMGYdplgenpaGEIC 469
Cdd:TIGR01923 231 IPaPLIEE-----AQQYglpIYLSYGMTET-CSQVTTATPEMLHaRPDVGRPLAGREIKIKVDNKEGH--------GEIM 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 470 IRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG 549
Cdd:TIGR01923 297 VKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVVP 375
|
490 500 510
....*....|....*....|....*....|.
gi 2065806855 550 ---DSFKSMLVAVVV----PNPETINRWAKD 573
Cdd:TIGR01923 376 kpdAEWGQVPVAYIVsesdISQAKLIAYLTE 406
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
72-564 |
1.37e-36 |
|
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: 143.61 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDF 151
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 VFVQdtkiKGLLEPDCKCAKRLK-AIVsftnvsdELSH-KASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTS 229
Cdd:cd05926 90 VLTP----KGELGPASRAASKLGlAIL-------ELALdVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 230 GTSGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAHIldrmneeyffrkgasvgyyHGDLNVLR---- 305
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNI-----TNTYKLTPDDRTLVVMPLFHV-------------------HGLVASLLstla 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 -----------------DDIQELKPTYLAGVPRvferIHegiqKALqeLNprrrlifnalykhklawmnrgysHSKASPM 368
Cdd:cd05926 215 aggsvvlpprfsastfwPDVRDYNATWYTAVPT----IH----QIL--LN-----------------------RPEPNPE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 369 ADFIAFRKIRdklggrirllvSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGG-TALGFPDEMCMLGTVGIPAVyNEI 447
Cdd:cd05926 262 SPPPKLRFIR-----------SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQmTSNPLPPGPRKPGSVGKPVG-VEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 448 RLeevaemgYDPLGEN-PA---GEICIRGQCMFSGYYKNPELTEEV-IKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
Cdd:cd05926 330 RI-------LDEDGEIlPPgvvGEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2065806855 523 qGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP 564
Cdd:cd05926 403 -GEKISPLEVDGVLLSHPAVLEAVAFGvpdEKYGEEVAAAVVLRE 446
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
78-507 |
4.14e-34 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 137.17 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQD- 156
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADg 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 -------TKIKGLLEPDCKCAKRLKAIVsftnVSDELSHKASEIGvkTYSWLDFLHMGREK--PEETNP--PkAFnictI 225
Cdd:COG0365 121 glrggkvIDLKEKVDEALEELPSLEHVI----VVGRTGADVPMEG--DLDWDELLAAASAEfePEPTDAddP-LF----I 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 226 MYTSGTSGDPKGVVLTH-----QAVATFVVGMDIfmdqfedkmTHDDVYLS--------------FLPLAHildrmneey 286
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHggylvHAATTAKYVLDL---------KPGDVFWCtadigwatghsyivYGPLLN--------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 287 ffrkGASVGYYHG-----DLNVLRDDIQELKPTYLAGVPRVFerihegiqkalqelnprRRLIfnalyKHKLAWMnRGYS 361
Cdd:COG0365 252 ----GATVVLYEGrpdfpDPGRLWELIEKYGVTVFFTAPTAI-----------------RALM-----KAGDEPL-KKYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 362 HSkaspmadfiafrkirdklggRIRLLVSGGAPLSPE-IEEFLRVTCCCfVVQGYGLTETLGGTALGFPDEMCMLGTVGI 440
Cdd:COG0365 305 LS--------------------SLRLLGSAGEPLNPEvWEWWYEAVGVP-IVDGWGQTETGGIFISNLPGLPVKPGSMGK 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065806855 441 PAVYNEIRLeeVAEMGyDPLGENPAGEICIRGQC--MFSGYYKNPELTEEVIKD---GWFHTGDIGEILPNG 507
Cdd:COG0365 364 PVPGYDVAV--VDEDG-NPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDG 432
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
222-573 |
8.71e-33 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 128.99 E-value: 8.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 222 ICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMdqfedKMTHDDVYLSFLPLAHI--LDRMNeeyffrKGASVG---Y 296
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL-----GFGGGDSWLLSLPLYHVggLAILV------RSLLAGaelV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 YHGDLNVLRDDIQELKPTYLAGVPRvferiheGIQKALQELNPRRRLifnalykhklawmnrgyshskaspmadfiafrk 376
Cdd:cd17630 71 LLERNQALAEDLAPPGVTHVSLVPT-------QLQRLLDSGQGPAAL--------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 377 irdklgGRIRLLVSGGAPLSPEI-EEF--LRVTCCCfvvqGYGLTETLGGTALGFPDEMCmLGTVGIPAVYNEIRLEEva 453
Cdd:cd17630 111 ------KSLRAVLLGGAPIPPELlERAadRGIPLYT----TYGMTETASQVATKRPDGFG-RGGVGVLLPGRELRIVE-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 454 emgydplgenpAGEICIRGQCMFSGYYkNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLE 533
Cdd:cd17630 178 -----------DGEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2065806855 534 NIFGQNSVVQDIWVYG---DSFKSMLVAVVVPN----PETINRWAKD 573
Cdd:cd17630 245 AALAAHPAVRDAFVVGvpdEELGQRPVAVIVGRgpadPAELRAWLKD 291
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
76-640 |
2.59e-32 |
|
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: 130.88 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 76 WKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVq 155
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 DTKikglLEPDCKCAkrlkaivsftnvsdelshkaseIGVKTYSWLdflhmgreKPEETNPPKAFNictimYTSGTSGDP 235
Cdd:cd12118 108 DRE----FEYEDLLA----------------------EGDPDFEWI--------PPADEWDPIALN-----YTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHQAVATFVVGMDIfmdqfEDKMTHDDVYLSFLPLAHildrmneeyffrkgaSVGYyhgdlnvlrddiqelkpTY 315
Cdd:cd12118 149 KGVVYHHRGAYLNALANIL-----EWEMKQHPVYLWTLPMFH---------------CNGW-----------------CF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 316 LAGVPRVferihEGIQKALQELNPRrrLIFNALYKHKLawmnrgySHSKASPMA-DFIAFRKIRDK--LGGRIRLLVsGG 392
Cdd:cd12118 192 PWTVAAV-----GGTNVCLRKVDAK--AIYDLIEKHKV-------THFCGAPTVlNMLANAPPSDArpLPHRVHVMT-AG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 393 APLSPEIeeFLRVTCCCF-VVQGYGLTETLGgtalgfpdemcmLGTVGI--PAvYNEIRLEEVA---------------E 454
Cdd:cd12118 257 APPPAAV--LAKMEELGFdVTHVYGLTETYG------------PATVCAwkPE-WDELPTEERArlkarqgvryvgleeV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 455 MGYDPLGENP-------AGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYV 527
Cdd:cd12118 322 DVLDPETMKPvprdgktIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENI 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 528 ALEHLENIFGQNSVVqdiwvygdsfksMLVAVV-VPNPetinRWAkdlgftkpfEELCSFPELKEHIiselKSTAE---- 602
Cdd:cd12118 401 SSVEVEGVLYKHPAV------------LEAAVVaRPDE----KWG---------EVPCAFVELKEGA----KVTEEeiia 451
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2065806855 603 --KNKLRKFEYIKAVAVETKPfdverdlVTATLKNRRNNL 640
Cdd:cd12118 452 fcREHLAGFMVPKTVVFGELP-------KTSTGKIQKFVL 484
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
78-549 |
5.12e-32 |
|
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: 130.72 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEPDCKcAKRLKAIVSFTNVSDELSHKASEIGVKTYSWLDFlHMGREKPEETNPPKAfnICTIMYTSGTSGDPKG 237
Cdd:cd17642 126 GLQKVLNVQKK-LKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGF-NEYDFKPPSFDRDEQ--VALIMNSSGSTGLPKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQ-AVATFVVGMD-IFMDQfedkMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHgdlnvlrddiqelkpty 315
Cdd:cd17642 202 VQLTHKnIVARFSHARDpIFGNQ----IIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMY----------------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 316 lagvprVFERihEGIQKALQElnprrrlifnalYKHKLAWMnrgyshskASPMADFIAFRKIRDKLG-GRIRLLVSGGAP 394
Cdd:cd17642 261 ------KFEE--ELFLRSLQD------------YKVQSALL--------VPTLFAFFAKSTLVDKYDlSNLHEIASGGAP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 LSPEIEEFL-RVTCCCFVVQGYGLTETLGgTALGFPDEMCMLGTVGIPAVYNEIRLeevaemgYDP-----LGENPAGEI 468
Cdd:cd17642 313 LSKEVGEAVaKRFKLPGIRQGYGLTETTS-AILITPEGDDKPGAVGKVVPFFYAKV-------VDLdtgktLGPNERGEL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 469 CIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWV 547
Cdd:cd17642 385 CVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGV 463
|
..
gi 2065806855 548 YG 549
Cdd:cd17642 464 AG 465
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
42-573 |
9.01e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.08 E-value: 9.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 42 TTAWDIFSKSVEKFPDNNMLGW--RRIvdekvgpymwkTYKEVYEEVLQIGSAL-RAVGAEPGCRVGIYGINCPQWIIA- 117
Cdd:PRK08314 10 TSLFHNLEVSARRYPDKTAIVFygRAI-----------SYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 118 ---MEACAahtlICVPLYDTLGSGAVDYIVEHAEIDFVFV-QD--TKIKGLLEpdckcAKRLK-AIVsfTNVSDELS--- 187
Cdd:PRK08314 79 yaiLRANA----VVVPVNPMNREEELAHYVTDSGARVAIVgSElaPKVAPAVG-----NLRLRhVIV--AQYSDYLPaep 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 188 -----------HKASEI-GVKTYSWLDFLHMGREKPEETNPPKafNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIF 255
Cdd:PRK08314 148 eiavpawlraePPLQALaPGGVVAWKEALAAGLAPPPHTAGPD--DLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 256 MDqfedkMTHDDVYLSFLPLAHILdrmneeyffrkgasvGYYHGdLNVlrddiqelkPTYLAG--Vprvferihegiqka 333
Cdd:PRK08314 226 SN-----STPESVVLAVLPLFHVT---------------GMVHS-MNA---------PIYAGAtvV-------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 334 lqeLNPR--RRLIFNALYKHKL-AWMNrgyshskASPMA-DFIAFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCC 409
Cdd:PRK08314 262 ---LMPRwdREAAARLIERYRVtHWTN-------IPTMVvDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 410 FVVQGYGLTETLGGTALGFPDE---MCMlgtvGIPAVYNEIR------LEEVaemgydPLGEnpAGEICIRGQCMFSGYY 480
Cdd:PRK08314 332 DYVEGYGLTETMAQTHSNPPDRpklQCL----GIPTFGVDARvidpetLEEL------PPGE--VGEIVVHGPQVFKGYW 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 481 KNPELTEEV-IK-DG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSVVQDIWVYG--DSFKS 554
Cdd:PRK08314 400 NRPEATAEAfIEiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINAS-GFKVWPAEVENLLYKHPAIQEACVIAtpDPRRG 478
|
570 580
....*....|....*....|....*...
gi 2065806855 555 MLV-AVVVPNP--------ETINRWAKD 573
Cdd:PRK08314 479 ETVkAVVVLRPeargktteEEIIAWARE 506
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
77-549 |
2.61e-31 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 126.69 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 77 KTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACaahtlicvplydtlgsgavdyivehaeidfvfvqd 156
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHAL----------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 tkikgllepdckcaKRLKAIVSFTN---VSDELSHKASEIGVKTYSwldflhmgrekpeetnppkafnICTIMYTSGTSG 233
Cdd:cd05912 47 --------------WLLGAEAVLLNtrlTPNELAFQLKDSDVKLDD----------------------IATIMYTSGTTG 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 234 DPKGVVLT---HQAVAtfvVGMDIFMDqfedkMTHDDVYLSFLPLAHI--LDRMneeyfFRK---GASVGYY-HGDLNVL 304
Cdd:cd05912 91 KPKGVQQTfgnHWWSA---IGSALNLG-----LTEDDNWLCALPLFHIsgLSIL-----MRSviyGMTVYLVdKFDAEQV 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 RDDIQELKPTYLAGVPRVFERIhegiqkalqelnprrrlifnalykhkLAWMNRGYSHSkaspmadfiaFRKIrdklggr 384
Cdd:cd05912 158 LHLINSGKVTIISVVPTMLQRL--------------------------LEILGEGYPNN----------LRCI------- 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 irLLvsGGAPLSPEIEEflrvTCCCF---VVQGYGLTETLGGT-ALGFPDEMCMLGTVGIPAVYNEIRLEEvaemgyDPL 460
Cdd:cd05912 195 --LL--GGGPAPKPLLE----QCKEKgipVYQSYGMTETCSQIvTLSPEDALNKIGSAGKPLFPVELKIED------DGQ 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 461 GENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNS 540
Cdd:cd05912 261 PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHP 339
|
....*....
gi 2065806855 541 VVQDIWVYG 549
Cdd:cd05912 340 AIKEAGVVG 348
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
78-572 |
2.76e-31 |
|
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: 126.82 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPlydtlgsgavdyivehaeidfvfvqdt 157
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVP--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaiVSFTNVSDELSHKASEIGVKT---YSWLDflhmgrekpeetnppkafNICTIMYTSGTSGD 234
Cdd:cd05935 56 -------------------INPMLKERELEYILNDSGAKVavvGSELD------------------DLALIPYTSGTTGL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 235 PKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAHildrmneeyffrkgasVGYYHGDLNVlrddiqelkPT 314
Cdd:cd05935 99 PKGCMHTHFSAAANALQS-----AVWTGLTPSDVILACLPLFH----------------VTGFVGSLNT---------AV 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 315 YLAGVPRVFERIHegiQKALQELNPRRRLIFnalykhklaWMNrgyshskASPM-ADFIAFRKIRDKLGGRIRLLVSGGA 393
Cdd:cd05935 149 YVGGTYVLMARWD---RETALELIEKYKVTF---------WTN-------IPTMlVDLLATPEFKTRDLSSLKVLTGGGA 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 394 PLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGfPDEMCMLGTVGIPAVYNEIRLEEvAEMGyDPLGENPAGEICIRGQ 473
Cdd:cd05935 210 PMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTN-PPLRPKLQCLGIP*FGVDARVID-IETG-RELPPNEVGEIVVRGP 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 474 CMFSGYYKNPELTEEV-IKDG---WFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSVVQDIWVYG 549
Cdd:cd05935 287 QIFKGYWNRPEETEESfIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
490 500 510
....*....|....*....|....*....|....
gi 2065806855 550 --DSFKSMLV-AVVVPNP--------ETINRWAK 572
Cdd:cd05935 366 vpDERVGEEVkAFIVLRPeyrgkvteEDIIEWAR 399
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
227-533 |
7.96e-30 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 124.32 E-value: 7.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 227 YTSGTSGDPKGVVLTHQAVATFVVgmdifmdQFED------KMTHDDVYLSFLPLAHILDrMNEEYF--FRKGASVGYYH 298
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGLVTSVA-------QQVDgenpnlYFHSDDVILCVLPMFHIYS-LNSVLLcgLRVGAAILIMP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 299 G-DLNVLRDDIQELKPTYLAGVPrvferihegiqkalqelnPrrrlIFNALYKhklawmnrgyshskaSPMADfiafrki 377
Cdd:PLN02246 258 KfEIGALLELIQRHKVTIAPFVP------------------P----IVLAIAK---------------SPVVE------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 378 RDKLGGrIRLLVSGGAPLSPEIEEFLRVTCCCFVV-QGYGLTEtlGGTALGfpdeMCM-------------LGTVgipaV 443
Cdd:PLN02246 294 KYDLSS-IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE--AGPVLA----MCLafakepfpvksgsCGTV----V 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 444 YNeirleevAEMG-YDP-----LGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKK 516
Cdd:PLN02246 363 RN-------AELKiVDPetgasLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLK 435
|
330
....*....|....*..
gi 2065806855 517 NLIKLsQGEYVALEHLE 533
Cdd:PLN02246 436 ELIKY-KGFQVAPAELE 451
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
46-573 |
1.11e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 124.11 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 46 DIFSKSVEKFPDNNMLgwrrIVDEKVGPYmwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHT 125
Cdd:PRK12583 22 DAFDATVARFPDREAL----VVRHQALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 126 LICVPLYDTLGSGAVDYIVEHAEIDFVFVQD------------TKIKGLLEPDC---KCAK--RLKAIVSFTnvsdelsh 188
Cdd:PRK12583 95 AILVNINPAYRASELEYALGQSGVRWVICADafktsdyhamlqELLPGLAEGQPgalACERlpELRGVVSLA-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 189 KASEIGVKTysWLDFLHMG----REKPEE-TNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVAT--FVVGMDIfmdqfed 261
Cdd:PRK12583 167 PAPPPGFLA--WHELQARGetvsREALAErQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNngYFVAESL------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 262 KMTHDDVYLSFLPLAHILDR-MNEEYFFRKGASVGY---YHGDLNVLRDdIQELKPTYLAGVPRVFerihegiqkaLQEL 337
Cdd:PRK12583 238 GLTEHDRLCVPVPLYHCFGMvLANLGCMTVGACLVYpneAFDPLATLQA-VEEERCTALYGVPTMF----------IAEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 338 NPRRRLIFnalykhklawmnrgyshskaspmaDFIAfrkirdklggrIRLLVSGGAPLSPEIEEflRVTC---CCFVVQG 414
Cdd:PRK12583 307 DHPQRGNF------------------------DLSS-----------LRTGIMAGAPCPIEVMR--RVMDemhMAEVQIA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 415 YGLTETLGGTALGFPDEMC--MLGTVGIPAVYNEIRLEEvAEMGYDPLGEnpAGEICIRGQCMFSGYYKNPELTEEVI-K 491
Cdd:PRK12583 350 YGMTETSPVSLQTTAADDLerRVETVGRTQPHLEVKVVD-PDGATVPRGE--IGELCTRGYSVMKGYWNNPEATAESIdE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 492 DGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG--DSF-KSMLVAVVVPNP---- 564
Cdd:PRK12583 427 DGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFGvpDEKyGEEIVAWVRLHPghaa 505
|
570
....*....|.
gi 2065806855 565 --ETINRWAKD 573
Cdd:PRK12583 506 seEELREFCKA 516
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
78-591 |
4.09e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 121.98 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWI-----IAMEACAAHTLicvplyDT-LGSGAVDYIVEHAEIDF 151
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVeahfgVPMAGAVLNTL------NTrLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 VFVqDTKIKGLLEPDCKCAKRLKAIVsfTNVSDELSHKASEIGVKTYSwlDFLHMGREKPEETNPPKAFNICTIMYTSGT 231
Cdd:PRK08162 119 LIV-DTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIGALDYE--AFLASGDPDFAWTLPADEWDAIALNYTSGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTHQAVATFVVGmdifmDQFEDKMTHDDVYLSFLPLAHIldrmNEEYF-----FRKGASVGYYHGDLNVLRD 306
Cdd:PRK08162 194 TGNPKGVVYHHRGAYLNALS-----NILAWGMPKHPVYLWTLPMFHC----NGWCFpwtvaARAGTNVCLRKVDPKLIFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 307 DIQELKPTYLAGVPRVFErihegiqkalqelnprrrLIFNAlykhklawmnrgyshskasPMADfiafrkiRDKLGGRIR 386
Cdd:PRK08162 265 LIREHGVTHYCGAPIVLS------------------ALINA-------------------PAEW-------RAGIDHPVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 387 LLVSGGAPLSPEIEEF----LRVTcccfvvQGYGLTETLGGTA----------LGFPDEMCMLGTVGIPAVYneirLEEV 452
Cdd:PRK08162 301 AMVAGAAPPAAVIAKMeeigFDLT------HVYGLTETYGPATvcawqpewdaLPLDERAQLKARQGVRYPL----QEGV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 453 AEMGYDPLGENPA-----GEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGeyv 527
Cdd:PRK08162 371 TVLDPDTMQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGG--- 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065806855 528 alehlENIfgqNSV-VQDIwVYgdSFKSMLVAVVVPNPETinRWAkdlgftkpfEELCSFPELKE 591
Cdd:PRK08162 447 -----ENI---SSIeVEDV-LY--RHPAVLVAAVVAKPDP--KWG---------EVPCAFVELKD 489
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
77-561 |
1.72e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 119.30 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 77 KTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQD 156
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 TKIKGLlepdckcakrlkAIVSFTNVSDELSHKASEIGVKTYSWLDFlhmgrekpeetnppkafnICTIMYTSGTSGDPK 236
Cdd:PRK03640 108 DFEAKL------------IPGISVKFAELMNGPKEEAEIQEEFDLDE------------------VATIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVVLTHQ-----AVATfVVGMDIfmdqfedkmTHDDVYLSFLPLAHI--LDRMneeyfFRK---GASVGYY-HGDLNVLR 305
Cdd:PRK03640 158 GVIQTYGnhwwsAVGS-ALNLGL---------TEDDCWLAAVPIFHIsgLSIL-----MRSviyGMRVVLVeKFDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 DDIQELKPTYLAGVPRVFERIhegiqkaLQELNprrrlifnalykhklawmNRGYSHSkaspmadfiaFRKIRdkLGGri 385
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRL-------LERLG------------------EGTYPSS----------FRCML--LGG-- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 rllvsGGAPLsPEIEEflrvtccCF-----VVQGYGLTETLGG-TALGFPDEMCMLGTVGIPAVYNEIRLEEvaemGYDP 459
Cdd:PRK03640 264 -----GPAPK-PLLEQ-------CKekgipVYQSYGMTETASQiVTLSPEDALTKLGSAGKPLFPCELKIEK----DGVV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 460 LGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQN 539
Cdd:PRK03640 327 VPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSH 405
|
490 500
....*....|....*....|....*
gi 2065806855 540 SVVQDIWVYG---DSFKSMLVAVVV 561
Cdd:PRK03640 406 PGVAEAGVVGvpdDKWGQVPVAFVV 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
78-566 |
2.36e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 116.62 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYdTLGSgaVD---YIVEHAEIDFVFV 154
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGS--LDdhaYVLEDAGISTLIV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 155 QDTKIK----GLLEpdcKCAKrLKAIvsftnvsdeLSHKASEIGVktyswlDFLHMGRekPEETNPPKAFN----ICTIM 226
Cdd:PRK06188 116 DPAPFVeralALLA---RVPS-LKHV---------LTLGPVPDGV------DLLAAAA--KFGPAPLVAAAlppdIAGLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 227 YTSGTSGDPKGVVLTHQAVATFVVgmdIFMDQFEdkMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVgyyhgdlnVLRD 306
Cdd:PRK06188 175 YTGGTTGKPKGVMGTHRSIATMAQ---IQLAEWE--WPADPRFLMCTPLSHAGGAFFLPTLLRGGTVI--------VLAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 307 -DIQElkptylagVPRVFERihEGIQKALqeLNPRrrLIFnALYKHKlawmnrgyshskASPMADFiafrkirdklgGRI 385
Cdd:PRK06188 242 fDPAE--------VLRAIEE--QRITATF--LVPT--MIY-ALLDHP------------DLRTRDL-----------SSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 RLLVSGGAPLSPE-----IEEFLRVtcccfVVQGYGLTE-----TLGGTALGFPDEMCMLGTVGIPAVYNEIRL-----E 450
Cdd:PRK06188 284 ETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEapmviTYLRKRDHDPDDPKRLTSCGRPTPGLRVALldedgR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 451 EVaemgydPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALE 530
Cdd:PRK06188 359 EV------AQGE--VGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPR 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 2065806855 531 HLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPET 566
Cdd:PRK06188 430 EVEDVLAEHPAVAQVAVIGvpdEKWGEAVTAVVVLRPGA 468
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
78-572 |
2.70e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 116.67 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICV---PLYDTL-------GSGAVDYIVeha 147
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTEReleyqlhDSGAKVILC--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 148 eIDFVFVQDTKIKGLLEPDCKCAKRLKAIVSFTN--VSDELSHKASEIGVKTySWLDFLHMGREKPEETNP-------PK 218
Cdd:PRK06710 128 -LDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKnlLYPFVQKKQSNLVVKV-SESETIHLWNSVEKEVNTgvevpcdPE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 219 AfNICTIMYTSGTSGDPKGVVLTHQ-AVATFVVGMDIFMDQFEDkmthDDVYLSFLPLAHIldrmneeyffrkgasvgyy 297
Cdd:PRK06710 206 N-DLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKEG----EEVVLGVLPFFHV------------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 298 HGDLNVLRDDIQELKPTYLagVPRV-FERIHEGIQKALQELNPRRRLIFNALYKhklawmnrgyshskaSPMadfiafrk 376
Cdd:PRK06710 262 YGMTAVMNLSIMQGYKMVL--IPKFdMKMVFEAIKKHKVTLFPGAPTIYIALLN---------------SPL-------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 377 IRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAEMG 456
Cdd:PRK06710 317 LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 457 YDPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIF 536
Cdd:PRK06710 397 ALPPGE--IGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2065806855 537 GQNSVVQDIWVYG--DSFKSMLVAVVVP-------NPETINRWAK 572
Cdd:PRK06710 474 YEHEKVQEVVTIGvpDPYRGETVKAFVVlkegtecSEEELNQFAR 518
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
78-593 |
5.47e-27 |
|
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: 114.65 E-value: 5.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEAC--AAHTLicVPLydtlgsgAVDYIVEHAEidfvfvq 155
Cdd:cd05945 18 TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAAlkAGHAY--VPL-------DASSPAERIR------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 dtKIKGLLEPDckcakrlkaivSFTNVSDELSHkaseigvktyswldflhmgrekpeetnppkafnictIMYTSGTSGDP 235
Cdd:cd05945 82 --EILDAAKPA-----------LLIADGDDNAY------------------------------------IIFTSGSTGRP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHQAVATFVVGMDifmDQFedKMTHDDVYLSFLPlahildrmneeyffrkgasvgyYHGDLNVLrddiqELKPTY 315
Cdd:cd05945 113 KGVQISHDNLVSFTNWML---SDF--PLGPGDVFLNQAP----------------------FSFDLSVM-----DLYPAL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 316 LAG-----VPRvferihegiqkalQELNPRRRLiFNALYKHKLA-WmnrgysHSKASPMADFIAFRKIRDKLGGRIRLLV 389
Cdd:cd05945 161 ASGatlvpVPR-------------DATADPKQL-FRFLAEHGITvW------VSTPSFAAMCLLSPTFTPESLPSLRHFL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 390 SGGAPLS-PEIEEFLRVTCCCFVVQGYGLTETLGG-TALGFPDE-MCMLGTVGIPAVYNEIRLEEVAEMGyDPLGENPAG 466
Cdd:cd05945 221 FCGEVLPhKTARALQQRFPDARIYNTYGPTEATVAvTYIEVTPEvLDGYDRLPIGYAKPGAKLVILDEDG-RPVPPGEKG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 467 EICIRGQCMFSGYYKNPELTEEVI----KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENIFGQNSVV 542
Cdd:cd05945 300 ELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGV 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2065806855 543 QD---IWVYGDSFKSMLVAVVVPNPETinrwakDLGFTKPFEElcsfpELKEHI 593
Cdd:cd05945 379 KEavvVPKYKGEKVTELIAFVVPKPGA------EAGLTKAIKA-----ELAERL 421
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
32-522 |
9.07e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 115.12 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 32 KGFPP-----ID-SEITTAWDIFSKSVEKFPDNnmlgwrrivdeKVGPYMWK--TYKEVYEEVLQIGSALRAVGAEPGCR 103
Cdd:PRK07059 7 KSYPPgvpaeIDaSQYPSLADLLEESFRQYADR-----------PAFICMGKaiTYGELDELSRALAAWLQSRGLAKGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 104 VGIYGINCPQWIIAMEAC--AAHTLICV-PLY----------DtlgSGA------------VDYIVEHAEIDFVFVQDTK 158
Cdd:PRK07059 76 VAIMMPNVLQYPVAIAAVlrAGYVVVNVnPLYtprelehqlkD---SGAeaivvlenfattVQQVLAKTAVKHVVVASMG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 159 ----IKGLLEPdcKCAKRLKAIVSFTNVSDELSHKASeigvktyswldfLHMGRE---KPEETNPPK-AFnictIMYTSG 230
Cdd:PRK07059 153 dllgFKGHIVN--FVVRRVKKMVPAWSLPGHVRFNDA------------LAEGARqtfKPVKLGPDDvAF----LQYTGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGVVLTHQAVATFVVGMDIFMDQFEDKMTHDD--VYLSFLPLAHIldrmneeYFFRKGASVGYYHGDLNVL---- 304
Cdd:PRK07059 215 TTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDqlNFVCALPLYHI-------FALTVCGLLGMRTGGRNILipnp 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 RDdiqelkptyLAGVPRVFERIHEGIQKALQELnprrrliFNALykhklawMNrgyshskaSPMADFIAFRKIRDKLGGr 384
Cdd:PRK07059 288 RD---------IPGFIKELKKYQVHIFPAVNTL-------YNAL-------LN--------NPDFDKLDFSKLIVANGG- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 irllvsGGAPLSPEIEEFLRVTCCcFVVQGYGLTETLGGTALGFPDEMCMLGTVG--IPAVYNEIRLEEVAEMgydPLGE 462
Cdd:PRK07059 336 ------GMAVQRPVAERWLEMTGC-PITEGYGLSETSPVATCNPVDATEFSGTIGlpLPSTEVSIRDDDGNDL---PLGE 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 463 npAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
Cdd:PRK07059 406 --PGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
78-566 |
2.30e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 113.72 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikglLEPdckCAKRLKAIVSFTNVSdELSHKASEIGVKTYSwlDFLhmgrekpEETNPPKAF------NICTIMYTSGT 231
Cdd:PRK07786 124 -----LAP---VATAVRDIVPLLSTV-VVAGGSSDDSVLGYE--DLL-------AEAGPAHAPvdipndSPALIMYTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTH-----QAVaTFVVGMDIFmdqfedkmTHDDVYLSFLPLAHILDRMNEEYFFRKGA-SVGYYHG--DLNV 303
Cdd:PRK07786 186 TGRPKGAVLTHanltgQAM-TCLRTNGAD--------INSDVGFVGVPLFHIAGIGSMLPGLLLGApTVIYPLGafDPGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 304 LRDDIQELKPTYLAGVPRVFERIhegiqKALQELNPRrrlifnALYKHKLAWmnrgyshsKASPMADFIaFRKIRDKLGG 383
Cdd:PRK07786 257 LLDVLEAEKVTGIFLVPAQWQAV-----CAEQQARPR------DLALRVLSW--------GAAPASDTL-LRQMAATFPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 384 RIRLLVSGGAPLSPeieeflrVTCccfVVQGygltetlggtalgfPDEMCMLGTVG--IPAVYNEIRLEEvaeMGYDPLG 461
Cdd:PRK07786 317 AQILAAFGQTEMSP-------VTC---MLLG--------------EDAIRKLGSVGkvIPTVAARVVDEN---MNDVPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 462 EnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSV 541
Cdd:PRK07786 370 E--VGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPD 446
|
490 500
....*....|....*....|....*...
gi 2065806855 542 VQDIWVYG---DSFKSMLVAVVVPNPET 566
Cdd:PRK07786 447 IVEVAVIGradEKWGEVPVAVAAVRNDD 474
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
222-610 |
6.62e-26 |
|
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: 110.93 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 222 ICTIMYTSGTSGDPKGVVLTHQAVATFVVgmdifmdQFEDKM--THDDVYLSFLPLAHIldrmneeyffrkgasVGYYHG 299
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIR-------QYAERLglGPGDVFLVASPMAHQ---------------TGFVYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 300 DLNVLrddiqelkptyLAGVPRVFERIhegiqkalqeLNPRRrlifnalykhKLAWMNR-GYSHSKASP--MADFIAFRK 376
Cdd:cd05903 153 FTLPL-----------LLGAPVVLQDI----------WDPDK----------ALALMREhGVTFMMGATpfLTDLLNAVE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 377 IRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGG-TALGFPDEMCMLGTVGIPAVYNEIRLEEVAEM 455
Cdd:cd05903 202 EAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAvTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 456 GYDPlgeNPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENI 535
Cdd:cd05903 282 TLAP---GVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 536 FGQNSVVQDIWVYGDSFKSM---LVAVVVPNPetinrwakdlGFTKPFEELCSF-----------PElKEHIISELKSTA 601
Cdd:cd05903 358 LLGHPGVIEAAVVALPDERLgerACAVVVTKS----------GALLTFDELVAYldrqgvakqywPE-RLVHVDDLPRTP 426
|
....*....
gi 2065806855 602 eKNKLRKFE 610
Cdd:cd05903 427 -SGKVQKFR 434
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
72-519 |
6.62e-26 |
|
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: 112.38 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLydtlGSGAVDYIVEHAEidf 151
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL----TVPPTYDEPNARL--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 vfvqdTKIKGLLE----PDCKCAKRLKAivSFTNVSDELSHKASEigvktyswLDFLHMGREKPEETN--PPKAFNICTI 225
Cdd:cd05906 108 -----RKLRHIWQllgsPVVLTDAELVA--EFAGLETLSGLPGIR--------VLSIEELLDTAADHDlpQSRPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 226 MYTSGTSGDPKGVVLTHQAVATFVVGMdIFMDQFedkmTHDDVYLSFLPLAHIldrmneeyffrkgASVGYYHgdlnvlr 305
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRNILARSAGK-IQHNGL----TPQDVFLNWVPLDHV-------------GGLVELH------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 ddiqeLKPTYLAGvprvfERIHEGIQKALQelNPRRRLifNALYKHKLA--WM-NRGYSHskaspMADFIAFRKIRDKLG 382
Cdd:cd05906 228 -----LRAVYLGC-----QQVHVPTEEILA--DPLRWL--DLIDRYRVTitWApNFAFAL-----LNDLLEEIEDGTWDL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 383 GRIRLLVSGGAPLS-PEIEEFLRVTCCC-----FVVQGYGLTETLGGT--ALGFP-------DEMCMLGTVgIPAVynEI 447
Cdd:cd05906 289 SSLRYLVNAGEAVVaKTIRRLLRLLEPYglppdAIRPAFGMTETCSGViySRSFPtydhsqaLEFVSLGRP-IPGV--SM 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065806855 448 RLeeVAEMGyDPLGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGeILPNGVLKIIDRKKNLI 519
Cdd:cd05906 366 RI--VDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLG-FLDNGNLTITGRTKDTI 434
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
78-564 |
7.30e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 112.08 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEPDCKCAKRLKAIVSFTNVSDELShkaseiGVKtyswlDFLHMGREKP---EETNPPKAFNICTIMYTSGTSGD 234
Cdd:PRK08008 119 FYPMYRQIQQEDATPLRHICLTRVALPADD------GVS-----SFTQLKAQQPatlCYAPPLSTDDTAEILFTSGTTSR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 235 PKGVVLTHQAVatfvvgmdIFMDQFED---KMTHDDVYLSFLPLAHILDRMN---------------EEYFFRKgasvgy 296
Cdd:PRK08008 188 PKGVVITHYNL--------RFAGYYSAwqcALRDDDVYLTVMPAFHIDCQCTaamaafsagatfvllEKYSARA------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 YHGDLNVLRDDIQELKP----TYLAGVPRVFERIHEgiqkaLQELnprrrLIF-NALYKHKLAWMNRgyshskaspmadf 371
Cdd:PRK08008 254 FWGQVCKYRATITECIPmmirTLMVQPPSANDRQHC-----LREV-----MFYlNLSDQEKDAFEER------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 372 iaFRkirdklggrIRLLVSggaplspeieeflrvtcccfvvqgYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLee 451
Cdd:PRK08008 311 --FG---------VRLLTS------------------------YGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEI-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 452 VAEMGyDPLGENPAGEICIRG---QCMFSGYYKNPELTEEVIK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYV 527
Cdd:PRK08008 354 RDDHN-RPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENV 431
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2065806855 528 ALEHLENIFGQNSVVQDIWVYG--DSFKSMLV-AVVVPNP 564
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGikDSIRDEAIkAFVVLNE 471
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
225-565 |
7.62e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 111.23 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATfvvGMDIFMDQFEdkMTHDDVYLSFLPLAHI----------LDRMNEEYFFRKGASV 294
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAA---DLDALAEAWQ--WTADDVLVHGLPLFHVhglvlgvlgpLRIGNRFVHTGRPTPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 295 GYYHGdlnvlrddiQELKPTYLAGVPRVFERIHE--GIQKALqelnprrrlifnalykhklawmnrgyshskaspmadfi 372
Cdd:PRK07787 208 AYAQA---------LSEGGTLYFGVPTVWSRIAAdpEAARAL-------------------------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 373 afrkirdklgGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRL--E 450
Cdd:PRK07787 241 ----------RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGER-RPGWVGLPLAGVETRLvdE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 451 EVAEMGYDplGENpAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKK-NLIKlSQGEYVA 528
Cdd:PRK07787 310 DGGPVPHD--GET-VGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGREStDLIK-SGGYRIG 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2065806855 529 LEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPE 565
Cdd:PRK07787 386 AGEIETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADD 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
78-544 |
1.17e-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: 110.05 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRA-VGAEPGCRVGIYGINCPQWIIAMEAC----AAHtlicVPLYDTLGSGAVDYIVEHAEIDFV 152
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVlkagAAY----VPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 153 FVQDTkikgllepdckcakrlkaivsftnVSDELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTS 232
Cdd:TIGR01733 77 LTDSA------------------------LASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 233 GDPKGVVLTHQAVATFVVGM--DIFMDQfedkmthDDVYLSFLPLAHildrmneeyffrkgasvgyyhgDLNVLrddiqE 310
Cdd:TIGR01733 133 GRPKGVVVTHRSLVNLLAWLarRYGLDP-------DDRVLQFASLSF----------------------DASVE-----E 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 311 LKPTYLAG-----VPRVferihegiqkalqELNPRRRLIFNALYKHKLAWMnrgysHSKASPMADFIAFRKIRDKlggRI 385
Cdd:TIGR01733 179 IFGALLAGatlvvPPED-------------EERDDAALLAALIAEHPVTVL-----NLTPSLLALLAAALPPALA---SL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 RLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIP----------AVYNEiRLEEVae 454
Cdd:TIGR01733 238 RLVILGGEALTPAlVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVPigrplantrlYVLDD-DLRPV-- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 455 mgydPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWF---------HTGDIGEILPNGVLKIIDRKKNLIKLSqGE 525
Cdd:TIGR01733 315 ----PVGV--VGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKIR-GY 387
|
490
....*....|....*....
gi 2065806855 526 YVALEHLENIFGQNSVVQD 544
Cdd:TIGR01733 388 RIELGEIEAALLRHPGVRE 406
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
202-522 |
1.91e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 111.01 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 202 DFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQ-AVATFVVGMDIFMDQFEDKMthdDVYLSFLPLAHIld 280
Cdd:PRK05677 189 DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRnLVANMLQCRALMGSNLNEGC---EILIAPLPLYHI-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 281 rmneeYFFRKGASVGYYHGDLNVLRDDiqelkptylagvPRVFERIHEGIQK----ALQELNPrrrlIFNALykhklawm 356
Cdd:PRK05677 264 -----YAFTFHCMAMMLIGNHNILISN------------PRDLPAMVKELGKwkfsGFVGLNT----LFVAL-------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 357 nrgySHSKASPMADFIAfrkirdklggrIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETlGGTALGFPDEMCMLG 436
Cdd:PRK05677 315 ----CNNEAFRKLDFSA-----------LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTET-SPVVSVNPSQAIQVG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 437 TVGIPAVYNEIRLeeVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDR 514
Cdd:PRK05677 379 TIGIPVPSTLCKV--IDDDGNElPLGE--VGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDR 454
|
....*...
gi 2065806855 515 KKNLIKLS 522
Cdd:PRK05677 455 KKDMILVS 462
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
78-610 |
1.95e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 110.90 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAM----EACAAHtlicVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:PRK06178 60 TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFfgilKLGAVH----VPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQDTKIKgLLEPDCKcAKRLKAIVsFTNVSDEL----------SHKASEIGVKtySWLDFLHMGREKPEETNPPKAF--N 221
Cdd:PRK06178 136 ALDQLAP-VVEQVRA-ETSLRHVI-VTSLADVLpaeptlplpdSLRAPRLAAA--GAIDLLPALRACTAPVPLPPPAldA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 222 ICTIMYTSGTSGDPKGVVLTHQ-----AVATFVVGMdifmdqfedKMTHDDVYLSFLPLahildrmneeyFFRKGASVGY 296
Cdd:PRK06178 211 LAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAV---------VGGEDSVFLSFLPE-----------FWIAGENFGL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 ----YHGDLNVL--RDDIQelkpTYLAGVPrvferiHEGIQKALQelnprrrLIFNA--LYKHKlAWMNRGYSHSKASPM 368
Cdd:PRK06178 271 lfplFSGATLVLlaRWDAV----AFMAAVE------RYRVTRTVM-------LVDNAveLMDHP-RFAEYDLSSLRQVRV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 369 ADFIafRKIRDKLGGRIRLLvsggaplspeieeflrvTCCCFVVQGYGLTETlgGTA----LGFP-DEMCMLGT---VGI 440
Cdd:PRK06178 333 VSFV--KKLNPDYRQRWRAL-----------------TGSVLAEAAWGMTET--HTCdtftAGFQdDDFDLLSQpvfVGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 441 PAVYNEIRLEEVAEMGYDPLGENpaGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIK 520
Cdd:PRK06178 392 PVPGTEFKICDFETGELLPLGAE--GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 521 LSqGEYVALEHLENIFGQNSVVQDIWVYG--DSFKSML-VAVVVPNP------ETINRWAKdlgftkpfEELCSF--PEL 589
Cdd:PRK06178 470 VN-GMSVFPSEVEALLGQHPAVLGSAVVGrpDPDKGQVpVAFVQLKPgadltaAALQAWCR--------ENMAVYkvPEI 540
|
570 580
....*....|....*....|.
gi 2065806855 590 KehIISELKSTAeKNKLRKFE 610
Cdd:PRK06178 541 R--IVDALPMTA-TGKVRKQD 558
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
78-535 |
6.56e-25 |
|
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: 108.57 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAePGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:cd05909 9 TYRKLLTGAIALARKLAKMTK-EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEPDCKCAKRLKAIVSFTNVSDELShKASEIGVKTYSWLDFLHMGREKPeeTNPPKAFNICTIMYTSGTSGDPKG 237
Cdd:cd05909 88 FIEKLKLHHLFDVEYDARIVYLEDLRAKIS-KADKCKAFLAGKFPPKWLLRIFG--VAPVQPDDPAVILFTSGSEGLPKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHILDRMNEEYF-FRKGASVGYYHGDLN--VLRDDIQELKPT 314
Cdd:cd05909 165 VVLSHKNLLANVEQITAIFD-----PNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPNPLDykKIPELIYDKKAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 315 YLAGVPrVFERIHegiqkalqelnprrrlifnALYKHKlawmnrgyshskaspmADFiafrkirdklgGRIRLLVSGGAP 394
Cdd:cd05909 240 ILLGTP-TFLRGY-------------------ARAAHP----------------EDF-----------SSLRLVVAGAEK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 LSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAemGYDPLGENPAGEICIRGQC 474
Cdd:cd05909 273 LKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE--THEEVPIGEGGLLLVRGPN 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 475 MFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENI 535
Cdd:cd05909 351 VMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-572 |
8.33e-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: 106.21 E-value: 8.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHQAVAT--FVVGMDIfmdqfedKMTHDDVYLSFLPLAH----ILDRMNEeyfFRKGASV 294
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNngYFIGERL-------GLTEQDRLCIPVPLFHcfgsVLGVLAC---LTHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 295 GY----YHGdLNVLRDdIQELKPTYLAGVPRVFERihegiqkalqELNPRRRLIFnalykhklawmnrgyshskaspmaD 370
Cdd:cd05917 73 VFpspsFDP-LAVLEA-IEKEKCTALHGVPTMFIA----------ELEHPDFDKF------------------------D 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 371 FiafrkirdklgGRIRLLVSGGAPLSPE----IEEFLRVTCccfVVQGYGLTETLGGTALGFPDEMC--MLGTVGIPAVY 444
Cdd:cd05917 117 L-----------SSLRTGIMAGAPCPPElmkrVIEVMNMKD---VTIAYGMTETSPVSTQTRTDDSIekRVNTVGRIMPH 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 445 NEIRLeeVAEMGYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQ 523
Cdd:cd05917 183 TEAKI--VDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2065806855 524 GEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP------ETINRWAK 572
Cdd:cd05917 260 GENIYPREIEEFLHTHPKVSDVQVVGvpdERYGEEVCAWIRLKEgaelteEDIKAYCK 317
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-566 |
8.49e-25 |
|
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: 107.61 E-value: 8.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:cd05930 14 TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTDPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaivsftnvsdelshkaseigvktyswldflhmgrekpeetnppkafNICTIMYTSGTSGDPKG 237
Cdd:cd05930 94 ---------------------------------------------------------------DLAYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGM-DIFMDQFEDKMTH------DD-VYLSFLPLA-----HILDRMNeeyffrkgasvgyyHGDLNVL 304
Cdd:cd05930 111 VMVEHRGLVNLLLWMqEAYPLTPGDRVLQftsfsfDVsVWEIFGALLagatlVVLPEEV--------------RKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 RDDIQELKPTYLAGVPRVFERIhegiqkaLQELNPRRrliFNALykhklawmnrgyshskaspmadfiafrkirdklggr 384
Cdd:cd05930 177 ADLLAEEGITVLHLTPSLLRLL-------LQELELAA---LPSL------------------------------------ 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 iRLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTETLGG-TALGFPDEMCMLGTVGI--P----AVY--NEiRLEEVae 454
Cdd:cd05930 211 -RLVLVGGEALPPDlVRRWRELLPGARLVNLYGPTEATVDaTYYRVPPDDEEDGRVPIgrPipntRVYvlDE-NLRPV-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 455 mgydPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFH-------TGDIGEILPNGVLKIIDRKKNLIKLSqG--- 524
Cdd:cd05930 287 ----PPGV--PGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVKIR-Gyri 359
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2065806855 525 -----EYVALEHlENIfGQNSVVqdiwVYGDSFKSM-LVAVVVPNPET 566
Cdd:cd05930 360 elgeiEAALLAH-PGV-REAAVV----AREDGDGEKrLVAYVVPDEGG 401
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
78-522 |
1.07e-24 |
|
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: 107.42 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAeidfvfvqdt 157
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakRLKAIVsfTNVSDelshkaseigvktyswldflhmgrekpeetnppkafnICTIMYTSGTSGDPKG 237
Cdd:cd05972 72 --------------GAKAIV--TDAED-------------------------------------PALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFMDQFEDKM---THDD-----VYLSFL-PLAHildrmneeyffrkGASVGYYHGD----LNVL 304
Cdd:cd05972 99 VLHTHSYPLGHIPTAAYWLGLRPDDIhwnIADPgwakgAWSSFFgPWLL-------------GATVFVYEGPrfdaERIL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rDDIQELKPTYLAGVPRVFERIhegiqkaLQELNPRRRLifnalykhklawmnrgyshskaspmadfiafrkirdklgGR 384
Cdd:cd05972 166 -ELLERYGVTSFCGPPTAYRML-------IKQDLSSYKF---------------------------------------SH 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETlGGTALGFPDEMCMLGTVGIPAVYNEIRLeeVAEMGyDPLGENP 464
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET-GLTVGNFPDMPVKPGSMGRPTPGYDVAI--IDDDG-RELPPGE 274
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 465 AGEICIRGQ--CMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
Cdd:cd05972 275 EGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
78-564 |
1.97e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 107.28 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDt 157
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakRLKAIVSftnvsdeLSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKG 237
Cdd:PRK06145 108 --------------EFDAIVA-------LETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHIldrmneEYFFRKGASVGYYHGDLNVLRDdiqelkptyla 317
Cdd:PRK06145 167 VMHSYGNLHWKSIDHVIALG-----LTASERLLVVGPLYHV------GAFDLPGIAVLWVGGTLRIHRE----------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 318 gvprvFERihegiQKALQelnprrrlifnALYKHKL--AWMnrgyshskASPMADFIAFRKIRDKLG-GRIRLLVSGGAP 394
Cdd:PRK06145 225 -----FDP-----EAVLA-----------AIERHRLtcAWM--------APVMLSRVLTVPDRDRFDlDSLAWCIGGGEK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 lSPE--IEEFLRVTCCCFVVQGYGLTETLGG-TALGFPDEMCMLGTVGIPAVYNEIRLEEvAEMGYDPLGENpaGEICIR 471
Cdd:PRK06145 276 -TPEsrIRDFTRVFTRARYIDAYGLTETCSGdTLMEAGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMK--GEICMR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 472 GQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG-- 549
Cdd:PRK06145 352 GPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIGvh 430
|
490
....*....|....*.
gi 2065806855 550 -DSFKSMLVAVVVPNP 564
Cdd:PRK06145 431 dDRWGERITAVVVLNP 446
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
204-522 |
2.11e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 107.99 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 204 LHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFEDK-----MTHDDVYLSFLPLAHI 278
Cdd:PRK12492 191 LRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmKEGQEVMIAPLPLYHI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 279 ldrmneeYFFRKGASVGYYHGDLNVL----RDD---IQELKPTYLAgvprvferihegiqkALQELNPrrrlIFNALYKH 351
Cdd:PRK12492 271 -------YAFTANCMCMMVSGNHNVLitnpRDIpgfIKELGKWRFS---------------ALLGLNT----LFVALMDH 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 352 KlawmnrgyshskaspmadfiAFRKIRdklGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDE 431
Cdd:PRK12492 325 P--------------------GFKDLD---FSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 432 MCMLGTVGIPAVYNEIRL--EEVAEMgydPLGENpaGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGV 508
Cdd:PRK12492 382 LARLGTVGIPVPGTALKVidDDGNEL---PLGER--GELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGF 456
|
330
....*....|....
gi 2065806855 509 LKIIDRKKNLIKLS 522
Cdd:PRK12492 457 VRIVDRKKDLIIVS 470
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
76-527 |
2.52e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.81 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 76 WkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQ 155
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 DTKIKGLLEPDckcakrlkAIVSFTNVSDELShkaseigvktyswldflhmgrekPEETNPPKAFNICTIMYTSGTSGDP 235
Cdd:PRK09088 102 DAVAAGRTDVE--------DLAAFIASADALE-----------------------PADTPSIPPERVSLILFTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHQAVATFVVGMDIFmdqfeDKMTHDDVYLSFLPLAHIldrmneeyffrkgasVGYyhgdlnvlrddIQELKPTY 315
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGVL-----GRVDAHSSFLCDAPMFHI---------------IGL-----------ITSVRPVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 316 LAG----VPRVFErihegiqkalqelnPRRRLifnalykHKLAWMNRGYSHSKASP-MADfiAFRKIRDKLGGRIRLL-- 388
Cdd:PRK09088 200 AVGgsilVSNGFE--------------PKRTL-------GRLGDPALGITHYFCVPqMAQ--AFRAQPGFDAAALRHLta 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 389 -VSGGAP-LSPEIEEFLRVTCCcfVVQGYGLTEtlGGTALGFPDEMCM----LGTVGIPAVYNEIRLeeVAEMGYD-PLG 461
Cdd:PRK09088 257 lFTGGAPhAAEDILGWLDDGIP--MVDGFGMSE--AGTVFGMSVDCDVirakAGAAGIPTPTVQTRV--VDDQGNDcPAG 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065806855 462 EnpAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYV 527
Cdd:PRK09088 331 V--PGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENV 394
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
204-583 |
1.19e-23 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 105.52 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 204 LHMGRE----KPEETNPPKAFnictIMYTSGTSGDPKGVVLTHQAVATFVvgmdifmdqfedkMTHDDVYLSF------- 272
Cdd:PRK08974 190 LHKGRRmqyvKPELVPEDLAF----LQYTGGTTGVAKGAMLTHRNMLANL-------------EQAKAAYGPLlhpgkel 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 273 ----LPLAHILD-RMNEEYFFRKGASvgyyhgdlNVL----RD---DIQELKP---TYLAGVprvferihegiqkalqel 337
Cdd:PRK08974 253 vvtaLPLYHIFAlTVNCLLFIELGGQ--------NLLitnpRDipgFVKELKKypfTAITGV------------------ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 338 nprrRLIFNALYK----HKLawmnrgyshskaspmaDFiafrkirdklgGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQ 413
Cdd:PRK08974 307 ----NTLFNALLNneefQEL----------------DF-----------SSLKLSVGGGMAVQQAVAERWVKLTGQYLLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 414 GYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLeeVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKD 492
Cdd:PRK08974 356 GYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKL--VDDDGNEvPPGE--PGELWVKGPQVMLGYWQRPEATDEVIKD 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 493 GWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSVVQDIwvygdsfksmlVAVVVPNP---ETINR 569
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMLHPKVLEV-----------AAVGVPSEvsgEAVKI 499
|
410
....*....|....*.
gi 2065806855 570 W--AKDLGFTKpfEEL 583
Cdd:PRK08974 500 FvvKKDPSLTE--EEL 513
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
225-564 |
1.43e-22 |
|
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: 99.27 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTH--------QAVATFvvgmdifmdqfedKMTHDDVYLSFLPLAHILDRmneeyffrkGASVGY 296
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHgnliaanlQLIHAM-------------GLTEADVYLNMLPLFHIAGL---------NLALAT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 YH-GDLNVLRD---------DIQELKPTYLAGVPRVFERIhegiqkaLQELnprrrlifnalykhklawmnrgyshskas 366
Cdd:cd17637 63 FHaGGANVVMEkfdpaealeLIEEEKVTLMGSFPPILSNL-------LDAA----------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 367 pmadfiafrkirDKLGGRIRLL--VSGgapL-SPE-IEEFLRVTCCCFVVqGYGLTETLGGTALGFPDEMCmlGTVGIPA 442
Cdd:cd17637 107 ------------EKSGVDLSSLrhVLG---LdAPEtIQRFEETTGATFWS-LYGQTETSGLVTLSPYRERP--GSAGRPG 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 443 VYNEIRLeeVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRK--KNLI 519
Cdd:cd17637 169 PLVRVRI--VDDNDRPvPAGE--TGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELI 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2065806855 520 KlSQGEYVALEHLENIFGQNSVVQDIWVYG--DS-FKSMLVAVVVPNP 564
Cdd:cd17637 245 K-PGGENVYPAEVEKVILEHPAIAEVCVIGvpDPkWGEGIKAVCVLKP 291
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
43-519 |
2.66e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 101.43 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 43 TAWDIFSKSVEKFPDNNMLgwrriVDEKVGpYMWkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACA 122
Cdd:PRK08315 17 TIGQLLDRTAARYPDREAL-----VYRDQG-LRW-TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 123 AHTLICV---PLYDTlgsGAVDYIVEHAEIDFVFVQDtKIKGL--------LEPDCKCAKR----------LKAIVSFtn 181
Cdd:PRK08315 90 KIGAILVtinPAYRL---SELEYALNQSGCKALIAAD-GFKDSdyvamlyeLAPELATCEPgqlqsarlpeLRRVIFL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 182 vsDELSHKAseigvkTYSWLDFLHMGREKPEET--------NPPKAFNIctiMYTSGTSGDPKGVVLTHQAVAT--FVVG 251
Cdd:PRK08315 164 --GDEKHPG------MLNFDELLALGRAVDDAElaarqatlDPDDPINI---QYTSGTTGFPKGATLTHRNILNngYFIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 252 MDIfmdqfedKMTHDDVYLSFLPLAH----ILDRMneeyffrkgASVGyyHG----------D-LNVLRDdIQELKPTYL 316
Cdd:PRK08315 233 EAM-------KLTEEDRLCIPVPLYHcfgmVLGNL---------ACVT--HGatmvypgegfDpLATLAA-VEEERCTAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 317 AGVPRVFerihegiqkaLQELNPRRRLIFNalykhklawmnrgYSHSKASPMAdfiafrkirdklggrirllvsgGAPlS 396
Cdd:PRK08315 294 YGVPTMF----------IAELDHPDFARFD-------------LSSLRTGIMA----------------------GSP-C 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 397 PEieEFLR----------VTCCcfvvqgYGLTETLGG---TALGFPDEMcMLGTVG--IPAVynEIRL------EEVaem 455
Cdd:PRK08315 328 PI--EVMKrvidkmhmseVTIA------YGMTETSPVstqTRTDDPLEK-RVTTVGraLPHL--EVKIvdpetgETV--- 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065806855 456 gydPLGEnpAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:PRK08315 394 ---PRGE--QGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-548 |
1.58e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 96.18 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQavaTFVVGMDIFMDQFEDkMTHDDVYLSFLPLAHI--LDRMNEEYFFRKGASVGYYHGDLN 302
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANK---TFFAVPDILQKEGLN-WVVGDVTYLPLPATHIggLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 303 VLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFnalykhklawmnrGYSHSKASPMADFIAFRKIRdklg 382
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGY-------------GGSRAIAADVRFIEATGLTN---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 383 grirllvsggaplspeieeflrvtcccfVVQGYGLTETLGGTALGFPDEMCMLGTVG--IPAVYNEIRLEEVAEMgydPL 460
Cdd:cd17635 145 ----------------------------TAQVYGLSETGTALCLPTDDDSIEINAVGrpYPGVDVYLAATDGIAG---PS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 461 GENpaGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNS 540
Cdd:cd17635 194 ASF--GTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEGVS 270
|
....*...
gi 2065806855 541 VVQDIWVY 548
Cdd:cd17635 271 GVQECACY 278
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
47-514 |
2.75e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 97.80 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 47 IFSKSVEKFPDNNMLGWrrivdekvGPYMWkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTL 126
Cdd:PRK07470 12 FLRQAARRFPDRIALVW--------GDRSW-TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 127 ICVPL----------YDTLGSGAVDYIV-----EHAEIdfvfVQDTkikgllepdckcAKRLKAIVSFTNVSDELSHKAs 191
Cdd:PRK07470 83 VWVPTnfrqtpdevaYLAEASGARAMIChadfpEHAAA----VRAA------------SPDLTHVVAIGGARAGLDYEA- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 192 eigvktyswLDFLHMGREKPE---ETNPPkafniCTIMYTSGTSGDPKGVVLTHQAVAtFVVgmdifMDQFEDKM---TH 265
Cdd:PRK07470 146 ---------LVARHLGARVANaavDHDDP-----CWFFFTSGTTGRPKAAVLTHGQMA-FVI-----TNHLADLMpgtTE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 266 DDVYLSFLPLAHildrmneeyffrkGASVgyyHGDLNVLRDDIQELKPTYLAGVPRVFerihegiqkALQElnpRRRL-- 343
Cdd:PRK07470 206 QDASLVVAPLSH-------------GAGI---HQLCQVARGAATVLLPSERFDPAEVW---------ALVE---RHRVtn 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 344 ------IFNALYKHKLAwmnRGYSHSKaspmadfiafrkirdklggrIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGL 417
Cdd:PRK07470 258 lftvptILKMLVEHPAV---DRYDHSS--------------------LRYVIYAGAPMYRADQKRALAKLGKVLVQYFGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 418 TETLGGT-----ALGFPDE--MCMLGTVGIPAVYNEIRLEEvAEMgyDPLGENPAGEICIRGQCMFSGYYKNPELTEEVI 490
Cdd:PRK07470 315 GEVTGNItvlppALHDAEDgpDARIGTCGFERTGMEVQIQD-DEG--RELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
|
490 500
....*....|....*....|....
gi 2065806855 491 KDGWFHTGDIGEILPNGVLKIIDR 514
Cdd:PRK07470 392 RDGWFRTGDLGHLDARGFLYITGR 415
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-641 |
3.04e-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: 97.44 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWII----AMEACAahtlICVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTaflgAIRAGI----VPVPVNTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQdtkikGLLEPdckcakRLKAIVSFTNVSDEL----SHKASEIGVKTYSWLDFLHMGREKPEETNPPkafNICTIMYTS 229
Cdd:cd05959 107 VS-----GELAP------VLAAALTKSEHTLVVlivsGGAGPEAGALLLAELVAAEAEQLKPAATHAD---DPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 230 GTSGDPKGVVLTHQ--AVATFVVGMDIFmdqfedKMTHDDVYLSFLPLAHILDRMNEEYF-FRKGASVGYYHGDLNVLR- 305
Cdd:cd05959 173 GSTGRPKGVVHLHAdiYWTAELYARNVL------GIREDDVCFSAAKLFFAYGLGNSLTFpLSVGATTVLMPERPTPAAv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 -DDIQELKPTYLAGVPRvferihegiqkalqelnprrrlIFNALYkhklawmnrgyshskASPMAdfiafrkiRDKLGGR 384
Cdd:cd05959 247 fKRIRRYRPTVFFGVPT----------------------LYAAML---------------AAPNL--------PSRDLSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLeeVAEMGYD-PLGEn 463
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRV-RYGTTGKPVPGYEVEL--RDEDGGDvADGE- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 464 pAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSVVQ 543
Cdd:cd05959 358 -PGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQHPAVL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 544 DIWVYG--DSFKSM-LVAVVVPNPEtinrwakdlgfTKPFEELcsFPELKEHIiselkstaeKNKLRKFEYIKAVavetk 620
Cdd:cd05959 436 EAAVVGveDEDGLTkPKAFVVLRPG-----------YEDSEAL--EEELKEFV---------KDRLAPYKYPRWI----- 488
|
570 580
....*....|....*....|..
gi 2065806855 621 pfDVERDL-VTATLKNRRNNLL 641
Cdd:cd05959 489 --VFVDELpKTATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
78-568 |
1.51e-20 |
|
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: 94.84 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaivsftnvsdelshkaseigvktyswldflhmgrekpeetnppkafNICTIMYTSGTSGDPKG 237
Cdd:cd05919 92 ---------------------------------------------------------------DIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVvgmdifmDQFEDK---MTHDDVYLSflplahiLDRMneeYF-FRKGASV--GYYHGDLNVLRDD---- 307
Cdd:cd05919 109 VMHAHRDPLLFA-------DAMAREalgLTPGDRVFS-------SAKM---FFgYGLGNSLwfPLAVGASAVLNPGwpta 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 308 ------IQELKPTYLAGVPrvferihegiqkalqelnprrrlifnALYKHKLAwmnrgyshSKASPMADFIAfrkirdkl 381
Cdd:cd05919 172 ervlatLARFRPTVLYGVP--------------------------TFYANLLD--------SCAGSPDALRS-------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 382 ggrIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLeeVAEMGYD-PL 460
Cdd:cd05919 210 ---LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAW-RLGSTGRPVPGYEIRL--VDEEGHTiPP 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 461 GEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNS 540
Cdd:cd05919 284 GE--EGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHP 360
|
490 500 510
....*....|....*....|....*....|.
gi 2065806855 541 VVQDIWVYG---DSFKSMLVAVVVPNPETIN 568
Cdd:cd05919 361 AVAEAAVVAvpeSTGLSRLTAFVVLKSPAAP 391
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
78-563 |
1.86e-20 |
|
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: 95.23 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDfVFVQDT 157
Cdd:TIGR03098 27 TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVR-LLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEPDCKCAKRLKAIVSFTNvsdelSHKASEI--GVKTYSWLDFLHMGREKPeetnPPKAF--NICTIMYTSGTSG 233
Cdd:TIGR03098 106 ERLDLLHPALPGCHDLRTLIIVGD-----PAHASEGhpGEEPASWPKLLALGDADP----PHPVIdsDMAAILYTSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 234 DPKGVVLTHqavATFVVGMDIFMDQFEDkmTHDDVYLSFLPLAHildrmneEYFFRKgASVGYYHGDLNVL------RDD 307
Cdd:TIGR03098 177 RPKGVVLSH---RNLVAGAQSVATYLEN--RPDDRLLAVLPLSF-------DYGFNQ-LTTAFYVGATVVLhdyllpRDV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 308 IQELKP---TYLAGVPRVFerihegIQKAlqelnprrrlifnalykhKLAWmnrgyshskasPMADFIAFRKIRDKlGGR 384
Cdd:TIGR03098 244 LKALEKhgiTGLAAVPPLW------AQLA------------------QLDW-----------PESAAPSLRYLTNS-GGA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 I-RLLVSGGAPLSPEIEEFLRvtcccfvvqgYGLTETLGGTALGfPDEM-CMLGTVG--IPAVynEIRLeeVAEMGYDPL 460
Cdd:TIGR03098 288 MpRATLSRLRSFLPNARLFLM----------YGLTEAFRSTYLP-PEEVdRRPDSIGkaIPNA--EVLV--LREDGSECA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 461 GENPaGEICIRGQCMFSGYYKNPELTEEVIK------DG--------WfhTGDIGEILPNGVLKIIDRKKNLIKLSqGEY 526
Cdd:TIGR03098 353 PGEE-GELVHRGALVAMGYWNDPEKTAERFRplppfpGElhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIKTS-GYR 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2065806855 527 VALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPN 563
Cdd:TIGR03098 429 VSPTEVEEVAYATGLVAEAVAFGvpdPTLGQAIVLVVTPP 468
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
42-617 |
1.87e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 95.58 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 42 TTAWDIFSKSVEKFPDNNMlgwrrIVDEKVGPYmwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIygiNCPQW---IIAM 118
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIA-----VVDNHGASY---TYSALDHAASRLANWLLAKGIEPGDRVAF---QLPGWcefTIIY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 119 EACAAHTLICVPLYDTLGSGAVDYIVEHAEIDfVFVQDTKIKG-----LLEPDCKCAKRLKAIVSFtnvsDELSHKASEI 193
Cdd:PRK06087 92 LACLKVGAVSVPLLPSWREAELVWVLNKCQAK-MFFAPTLFKQtrpvdLILPLQNQLPQLQQIVGV----DKLAPATSSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 194 gvkTYSWLdflhMGREKPEETNPPKAFN-ICTIMYTSGTSGDPKGVVLTHQAV----ATFVVGMDIfmdqfedkmTHDDV 268
Cdd:PRK06087 167 ---SLSQI----IADYEPLTTAITTHGDeLAAVLFTSGTEGLPKGVMLTHNNIlaseRAYCARLNL---------TWQDV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 269 YLSFLPLAHildrmneeyffrkgaSVGYYHGdlnvlrddiqeLKPTYLAGVPRVFERIHEGiQKALQELNprrrlifnal 348
Cdd:PRK06087 231 FMMPAPLGH---------------ATGFLHG-----------VTAPFLIGARSVLLDIFTP-DACLALLE---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 349 yKHKLAWMnrgyshSKASPmadFI-----AFRKIRDKLGGrIRLLVSGGAPLsPEieeflRVTCCCfvvQGYG--LTETL 421
Cdd:PRK06087 274 -QQRCTCM------LGATP---FIydllnLLEKQPADLSA-LRFFLCGGTTI-PK-----KVAREC---QQRGikLLSVY 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 422 GGT-----ALGFPDEmC---MLGTVGIPAVYNEIRLeeVAEMGYD-PLGENpaGEICIRGQCMFSGYYKNPELTEEVI-K 491
Cdd:PRK06087 334 GSTessphAVVNLDD-PlsrFMHTDGYAAAGVEIKV--VDEARKTlPPGCE--GEEASRGPNVFMGYLDEPELTARALdE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 492 DGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPETin 568
Cdd:PRK06087 409 EGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVVAmpdERLGERSCAYVVLKAPH-- 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 569 rwakdlgFTKPFEELCSFPELK--------EHI--ISELKSTAeKNKLRKFEYIKAVAV 617
Cdd:PRK06087 486 -------HSLTLEEVVAFFSRKrvakykypEHIvvIDKLPRTA-SGKIQKFLLRKDIMR 536
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
78-562 |
2.10e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 94.67 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDt 157
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlkaivsftnvsdELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKafNICTIMYTSGTSGDPKG 237
Cdd:cd12116 93 ---------------------------ALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPD--DLAYVIYTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMdifMDQFEdkMTHDDVYLS-------------FLPLAHildrmneeyffrkGASVGYYHGDLNV- 303
Cdd:cd12116 144 VVVSHRNLVNFLHSM---RERLG--LGPGDRLLAvttyafdisllelLLPLLA-------------GARVVIAPRETQRd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 304 ---LRDDIQELKPTYLAGVPRVFerihegiqkalqelnprrRLIFNAlykhklAWMNRgyshskaspmadfiafrkirdk 380
Cdd:cd12116 206 peaLARLIEAHSITVMQATPATW------------------RMLLDA------GWQGR---------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 381 lgGRIRLLVsGGAPLSPEI-EEFLRVTCCcfVVQGYGLTETLGGTALGFPDEMCMLGTVGIPA----VYneirleeVAEM 455
Cdd:cd12116 240 --AGLTALC-GGEALPPDLaARLLSRVGS--LWNLYGPTETTIWSTAARVTAAAGPIPIGRPLantqVY-------VLDA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 456 GYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDG--------WFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYV 527
Cdd:cd12116 308 ALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRI 386
|
490 500 510
....*....|....*....|....*....|....*..
gi 2065806855 528 ALEHLENIFGQNSVVQD--IWVYGDSFKSMLVAVVVP 562
Cdd:cd12116 387 ELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVL 423
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
78-640 |
2.17e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 94.42 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIdfvfvqdt 157
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcakrlKAIVsfTNVSDELShkaseigvktyswldflhmgrekpeetnppkafnicTIMYTSGTSGDPKG 237
Cdd:cd05971 80 ----------------SALV--TDGSDDPA------------------------------------LIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGmdifmdqfeDKMTHDdvylsFLPlahildrmNEEYFFRKGASVGYYHGDLNVLRddiqelkPTYLA 317
Cdd:cd05971 106 ALHAHRVLLGHLPG---------VQFPFN-----LFP--------RDGDLYWTPADWAWIGGLLDVLL-------PSLYF 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 318 GVPRVFERihegiqkaLQELNPRRRLIFNALYKHKLAWMnrgyshsKASPMADFIAFRKIRDKLGGRIRLLVSGGAPLSP 397
Cdd:cd05971 157 GVPVLAHR--------MTKFDPKAALDLMSRYGVTTAFL-------PPTALKMMRQQGEQLKHAQVKLRAIATGGESLGE 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 398 EIEEFLRVTCCCFVVQGYGLTET---LGGTALGFPDEMcmlGTVGIPAVYNEIRLeeVAEMGyDPLGENPAGEICIRGQC 474
Cdd:cd05971 222 ELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIKP---GSMGKPIPGHRVAI--VDDNG-TPLPPGEVGEIAVELPD 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 475 --MFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYG--D 550
Cdd:cd05971 296 pvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAAVVGipD 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 551 SFKSMLV-AVVVPNPetinrwakdlGFTkPFEELCSfpELKEHIiselkstaeKNKLRKFEYIKAV-AVETKPfdverdl 628
Cdd:cd05971 375 PIRGEIVkAFVVLNP----------GET-PSDALAR--EIQELV---------KTRLAAHEYPREIeFVNELP------- 425
|
570
....*....|..
gi 2065806855 629 VTATLKNRRNNL 640
Cdd:cd05971 426 RTATGKIRRREL 437
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
43-567 |
3.51e-20 |
|
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: 94.11 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 43 TAWDIFSKSVEKFPDNNMlgwrrIVDEKVGPYMwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACA 122
Cdd:cd05923 2 TVFEMLRRAASRAPDACA-----IADPARGLRL--TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 123 AHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDtkIKGLLEPDCKCAKRLKAivsftnVSDELSHKASEigvktySWLD 202
Cdd:cd05923 75 RLGAVPALINPRLKAAELAELIERGEMTAAVIAV--DAQVMDAIFQSGVRVLA------LSDLVGLGEPE------SAGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 203 FLHMGREKPEETnppkAFnictIMYTSGTSGDPKGVVLTHQAVATFVVGMdifMDQFEDKMTHDDVYLSFLPLAHILDrm 282
Cdd:cd05923 141 LIEDPPREPEQP----AF----VFYTSGTTGLPKGAVIPQRAAESRVLFM---STQAGLRHGRHNVVLGLMPLYHVIG-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 283 neeyFFRKGASVGYYHGDLNVLRDD--------IQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNAlykhklA 354
Cdd:cd05923 208 ----FFAVLVAALALDGTYVVVEEFdpadalklIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAG------A 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 355 WMNRGyshskaspmadfiAFRKIRDKLGGRIrllvsggaplspeieeflrvtcccfvVQGYGLTETLGGTALGFPDEmcm 434
Cdd:cd05923 278 TMPDA-------------VLERVNQHLPGEK--------------------------VNIYGTTEAMNSLYMRDART--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 435 lGTVGIPAVYNEIRLEEVAEMGYDPLGENPAGEICIR--GQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKII 512
Cdd:cd05923 316 -GTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRIL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2065806855 513 DRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPETI 567
Cdd:cd05923 395 GRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvadERWGQSVTACVVPREGTL 451
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
177-566 |
9.61e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.37 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 177 VSFTNVSDELSHKASEIGVKTYSWLDFlhmgrEKPEETNPP--KAFNICTIMYTSGTSGDPKGVVLTHQavaTFVVGMDI 254
Cdd:PLN02574 158 VPVIGVPENYDFDSKRIEFPKFYELIK-----EDFDFVPKPviKQDDVAAIMYSSGTTGASKGVVLTHR---NLIAMVEL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 255 FM----DQFEDKMThDDVYLSFLPLAHILDRMneeyFFRKG------ASVGYYHGDLNVLRDDIQELKPTYLAGVPrvfe 324
Cdd:PLN02574 230 FVrfeaSQYEYPGS-DNVYLAALPMFHIYGLS----LFVVGllslgsTIVVMRRFDASDMVKVIDRFKVTHFPVVP---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 325 rihegiqkalqelnPrrrlIFNALYKhklawmnrgyshsKASPMADFIAfrkirdklgGRIRLLVSGGAPLSPE-IEEFL 403
Cdd:PLN02574 301 --------------P----ILMALTK-------------KAKGVCGEVL---------KSLKQVSCGAAPLSGKfIQDFV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 404 RVTCCCFVVQGYGLTETLGGTALGFPDE-MCMLGTVGIPAVYNEIRLEEVAEMGYDPLGEnpAGEICIRGQCMFSGYYKN 482
Cdd:PLN02574 341 QTLPHVDFIQGYGMTESTAVGTRGFNTEkLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGN--CGELWIQGPGVMKGYLNN 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 483 PELTE-EVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWVYGDSFK---SMLVA 558
Cdd:PLN02574 419 PKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVA 497
|
....*...
gi 2065806855 559 VVVPNPET 566
Cdd:PLN02574 498 FVVRRQGS 505
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
78-574 |
9.95e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 93.31 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALR-AVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEiDFVFVQD 156
Cdd:PRK05620 40 TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAE-DEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 TKIK---GLLEPDCKCAkRLKAIVSFTNVSDELSHKASEIGVKTY-SWLDflhmGR-------EKPEETnppkAFNICti 225
Cdd:PRK05620 119 PRLAeqlGEILKECPCV-RAVVFIGPSDADSAAAHMPEGIKVYSYeALLD----GRstvydwpELDETT----AAAIC-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 226 mYTSGTSGDPKGVVLTHQAVatFVVGMDIF-MDQFedKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNV- 303
Cdd:PRK05620 188 -YSTGTTGAPKGVVYSHRSL--YLQSLSLRtTDSL--AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSAp 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 304 -LRDDIQELKPTYLAGVPRVFerihegIQKALQEL-NPRRRLIFNALYkhklawmnrgyshskaspmadfiafrkirdkl 381
Cdd:PRK05620 263 tLAKIIATAMPRVAHGVPTLW------IQLMVHYLkNPPERMSLQEIY-------------------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 382 ggrirllvSGGAPLSPEI----EEFLRVTcccfVVQGYGLTETLGgtalgfpdemcmLGTVGIP--AVYNEIRLEEVAEM 455
Cdd:PRK05620 305 --------VGGSAVPPILikawEERYGVD----VVHVWGMTETSP------------VGTVARPpsGVSGEARWAYRVSQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 456 GYDPLG---------------ENPAGEICIRGQCMFSGYYKNP-----------------ELTEEVIKDGWFHTGDIGEI 503
Cdd:PRK05620 361 GRFPASleyrivndgqvmestDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedveDANDRFTADGWLRTGDVGSV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 504 LPNGVLKIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVV------PNPETINRWAKDL 574
Cdd:PRK05620 441 TRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIGypdDKWGERPLAVTVlapgiePTRETAERLRDQL 519
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
78-565 |
1.31e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 92.73 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQW-IIAMEACAAHTLIcvplydtlgSGA--------VDYIVEHAE 148
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYgIVALGIMAAGGVF---------SGAnptaleseIKKQAEAAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 149 IDFVFVQDT---KIKGLlepdckcakRLKAIVsftnvsdeLSHKASEIGVktySWLDFLHMGrEKPEETNPPKAF---NI 222
Cdd:PLN02330 128 AKLIVTNDTnygKVKGL---------GLPVIV--------LGEEKIEGAV---NWKELLEAA-DRAGDTSDNEEIlqtDL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 223 CTIMYTSGTSGDPKGVVLTHQAV------ATFVVGmdifmdqfeDKMTHDDVYLSFLPLAHI--LDRMNEEYFFRKGASV 294
Cdd:PLN02330 187 CALPFSSGTTGISKGVMLTHRNLvanlcsSLFSVG---------PEMIGQVVTLGLIPFFHIygITGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 295 GYYHGDLNVLRDDIQELKPTYLAGVPrvferihegiqkalqelnPrrrlIFNALYKhklawmnrgyshskaSPMADFIAF 374
Cdd:PLN02330 258 VMSRFELRTFLNALITQEVSFAPIVP------------------P----IILNLVK---------------NPIVEEFDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 375 RKIRdklggrIRLLVSGGAPLSPEI-----EEFLRVTcccfVVQGYGLTE----TLggtALGFPDE---MCMLGTVGIPA 442
Cdd:PLN02330 301 SKLK------LQAIMTAAAPLAPELltafeAKFPGVQ----VQEAYGLTEhsciTL---THGDPEKghgIAKKNSVGFIL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 443 VYNEIRLeevaemgYDP-----LGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKK 516
Cdd:PLN02330 368 PNLEVKF-------IDPdtgrsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIK 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2065806855 517 NLIKLsQGEYVALEHLENIFGQNSVVQDiwvygdsfksmlvAVVVPNPE 565
Cdd:PLN02330 441 ELIKY-KGFQVAPAELEAILLTHPSVED-------------AAVVPLPD 475
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
224-564 |
2.31e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 92.00 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 224 TIMYTSGTSGDPKGVVLTHQ----AVATFVVG--MDIFmdqfedkmthdDVYLSFLPLAHIldrmNEEYF-----FRKGA 292
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRgaylSTLSAIIGweMGTC-----------PVYLWTLPMFHC----NGWTFtwgtaARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 293 SVGYYHGDLNVLRDDIQELKPTYLAGVPRVFERIHEGiqkalqelnprrrlifnalykhklawmNRGYSHSKASPmadfi 372
Cdd:PLN03102 255 SVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---------------------------NSLDLSPRSGP----- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 373 afrkirdklggrIRLLVSGGAPLSPEIEEFLRVTcccF-VVQGYGLTETLGGTAL--------GFPDEMCM--------- 434
Cdd:PLN03102 303 ------------VHVLTGGSPPPAALVKKVQRLG---FqVMHAYGLTEATGPVLFcewqdewnRLPENQQMelkarqgvs 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 435 -LGTVGIPaVYNEIRLEEVaemgydPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIID 513
Cdd:PLN03102 368 iLGLADVD-VKNKETQESV------PRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKD 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 514 RKKNLIkLSQGEYVALEHLENIfgqnsvvqdIWVYGDSFKSMLVAvvVPNP 564
Cdd:PLN03102 441 RSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVA--MPHP 479
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
34-522 |
3.37e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.48 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 34 FPP-IDSEIT-----TAWDIFSKSVEKFPDnnmlgwrRIVDEKVGPYMwkTYKEVYEEVLQIGSALRAV-GAEPGCRVGI 106
Cdd:PRK08751 11 YPAgVAAEIDleqfrTVAEVFATSVAKFAD-------RPAYHSFGKTI--TYREADQLVEQFAAYLLGElQLKKGDRVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 107 YGINCPQWIIAMEA--CAAHTLICV-PLYDT-------LGSGAVDYIVEHAEIDFV--FVQDTKIKGLLEPD----CKCA 170
Cdd:PRK08751 82 MMPNCLQYPIATFGvlRAGLTVVNVnPLYTPrelkhqlIDSGASVLVVIDNFGTTVqqVIADTPVKQVITTGlgdmLGFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 171 KRlkAIVSFtnVSDELSHKASEIGVK-TYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFV 249
Cdd:PRK08751 162 KA--ALVNF--VVKYVKKLVPEYRINgAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 250 VGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYFFRKGASVGYYHGDLNVLRDDIQELKPTYLAGVPRVferiheg 329
Cdd:PRK08751 238 QQAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 330 iqkalqelnprrRLIFNALYKhklawmnrgyshskaSPMADFIAFRKIRDKLGGrirllvsGGAPLSPEIEEFLRVTCCC 409
Cdd:PRK08751 311 ------------NTLFNGLLN---------------TPGFDQIDFSSLKMTLGG-------GMAVQRSVAERWKQVTGLT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 410 fVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAEMGYdPLGEnpAGEICIRGQCMFSGYYKNPELTEEV 489
Cdd:PRK08751 357 -LVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVL-AIGE--IGELCIKGPQVMKGYWKRPEETAKV 432
|
490 500 510
....*....|....*....|....*....|....
gi 2065806855 490 IK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
Cdd:PRK08751 433 MDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVS 466
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
217-609 |
3.56e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 91.27 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 217 PKAFNICTIMYTSGTSGDPKGVVLTHQavaTFVVGMDIFMDQFedKMTHDDVYLSFLPLAHIldrmneeyffrkgasVGY 296
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTAN---TLMANIVPYAERL--GLGADDVILMASPMAHQ---------------TGF 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 YHGdlnvlrddiqELKPTYLagvprvferiheGIQKALQEL-NPRR--RLIfnalYKHKLAWMnrgyshSKASP-MADFI 372
Cdd:PRK13295 254 MYG----------LMMPVML------------GATAVLQDIwDPARaaELI----RTEGVTFT------MASTPfLTDLT 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 373 AFRKIRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTET--LGGTALGFPDEMcMLGTVGIPAVYNEIRLe 450
Cdd:PRK13295 302 RAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENgaVTLTKLDDPDER-ASTTDGCPLPGVEVRV- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 451 eVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEeVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVAL 529
Cdd:PRK13295 380 -VDADGAPlPAGQ--IGRLQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 530 EHLENIFGQNSVVQDIWV--YGDS-FKSMLVAVVVPNP------ETINRWAKDLGFTKPFeelcsFPELKEhIISELKST 600
Cdd:PRK13295 455 VEIEALLYRHPAIAQVAIvaYPDErLGERACAFVVPRPgqsldfEEMVEFLKAQKVAKQY-----IPERLV-VRDALPRT 528
|
....*....
gi 2065806855 601 AeKNKLRKF 609
Cdd:PRK13295 529 P-SGKIQKF 536
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
46-652 |
4.48e-19 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 92.23 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 46 DIFSKSVEKFPDNNMLGwrriVDEKVGPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHT 125
Cdd:PTZ00297 431 EMWERSVTRHSTFRCLG----QTSESGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYG 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 126 LICVPLYDTlGSGAVDYIVEHaEIDFVFVQDTKIKGLLEpdCKcAKRLKAIVSFTNVSDELSHK-ASEIGVKTYSWLDFL 204
Cdd:PTZ00297 507 FTTLPLVGK-GSTMRTLIDEH-KIKVVFADRNSVAAILT--CR-SRKLETVVYTHSFYDEDDHAvARDLNITLIPYEFVE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 205 HMGREKPEetnPPKAFNICTIMYT-------SGTSGDPKGVVLTHQAV---ATFVVGMDIFMDQFedkmtHDDVYLSFLP 274
Cdd:PTZ00297 582 QKGRLCPV---PLKEHVTTDTVFTyvvdnttSASGDGLAVVRVTHADVlrdISTLVMTGVLPSSF-----KKHLMVHFTP 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 275 LAHILDRMNEEYFFRKGASVGYYhgDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKHKLA 354
Cdd:PTZ00297 654 FAMLFNRVFVLGLFAHGSAVATV--DAAHLQRAFVKFQPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSR 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 355 WMNrgySHSKASPMADFIAFRKIRDKLGGRIR--LLVSGGAPLSPEIEEFLRVtccCFVVQgygLTETLGGTALGfpdeM 432
Cdd:PTZ00297 732 LIN---IHRRDSSLLRFIFFRATQELLGGCVEkiVLCVSEESTSFSLLEHISV---CYVPC---LREVFFLPSEG----V 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 433 CMLGtvGIPAVYNEIRLEEVAemgyDPLGENPAGEICI--RGQcmfsgyyknPELTEEvIKDGWFHTGD---IGEilPNG 507
Cdd:PTZ00297 799 FCVD--GTPAPSLQVDLEPFD----EPSDGAGIGQLVLakKGE---------PRRTLP-IAAQWKRDRTlrlLGP--PLG 860
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 508 VLKIIdrkknliklsQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSmLVAVVVPNPETIN---RWAKDLGFTKPFEELC 584
Cdd:PTZ00297 861 ILLPV----------AYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfewRQSHCMGEGGGPARQL 929
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065806855 585 SFPELKEH----IISELKSTAEKNKLRKFEYIKAVAVETKPFDVERDLVTATLKNRRNNLLKYYQVQIDEMY 652
Cdd:PTZ00297 930 GWTELVAYasslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
221-549 |
7.86e-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: 87.94 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTH-QAVATFVVGMDIfmdqfeDKMTHDDVYLSFLPLAHildrmneEYFFRKGASVGYYHG 299
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADC------ADLTEDDRYLIINPFFH-------TFGYKAGIVACLLTG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 300 ---------DLNVLRDDIQELKPTYLAGVPRVFerihegiQKALQElnPRRRlifnalyKHKLAWMNRGYSHSKASPMad 370
Cdd:cd17638 68 atvvpvavfDVDAILEAIERERITVLPGPPTLF-------QSLLDH--PGRK-------KFDLSSLRAAVTGAATVPV-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 371 fIAFRKIRDKLGGRIrllvsggaplspeieeflrvtcccfVVQGYGLTETLGGTalgfpdeMCMLG--------TVGIPA 442
Cdd:cd17638 130 -ELVRRMRSELGFET-------------------------VLTAYGLTEAGVAT-------MCRPGddaetvatTCGRAC 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 443 VYNEIRLEEvaemgydplgenpAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkL 521
Cdd:cd17638 177 PGFEVRIAD-------------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY-I 242
|
330 340
....*....|....*....|....*...
gi 2065806855 522 SQGEYVALEHLENIFGQNSVVQDIWVYG 549
Cdd:cd17638 243 VGGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
78-602 |
1.13e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 89.95 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikGLLEPDCKCAKRLKAIVSFTNVSDELSHKAS-EIGVKTYswldfLHMGREKPEETNPPKAFnictIMYTSGTSGDPK 236
Cdd:PRK05852 125 ---GPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSvHLDAATE-----PTPATSTPEGLRPDDAM----IMFTGGTTGLPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVVLTHQAVATFVVGMdIFMDQFEDKmthdDVYLSFLPLAH-------ILDRMNEeyffrKGASVGYYHGDLN--VLRDD 307
Cdd:PRK05852 193 MVPWTHANIASSVRAI-ITGYRLSPR----DATVAVMPLYHghgliaaLLATLAS-----GGAVLLPARGRFSahTFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 308 IQELKPTYLAGVPRvferIHE-GIQKALQELNPRRRlifnalykhklawmnrgyshskaspmadfIAFRKIRdklggrir 386
Cdd:PRK05852 263 IKAVGATWYTAVPT----IHQiLLERAATEPSGRKP-----------------------------AALRFIR-------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 387 llvSGGAPLSPEIEEFLRVTCCCFVVQGYGLTET---LGGTAL-GFPDEMCMLGTVGIPAVYNEIRLEEVAEMGYdPLGE 462
Cdd:PRK05852 302 ---SCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqVTTTQIeGIGQTENPVVSTGLVGRSTGAQIRIVGSDGL-PLPA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 463 NPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSVV 542
Cdd:PRK05852 378 GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065806855 543 QDIWVYGD---SFKSMLVAVVVPNpETINRWAKDL-GFTK----PFEELCSFpelkeHIISELKSTAE 602
Cdd:PRK05852 457 MEAAVFGVpdqLYGEAVAAVIVPR-ESAPPTAEELvQFCRerlaAFEIPASF-----QEASGLPHTAK 518
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
78-519 |
1.59e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 89.16 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDfVFVQDT 157
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA-LVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLEPdckCAKRLKAIVSFTNVSD------ELSHKASEigvktyswlDFlhmgrekpeETNPPKAFNICTIMYTSGT 231
Cdd:PRK07514 109 ANFAWLSK---IAAAAGAPHVETLDADgtgsllEAAAAAPD---------DF---------ETVPRGADDLAAILYTSGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTHQAVAT-FVVGMDIFmdqfedKMTHDDVYLSFLPLAHIldrmneeyffrkgasvgyyHG---DLNVlrdd 307
Cdd:PRK07514 168 TGRSKGAMLSHGNLLSnALTLVDYW------RFTPDDVLIHALPIFHT-------------------HGlfvATNV---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 308 iqelkpTYLAGVPRVFerihegiqkaLQELNPRRrlifnalykhKLAWMNRG---------YSHSKASPMADfiafrkir 378
Cdd:PRK07514 219 ------ALLAGASMIF----------LPKFDPDA----------VLALMPRAtvmmgvptfYTRLLQEPRLT-------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 379 DKLGGRIRLLVSGGAPLSPEI-EEFLRVTcccfvvqG------YGLTETlggtalgfpdemCML-----------GTVGI 440
Cdd:PRK07514 265 REAAAHMRLFISGSAPLLAEThREFQERT-------GhailerYGMTET------------NMNtsnpydgerraGTVGF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 441 PAVYNEIRLEEVAEMGYDPLGEnpAGEICIRGQCMFSGYYKNPELT-EEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:PRK07514 326 PLPGVSLRVTDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPEKTaEEFRADGFFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
216-542 |
2.14e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 89.98 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 216 PPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGM-DIFMdqfedkMTHDDVYLSFLPLAHildrmneeyffrkgaSV 294
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQIsDVFN------LRNDDVILSSLPFFH---------------SF 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 295 GYYHGDLNVLrddiqelkptyLAGVPRVFeriH------EGIQKALQelnprrrlifnalyKHKLAWMN------RGYS- 361
Cdd:PRK08633 837 GLTVTLWLPL-----------LEGIKVVY---HpdptdaLGIAKLVA--------------KHRATILLgtptflRLYLr 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 362 HSKASPmADFiafrkirdklgGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEM--------- 432
Cdd:PRK08633 889 NKKLHP-LMF-----------ASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVLaadfkrqtg 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 433 CMLGTVGIPAVYNEIRLeeVAEMGYDPLGENPAGEICIRG-QCMfSGYYKNPELTEEVIKD----GWFHTGDIGEILPNG 507
Cdd:PRK08633 957 SKEGSVGMPLPGVAVRI--VDPETFEELPPGEDGLILIGGpQVM-KGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDG 1033
|
330 340 350
....*....|....*....|....*....|....*....
gi 2065806855 508 VLKIIDRKKNLIKLSqGEYVAL----EHLENIFGQNSVV 542
Cdd:PRK08633 1034 FLTITDRYSRFAKIG-GEMVPLgaveEELAKALGGEEVV 1071
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
29-519 |
8.80e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 87.32 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 29 LSEKGFPpidseiTTAWDIFSKSVEKFPDNNMLGWRRIVDEKVGPYMWkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYG 108
Cdd:PRK07529 18 LAARDLP------ASTYELLSRAAARHPDAPALSFLLDADPLDRPETW-TYAELLADVTRTANLLHSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 109 INCPQWIIAMEACAAhTLICVPLYDTLGSGAVdyivehAEIdfvfVQDTKIKGLL----EPDCKCAKR----------LK 174
Cdd:PRK07529 91 PNLPETHFALWGGEA-AGIANPINPLLEPEQI------AEL----LRAAGAKVLVtlgpFPGTDIWQKvaevlaalpeLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 175 AIVSfTNVSDELSHKASEI-----GVKTYSWLDFL-HMGREKPEETNPPKAFN---ICTIMYTSGTSGDPKGVVLTH--Q 243
Cdd:PRK07529 160 TVVE-VDLARYLPGPKRLAvplirRKAHARILDFDaELARQPGDRLFSGRPIGpddVAAYFHTGGTTGMPKLAQHTHgnE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 244 AVATFVVGMDIFMDqfedkmtHDDVYLSFLPLAHIldrmNEEY------FFRkGASV------GYyhgdlnvlRDD---- 307
Cdd:PRK07529 239 VANAWLGALLLGLG-------PGDTVFCGLPLFHV----NALLvtglapLAR-GAHVvlatpqGY--------RGPgvia 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 308 -----IQELKPTYLAGVPRVFerihegiqkalqelnprrrlifNALykhklawMNRgyshskasPmadfIAFRKIrdklg 382
Cdd:PRK07529 299 nfwkiVERYRINFLSGVPTVY----------------------AAL-------LQV--------P----VDGHDI----- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 383 GRIRLLVSGGAPLSPE-IEEFLRVTCCCfVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLEEVAEMGYDP-- 459
Cdd:PRK07529 333 SSLRYALCGAAPLPVEvFRRFEAATGVR-IVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVILDDAGRYLrd 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065806855 460 LGENPAGEICIRGQCMFSGYyknpeLTEE-----VIKDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:PRK07529 412 CAVDEVGVLCIAGPNVFSGY-----LEAAhnkglWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
48-565 |
1.89e-17 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 85.84 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 48 FSKSVEKFPDNNMLgwrRIVDEKVgpymwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIA----MEACAA 123
Cdd:cd17655 3 FEEQAEKTPDHTAV---VFEDQTL------TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGilgiLKAGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 124 HtlicVPLYDTLGSGAVDYIVEHAEIDFVFVQdtkikgllepdckcaKRLKAIVSFTNVSDELSHKASEIGVKTYswldf 203
Cdd:cd17655 74 Y----LPIDPDYPEERIQYILEDSGADILLTQ---------------SHLQPPIAFIGLIDLLDEDTIYHEESEN----- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 204 LHmgrekpeetNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFEdkmtHDDVYLsFLPLA------- 276
Cdd:cd17655 130 LE---------PVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGE----HLRVAL-FASISfdasvte 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 277 --HILDRMNEEYFFRKgASVGYYHGDLNVLRD---DIQELKPTYLagvprvferihegiqkalQELNPrrrlifnalykh 351
Cdd:cd17655 196 ifASLLSGNTLYIVRK-ETVLDGQALTQYIRQnriTIIDLTPAHL------------------KLLDA------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 352 klawmnrgyshskaspmadfiafrkIRDKLGGRIRLLVSGGAPLSPE-IEEFL-RVTCCCFVVQGYGLTETLGGTALGFP 429
Cdd:cd17655 245 -------------------------ADDSEGLSLKHLIVGGEALSTElAKKIIeLFGTNPTITNAYGPTETTVDASIYQY 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 430 DEMCMLGT---VGIPAVYNEIRLEEvAEMGYDPLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWF-------HTGD 499
Cdd:cd17655 300 EPETDQQVsvpIGKPLGNTRIYILD-QYGRPQPVGV--AGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermyRTGD 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 500 IGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENIFGQNSVVQD---IWVYGDSFKSMLVAVVVPNPE 565
Cdd:cd17655 377 LARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavvIARKDEQGQNYLCAYIVSEKE 444
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
386-575 |
1.93e-17 |
|
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: 85.97 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 RLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETL-GGTALGFPDEMcMLGTVGIP-AVYNEIRLeeVAEMGYD-PLGE 462
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLvNYTRLDDPEEV-ILTTQGRPiSPDDEVRI--VDEDGNPvPPGE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 463 npAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSV 541
Cdd:COG1021 380 --VGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRG-GEKIAAEEVENLLLAHPA 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2065806855 542 VQDIWVYG--DSF---KSmlVAVVVPN-----PETINRWAKDLG 575
Cdd:COG1021 457 VHDAAVVAmpDEYlgeRS--CAFVVPRgepltLAELRRFLRERG 498
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
78-519 |
3.99e-17 |
|
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: 84.98 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAePGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAvdyivehaeidfvfvqdt 157
Cdd:cd05931 26 TYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRH------------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllepdckcAKRLKAIVSFTNVSDELSHKASEIGVKTYSW------------LDFLHMGREKPEETNPPKAFNICTI 225
Cdd:cd05931 87 ------------AERLAAILADAGPRVVLTTAAALAAVRAFAAsrpaagtprllvVDLLPDTSAADWPPPSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 226 MYTSGTSGDPKGVVLTHQAVATFVVGMdifMDQFEdkMTHDDVYLSFLPLAHildrmneeyffrkgasvgyyhgdlnvlr 305
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQI---RRAYG--LDPGDVVVSWLPLYH---------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 dD---IQELKPTYLAGVPRVFERIHEGIQKalqelnPRR--RLIfnalykhklawmnrgySHSKA--SPMADFiAF---- 374
Cdd:cd05931 202 -DmglIGGLLTPLYSGGPSVLMSPAAFLRR------PLRwlRLI----------------SRYRAtiSAAPNF-AYdlcv 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 375 RKIRD-KLGG----RIRLLVSGGAPLSPE-IEEF--------LRVTCccfVVQGYGLTE-TL---------GGTALGFPD 430
Cdd:cd05931 258 RRVRDeDLEGldlsSWRVALNGAEPVRPAtLRRFaeafapfgFRPEA---FRPSYGLAEaTLfvsggppgtGPVVLRVDR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 431 EM---------------CMLGTVGIPAVYNEIRLeeVAEMGYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIK---- 491
Cdd:cd05931 335 DAlagravavaaddpaaRELVSCGRPLPDQEVRI--VDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaa 412
|
490 500 510
....*....|....*....|....*....|.
gi 2065806855 492 ---DGWFHTGDIGEILpNGVLKIIDRKKNLI 519
Cdd:cd05931 413 tdeGGWLRTGDLGFLH-DGELYITGRLKDLI 442
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
62-535 |
4.25e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 84.80 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 62 GWRRIVDEKV-GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQ----WIIAMEACAahtlICVPLYDTLG 136
Cdd:PRK06018 24 GNREVVTRSVeGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRhleaWYGIMGIGA----ICHTVNPRLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 137 SGAVDYIVEHAEiDFVFVQDTKIKGLLEpdcKCAKRLKAIVSFTNVSDElSH---------KASEIGVK----TYSWLDF 203
Cdd:PRK06018 100 PEQIAWIINHAE-DRVVITDLTFVPILE---KIADKLPSVERYVVLTDA-AHmpqttlknaVAYEEWIAeadgDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 204 lhmgrekPEETnppkafnICTIMYTSGTSGDPKGVVLTHQA--VATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHildr 281
Cdd:PRK06018 175 -------DENT-------AAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALG-----TSAADTMLPVVPLFH---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 282 MNEEYFFRKGASVGYYHGDLNVLRD--DIQEL----KPTYLAGVPRVFERIHEGIQKAlqelnprrrlifnalyKHKLAW 355
Cdd:PRK06018 232 ANSWGIAFSAPSMGTKLVMPGAKLDgaSVYELldteKVTFTAGVPTVWLMLLQYMEKE----------------GLKLPH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 356 MNRGYSHSKASPMADFIAFRKIrdklggrirllvsggaplspEIEeflrvtcccfVVQGYGLTetlggtalgfpdEMCML 435
Cdd:PRK06018 296 LKMVVCGGSAMPRSMIKAFEDM--------------------GVE----------VRHAWGMT------------EMSPL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 436 GTVG-IPAVYNEI----RLEEVAEMGYDPLG-----------ENP-----AGEICIRGQCMFSGYYKnpELTEEVIKDGW 494
Cdd:PRK06018 334 GTLAaLKPPFSKLpgdaRLDVLQKQGYPPFGvemkitddagkELPwdgktFGRLKVRGPAVAAAYYR--VDGEILDDDGF 411
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2065806855 495 FHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEHLENI 535
Cdd:PRK06018 412 FDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLENL 451
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
66-535 |
6.39e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 84.37 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 66 IVDEKV-GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIV 144
Cdd:PRK07008 28 IVSRRVeGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 145 EHAEIDFVFVqDTKIKGLLEpdcKCAKRLKAIVSFTNVSDELSHKASEIGVKTYSWLdflhMGREKPEETNPP----KAF 220
Cdd:PRK07008 108 NHAEDRYVLF-DLTFLPLVD---ALAPQCPNVKGWVAMTDAAHLPAGSTPLLCYETL----VGAQDGDYDWPRfdenQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICtimYTSGTSGDPKGVVLTHQAVAtfvvgMDIFMDQFEDKM--THDDVYLSFLPLAHIldrmNEEYFFRKGASVGYY- 297
Cdd:PRK07008 180 SLC---YTSGTTGNPKGALYSHRSTV-----LHAYGAALPDAMglSARDAVLPVVPMFHV----NAWGLPYSAPLTGAKl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 298 -----HGDLNVLRDDIQELKPTYLAGVPRVFerihegiQKALQELNPrrrlifNALykhKLAWMNRGYSHSKASPMADFI 372
Cdd:PRK07008 248 vlpgpDLDGKSLYELIEAERVTFSAGVPTVW-------LGLLNHMRE------AGL---RFSTLRRTVIGGSACPPAMIR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 373 AFRkirDKLGGRirllvsggaplspeieeflrvtcccfVVQGYGLTE--------TLGGTALGFPDE--MCMLGTVGiPA 442
Cdd:PRK07008 312 TFE---DEYGVE--------------------------VIHAWGMTEmsplgtlcKLKWKHSQLPLDeqRKLLEKQG-RV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 443 VYNeIRLEEVAEMGYD-PLGENPAGEICIRGQCMFSGYYKNpelTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKl 521
Cdd:PRK07008 362 IYG-VDMKIVGDDGRElPWDGKAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIK- 436
|
490
....*....|....
gi 2065806855 522 SQGEYVALEHLENI 535
Cdd:PRK07008 437 SGGEWISSIDIENV 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-519 |
4.44e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 80.22 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHQAVATfvvgmDIFMDQFEDKMTHDDVYLSFLPLAHILDRMNEEYF-FRKGASV----- 294
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVY-----NAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVvlagp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 295 -GYYhgDLNVLRDD---IQELKPTYLAGVPRVferihegiqkalqelnprrrlifnalykhklawmnrgYSHSKASPM-A 369
Cdd:cd05944 78 aGYR--NPGLFDNFwklVERYRITSLSTVPTV-------------------------------------YAALLQVPVnA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 370 DFiafrkirdklgGRIRLLVSGGAPLSPE----IEEFLRVTcccfVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYN 445
Cdd:cd05944 119 DI-----------SSLRFAMSGAAPLPVElrarFEDATGLP----VVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYA 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 446 EIRLEEVAEMGYD--PLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:cd05944 184 RVRIKVLDGVGRLlrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI 259
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
30-566 |
4.86e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 81.34 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 30 SEKGFPPIDSeitTAWDIFSKSVEKFPDNNMLgwrrIVDEKvgpymWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGI 109
Cdd:PRK06155 12 AVDPLPPSER---TLPAMLARQAERYPDRPLL----VFGGT-----RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 110 NCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIKGL--LEPDCKCAKRLKAIvsftnvsDELS 187
Cdd:PRK06155 80 NRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaADPGDLPLPAVWLL-------DAPA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 188 HKASEIGVKT--YSWLDflhmgreKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHqavATFVVGMDIFMDQFEdkMTH 265
Cdd:PRK06155 153 SVSVPAGWSTapLPPLD-------APAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWWGRNSAEDLE--IGA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 266 DDVYLSFLPLAHI------------------LDRMNEEYFF----RKGASVGYYHGdlnvlrddiqELKPTYLAGVPRVF 323
Cdd:PRK06155 221 DDVLYTTLPLFHTnalnaffqallagatyvlEPRFSASGFWpavrRHGATVTYLLG----------AMVSILLSQPARES 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 324 ERIHegiqkalqelnprrRLifnalykhKLAWmnrgyshSKASPMADFIAFRKirdklggriRLlvsgGAPLspeieefl 403
Cdd:PRK06155 291 DRAH--------------RV--------RVAL-------GPGVPAALHAAFRE---------RF----GVDL-------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 404 rvtcccfvVQGYGLTETLGGTALGFPDEMCmlGTVGIPAVYNEIRleeVAEMGYDPLGENPAGEICIRGQ---CMFSGYY 480
Cdd:PRK06155 321 --------LDGYGSTETNFVIAVTHGSQRP--GSMGRLAPGFEAR---VVDEHDQELPDGEPGELLLRADepfAFATGYF 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 481 KNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYgdSFKSML---- 556
Cdd:PRK06155 388 GMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVF--PVPSELgede 464
|
570
....*....|.
gi 2065806855 557 -VAVVVPNPET 566
Cdd:PRK06155 465 vMAAVVLRDGT 475
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
46-587 |
5.02e-16 |
|
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: 80.82 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 46 DIFSKSVEKFPDNN--MLGWRRIvdekvgpymwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIA----ME 119
Cdd:cd17653 1 DAFERIAAAHPDAVavESLGGSL-----------TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAilaiLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 120 ACAAHtlicVPLYDTLGSGAVDYIVEHAEidfvfvqdtkikgllepdckcakrlKAIVSFTNVSDELSHkaseigvktys 199
Cdd:cd17653 70 AGAAY----VPLDAKLPSARIQAILRTSG-------------------------ATLLLTTDSPDDLAY----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 200 wldflhmgrekpeetnppkafnictIMYTSGTSGDPKGVVLTHQAVATFVvgmdifmDQFEDKM--THDDVYLSFLPLAh 277
Cdd:cd17653 110 -------------------------IIFTSGSTGIPKGVMVPHRGVLNYV-------SQPPARLdvGPGSRVAQVLSIA- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 278 iLDRMNEEYFfrkgaSVGYYHGDLnVLRDDiqelkPTYLAGVPRVFERIHeGIQKALQELNPRRrlifnalykhklawmn 357
Cdd:cd17653 157 -FDACIGEIF-----STLCNGGTL-VLADP-----SDPFAHVARTVDALM-STPSILSTLSPQD---------------- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 358 rgYShskaspmadfiafrkirdklggRIRLLVSGGAPLSPE-IEEFLRVTCccfVVQGYGLTETLGGTALG--FPDEMCm 434
Cdd:cd17653 208 --FP----------------------NLKTIFLGGEAVPPSlLDRWSPGRR---LYNAYGPTECTISSTMTelLPGQPV- 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 435 lgTVGIPAVYNEIRLEEVAEMgydPLGENPAGEICIRGQCMFSGYYKNPELT-EEVIKDGWFH------TGDIGEILPNG 507
Cdd:cd17653 260 --TIGKPIPNSTCYILDADLQ---PVPEGVVGEICISGVQVARGYLGNPALTaSKFVPDPFWPgsrmyrTGDYGRWTEDG 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 508 VLKIIDRKKNLIKLsQGEYVALEHLEN-IFGQNSVVQD--IWVYGDSfksmLVAVVVpnPETIN------RWAKDL-GFT 577
Cdd:cd17653 335 GLEFLGREDNQVKV-RGFRINLEEIEEvVLQSQPEVTQaaAIVVNGR----LVAFVT--PETVDvdglrsELAKHLpSYA 407
|
570
....*....|..
gi 2065806855 578 KP--FEELCSFP 587
Cdd:cd17653 408 VPdrIIALDSFP 419
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
78-549 |
5.94e-16 |
|
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: 80.62 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIdfvfvqdt 157
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kiKGLLepdckcakrlkaivsftnVSDELSHKaseigvktyswldflhMGREKPeetnppkafniCTIMYTSGTSGDPKG 237
Cdd:cd05969 74 --KVLI------------------TTEELYER----------------TDPEDP-----------TLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVVGMDIFMDQFEDKM---THD------DVYLSFLPLAHildrmneeyffrkGASVGYYHGDLNVLR--D 306
Cdd:cd05969 107 VLHVHDAMIFYYFTGKYVLDLHPDDIywcTADpgwvtgTVYGIWAPWLN-------------GVTNVVYEGRFDAESwyG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 307 DIQELKPTYLAGVPRVFERI-HEGIQKAlqelnprrrlifnalykhklawmnRGYSHSKaspmadfiafrkirdklggrI 385
Cdd:cd05969 174 IIERVKVTVWYTAPTAIRMLmKEGDELA------------------------RKYDLSS--------------------L 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 RLLVSGGAPLSPEI----EEFLRVTcccfVVQGYGLTETLGGTALGFPDEMCMLGTVG--IPAVYNEIrleeVAEMGyDP 459
Cdd:cd05969 210 RFIHSVGEPLNPEAirwgMEVFGVP----IHDTWWQTETGSIMIANYPCMPIKPGSMGkpLPGVKAAV----VDENG-NE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 460 LGENPAGEICIRGQ--CMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFG 537
Cdd:cd05969 281 LPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALM 359
|
490
....*....|..
gi 2065806855 538 QNSVVQDIWVYG 549
Cdd:cd05969 360 EHPAVAEAGVIG 371
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
221-638 |
7.22e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 81.00 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHQAVAT------FVVGMDifmdqfedkmtHDDVYLSFLPLAHIldrmneeyffrkgasv 294
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVqslakiAIVGYG-----------EDDVYLHTAPLCHI---------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 295 GYYHGDLNVLrddiqelkptyLAGVPRVFerihegiqkaLQELNPRrrLIFNALYKHKLAWMNrgyshSKASPMADFIAF 374
Cdd:PLN02860 226 GGLSSALAML-----------MVGACHVL----------LPKFDAK--AALQAIKQHNVTSMI-----TVPAMMADLISL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 375 --RKIRDKLGGRIRLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTE--------TLGGTALGFPDEMCMLGT------ 437
Cdd:PLN02860 278 trKSMTWKVFPSVRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEacssltfmTLHDPTLESPKQTLQTVNqtksss 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 438 --------VGIPAVYNEIRLeevaemGYDplGENPAGEICIRGQCMFSGYY-KNPELTEEVIKDGWFHTGDIGEILPNGV 508
Cdd:PLN02860 358 vhqpqgvcVGKPAPHVELKI------GLD--ESSRVGRILTRGPHVMLGYWgQNSETASVLSNDGWLDTGDIGWIDKAGN 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 509 LKIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYG--DS-FKSMLVAVVVPNPETInrWA-KDLGFTKPFEELC 584
Cdd:PLN02860 430 LWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGvpDSrLTEMVVACVRLRDGWI--WSdNEKENAKKNLTLS 506
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2065806855 585 SfpelkehiiSELKSTAEKNKLRKFEYIKAVAVETKPFDverdlVTATLKNRRN 638
Cdd:PLN02860 507 S---------ETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRD 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
385-568 |
8.87e-16 |
|
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: 80.45 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETL-GGTALGFPDEMcMLGTVGIPAV-YNEIRLeeVAEMGyDPLGE 462
Cdd:cd05920 257 LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLlNYTRLDDPDEV-IIHTQGRPMSpDDEIRV--VDEEG-NPVPP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 463 NPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSV 541
Cdd:cd05920 333 GEEGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPA 411
|
170 180 190
....*....|....*....|....*....|..
gi 2065806855 542 VQDIWVYG--DSF---KSmlVAVVVPNPETIN 568
Cdd:cd05920 412 VHDAAVVAmpDELlgeRS--CAFVVLRDPPPS 441
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
72-519 |
1.27e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 79.84 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 72 GPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLydtlgsgAVDYIVEHaEIDF 151
Cdd:cd05908 11 KKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV-------SIGSNEEH-KLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 VFVQDTKIKGLLEPDCKCAKRLKaivsftnvsDELshkaseigvktyswldflhmgrekpeetnppkAFnictIMYTSGT 231
Cdd:cd05908 83 NKVWNTLKNPYLITEEEVLCELA---------DEL--------------------------------AF----IQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTHQavaTFVVGMDIFMDQFEdkMTHDDVYLSFLPLAHILdrmneeyffrkGASVGYyhgdlnvlrddiqeL 311
Cdd:cd05908 118 TGDPKGVMLTHE---NLVHNMFAILNSTE--WKTKDRILSWMPLTHDM-----------GLIAFH--------------L 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 312 KPTYlagvprvferihEGIQkalQELNPRRRLIfnalyKHKLAWMNRGYSHSK---ASP------MADFIAFRKIRDKLG 382
Cdd:cd05908 168 APLI------------AGMN---QYLMPTRLFI-----RRPILWLKKASEHKAtivSSPnfgykyFLKTLKPEKANDWDL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 383 GRIRLLVSGGAPLSPE-IEEF--------LRVTCCCFVvqgYGLTE-----------------TLG--GTALGFPDEM-- 432
Cdd:cd05908 228 SSIRMILNGAEPIDYElCHEFldhmskygLKRNAILPV---YGLAEasvgaslpkaqspfktiTLGrrHVTHGEPEPEvd 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 433 -----CM-LGTVGIPAVYNEIRLEEVAEMGydpLGENPAGEICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEILp 505
Cdd:cd05908 305 kkdseCLtFVEVGKPIDETDIRICDEDNKI---LPDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR- 380
|
490
....*....|....
gi 2065806855 506 NGVLKIIDRKKNLI 519
Cdd:cd05908 381 NGRLVITGREKDII 394
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
78-521 |
2.53e-15 |
|
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: 80.29 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEAC----AAhtliCVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVlkagAA----YVPLDPAYPAERLAYMLEDAGARLVL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQDtkikgllepdckcakrlkaivsftnvsdELSHKASEIGVKTYSwLDFLHMGREkpEETNPPKAF---NICTIMYTSG 230
Cdd:COG1020 579 TQS----------------------------ALAARLPELGVPVLA-LDALALAAE--PATNPPVPVtpdDLAYVIYTSG 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGVVLTHQAVATFVVGMdifMDQFEdkMTHDDVYLS-------------FLPLAHildrmneeyffrkGASVgyy 297
Cdd:COG1020 628 STGRPKGVMVEHRALVNLLAWM---QRRYG--LGPGDRVLQfaslsfdasvweiFGALLS-------------GATL--- 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 298 hgdlnVLRDDIQELKPTYLAgvprvfERIHEgiqkalqelnprrrlifnalykhklawmnRGYSHSKASPMAdFIAFRKI 377
Cdd:COG1020 687 -----VLAPPEARRDPAALA------ELLAR-----------------------------HRVTVLNLTPSL-LRALLDA 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 378 RDKLGGRIRLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTE-TLGGTALGFPDEMCMLGTVGI--P----AVY--NEi 447
Cdd:COG1020 726 APEALPSLRLVLVGGEALPPElVRRWRARLPGARLVNLYGPTEtTVDSTYYEVTPPDADGGSVPIgrPiantRVYvlDA- 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 448 RLEEVaemgydPLGEnpAGEICIRGQCMFSGYYKNPELTEE------VIKDG--WFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:COG1020 805 HLQPV------PVGV--PGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQV 876
|
..
gi 2065806855 520 KL 521
Cdd:COG1020 877 KI 878
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
78-591 |
3.26e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 79.12 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPqwiiAM-EA-----CAAHTLICVPLydTLGSGAVDYIVEHAEIDF 151
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP----AMyEAhfgvpMAGAVVNCVNI--RLNAPTIAFLLEHSKSEV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 152 VFVQ-------DTKIKGLLEPDCKCAKRLKAIVSFTNVSDELSHKASeIGVKTYSWLDFLHMGreKPE-ETNPPK-AFNI 222
Cdd:PLN02479 121 VMVDqefftlaEEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYA-LGKGAIEYEKFLETG--DPEfAWKPPAdEWQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 223 CTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAH---------ILDRMNEEYFFRKGAS 293
Cdd:PLN02479 198 IALGYTSGTTASPKGVVLHHRGAYLMALSNALIWG-----MNEGAVYLWTLPMFHcngwcftwtLAALCGTNICLRQVTA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 294 VGYYHGdlnvlrddIQELKPTYLAGVPRVFErihegiqkalqelnprrrLIFNAlykhklawmnrgyshskasPMADFIA 373
Cdd:PLN02479 273 KAIYSA--------IANYGVTHFCAAPVVLN------------------TIVNA-------------------PKSETIL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 374 frkirdKLGGRIRLLVSGGAP----LSPEIEEFLRVTcccfvvQGYGLTETLGgtalgfPDEMCmlgtvGIPAVYNEIRL 449
Cdd:PLN02479 308 ------PLPRVVHVMTAGAAPppsvLFAMSEKGFRVT------HTYGLSETYG------PSTVC-----AWKPEWDSLPP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 450 EEVAEM------------GYD----------PLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNG 507
Cdd:PLN02479 365 EEQARLnarqgvryigleGLDvvdtktmkpvPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDG 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 508 VLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVqdiwvygdsfksmLVAVVVPNPEtiNRWAkdlgftkpfEELCSFP 587
Cdd:PLN02479 445 YIEIKDRSKDII-ISGGENISSLEVENVVYTHPAV-------------LEASVVARPD--ERWG---------ESPCAFV 499
|
....
gi 2065806855 588 ELKE 591
Cdd:PLN02479 500 TLKP 503
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
91-534 |
3.96e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 78.25 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 91 SALRAVGAEPGCRVGIYGINCPQWI-----IAMEACAAhTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDTKIKGLlep 165
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTYIelsfaVAYAGGRL-GLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 166 dckcakRLKAIVSFtnvSDELSHKASEIgvktyswldflhMGREKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQ-- 243
Cdd:cd05922 84 ------RDALPASP---DPGTVLDADGI------------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQnl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 244 -----AVATFVvgmdifmdqfedKMTHDDVYLSFLPLAHI--LDRMNEEyfFRKGASV----GYYHGDLNVlrDDIQELK 312
Cdd:cd05922 143 lanarSIAEYL------------GITADDRALTVLPLSYDygLSVLNTH--LLRGATLvltnDGVLDDAFW--EDLREHG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 313 PTYLAGVPRVFERIhegiqkalqelnprRRLIFNALykhklawmnrGYSHskaspmadfiafrkirdklggrIRLLVSGG 392
Cdd:cd05922 207 ATGLAGVPSTYAML--------------TRLGFDPA----------KLPS----------------------LRYLTQAG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 393 APLSPE-IEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMC-MLGTVGIPAVYNEIRLEEVAEMgydPLGENPAGEICI 470
Cdd:cd05922 241 GRLPQEtIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILeKPGSIGLAIPGGEFEILDDDGT---PTPPGEPGEIVH 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065806855 471 RGQCMFSGYYKNP-ELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLEN 534
Cdd:cd05922 318 RGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
225-600 |
5.57e-15 |
|
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: 77.97 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATfvvGMDIFMDQFEdkMTHDDVYLSFlplahildrmneeyffrkgASvgyYHGDLNvl 304
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRALST---SALAHGRALG--LTSESRVLQF-------------------AS---YTFDVS-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rddIQELKPTYLAG----VPRVFERIhEGIQKALQELNPrrrlifnalykhklawmnrgySHSKASP-MADFIAFRKIRD 379
Cdd:cd05918 162 ---ILEIFTTLAAGgclcIPSEEDRL-NDLAGFINRLRV---------------------TWAFLTPsVARLLDPEDVPS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 380 klggrIRLLVSGGAPLSPE-IEEFL-RVTcccfVVQGYGLTETLGGTALGFPDEMCMLGTVG--IPAV------YNEIRL 449
Cdd:cd05918 217 -----LRTLVLGGEALTQSdVDTWAdRVR----LINAYGPAECTIAATVSPVVPSTDPRNIGrpLGATcwvvdpDNHDRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 450 EevaemgydPLGEnpAGEICIRGQCMFSGYYKNPELTEEV-IKD-GW------------FHTGDIGEILPNGVLKIIDRK 515
Cdd:cd05918 288 V--------PIGA--VGELLIEGPILARGYLNDPEKTAAAfIEDpAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 516 KNLIKLsQGEYVAL----EHLENIFGQNS--VVQDIWVYGDSFKSMLVAVVVPNPETINRWAKDLGFTKPFEElcsFPEL 589
Cdd:cd05918 358 DTQVKI-RGQRVELgeieHHLRQSLPGAKevVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDE---FRAL 433
|
410
....*....|.
gi 2065806855 590 KEHIISELKST 600
Cdd:cd05918 434 VAELRSKLRQR 444
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
78-254 |
8.62e-15 |
|
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: 77.92 E-value: 8.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQD- 156
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 -------TKIKGLLEPDCK-CAKRLKAIVSFTNVSDELSHKASEIgvktySWLDFLHMGREKPEETNPPkafNICTIMYT 228
Cdd:cd05968 173 ftrrgreVNLKEEADKACAqCPTVEKVVVVRHLGNDFTPAKGRDL-----SYDEEKETAGDGAERTESE---DPLMIIYT 244
|
170 180 190
....*....|....*....|....*....|.
gi 2065806855 229 SGTSGDPKGVVLTH-----QAVATFVVGMDI 254
Cdd:cd05968 245 SGTTGKPKGTVHVHagfplKAAQDMYFQFDL 275
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
56-621 |
9.96e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.78 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 56 PDNNMLGWRRIVDekvGPYMWKTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPL---Y 132
Cdd:PRK12582 63 PDRPWLAQREPGH---GQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 133 DTLGSG--AVDYIVEHAEIDFVFVQD-----TKIKGLLEPDCKC-----------AKRLKAIVSfTNVSDELSHKASEIG 194
Cdd:PRK12582 140 SLMSHDhaKLKHLFDLVKPRVVFAQSgapfaRALAALDLLDVTVvhvtgpgegiaSIAFADLAA-TPPTAAVAAAIAAIT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 195 VKTyswldflhmgrekpeetnppkafnICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfEDKMTHDDVYLSFLP 274
Cdd:PRK12582 219 PDT------------------------VAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRP--REPDPPPPVSLDWMP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 275 LAHILdrmneeyffrkGASVGYYhgdlNVLRDD----IQELKPtylagVPRVFeriHEGIqKALQELNPRrrLIFNAlyk 350
Cdd:PRK12582 273 WNHTM-----------GGNANFN----GLLWGGgtlyIDDGKP-----LPGMF---EETI-RNLREISPT--VYGNV--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 351 hklawmNRGYShSKASPMADFIAFRKirdKLGGRIRLLVSGGAPLSPEIEEFL-----RVTCCCFVV-QGYGLTETlGGT 424
Cdd:PRK12582 324 ------PAGYA-MLAEAMEKDDALRR---SFFKNLRLMAYGGATLSDDLYERMqalavRTTGHRIPFyTGYGATET-APT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 425 ALGFPDEMCMLGTVGIPAVYNEIRLEevaemgydplgenPAG---EICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDI 500
Cdd:PRK12582 393 TTGTHWDTERVGLIGLPLPGVELKLA-------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 501 GEIL-PNgvlkiiDRKKNLI---------KLSQGEYVALEHL--ENIFGQNSVVQDIWVYGDSfKSMLVAVVVPNPETIN 568
Cdd:PRK12582 460 ARFVdPD------DPEKGLIfdgrvaedfKLSTGTWVSVGTLrpDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACR 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 569 RWAKDLGFTkpFEELCSFPELKEHI---ISELKSTAEKNKLRkfeyIKAVAVETKP 621
Cdd:PRK12582 533 QLAGDPDAA--PEDVVKHPAVLAILregLSAHNAEAGGSSSR----IARALLMTEP 582
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
223-564 |
3.74e-14 |
|
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: 73.88 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 223 CTIMYTSGTSGDPKGVVLTHQAVATfvvgMDIFMDQFEDkMTHDDVYLSFLPLAHILDRMneeyffrkgASVGYYH-GDL 301
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLA----QALVLAVLQA-IDEGTVFLNSGPLFHIGTLM---------FTLATFHaGGT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 302 NVL--RDDIQEL-------KPTYLAGVPRVFERIHEgiqkalqeLNPRRRLIFNALykhklawmnRGYSHSKASPMadfi 372
Cdd:cd17636 69 NVFvrRVDAEEVlelieaeRCTHAFLLPPTIDQIVE--------LNADGLYDLSSL---------RSSPAAPEWND---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 373 afrkirdklggrirllvsggaPLSPEIEEFLRVtcccfvVQGYGLTETLGGT---ALGFPDemcmLGTVGIPAVYNEIRL 449
Cdd:cd17636 128 ---------------------MATVDTSPWGRK------PGGYGQTEVMGLAtfaALGGGA----IGGAGRPSPLVQVRI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 450 eeVAEMGYD-PLGEnpAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVA 528
Cdd:cd17636 177 --LDEDGREvPDGE--VGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIY 251
|
330 340 350
....*....|....*....|....*....|....*....
gi 2065806855 529 LEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP 564
Cdd:cd17636 252 PAEVERCLRQHPAVADAAVIGvpdPRWAQSVKAIVVLKP 290
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
200-547 |
9.83e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 73.75 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 200 WLDFLHMGREKPEETNPPKAFN---ICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqFEDkmtHDDVYLSfLPLA 276
Cdd:PRK09029 112 TFSALTSLHLQLVEGAHAVAWQpqrLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMP-FTA---QDSWLLS-LPLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 277 H-----ILDRmneeyFFRKGASVgyYHGDLNVLRDDIQ-----ELKPTYLagvprvferihegiqkalqelnprRRLIfn 346
Cdd:PRK09029 187 HvsgqgIVWR-----WLYAGATL--VVRDKQPLEQALAgcthaSLVPTQL------------------------WRLL-- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 347 alykhklawmnrgysHSKASPMAdfiaFRKIrdklggrirLLvsGGAPLSPEIEEFLR---VTCCCfvvqGYGLTEtLGG 423
Cdd:PRK09029 234 ---------------DNRSEPLS----LKAV---------LL--GGAAIPVELTEQAEqqgIRCWC----GYGLTE-MAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 424 T-----ALGFPDemcmlgtVGIPAVYNEIRLEEvaemgydplgenpaGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTG 498
Cdd:PRK09029 279 TvcakrADGLAG-------VGSPLPGREVKLVD--------------GEIWLRGASLALGYWRQGQLVPLVNDEGWFATR 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2065806855 499 DIGEILpNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWV 547
Cdd:PRK09029 338 DRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
78-566 |
1.30e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 73.91 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVgAEPGCR--VGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVfVQ 155
Cdd:PRK13388 28 TWREVLAEAAARAAALIAL-ADPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLL-VT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 DTKIKGLLE----PDckcakrlkaiVSFTNVSDElshkaseigvktySWLDFLHM-GREKPEEtnPPKAFNICTIMYTSG 230
Cdd:PRK13388 106 DAEHRPLLDgldlPG----------VRVLDVDTP-------------AYAELVAAaGALTPHR--EVDAMDPFMLIFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGVVLTHQAVATFVVGMdifMDQFEdkMTHDDV-YLSfLPLAHILDRMneeyffrKGASVGYYHGDLNVLR---- 305
Cdd:PRK13388 161 TTGAPKAVRCSHGRLAFAGRAL---TERFG--LTRDDVcYVS-MPLFHSNAVM-------AGWAPAVASGAAVALPakfs 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 -----DDIQELKPTYLAGVPRVFERIHEGIQKALQELNPRRRLIFNalykhklawmnrgyshsKASPmadfiafrkiRDk 380
Cdd:PRK13388 228 asgflDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGN-----------------EASP----------RD- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 381 lggrirllvsggaplspeIEEFLRvTCCCFVVQGYGLTETlGGTALgfPDEMCMLGTVGIPA----VYNEIRLEEVAEMG 456
Cdd:PRK13388 280 ------------------IAEFSR-RFGCQVEDGYGSSEG-AVIVV--REPGTPPGSIGRGApgvaIYNPETLTECAVAR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 457 YDPLGE--NPA---GEICIR-GQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALE 530
Cdd:PRK13388 338 FDAHGAllNADeaiGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVD-GENLSAA 416
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2065806855 531 HLENIFGQNSVVQDIWVY-------GDsfkSMLVAVVVPNPET 566
Cdd:PRK13388 417 PIERILLRHPAINRVAVYavpdervGD---QVMAALVLRDGAT 456
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
225-562 |
1.90e-13 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 72.79 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATFVvgmDIFMDQFEdkMTHDDVYLSFLPLAhiLDRMNEEYF--FRKGASVgyyhgdln 302
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHC---QATAERYG--LTPGDRELQFASFN--FDGAHEQLLppLICGACV-------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 303 VLRDDIQELKPTYLAgvprvfERIHEGIQKALQelnprrrliFNALYKHKLA-WMNRGYSHSKASpmadfiafrkirdkl 381
Cdd:cd17649 164 VLRPDELWASADELA------EMVRELGVTVLD---------LPPAYLQQLAeEADRTGDGRPPS--------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 382 ggrIRLLVSGGAPLSPEieeFLRVTCCCFV--VQGYGLTETLgGTALGF---PDEMCMLGTVGIPAVyneIRLEEVAEMG 456
Cdd:cd17649 214 ---LRLYIFGGEALSPE---LLRRWLKAPVrlFNAYGPTEAT-VTPLVWkceAGAARAGASMPIGRP---LGGRSAYILD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 457 YD--PLGENPAGEICIRGQCMFSGYYKNPELT-EEVIKDG-------WFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEY 526
Cdd:cd17649 284 ADlnPVPVGVTGELYIGGEGLARGYLGRPELTaERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFR 362
|
330 340 350
....*....|....*....|....*....|....*....
gi 2065806855 527 VALEHLENIFGQNSVVQDIWVY---GDSFKSmLVAVVVP 562
Cdd:cd17649 363 IELGEIEAALLEHPGVREAAVValdGAGGKQ-LVAYVVL 400
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
385-522 |
2.04e-13 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 73.30 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTAlGFPdemCML---GTVGIPAVYNEIRLEEvAEMGYDPLG 461
Cdd:cd05970 303 LRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIA-TFP---WMEpkpGSMGKPAPGYEIDLID-REGRSCEAG 377
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 462 ENpaGEICIRGQ-----CMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
Cdd:cd05970 378 EE--GEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
225-539 |
2.29e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 72.93 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHqavATFVVGMDIFMDQFEDKmtHDDVYLSFLPLAHildrmneEYFFRKGAsvgyyhgdlnvl 304
Cdd:PRK06334 188 ILFTSGTEKLPKGVPLTH---ANLLANQRACLKFFSPK--EDDVMMSFLPPFH-------AYGFNSCT------------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rddiqeLKPTyLAGVPRVFerihegiqkALQELNPRRrlIFNALYKHKLAWMNrgyshskASPM-ADFI--AFRKIRDKL 381
Cdd:PRK06334 244 ------LFPL-LSGVPVVF---------AYNPLYPKK--IVEMIDEAKVTFLG-------STPVfFDYIlkTAKKQESCL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 382 GGrIRLLVSGGAPLSPEI-EEFLRVTCCCFVVQGYGLTE---TLGGTALGFP-DEMCmlgtVGIPAVYNEIRLeeVAEMG 456
Cdd:PRK06334 299 PS-LRFVVIGGDAFKDSLyQEALKTFPHIQLRQGYGTTEcspVITINTVNSPkHESC----VGMPIRGMDVLI--VSEET 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 457 YDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLEN 534
Cdd:PRK06334 372 KVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALES 450
|
....*....
gi 2065806855 535 I----FGQN 539
Cdd:PRK06334 451 IlmegFGQN 459
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
78-500 |
3.87e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.41 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVgAEPG--CRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVq 155
Cdd:PRK07867 30 SWREHIRGSAARAAALRAR-LDPTrpPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 DTKIKGLLepdckcakrlkaivsftnvsDELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDP 235
Cdd:PRK07867 108 ESAHAELL--------------------DGLDPGVRVINVDSPAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVVLTHQAVATFVVGMdifMDQFEdkMTHDDV-YLSfLPLAHILDRMneeyffrKGASVGYYHGDLNVLRddiqelkpt 314
Cdd:PRK07867 168 KAVRCTHRKVASAGVML---AQRFG--LGPDDVcYVS-MPLFHSNAVM-------AGWAVALAAGASIALR--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 315 ylagvpRVFErihegiqkALQELNPRRRliFNALYKHklaWMNRGYSHSKASPMADFIAFRKIRDKLGGRirllvsgGAP 394
Cdd:PRK07867 226 ------RKFS--------ASGFLPDVRR--YGATYAN---YVGKPLSYVLATPERPDDADNPLRIVYGNE-------GAP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 lsPEIEEFLRvTCCCFVVQGYGLTEtlGGTAL----GFPDemcmlGTVGIP----AVYNEIRLEEVAEMGYDPLGENPA- 465
Cdd:PRK07867 280 --GDIARFAR-RFGCVVVDGFGSTE--GGVAItrtpDTPP-----GALGPLppgvAIVDPDTGTECPPAEDADGRLLNAd 349
|
410 420 430
....*....|....*....|....*....|....*....
gi 2065806855 466 ---GEIC-IRGQCMFSGYYKNPELTEEVIKDGWFHTGDI 500
Cdd:PRK07867 350 eaiGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDL 388
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
78-565 |
1.91e-12 |
|
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: 69.92 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAM----EACAAHtlicVPLYDTLGSGAVDYIVEhaeidfvf 153
Cdd:cd12117 24 TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALlavlKAGAAY----VPLDPELPAERLAFMLA-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 vqDTKIKGLLepdckcakrlkaivsftnvsdelSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAF---NICTIMYTSG 230
Cdd:cd12117 92 --DAGAKVLL-----------------------TDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVspdDLAYVMYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGVVLTHQAVATFVVGMDiFMDqfedkMTHDDVYLSFLPLAhiLDRMNEEYF--FRKGAS-VGYYHG---DLNVL 304
Cdd:cd12117 147 STGRPKGVAVTHRGVVRLVKNTN-YVT-----LGPDDRVLQTSPLA--FDASTFEIWgaLLNGARlVLAPKGtllDPDAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 RDDIQELKPTYL---AGVprvferihegiqkalqelnprrrliFNALykhklawmnrgyshskaspmADFIAfrkirDKL 381
Cdd:cd12117 219 GALIAEEGVTVLwltAAL-------------------------FNQL--------------------ADEDP-----ECF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 382 GGrIRLLVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTE-TLGGTALGFPDEMCMLGTV--GIP----AVYNEIRLEEVA 453
Cdd:cd12117 249 AG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTEnTTFTTSHVVTELDEVAGSIpiGRPiantRVYVLDEDGRPV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 454 emgydPLGEnpAGEICIRGQCMFSGYYKNPELTEEV-IKDGW------FHTGDIGEILPNGVLKIIDRKKNLIKLsQGEY 526
Cdd:cd12117 328 -----PPGV--PGELYVGGDGLALGYLNRPALTAERfVADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFR 399
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2065806855 527 VALEHLENIFGQNSVVQDIWVY---GDSFKSMLVAVVVPNPE 565
Cdd:cd12117 400 IELGEIEAALRAHPGVREAVVVvreDAGGDKRLVAYVVAEGA 441
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
79-535 |
6.73e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.50 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 79 YKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVfvqdtk 158
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAA------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 159 ikgLLEPDCKCAkrlkaivsfTNVSDELSHKASEIGVKTYSWL-DFLHMGREKPEETNPPK-AFNICTIMYTSGTSGDPK 236
Cdd:PRK05857 118 ---LVAPGSKMA---------SSAVPEALHSIPVIAVDIAAVTrESEHSLDAASLAGNADQgSEDPLAMIFTSGTTGEPK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVVLTHQavaTFVVGMDIFMDQ---FEDKMTHDDVYlSFLPLAHIldrmneeyffrkgasvGYYHGDLNVLrddiqelkp 313
Cdd:PRK05857 186 AVLLANR---TFFAVPDILQKEglnWVTWVVGETTY-SPLPATHI----------------GGLWWILTCL--------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 314 tylagvprvferIHEG--IQKALQELNPRRRLIFNALYKHKLAwmnrgyshskASPMADFIAFRKIRDKLGGRIRLLVSG 391
Cdd:PRK05857 237 ------------MHGGlcVTGGENTTSLLEILTTNAVATTCLV----------PTLLSKLVSELKSANATVPSLRLVGYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 392 GAPLSPEIEEFLRVTCCcFVVQGYGLTETlGGTALGFPDEMCML-----GTVGIPavYNEIRLEEVAEMGYDPLGENPA- 465
Cdd:PRK05857 295 GSRAIAADVRFIEATGV-RTAQVYGLSET-GCTALCLPTDDGSIvkieaGAVGRP--YPGVDVYLAATDGIGPTAPGAGp 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065806855 466 ----GEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENI 535
Cdd:PRK05857 371 sasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI 443
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-642 |
7.13e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 68.23 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWI-IAMEACAAHTLICVpLYDTLGSGAVDYIVEHAEIDFVFVqD 156
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLeAYFAVPGMGAVLHT-ANPRLSPKEIAYILNHAEDKVLLF-D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 TKIKGLLEpdckcakrlKAIVSFTNVSDELSHKAseigvKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTSGDPK 236
Cdd:cd05915 104 PNLLPLVE---------AIRGELKTVQHFVVMDE-----KAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVVLTHQAVATFVVGMDIFMDQFEDKMThddVYLSFLPLAHILDRMneeYFFrkgaSVGYYHGDLNVLRDDIQElkptyl 316
Cdd:cd05915 170 GVVYSHRALVLHSLAASLVDGTALSEKD---VVLPVVPMFHVNAWC---LPY----AATLVGAKQVLPGPRLDP------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 317 agvprvferihegiqkalqelnprrRLIFNALYKHKLAwmNRGYShskaSPMADFIAFRK--IRDKLGGRIRLLVSGGAP 394
Cdd:cd05915 234 -------------------------ASLVELFDGEGVT--FTAGV----PTVWLALADYLesTGHRLKTLRRLVVGGSAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 395 lsPEIEEFLRVTCCCFVVQGYGLTETLG-GTAL-------GFPDE--MCMLGTVGIPAVYNEIRLEEVAEMGYdPLGENP 464
Cdd:cd05915 283 --PRSLIARFERMGVEVRQGYGLTETSPvVVQNfvkshleSLSEEekLTLKAKTGLPIPLVRLRVADEEGRPV-PKDGKA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 465 AGEICIRGQCMFSGYYKNPELTE-EVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIFGQNSVVQ 543
Cdd:cd05915 360 LGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 544 DiwvygdsfksmlvAVVVPNPEtinrwaKDLGftkpfEELCSFPELKEHIISElKSTAE--KNKLRKFEYIKAVAVETKp 621
Cdd:cd05915 439 E-------------AAVVAIPH------PKWQ-----ERPLAVVVPRGEKPTP-EELNEhlLKAGFAKWQLPDAYVFAE- 492
|
570 580
....*....|....*....|.
gi 2065806855 622 fDVERdlvTATLKNRRNNLLK 642
Cdd:cd05915 493 -EIPR---TSAGKFLKRALRE 509
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
78-574 |
1.28e-11 |
|
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: 67.73 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEAC----AAHTLIcvplydtLGSGAVDYI---VEHAEID 150
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACarigAIHSVV-------FGGFAAKELasrIDDAKPK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 151 FVFVQDTKI-------------KGLLEPDCKCAKRLkaIVSFTNVSDELSHKAseigvKTYSWLDFLHMGRekPEETNPP 217
Cdd:cd05967 157 LIVTASCGIepgkvvpykplldKALELSGHKPHHVL--VLNRPQVPADLTKPG-----RDLDWSELLAKAE--PVDCVPV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 218 KAFNICTIMYTSGTSGDPKGVVLTH--QAVAtFVVGMDIFMDqfedkMTHDDV--------------YLSFLPLAHildr 281
Cdd:cd05967 228 AATDPLYILYTSGTTGKPKGVVRDNggHAVA-LNWSMRNIYG-----IKPGDVwwaasdvgwvvghsYIVYGPLLH---- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 282 mneeyffrkGASVGYYHGdlnvlrddiqelKPTylaGVPR--VFERIHEgiqkalqelnprrrlifnalyKHKLAWMnrg 359
Cdd:cd05967 298 ---------GATTVLYEG------------KPV---GTPDpgAFWRVIE---------------------KYQVNAL--- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 360 YShskaSPMAdFIAFRK-------IRDKLGGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTET---LGGTALGFP 429
Cdd:cd05967 330 FT----APTA-IRAIRKedpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgwpITANPVGLE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 430 DEMCMLGTVGIPAV-YNeirLEEVAEMGyDPLGENPAGEICIRGQ----CMfSGYYKNPELTEEVI---KDGWFHTGDIG 501
Cdd:cd05967 405 PLPIKAGSPGKPVPgYQ---VQVLDEDG-EPVGPNELGNIVIKLPlppgCL-LTLWKNDERFKKLYlskFPGYYDTGDAG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 502 EILPNGVLKIIDRKKNLI-----KLSQGEyvalehLENIFGQNSVVQDIWVYG--DSFKSML-VAVVVPNpETINRWAKD 573
Cdd:cd05967 480 YKDEDGYLFIMGRTDDVInvaghRLSTGE------MEESVLSHPAVAECAVVGvrDELKGQVpLGLVVLK-EGVKITAEE 552
|
.
gi 2065806855 574 L 574
Cdd:cd05967 553 L 553
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
78-565 |
1.84e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.09 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMeaCAAHTLIC-VPLYDTLGSG-AVDYIVEHAEIDFVFVq 155
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEAL--LAANRIGAdILLLNTSFAGpALAEVVTREGVDTVIY- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 156 DTKIKGLLE---PDCKCAKRlkaIVSFTNVSDELSHKAseigvktyswLDFLHMGREKPEETNPPKafnicTIMYTSGTS 232
Cdd:PRK13382 147 DEEFSATVDralADCPQATR---IVAWTDEDHDLTVEV----------LIAAHAGQRPEPTGRKGR-----VILLTSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 233 GDPKGVvlTHQAVATFVVGMDIfMDQFedKMTHDDVYLSFLPLAH----------------ILDRMNeeyfFRKGASVgy 296
Cdd:PRK13382 209 GTPKGA--RRSGPGGIGTLKAI-LDRT--PWRAEEPTVIVAPMFHawgfsqlvlaaslactIVTRRR----FDPEATL-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 yhgdlnvlrDDIQELKPTYLAGVPRVFERIhegiqkalQELNPrrrlifnalykhklawmnrgyshskaspmadfiafrK 376
Cdd:PRK13382 278 ---------DLIDRHRATGLAVVPVMFDRI--------MDLPA------------------------------------E 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 377 IRDKLGGR-IRLLVSGGAPLSPEI-----EEFLRVtcccfVVQGYGLTETlGGTALGFPDEM-CMLGTVGIPAVYNEIRL 449
Cdd:PRK13382 305 VRNRYSGRsLRFAAASGSRMRPDVviafmDQFGDV-----IYNNYNATEA-GMIATATPADLrAAPDTAGRPAEGTEIRI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 450 --EEVAEMgydPLGEnpAGEICIRGQCMFSGYykNPELTEEVIkDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYV 527
Cdd:PRK13382 379 ldQDFREV---PTGE--VGTIFVRNDTQFDGY--TSGSTKDFH-DGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENV 449
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2065806855 528 ALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPE 565
Cdd:PRK13382 450 YPIEVEKTLATHPDVAEAAVIGvddEQYGQRLAAFVVLKPG 490
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
221-573 |
2.31e-11 |
|
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: 65.50 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHQA-VATFVVGMDIFMDQFEDKMthddvyLSFLPLAHILDRMNEEY-FFRKGASVGYYH 298
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDAI------LAPGPLSHSLFLYGAISaLYLGGTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 299 GDLNVLRDDIQELKPTYLAGVPRVFErihegiqkalqelnprrrlifnALYKHklawmnrGYSHSKaspmadfiafrkir 378
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQ----------------------ALART-------LEPESK-------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 379 dklggrIRLLVSGGAPLSPEIEEFLRVTcccF----VVQGYGLTETLGGTALgFPDEMCMLGTVGIPAVYNEIRLEEVae 454
Cdd:cd17633 112 ------IKSIFSSGQKLFESTKKKLKNI---FpkanLIEFYGTSELSFITYN-FNQESRPPNSVGRPFPNVEIEIRNA-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 455 mgydplGENPAGEICIRGQCMFSGYYKNPELTeeviKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLEN 534
Cdd:cd17633 180 ------DGGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2065806855 535 IFGQNSVVQDIWVYGDS---FKSMLVAVVV---PNPETINRWAKD 573
Cdd:cd17633 249 VLKAIPGIEEAIVVGIPdarFGEIAVALYSgdkLTYKQLKRFLKQ 293
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
79-519 |
2.43e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.57 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 79 YKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEhaeidfvfvqdtK 158
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIA------------Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 159 IKGLLEpDCKCAkrlkAIVsftnVSDELSHKASEI-----GVKTYSWLDFlHMGREKPEETNPPKAFNICTIMYTSGTSG 233
Cdd:PRK09192 120 LRGMLA-SAQPA----AII----TPDELLPWVNEAthgnpLLHVLSHAWF-KALPEADVALPRPTPDDIAYLQYSSGSTR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 234 DPKGVVLTHQAVATFVVGmdIFMDQFedKMTHDDVYLSFLPLAHilDrMneeyffrkgASVGYyhgdlnVLRDDIQELKP 313
Cdd:PRK09192 190 FPRGVIITHRALMANLRA--ISHDGL--KVRPGDRCVSWLPFYH--D-M---------GLVGF------LLTPVATQLSV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 314 TYLAgvPRVFERihegiqKALQELnprrrlifnalykhKLAWMNRGySHSKASPMADFIAFRKIRDK-LGG----RIRLL 388
Cdd:PRK09192 248 DYLP--TRDFAR------RPLQWL--------------DLISRNRG-TISYSPPFGYELCARRVNSKdLAEldlsCWRVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 389 VSGGAPLSPEI-EEFLRvtccCFVVQG---------YGLTE-TLggtALGFPDEMC----------MLGTVGI------- 440
Cdd:PRK09192 305 GIGADMIRPDVlHQFAE----AFAPAGfddkafmpsYGLAEaTL---AVSFSPLGSgivveevdrdRLEYQGKavapgae 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 441 PAVYNEI----------RLEEVAEMGyDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILpNGVLK 510
Cdd:PRK09192 378 TRRVRTFvncgkalpghEIEIRNEAG-MPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLY 455
|
....*....
gi 2065806855 511 IIDRKKNLI 519
Cdd:PRK09192 456 ITGRAKDLI 464
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
62-564 |
2.97e-11 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 66.30 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 62 GWRRIvdekvgpymwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWII----AMEACAAHTLICvPLYDTLGS 137
Cdd:cd05921 22 GWRRV-----------TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALmalaAMYAGVPAAPVS-PAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 138 --GAVDYIVEHAEIDFVFVQDTKikgllepdcKCAKRLKAIVSfTNVSDELSHKASEiGVKTYSWLDFLHMgrekPEETN 215
Cdd:cd05921 90 dlAKLKHLFELLKPGLVFAQDAA---------PFARALAAIFP-LGTPLVVSRNAVA-GRGAISFAELAAT----PPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 216 PPKAFN------ICTIMYTSGTSGDPKGVVLTHQAVATFVVGMdifMDQFEDKMTHDDVYLSFLPLAHILD-RMNEEYFF 288
Cdd:cd05921 155 VDAAFAavgpdtVAKFLFTSGSTGLPKAVINTQRMLCANQAML---EQTYPFFGEEPPVLVDWLPWNHTFGgNHNFNLVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 289 RKGASvgYY-------HGDLNVLRDDIQELKPTYLAGVPRVFERIHEGIQK--ALqelnpRRRLifnalykhklawmnrg 359
Cdd:cd05921 232 YNGGT--LYiddgkpmPGGFEETLRNLREISPTVYFNVPAGWEMLVAALEKdeAL-----RRRF---------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 360 yshskaspmadfiaFRkirdklggRIRLLVSGGAPLSPEIEEFL----------RVTcccfVVQGYGLTETlGGTALG-- 427
Cdd:cd05921 289 --------------FK--------RLKLMFYAGAGLSQDVWDRLqalavatvgeRIP----MMAGLGATET-APTATFth 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 428 FPDEMCmlGTVGIPAVYNEIRLEevaemgydplgenPAG---EICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGDIGEI 503
Cdd:cd05921 342 WPTERS--GLIGLPAPGTELKLV-------------PSGgkyEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAKL 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065806855 504 L----PNGVLKIIDRKKNLIKLSQGEYVALEHLEN--IFGQNSVVQDIWVYGDSfKSMLVAVVVPNP 564
Cdd:cd05921 407 AdpddPAKGLVFDGRVAEDFKLASGTWVSVGPLRAraVAACAPLVHDAVVAGED-RAEVGALVFPDL 472
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
78-565 |
7.57e-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: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQdt 157
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikglLEPDCKCAkrlkaIVSFTNVSDELSHKASEIGVKTYSWLDFLhmgrekpeetnppkAFnictIMYTSGTSGDPKG 237
Cdd:cd12114 92 -----GPDAQLDV-----AVFDVLILDLDALAAPAPPPPVDVAPDDL--------------AY----VIFTSGSTGTPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 238 VVLTHQAVATFVvgmdifmDQFEDKM--THDDVYLSFLPLAH---ILDrmneeyFF---RKGASVgyyhgdlnVLRDDIQ 309
Cdd:cd12114 144 VMISHRAALNTI-------LDINRRFavGPDDRVLALSSLSFdlsVYD------IFgalSAGATL--------VLPDEAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 310 ELKPTYLA------------GVPRVFERIHEgIQKALQELNPRRRLIFnalykhklawmnrgysHSkaspmADFIAF--- 374
Cdd:cd12114 203 RRDPAHWAelierhgvtlwnSVPALLEMLLD-VLEAAQALLPSLRLVL----------------LS-----GDWIPLdlp 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 375 RKIRdKLGGRIRLLVSGGAplspeieeflrvtcccfvvqgyglTETlggtalgfpdemcmlgtvGIPAVYNEIR--LEEV 452
Cdd:cd12114 261 ARLR-ALAPDARLISLGGA------------------------TEA------------------SIWSIYHPIDevPPDW 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 453 AEMGY------------DPLGEN-P---AGEICIRGQCMFSGYYKNPELTEE---VIKDG--WFHTGDIGEILPNGVLKI 511
Cdd:cd12114 298 RSIPYgrplanqryrvlDPRGRDcPdwvPGELWIGGRGVALGYLGDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEF 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 512 IDRKKNLIKLS-----QGEY-VALEHLENIfgQNSVVQdiwVYGDSFKSMLVAVVVPNPE 565
Cdd:cd12114 378 LGRRDGQVKVRgyrieLGEIeAALQAHPGV--ARAVVV---VLGDPGGKRLAAFVVPDND 432
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
385-535 |
8.86e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.37 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPE-----IEEF-LRVtcccfvVQGYGLTETLGGTALGFPdeM-CMLGTVG--IPAVynEIRLEEVAem 455
Cdd:PRK06814 909 LRYVFAGAEKVKEEtrqtwMEKFgIRI------LEGYGVTETAPVIALNTP--MhNKAGTVGrlLPGI--EYRLEPVP-- 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 456 gydplGENPAGEICIRGQCMFSGYYK--NPELTEEvIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLE 533
Cdd:PRK06814 977 -----GIDEGGRLFVRGPNVMLGYLRaeNPGVLEP-PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVE 1049
|
..
gi 2065806855 534 NI 535
Cdd:PRK06814 1050 EL 1051
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
23-242 |
9.07e-11 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 64.91 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 23 PVYRNLLSEKGFPPI----DSEITTAWDIFSKSVEKFPDNNMLGWRRivDEKVGPYMWkTYKEVYEEVLQIGSALRAVGA 98
Cdd:cd17634 30 QKVKNTSFAPGAPSIkwfeDATLNLAANALDRHLRENGDRTAIIYEG--DDTSQSRTI-SYRELHREVCRFAGTLLDLGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 99 EPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDtkikGLLEP----DCKCAKRLK 174
Cdd:cd17634 107 KKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD----GGVRAgrsvPLKKNVDDA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065806855 175 AIVSFTNVSDELSHK--ASEIGVKTYSWLDFLHMGREKP--EETNPPKAFNICTIMYTSGTSGDPKGVVLTH 242
Cdd:cd17634 183 LNPNVTSVEHVIVLKrtGSDIDWQEGRDLWWRDLIAKASpeHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
78-522 |
1.04e-10 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 64.29 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLyDtlgsgaVDYivehaeidfvfvqdt 157
Cdd:cd17651 22 TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL-D------PAY--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikgllePdckcAKRLKAIVSFTNVS-----DELSHKASEIGVKTYSWLDFLHMGREKPEETNPPKAFNICTIMYTSGTS 232
Cdd:cd17651 80 -------P----AERLAFMLADAGPVlvlthPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 233 GDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAhiLDrmneeyffrkgASVgyyhgdlnvlrddiQELK 312
Cdd:cd17651 149 GRPKGVVMPHRSLANLVAWQARASS-----LGPGARTLQFAGLG--FD-----------VSV--------------QEIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 313 PTYLAGvprvferihegiqKALQELNPRRRLIFNALykhkLAWMN-RGYSHSKA-SPMADFIAFRKIR-DKLGGRIRLLV 389
Cdd:cd17651 197 STLCAG-------------ATLVLPPEEVRTDPPAL----AAWLDeQRISRVFLpTVALRALAEHGRPlGVRLAALRYLL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 390 SGGAPLS--PEIEEFLRVTCCCFVVQGYGLTETLGGTAL---GFPDEMCMLGTVGIPAVYNEIRleeVAEMGYDPLGENP 464
Cdd:cd17651 260 TGGEQLVltEDLREFCAGLPGLRLHNHYGPTETHVVTALslpGDPAAWPAPPPIGRPIDNTRVY---VLDAALRPVPPGV 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065806855 465 AGEICIRGQCMFSGYYKNPELTEE-VIKDGW------FHTGDIGEILPNGVLKIIDRKKNLIKLS 522
Cdd:cd17651 337 PGELYIGGAGLARGYLNRPELTAErFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIR 401
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
459-593 |
1.37e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.15 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 459 PLGENpaGEICIRGQCMFSGYYKNPELTEEVIK--DGW--FHTGDIGeILPNGVLKIIDRKKNLIKLSqGEYVALEHLEN 534
Cdd:PRK04813 340 PDGEQ--GEIVISGPSVSKGYLNNPEKTAEAFFtfDGQpaYHTGDAG-YLEDGLLFYQGRIDFQIKLN-GYRIELEEIEQ 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065806855 535 IFGQNSVVQD---IWVYGDSFKSMLVAVVVPNPetiNRWAKDLGFTKPFEElcsfpELKEHI 593
Cdd:PRK04813 416 NLRQSSYVESavvVPYNKDHKVQYLIAYVVPKE---EDFEREFELTKAIKK-----ELKERL 469
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
78-564 |
1.62e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 63.99 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDt 157
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKG------LLEPDCKCAKRLKAIVSFTNVSDELSHKASEIGVKTYSwldfLHMGREKPEETNPPKAFNICTIMYT-SG 230
Cdd:PRK06164 116 GFKGidfaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFA----LPDPAPPAAAGERAADPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGV------VLTHQAVATFVVGMDifmdqfedkmtHDDVYLSFLPLAHIldrmneeyfFRKGASVGYYHGdlnvl 304
Cdd:PRK06164 192 TTSGPKLVlhrqatLLRHARAIARAYGYD-----------PGAVLLAALPFCGV---------FGFSTLLGALAG----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rddiqelkptylaGVPRVFERIHEGIQKAlqelnprrrlifNALYKHKLawmnrgySHSKASPMAdfiaFRKIRDKLGGR 384
Cdd:PRK06164 247 -------------GAPLVCEPVFDAARTA------------RALRRHRV-------THTFGNDEM----LRRILDTAGER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 ---IRLLVSGGAPLSPEIEEFLRVTCCC-FVVQG-YGLTETLGGTALG--FPDEMCMLGTVGIPAvYNEIRLEEVAEMGY 457
Cdd:PRK06164 291 adfPSARLFGFASFAPALGELAALARARgVPLTGlYGSSEVQALVALQpaTDPVSVRIEGGGRPA-SPEARVRARDPQDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 458 DPLGENPAGEICIRGQCMFSGYYKNPELTEEVIK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLENIF 536
Cdd:PRK06164 370 ALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHAL 448
|
490 500 510
....*....|....*....|....*....|
gi 2065806855 537 GQNSVVQDIWVYGDSF--KSMLVAVVVPNP 564
Cdd:PRK06164 449 EALPGVAAAQVVGATRdgKTVPVAFVIPTD 478
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
386-573 |
2.39e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 63.09 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 RLLVSGGAPLSPEIEEF-----LRVTCCcfvvqgYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLEevaemgydpL 460
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTETASQIATLKPDDF-LAGNNSSGQVLPHAQIT---------I 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 461 GENPAGEICIRGQCMFSGYYknPELTEeviKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNS 540
Cdd:PRK07445 297 PANQTGNITIQAQSLALGYY--PQILD---SQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATG 370
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2065806855 541 VVQDIWVYG--DS-FKSMLVAVVVPN-----PETINRWAKD 573
Cdd:PRK07445 371 LVQDVCVLGlpDPhWGEVVTAIYVPKdpsisLEELKTAIKD 411
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
62-499 |
4.27e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.59 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 62 GWRRIvdekvgpymwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWiiAMEACAAHTL---ICV--PLYDTLG 136
Cdd:PRK08180 66 GWRRL-----------TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEH--ALLALAAMYAgvpYAPvsPAYSLVS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 137 S--GAVDYIVEHAEIDFVFVQDTKikgllepdcKCAKRLKAIV-SFTNVsdeLSHKASEIGVKTYSWLDFLhmgrEKPEE 213
Cdd:PRK08180 133 QdfGKLRHVLELLTPGLVFADDGA---------AFARALAAVVpADVEV---VAVRGAVPGRAATPFAALL----ATPPT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 214 TNPPKAFN------ICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFEDKmthDDVYLSFLPLAHILdrmneeyf 287
Cdd:PRK08180 197 AAVDAAHAavgpdtIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEE---PPVLVDWLPWNHTF-------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 288 frkGAS--VGYyhgdlnVLRDD----IQELKPTylagvPrvfERIHEGIqKALQELNPRrrLIFNalykhklawMNRGYS 361
Cdd:PRK08180 266 ---GGNhnLGI------VLYNGgtlyIDDGKPT-----P---GGFDETL-RNLREISPT--VYFN---------VPKGWE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 362 HskaspMADfiAFRK---IRDKLGGRIRLLVSGGAPLSPEIEEFL----------RVTCCCfvvqGYGLTETlGGTAL-- 426
Cdd:PRK08180 317 M-----LVP--ALERdaaLRRRFFSRLKLLFYAGAALSQDVWDRLdrvaeatcgeRIRMMT----GLGMTET-APSATft 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065806855 427 GFPDEMcmLGTVGIPAVYNEIRLeeVaemgydplgenPAG---EICIRGQCMFSGYYKNPELTEEVI-KDGWFHTGD 499
Cdd:PRK08180 385 TGPLSR--AGNIGLPAPGCEVKL--V-----------PVGgklEVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
78-562 |
5.06e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.26 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAM----EACAAHtlicVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLlavlKAGGAY----VPLDPEYPQDRLAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQDTKIKGLLEPDckcakRLKAIVsFTNVSDELSHKAseigvktyswldflhmgrekpeETNPPKAF---NICTIMYTSG 230
Cdd:PRK12467 615 TQSHLLAQLPVPA-----GLRSLC-LDEPADLLCGYS----------------------GHNPEVALdpdNLAYVIYTSG 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAhiLDRMNEEYF--FRKGASV---GY-YHGDLNVL 304
Cdd:PRK12467 667 STGQPKGVAISHGALANYVCVI-----AERLQLAADDSMLMVSTFA--FDLGVTELFgaLASGATLhllPPdCARDAEAF 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 RDDIQELKPTYLAGVPRVFERIhegIQKALQEL-NPRRRLIFnalykhklawmnrgyshskaspmadfiafrkirdklGG 383
Cdd:PRK12467 740 AALMADQGVTVLKIVPSHLQAL---LQASRVALpRPQRALVC------------------------------------GG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 384 RIrLLVSGGAP---LSPEieeflrvtccCFVVQGYGLTETlggtalgfpdemcmlgTVGIpaVYNEIRLEEVaEMGYDPL 460
Cdd:PRK12467 781 EA-LQVDLLARvraLGPG----------ARLINHYGPTET----------------TVGV--STYELSDEER-DFGNVPI 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 461 GE--------------NPA-----GEICIRGQCMFSGYYKNPELTEEVI------KDG--WFHTGDIGEILPNGVLKIID 513
Cdd:PRK12467 831 GQplanlglyildhylNPVpvgvvGELYIGGAGLARGYHRRPALTAERFvpdpfgADGgrLYRTGDLARYRADGVIEYLG 910
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 514 RKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWV--YGDSFKSMLVAVVVP 562
Cdd:PRK12467 911 RMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQLVAYLVP 960
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-562 |
7.11e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIA----MEACAAHtlicVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVAllavLKAGGAY----VPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQdtkiKGLLEpdckcakRLKAIVSFTNVSdelshkaseigVKTYSWLdflhmgREKPEeTNPPKAF---NICTIMYTSG 230
Cdd:PRK12316 2106 TQ----RHLLE-------RLPLPAGVARLP-----------LDRDAEW------ADYPD-TAPAVQLageNLAYVIYTSG 2156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 231 TSGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAhiLDRMNEEYF--FRKGASVgyyhgdlnVLRDDI 308
Cdd:PRK12316 2157 STGLPKGVAVSHGALVAHCQAA-----GERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 309 QelkptYLAGvpRVFERIHE-GIQKAlqelnprrrlIFNALYKHKLAwmnrgySHSKaspmadfiafrkiRDKLGGRIRL 387
Cdd:PRK12316 2222 L-----WDPE--QLYDEMERhGVTIL----------DFPPVYLQQLA------EHAE-------------RDGRPPAVRV 2265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 388 LVSGGAPLSPE-IEEFLRVTCCCFVVQGYGLTETLGgTALGF---PDEMCMLGTVGIPAVYNEIRLEeVAEMGYDPLGEN 463
Cdd:PRK12316 2266 YCFGGEAVPAAsLRLAWEALRPVYLFNGYGPTEAVV-TPLLWkcrPQDPCGAAYVPIGRALGNRRAY-ILDADLNLLAPG 2343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 464 PAGEICIRGQCMFSGYYKNPELT-EEVIKDGW-------FHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENI 535
Cdd:PRK12316 2344 MAGELYLGGEGLARGYLNRPGLTaERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEAR 2422
|
490 500
....*....|....*....|....*....
gi 2065806855 536 FGQNSVVQDIWVYGDSFKS--MLVAVVVP 562
Cdd:PRK12316 2423 LQAHPAVREAVVVAQDGASgkQLVAYVVP 2451
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
78-521 |
8.03e-10 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 61.52 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIygincpqwiiAMEACAAhtLIcVPLYDTLGSGAVdyivehaeidfvFVQdt 157
Cdd:cd17646 25 TYRELDERANRLAHLLRARGVGPEDRVAV----------LLPRSAD--LV-VALLAVLKAGAA------------YLP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikglLEPDCKcAKRLKAIVS------FTNVSDELSHKASEIGVKTYSWLDFLHMGREKPEEtnPPKAFNICTIMYTSGT 231
Cdd:cd17646 78 -----LDPGYP-ADRLAYMLAdagpavVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV--PPRPDNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 232 SGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAhiLDRMNEEYF--FRKGASV------GyyHGDLNV 303
Cdd:cd17646 150 TGRPKGVMVTHAGIVNRLLWM-----QDEYPLGPGDRVLQKTPLS--FDVSVWELFwpLVAGARLvvarpgG--HRDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 304 LRDDIQELKPTYLAGVP---RVFerihegiqkaLQELNPRRRlifnalykhklawmnrgyshskASpmadfiafrkirdk 380
Cdd:cd17646 221 LAALIREHGVTTCHFVPsmlRVF----------LAEPAAGSC----------------------AS-------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 381 lggrIRLLVSGGAPLSPEI-EEFLRVTCCCFvVQGYGLTETlggtalgfpdemcmlgTVGIPAVyneiRLEEVAEMGYDP 459
Cdd:cd17646 255 ----LRRVFCSGEALPPELaARFLALPGAEL-HNLYGPTEA----------------AIDVTHW----PVRGPAETPSVP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 460 LGE--------------NP-----AGEICIRGQCMFSGYYKNPELTEEVIKDGWF-------HTGDIGEILPNGVLKIID 513
Cdd:cd17646 310 IGRpvpntrlyvlddalRPvpvgvPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLG 389
|
....*...
gi 2065806855 514 RKKNLIKL 521
Cdd:cd17646 390 RSDDQVKI 397
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
204-565 |
1.31e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 204 LHMGREKPEETNPPK---AFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAhiLD 280
Cdd:PRK12316 3177 LDRGDENYAEANPAIrtmPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG-----LGVGDRVLQFTTFS--FD 3249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 281 RMNEEYF--FRKGASVgyyhgdlnVLRDDIQELKPTYLAGVPR-----VFERIHEGIQKALQELNPRRRlifnalykhkl 353
Cdd:PRK12316 3250 VFVEELFwpLMSGARV--------VLAGPEDWRDPALLVELINsegvdVLHAYPSMLQAFLEEEDAHRC----------- 3310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 354 awmnrgyshskaspmadfiafrkirdklgGRIRLLVSGGAPLSPEIEEflRVTCCCFVVQGYGLTET-LGGTALGFPDEM 432
Cdd:PRK12316 3311 -----------------------------TSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEAtITVTHWQCVEEG 3359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 433 CMLGTVGIPAVYNEIRLeevAEMGYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWF-------HTGDIGEILP 505
Cdd:PRK12316 3360 KDAVPIGRPIANRACYI---LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlyRTGDLARYRA 3436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 506 NGVLKIIDRKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWVYGDSFKSmLVAVVVPNPE 565
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
214-568 |
1.34e-09 |
|
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: 60.91 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 214 TNPPkafNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAhiLDRMNEEYF--FRKG 291
Cdd:cd17644 103 TQPE---NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGL-----IKEYGITSSDRVLQFASIA--FDVAAEEIYvtLLSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 292 ASVgyyhgdlnVLRDDIQELKPTYLAGVPRvferihegiQKALQELNprrrliFNALYKHKlaWMNRGYSHSKASPMAdf 371
Cdd:cd17644 173 ATL--------VLRPEEMRSSLEDFVQYIQ---------QWQLTVLS------LPPAYWHL--LVLELLLSTIDLPSS-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 372 iafrkirdklggrIRLLVSGGAPLSPEIEEFLRVTCCCFV--VQGYGLTE-TLGGTA--LGFPDEMCMLG-TVGIP---- 441
Cdd:cd17644 226 -------------LRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEaTIAATVcrLTQLTERNITSvPIGRPiant 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 442 AVYneirleeVAEMGYDPLGENPAGEICIRGQCMFSGYYKNPELT-EEVIKDGWFH--------TGDIGEILPNGVLKII 512
Cdd:cd17644 293 QVY-------ILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTaEKFISHPFNSseserlykTGDLARYLPDGNIEYL 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065806855 513 DRKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWVY------GDSFksmLVAVVVPNPETIN 568
Cdd:cd17644 366 GRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVIvredqpGNKR---LVAYIVPHYEESP 423
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
78-615 |
2.21e-09 |
|
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: 60.18 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALR-AVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFvqd 156
Cdd:cd05958 12 TYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 157 tkikgllepdckCAKRLKAivsftnvSDElshkaseigvktyswldflhmgrekpeetnppkafnICTIMYTSGTSGDPK 236
Cdd:cd05958 89 ------------CAHALTA-------SDD------------------------------------ICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVVLTHQAV-ATFvvgmDIFMDQFEdKMTHDDVYLSFLPLAHILDRMNEEYF-FRKGASVGYYHGDL-NVLRDDIQELKP 313
Cdd:cd05958 114 ATMHFHRDPlASA----DRYAVNVL-RLREDDRFVGSPPLAFTFGLGGVLLFpFGVGASGVLLEEATpDLLLSAIARYKP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 314 TYLAGVPRVFERIHEGIQKALQELNPRRRLIfnalykhklawmnrgySHSKASPMADFIAFRKirdklggrirllvSGGA 393
Cdd:cd05958 189 TVLFTAPTAYRAMLAHPDAAGPDLSSLRKCV----------------SAGEALPAALHRAWKE-------------ATGI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 394 PLspeieeflrvtcccfvVQGYGLTETLGGTALGFPDEMcMLGTVGIPAVYNEIRLeeVAEMGYD-PLGEnpAGEICIRG 472
Cdd:cd05958 240 PI----------------IDGIGSTEMFHIFISARPGDA-RPGATGKPVPGYEAKV--VDDEGNPvPDGT--IGRLAVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 473 QcmfSGYYKNPELTEE-VIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEHLENIFGQNSVVQDIWVYG-- 549
Cdd:cd05958 299 P---TGCRYLADKRQRtYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECAVVGhp 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065806855 550 DSFKSMLV-AVVVPNPETInrwakdlgftkPFEELCSfpELKEHIiselkstaeKNKLRKFEYIKAV 615
Cdd:cd05958 375 DESRGVVVkAFVVLRPGVI-----------PGPVLAR--ELQDHA---------KAHIAPYKYPRAI 419
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
221-573 |
2.39e-09 |
|
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: 59.88 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHQAVATFVvgmDIFMDQFEdkMTHDDVYLSFlplahildrmneeyffrkgASVGYyhgD 300
Cdd:cd17645 105 DLAYVIYTSGSTGLPKGVMIEHHNLVNLC---EWHRPYFG--VTPADKSLVY-------------------ASFSF---D 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 301 LNVLrddiqELKPTYLAGVprvferihegiqkALQELNPRRRLIFNALykhklawmNRgYSHSKA-------SPMADfiA 373
Cdd:cd17645 158 ASAW-----EIFPHLTAGA-------------ALHVVPSERRLDLDAL--------ND-YFNQEGitisflpTGAAE--Q 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 374 FRKIRDKlggRIRLLVSGGAPLSPEIEEFLRVtcccfvVQGYGLTE-TLGGTALGFPDEMcmlGTVGIPAVYNEIRLEEV 452
Cdd:cd17645 209 FMQLDNQ---SLRVLLTGGDKLKKIERKGYKL------VNNYGPTEnTVVATSFEIDKPY---ANIPIGKPIDNTRVYIL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 453 AE-MGYDPLGenPAGEICIRGQCMFSGYYKNPELTEE-------VIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQG 524
Cdd:cd17645 277 DEaLQLQPIG--VAGELCIAGEGLARGYLNRPELTAEkfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RG 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 525 EYVALEHLENIFGQNSVVQDIWVY----GDSFKSMLVAVVVP---NPETINRWAKD 573
Cdd:cd17645 354 YRIEPGEIEPFLMNHPLIELAAVLakedADGRKYLVAYVTAPeeiPHEELREWLKN 409
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
225-564 |
2.70e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 60.09 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVV--LTHQAVATFVVGMDIFMDQFedKMTHDDVYLSFLPLAH------------------ILDRMNE 284
Cdd:PRK13391 159 MLYSSGTTGRPKGIKrpLPEQPPDTPLPLTAFLQRLW--GFRSDMVYLSPAPLYHsapqravmlvirlggtviVMEHFDA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 285 EYFFRKgasvgyyhgdlnvlrddIQELKPTYLAGVPRVFERIHegiqkalqelnprrrlifnalykhKLAWMNRG-YSHS 363
Cdd:PRK13391 237 EQYLAL-----------------IEEYGVTHTQLVPTMFSRML------------------------KLPEEVRDkYDLS 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 364 KaspmadfiafrkirdklggrIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAV 443
Cdd:PRK13391 276 S--------------------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 444 YN-EIRLEEVAEMgydPLGEnpAGEICIRGQCMFSgYYKNPELTEEVIKD--GWFHTGDIGEILPNGVLKIIDRKKNLIk 520
Cdd:PRK13391 336 GDlHILDDDGAEL---PPGE--PGTIWFEGGRPFE-YLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMI- 408
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2065806855 521 LSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP 564
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGvpnEDLGEEVKAVVQPVD 455
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
78-565 |
5.88e-09 |
|
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: 58.87 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIA----MEACAAHtlicVPLYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVAllavLKAGAAY----VPLDPAYPPERLRFILEDAQARLVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQdtkikgllepdckcakrlkaivsftnvSDELSHkaseigvktyswldflhmgrekpeetnppkafnictIMYTSGTSG 233
Cdd:cd12115 102 TD---------------------------PDDLAY------------------------------------VIYTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 234 DPKGVVLTHQAVATFvvgMDIFMDQF-EDKM---------THD-DVYLSFLPLAHildrmneeyffrkGASVgyyhgdln 302
Cdd:cd12115 119 RPKGVAIEHRNAAAF---LQWAAAAFsAEELagvlastsiCFDlSVFELFGPLAT-------------GGKV-------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 303 VLRDDIQELkptylagvprvferIHEGIQKALQELN--PrrrlifnalykhklawmnrgyshskaSPMADFIAfrkiRDK 380
Cdd:cd12115 175 VLADNVLAL--------------PDLPAAAEVTLINtvP--------------------------SAAAELLR----HDA 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 381 LGGRIRLLVSGGAPLSPE----IEEFLRVTCccfVVQGYGLTE-TLGGTALGFPDEMCMLGTVGIP----AVYneirlee 451
Cdd:cd12115 211 LPASVRVVNLAGEPLPRDlvqrLYARLQVER---VVNLYGPSEdTTYSTVAPVPPGASGEVSIGRPlantQAY------- 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 452 VAEMGYDPLGENPAGEICIRGQCMFSGYYKNPELTEEVIKDGWFH-------TGDIGEILPNGVLKIIDRKKNLIKL--- 521
Cdd:cd12115 281 VLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQVKVrgf 360
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2065806855 522 --SQGEyvaLEH-LENIFGQNSVVQDIWVYGDSFKSmLVAVVVPNPE 565
Cdd:cd12115 361 riELGE---IEAaLRSIPGVREAVVVAIGDAAGERR-LVAYIVAEPG 403
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
66-573 |
6.02e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 58.79 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 66 IVDEKvGPYmwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACA---AHTLicvpLYDTlGSGAVDy 142
Cdd:PRK07788 68 LIDER-GTL---TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGkvgARII----LLNT-GFSGPQ- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 143 IVEHAE---IDFVFVQD--TKIKGLLEPDckcAKRLKAIVSFTnvsDELSHKASEIGVktyswLDFLHMGREKPEETNPP 217
Cdd:PRK07788 138 LAEVAAregVKALVYDDefTDLLSALPPD---LGRLRAWGGNP---DDDEPSGSTDET-----LDDLIAGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 218 KAFNIctIMYTSGTSGDPKGVVLTHQavatfvvgmdifmdqfedkmthddvyLSFLPLAHILDR----MNEEY------F 287
Cdd:PRK07788 207 KPGGI--VILTSGTTGTPKGAPRPEP--------------------------SPLAPLAGLLSRvpfrAGETTllpapmF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 288 FRKG---ASVGYYHGDLNVLR---------DDIQELKPTYLAGVPRVFERIHEGIQKALQelnprrrlifnalykhklaw 355
Cdd:PRK07788 259 HATGwahLTLAMALGSTVVLRrrfdpeatlEDIAKHKATALVVVPVMLSRILDLGPEVLA-------------------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 356 mnrGYSHSkaspmadfiafrkirdklggRIRLLVSGGAPLSPEI-----EEFLRVTCccfvvQGYGLTETLGGTALGfPD 430
Cdd:PRK07788 319 ---KYDTS--------------------SLKIIFVSGSALSPELatralEAFGPVLY-----NLYGSTEVAFATIAT-PE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 431 EMCML-GTVGIPAVYNEIRLeevaemgYD----PLGENPAGEICIRGQCMFSGYY--KNPElteevIKDGWFHTGDIGEI 503
Cdd:PRK07788 370 DLAEApGTVGRPPKGVTVKI-------LDengnEVPRGVVGRIFVGNGFPFEGYTdgRDKQ-----IIDGLLSSGDVGYF 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 504 LPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP------ETINRWAKD 573
Cdd:PRK07788 438 DEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIGvddEEFGQRLRAFVVKAPgaaldeDAIKDYVRD 515
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
39-612 |
7.83e-09 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 58.63 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 39 SEITTAWDIFSKSVEKfPDNNMLGWrriVDEKVGPYMWkTYKEVYEEVLQIGSALR-AVGAEPGCRVGIYGINCPQWIIA 117
Cdd:cd05928 9 SDVLDQWADKEKAGKR-PPNPALWW---VNGKGDEVKW-SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 118 MEACAAHTLICVPLYDTLGSGAVDYivehaeidfvFVQDTKIKGLLEPDcKCAKRLKAIVS-FTNVSDEL--SHKASEig 194
Cdd:cd05928 84 NVACIRTGLVFIPGTIQLTAKDILY----------RLQASKAKCIVTSD-ELAPEVDSVASeCPSLKTKLlvSEKSRD-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 195 vktySWLDFLHMGREKPEETN--PPKAFNICTIMYTSGTSGDPKGVVLTHQAVAT-FVVGMDIFMDqfedkMTHDDVYLS 271
Cdd:cd05928 151 ----GWLNFKELLNEASTEHHcvETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLgLKVNGRYWLD-----LTASDIMWN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 272 FLPLAHILDRMNEEYF-FRKGASVGYYH---GDLNVLRDDIQELKPTYLAGVPRVFerihegiqkalqelnprRRLIFNA 347
Cdd:cd05928 222 TSDTGWIKSAWSSLFEpWIQGACVFVHHlprFDPLVILKTLSSYPITTFCGAPTVY-----------------RMLVQQD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 348 LYKHKLAwmnrgyshskaspmadfiafrkirdklggRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETlGGTALG 427
Cdd:cd05928 285 LSSYKFP-----------------------------SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTET-GLICAN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 428 FPDEMCMLGTVGIPAVYNEIRLeeVAEMGyDPLGENPAGEICIRGQ-----CMFSGYYKNPELTEEVIKDGWFHTGDIGE 502
Cdd:cd05928 335 FKGMKIKPGSMGKASPPYDVQI--IDDNG-NVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGI 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 503 ILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVVQDIWVYG--DSFKSMLV-AVVVPNPETINRWAKDLgfTKp 579
Cdd:cd05928 412 MDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVESAVVSspDPIRGEVVkAFVVLAPQFLSHDPEQL--TK- 487
|
570 580 590
....*....|....*....|....*....|...
gi 2065806855 580 feelcsfpELKEHIISelkSTAEKNKLRKFEYI 612
Cdd:cd05928 488 --------ELQQHVKS---VTAPYKYPRKVEFV 509
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
222-566 |
9.26e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 57.75 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 222 ICTIMYTSGTSGDPKGVVLThqaVATFVVGMDifmdqfedkMTHDDV-----YLSFLPLAHIldrmneeyffrkgasvgy 296
Cdd:PRK07824 37 VALVVATSGTTGTPKGAMLT---AAALTASAD---------ATHDRLggpgqWLLALPAHHI------------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 297 yhGDLNVL-RDDIQELKPTYLaGVPRVFERihEGIQKALQELNPRRRliFNALYKHKLAwmnrgyshsKAspMADFIAFR 375
Cdd:PRK07824 87 --AGLQVLvRSVIAGSEPVEL-DVSAGFDP--TALPRAVAELGGGRR--YTSLVPMQLA---------KA--LDDPAATA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 376 KIRDklggrIRLLVSGGAPLSPEIEEF---LRVTcccfVVQGYGLTETLGGtalgfpdemCMLGTVGIPAVynEIRLEEv 452
Cdd:PRK07824 149 ALAE-----LDAVLVGGGPAPAPVLDAaaaAGIN----VVRTYGMSETSGG---------CVYDGVPLDGV--RVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 453 aemgydplgenpaGEICIRGQCMFSGYyKNPELTEEVIKDGWFHTGDIGEiLPNGVLKIIDRKKNLIKlSQGEYVALEHL 532
Cdd:PRK07824 208 -------------GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAIS-TGGLTVLPQVV 271
|
330 340 350
....*....|....*....|....*....|....*..
gi 2065806855 533 ENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPET 566
Cdd:PRK07824 272 EAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGP 308
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
78-242 |
1.02e-08 |
|
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: 58.44 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLI---CVPlyDTLGSGAVD------------- 141
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwssCSP--DFGVPGVLDrfgqiepkvlfav 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 142 --YIVEHAEIDfvfvQDTKIKGLLE--PDckcakrLKAIVSFTNVSDELSHKASEIGvKTYSWLDFLHMGREKPEETNPP 217
Cdd:cd05943 178 daYTYNGKRHD----VREKVAELVKglPS------LLAVVVVPYTVAAGQPDLSKIA-KALTLEDFLATGAAGELEFEPL 246
|
170 180
....*....|....*....|....*
gi 2065806855 218 KAFNICTIMYTSGTSGDPKGVVLTH 242
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGA 271
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
225-599 |
1.34e-08 |
|
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: 57.48 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATFVVGMDifmDQFEdkmthddvyLSFLPLAHI-LDRMNEEYFFRKGASVGYYHGDLNV 303
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAHAAHAWR---REYE---------LDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 304 LRDDIQelkptylagvprvferihegiqkalqeLNPRRrlIFNALYKHKLAWMNrgYSHSKASPMADFIAFRKIRDKlgg 383
Cdd:cd17650 166 CPDEVK---------------------------LDPAA--LYDLILKSRITLME--STPALIRPVMAYVYRNGLDLS--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 384 RIRLLVSG--GAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTAL--GFPDEMCMLGTVGIPAVYNEIRLEEVAE-MGYD 458
Cdd:cd17650 212 AMRLLIVGsdGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYyeEGRDPLGDSANVPIGRPLPNTAMYVLDErLQPQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 459 PLGenPAGEICIRGQCMFSGYYKNPELTEEVIKDGWF-------HTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEH 531
Cdd:cd17650 292 PVG--VAGELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGE 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 532 LENIFGQNSVVQDIWV---YGDSFKSMLVAVVVPNpETINrWAkdlgftkpfeelcsfpELKEHIISELKS 599
Cdd:cd17650 369 IESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA-ATLN-TA----------------ELRAFLAKELPS 421
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
213-563 |
2.11e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 213 ETNPPKAF---NICTIMYTSGTSGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAhiLDRMNEEYF-- 287
Cdd:PRK12316 4684 AHDPAVRLhpdNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT-----GERYELTPDDRVLQFMSFS--FDGSHEGLYhp 4756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 288 FRKGASVgyyhgdlnVLRDDIQELkPTYLagvprvFERIHEgiqkalQELNprrRLIFNALYKHKLAwmnrgySHSKasp 367
Cdd:PRK12316 4757 LINGASV--------VIRDDSLWD-PERL------YAEIHE------HRVT---VLVFPPVYLQQLA------EHAE--- 4803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 368 madfiafrkiRDKLGGRIRLLVSGGAPLSP-EIEEFLRVTCCCFVVQGYGLTET---------LGGTALGfPDEMCMLGT 437
Cdd:PRK12316 4804 ----------RDGEPPSLRVYCFGGEAVAQaSYDLAWRALKPVYLFNGYGPTETtvtvllwkaRDGDACG-AAYMPIGTP 4872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 438 VGIPAVYneirleeVAEMGYDPLGENPAGEICIRGQCMFSGYYKNPELT-EEVIKDGW-------FHTGDIGEILPNGVL 509
Cdd:PRK12316 4873 LGNRSGY-------VLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTaERFVPDPFgapggrlYRTGDLARYRADGVI 4945
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 510 KIIDRKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWVYGD--SFKSMLVAVVVPN 563
Cdd:PRK12316 4946 DYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPQ 5000
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
385-567 |
2.34e-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: 56.81 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETlggTAL--GFPDEMCMLGTVGIPAVYNEIRLeevaemgYDPLGe 462
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET---TALvgNSPGQPVKAGSMGRPLPGYRVAL-------LDPDG- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 463 NPA--GEICI-----RGQCMFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEhLENI 535
Cdd:cd05974 271 APAteGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE-LESV 349
|
170 180 190
....*....|....*....|....*....|..
gi 2065806855 536 FGQNSVVQDiwvygdsfksmlvAVVVPNPETI 567
Cdd:cd05974 350 LIEHPAVAE-------------AAVVPSPDPV 368
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
385-565 |
1.20e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 54.70 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 IRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYNEIRLeeVAEMGyDPLGENP 464
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRF--VDEDG-RPLPQGE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 465 AGEICIRGQCM--FSgYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQNSVV 542
Cdd:PRK12406 350 IGEIYSRIAGNpdFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180
....*....|....*....|....*.
gi 2065806855 543 QDIWVYG--DS-FKSMLVAVVVPNPE 565
Cdd:PRK12406 428 HDCAVFGipDAeFGEALMAVVEPQPG 453
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
353-522 |
1.23e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.77 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 353 LAWM-NRGYSHSKASPMA-DFIA--FRKIRDKLGGRIRLLVSGGAPLSPE-IEEFLRVTC-----CCFVVQGYGLTET-- 420
Cdd:PRK05851 238 LSWLsDSRATLTAAPNFAyNLIGkyARRVSDVDLGALRVALNGGEPVDCDgFERFATAMApfgfdAGAAAPSYGLAEStc 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 421 -----LGGTALGFpDEMCMLGTVG----------IPAVynEIRLEEVAEMGydPLGENPAGEICIRGQCMFSGYyknpeL 485
Cdd:PRK05851 318 avtvpVPGIGLRV-DEVTTDDGSGarrhavlgnpIPGM--EVRISPGDGAA--GVAGREIGEIEIRGASMMSGY-----L 387
|
170 180 190
....*....|....*....|....*....|....*...
gi 2065806855 486 TEEVIK-DGWFHTGDIGeILPNGVLKIIDRKKNLIKLS 522
Cdd:PRK05851 388 GQAPIDpDDWFPTGDLG-YLVDGGLVVCGRAKELITVA 424
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
223-563 |
2.05e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 54.13 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 223 CTIMYTSGTSGDPKGVVLTHQavaTFVVGMDIFMDQFedKMTHDDVYLSFLPL----------AHILDRMNeeyfFRKGA 292
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHG---MFEAQIEALREDY--GIEPGEIDLPTFPLfalfgpalgmTSVIPDMD----PTRPA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 293 SVgyyhgDLNVLRDDIQELKPTYLAGVPRVFERI-HEGIQKALQeLNPRRRLIfnalykhklawmnrgyshskaspmadf 371
Cdd:PRK09274 248 TV-----DPAKLFAAIERYGVTNLFGSPALLERLgRYGEANGIK-LPSLRRVI--------------------------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 372 iafrkirdklggrirllvSGGAPLSPE-IEEFLRVtcccF-----VVQGYGLTETL-----GGTA-LGFPDEM--CMLGT 437
Cdd:PRK09274 295 ------------------SAGAPVPIAvIERFRAM----LppdaeILTPYGATEALpissiESREiLFATRAAtdNGAGI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 438 -VGIPAVYNEIRLEEVAEMGYD------PLGENPAGEICIRGQCMFSGYYKNPELTEEV-IKDG----WFHTGDIGEILP 505
Cdd:PRK09274 353 cVGRPVDGVEVRIIAISDAPIPewddalRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDA 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2065806855 506 NGVLKIIDRKKNLIKLSQGEYVAlEHLENIFGQNSVVqdiwvygdsFKSMLVAVVVPN 563
Cdd:PRK09274 433 QGRLWFCGRKAHRVETAGGTLYT-IPCERIFNTHPGV---------KRSALVGVGVPG 480
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
225-535 |
2.55e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.95 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLSFLPLAHILdrmneeyffrkGASVGYYhgdlnvl 304
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSLLANVEQIKTIAD-----FTPNDRFMSALPLFHSF-----------GLTVGLF------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rddiqelkpTYLAGVPRVF---ERIHEGIqkaLQELNPRRR---LIFNALYKHKLAWMNRGYshskaspmaDFiafrkir 378
Cdd:PRK08043 427 ---------TPLLTGAEVFlypSPLHYRI---VPELVYDRNctvLFGTSTFLGNYARFANPY---------DF------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 379 dklgGRIRLLVSGGAPLSPEIEEFLRVTCCCFVVQGYGLTETLGGTALGFPdeM-CMLGTVG--IPAVynEIRLEEVAem 455
Cdd:PRK08043 479 ----ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP--MaAKPGTVGriLPGM--DARLLSVP-- 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 456 gydplGENPAGEICIRGQCMFSGYYK--NP--------ELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGE 525
Cdd:PRK08043 549 -----GIEQGGRLQLKGPNIMNGYLRveKPgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GE 622
|
330
....*....|
gi 2065806855 526 YVALEHLENI 535
Cdd:PRK08043 623 MVSLEMVEQL 632
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
78-564 |
4.32e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 52.98 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDt 157
Cdd:PRK08276 13 TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 kikGLLEPdckcAKRLKAIVSFTnVSDELSHKASEIGVKTYS-WLDflhmgrEKPEETNPPKAFNiCTIMYTSGTSGDPK 236
Cdd:PRK08276 92 ---ALADT----AAELAAELPAG-VPLLLVVAGPVPGFRSYEeALA------AQPDTPIADETAG-ADMLYSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 237 GVV--LTH----QAVATFVVGMDIFMDQFEDkmthdDVYLSFLPLAHildrmneeyffrkgASVGYYHGdlNVLRddiqe 310
Cdd:PRK08276 157 GIKrpLPGldpdEAPGMMLALLGFGMYGGPD-----SVYLSPAPLYH--------------TAPLRFGM--SALA----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 311 lkptyLAGVPRVFERIhegiqKALQELnprrRLIfnalYKHKLawmnrgySHSKASPmADFIAFRKIRDKLGGR-----I 385
Cdd:PRK08276 211 -----LGGTVVVMEKF-----DAEEAL----ALI----ERYRV-------THSQLVP-TMFVRMLKLPEEVRARydvssL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 386 RLLVSGGAPLSPE------------IEEFlrvtcccfvvqgYGLTETLGGTALGFPDEMCMLGTVGiPAVYNEIRLeeVA 453
Cdd:PRK08276 265 RVAIHAAAPCPVEvkramidwwgpiIHEY------------YASSEGGGVTVITSEDWLAHPGSVG-KAVLGEVRI--LD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 454 EMGyDPLgenPAGEICI----RGQCMFSgYYKNPELTEEV-IKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVA 528
Cdd:PRK08276 330 EDG-NEL---PPGEIGTvyfeMDGYPFE-YHNDPEKTAAArNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVNIY 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 2065806855 529 LEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNP 564
Cdd:PRK08276 404 PQEIENLLVTHPKVADVAVFGvpdEEMGERVKAVVQPAD 442
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-566 |
5.13e-07 |
|
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: 52.76 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATFVvgMDIFMDQFEDKMTHDDVYLSFLPLAHILD-RMNEEYFFRKGASVGYYHGD-LN 302
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDN--DTLMAAALGFGPGADSVYLSPAPLYHAAPfRWSMTALFMGGTLVLMEKFDpEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 303 VLRDdIQELKPTYLAGVPRVFERIhegiqKALQElNPRRRLIFNALykhKLAWmnrgysHSkASPMADFIAFRKIrdKLG 382
Cdd:cd05929 208 FLRL-IERYRVTFAQFVPTMFVRL-----LKLPE-AVRNAYDLSSL---KRVI------HA-AAPCPPWVKEQWI--DWG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 383 GrirllvsggaplsPEIEEFlrvtcccfvvqgYGLTETLGGTALGFPDEMCMLGTVGIPAVyNEIRLeevaemgydpLGE 462
Cdd:cd05929 269 G-------------PIIWEY------------YGGTEGQGLTIINGEEWLTHPGSVGRAVL-GKVHI----------LDE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 463 N----PAGEIcirGQCMFSG-----YYKNPELT-EEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHL 532
Cdd:cd05929 313 DgnevPPGEI---GEVYFANgpgfeYTNDPEKTaAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEI 388
|
330 340 350
....*....|....*....|....*....|....*..
gi 2065806855 533 ENIFGQNSVVQDIWVYG---DSFKSMLVAVVVPNPET 566
Cdd:cd05929 389 ENALIAHPKVLDAAVVGvpdEELGQRVHAVVQPAPGA 425
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
78-242 |
5.32e-07 |
|
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: 52.95 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEAC----AAHTLIcvplYDTLGSGAVDYIVEHAEIDFVF 153
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACarigAVHSVV----FAGFSAESLADRINDAQCKLVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 154 VQD-----TKIKGLLEpdcKCAKRLKAIVSFTNVsdeLSHKASEIGVKTYSWLDF-LH--MGREKPE-ETNPPKAFNICT 224
Cdd:cd05966 162 TADggyrgGKVIPLKE---IVDEALEKCPSVEKV---LVVKRTGGEVPMTEGRDLwWHdlMAKQSPEcEPEWMDSEDPLF 235
|
170
....*....|....*...
gi 2065806855 225 IMYTSGTSGDPKGVVLTH 242
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTT 253
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
78-533 |
5.48e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 52.47 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIY---GINCPQWIIAMEACAAHTLICVPLYDtlgsgavdyivehaeidfvfv 154
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRcdrGTESPVAILAILFLGAAYAPIDPASP--------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 155 qdtkikgllePDCKCAKRLKAIVSFTNVSDELSHKASeigvktYSWLDFLHMgrekpeetNPPKAFNICTIMYTSGTSGD 234
Cdd:cd17654 77 ----------EQRSLTVMKKCHVSYLLQNKELDNAPL------SFTPEHRHF--------NIRTDECLAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 235 PKGVVLTHQAVATFVVGmdiFMDQFedKMTHDDVYLSFLPLahILDRMNEEYF--FRKGASVGYYHGDLNVLR---DDI- 308
Cdd:cd17654 133 PKIVAVPHKCILPNIQH---FRSLF--NITSEDILFLTSPL--TFDPSVVEIFlsLSSGATLLIVPTSVKVLPsklADIl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 309 -QELKPTYLAGVPRVFERIheGIQKALQELnprrrlifnaLYKHKlawmnrgyshskaspmadfiafrkirdklggRIRL 387
Cdd:cd17654 206 fKRHRITVLQATPTLFRRF--GSQSIKSTV----------LSATS-------------------------------SLRV 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 388 LVSGGAP------LSPEIEEFLRVTcccfVVQGYGLTET------------LGGTALGFPdemcMLGTVgipavyNEIRl 449
Cdd:cd17654 243 LALGGEPfpslviLSSWRGKGNRTR----IFNIYGITEVscwalaykvpeeDSPVQLGSP----LLGTV------IEVR- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 450 eevaemgyDPLGENPAGEICIRGQ---CMFSGYYKNPELTeevikdgWFHTGDIGEIlPNGVLKIIDRKKNLIKlSQGEY 526
Cdd:cd17654 308 --------DQNGSEGTGQVFLGGLnrvCILDDEVTVPKGT-------MRATGDFVTV-KDGELFFLGRKDSQIK-RRGKR 370
|
....*..
gi 2065806855 527 VALEHLE 533
Cdd:cd17654 371 INLDLIQ 377
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
225-566 |
7.48e-07 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 51.87 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATFVvgmDIFMDQFEdkMTHDDVYLSFlplahildrmneeyffrkgASVGYyhgDLNVL 304
Cdd:cd17652 98 VIYTSGSTGRPKGVVVTHRGLANLA---AAQIAAFD--VGPGSRVLQF-------------------ASPSF---DASVW 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rddiqELKPTYLAG-----VPRvfERIHEGiqKALQELNPRRRLIFNALYKHKLAWMnrgyshskasPMADFIAfrkird 379
Cdd:cd17652 151 -----ELLMALLAGatlvlAPA--EELLPG--EPLADLLREHRITHVTLPPAALAAL----------PPDDLPD------ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 380 klggrIRLLVSGGAPLSPEIEEFLRVTCCcfVVQGYGLTE-TLGGTALGFPDEMCMLgTVGIPAVYNEI-----RLEEVa 453
Cdd:cd17652 206 -----LRTLVVAGEACPAELVDRWAPGRR--MINAYGPTEtTVCATMAGPLPGGGVP-PIGRPVPGTRVyvldaRLRPV- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 454 emgydPLGEnpAGEICIRGQCMFSGYYKNPELT-EEVIKDGW-------FHTGDIGEILPNGVLKIIDRKKNLIKLsQGE 525
Cdd:cd17652 277 -----PPGV--PGELYIAGAGLARGYLNRPGLTaERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKI-RGF 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2065806855 526 YVALEHLENIFGQNSVVQD--IWVYGD-SFKSMLVAVVVPNPET 566
Cdd:cd17652 349 RIELGEVEAALTEHPGVAEavVVVRDDrPGDKRLVAYVVPAPGA 392
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-560 |
9.55e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 51.61 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQavatfvvgmDIFMDQFE-----------DKMTHDD-------VYLSFLPLAHildrmneey 286
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQE---------DIFRMLMGgadfgtgeftpSEDAHKAaaaaagtVMFPAPPLMH--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 287 ffrkGASVGYYHGDLNvlrddiqelkptylaGVPRVFerIHEgiqkalQELNPRRrlIFNALYKHKLAWMNRgYSHSKAS 366
Cdd:cd05924 70 ----GTGSWTAFGGLL---------------GGQTVV--LPD------DRFDPEE--VWRTIEKHKVTSMTI-VGDAMAR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 367 PMADfiAFRKIRDKLGGRIRLLVSGGAPLSPEI-EEFLRVTCCCFVVQGYGLTETlGGTALGFPDEMCMLGTVGIPAVYN 445
Cdd:cd05924 120 PLID--ALRDAGPYDLSSLFAISSGGALLSPEVkQGLLELVPNITLVDAFGSSET-GFTGSGHSAGSGPETGPFTRANPD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 446 EIRLEEvaEMGYDPLGENPAGEICIRGQcMFSGYYKNPELTEE--VIKDG--WFHTGDIGEILPNGVLKIIDRKKNLIKl 521
Cdd:cd05924 197 TVVLDD--DGRVVPPGSGGVGWIARRGH-IPLGYYGDEAKTAEtfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCIN- 272
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2065806855 522 SQGEYVALEHLENIFGQNSVVQDIWVYG---DSFKSMLVAVV 560
Cdd:cd05924 273 TGGEKVFPEEVEEALKSHPAVYDVLVVGrpdERWGQEVVAVV 314
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
228-519 |
3.87e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 49.99 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 228 TSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFEDKmthdDVYLSFLPLAHilDrMneeyffrkgASVGYyhgdLNVlrdd 307
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVET----DVMVSWLPLFH--D-M---------GMVGF----LTV---- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 308 iqelkPTYlAGVPRVFerihegiqkalqeLNP----RRRLIFNALY-KHK---LAWMNRGYShskaspmadFIAFRKIRD 379
Cdd:PRK07768 216 -----PMY-FGAELVK-------------VTPmdflRDPLLWAELIsKYRgtmTAAPNFAYA---------LLARRLRRQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 380 KLGGR-----IRLLVSGGAPLSPE-IEEF--------LRVTCccfVVQGYGLTE-TLggtALGFP--------DEMCM-- 434
Cdd:PRK07768 268 AKPGAfdlssLRFALNGAEPIDPAdVEDLldagarfgLRPEA---ILPAYGMAEaTL---AVSFSpcgaglvvDEVDAdl 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 435 -----------------LGTVGIPAVYNEIRLeeVAEMGyDPLGENPAGEICIRGQCMFSGYyknpeLTEE-----VIKD 492
Cdd:PRK07768 342 laalrravpatkgntrrLATLGPPLPGLEVRV--VDEDG-QVLPPRGVGVIELRGESVTPGY-----LTMDgfipaQDAD 413
|
330 340
....*....|....*....|....*..
gi 2065806855 493 GWFHTGDIGEILPNGVLKIIDRKKNLI 519
Cdd:PRK07768 414 GWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
78-565 |
5.25e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDfVFVQDT 157
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR-VLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 KIKGLLepdCKCAKRLKAIVSFTNVSDELSHKASEIGVktyswldflhmgrekpeeTNPPKAFNIC--TIMYTSGTSGDP 235
Cdd:PRK13390 105 ALDGLA---AKVGADLPLRLSFGGEIDGFGSFEAALAG------------------AGPRLTEQPCgaVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 236 KGVV--LTHQAVAT----FVVGMDIFMDqfedkMTHDDVYLSFLPLAHILD-RMNEEYFFRKGASVGYYHGDLNVLRDDI 308
Cdd:PRK13390 164 KGIQpdLPGRDVDApgdpIVAIARAFYD-----ISESDIYYSSAPIYHAAPlRWCSMVHALGGTVVLAKRFDAQATLGHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 309 QELKPTYLAGVPRVFERihegiqkaLQELNP--RRRLIFNALykhklawmnRGYSHSKASPMADfiAFRKIRDKLGgrir 386
Cdd:PRK13390 239 ERYRITVTQMVPTMFVR--------LLKLDAdvRTRYDVSSL---------RAVIHAAAPCPVD--VKHAMIDWLG---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 387 llvsggaplsPEIEEFlrvtcccfvvqgYGLTETLGGTALGFPDEMCMLGTVGiPAVYNEIRLEEvaemgyDPLGENPAG 466
Cdd:PRK13390 296 ----------PIVYEY------------YSSTEAHGMTFIDSPDWLAHPGSVG-RSVLGDLHICD------DDGNELPAG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 467 EICI----RGQCMFSgYYKNPELTEEVIKDG---WFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEHLENIFGQN 539
Cdd:PRK13390 347 RIGTvyfeRDRLPFR-YLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMH 424
|
490 500
....*....|....*....|....*.
gi 2065806855 540 SVVQDIWVYGdsfksmlvavvVPNPE 565
Cdd:PRK13390 425 PAVHDVAVIG-----------VPDPE 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
78-601 |
1.02e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 48.62 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGcRVGIYGINCPQWIIAMEACAAHTLICVPLyDTLGSGavDYIVEH---AEIDFVFV 154
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPL-DIKWKQ--DELKERlaiSNADMIVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 155 QDTKIKGLLEPDCkcakrlkAIVSFTNVSDELSHKASEIGVKTYSWLDFLHMGrekpeetnppkafnictimYTSGTSGD 234
Cdd:PRK07638 104 ERYKLNDLPDEEG-------RVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMG-------------------FTSGSTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 235 PKGVVLTHQA-VATFVVGMDIFmdqfedKMTHDDVYLSFLPLAHILdrmneeyfFRKGA-SVGYYHGDLNVLR------- 305
Cdd:PRK07638 158 PKAFLRAQQSwLHSFDCNVHDF------HMKREDSVLIAGTLVHSL--------FLYGAiSTLYVGQTVHLMRkfipnqv 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 306 -DDIQELKPTYLAGVPRVFErihegiqkalqelnprrrlifnALYKHKlawmnrgyshskaspmadfiAFRKIRDKLggr 384
Cdd:PRK07638 224 lDKLETENISVMYTVPTMLE----------------------SLYKEN--------------------RVIENKMKI--- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 385 irllVSGGAPLSPEIEE-----FLRVTCCCFvvqgYGLTETLGGTALGFPDEMCMLGTVGIP--AVYNEIRleevaemgy 457
Cdd:PRK07638 259 ----ISSGAKWEAEAKEkikniFPYAKLYEF----YGASELSFVTALVDEESERRPNSVGRPfhNVQVRIC--------- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 458 dplgeNPAGEICIRGQC---------MFSGYYKNPELTEEVIKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVA 528
Cdd:PRK07638 322 -----NEAGEEVQKGEIgtvyvkspqFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIF 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 529 LEHLENIFGQNSVVQDIWVYG--DSF-KSMLVAVVV--PNPETINRWAKdlgftkpfEELCSFPELKE-HIISELKSTA 601
Cdd:PRK07638 396 PEEIESVLHEHPAVDEIVVIGvpDSYwGEKPVAIIKgsATKQQLKSFCL--------QRLSSFKIPKEwHFVDEIPYTN 466
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
78-245 |
1.27e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 48.21 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACA--------------------------AHTLIC--- 128
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACArigavhsvvfggfsaealadriidagAKLVITade 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 129 -------VPLYDtlgsgAVDYIVEHAE-IDFVFVqdtkikgllepdckcAKRLKAIVSFTNVSDELSHKASEiGVKTYSw 200
Cdd:PRK00174 180 gvrggkpIPLKA-----NVDEALANCPsVEKVIV---------------VRRTGGDVDWVEGRDLWWHELVA-GASDEC- 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 201 ldflhmgreKPEETN---PpkAFnictIMYTSGTSGDPKGVV-----------LTHQAV 245
Cdd:PRK00174 238 ---------EPEPMDaedP--LF----ILYTSGSTGKPKGVLhttggylvyaaMTMKYV 281
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
344-561 |
3.09e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 47.04 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 344 IFNALYKHKLawmnrgySHSKASPmadfIAFR----------KIRDKLG-GRIRLLVSGGAPLSPEIEEFL--RVTCCCf 410
Cdd:PTZ00237 341 LWNTIEKHKV-------THTLTLP----KTIRyliktdpeatIIRSKYDlSNLKEIWCGGEVIEESIPEYIenKLKIKS- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 411 vVQGYGLTETLGGTALGFPDEMCMLGTVGIPAVYneIRLEEVAEMGYDpLGENPAGEICIR---GQCMFSGYYKNPELTE 487
Cdd:PTZ00237 409 -SRGYGQTEIGITYLYCYGHINIPYNATGVPSIF--IKPSILSEDGKE-LNVNEIGEVAFKlpmPPSFATTFYKNDEKFK 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065806855 488 EVIKD--GWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEHLE-NIFGQNSVVQ--DIWVYGDSFKSMLVAVVV 561
Cdd:PTZ00237 485 QLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKIS-GNKVQLNTIEtSILKHPLVLEccSIGIYDPDCYNVPIGLLV 562
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
46-277 |
3.42e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.79 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 46 DIFSKSVEKFPDNNML--GWRRIvdekvgpymwkTYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACA- 122
Cdd:PRK08279 41 DVFEEAAARHPDRPALlfEDQSI-----------SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 123 --AhtliCVPLYDTLGSGAVdyiVEHAeidfvfvqdtkIkGLLEP-----DCKCAKRLKAIVSFTNVSDELSHKASEIGV 195
Cdd:PRK08279 110 lgA----VVALLNTQQRGAV---LAHS-----------L-NLVDAkhlivGEELVEAFEEARADLARPPRLWVAGGDTLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 196 KTYSWLDFLHMGR----EKPEETNPPKAFNICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDqfedkMTHDDVYLS 271
Cdd:PRK08279 171 DPEGYEDLAAAAAgaptTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR-----LTPDDVLYC 245
|
....*.
gi 2065806855 272 FLPLAH 277
Cdd:PRK08279 246 CLPLYH 251
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
223-565 |
8.04e-05 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 45.42 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 223 CTIMYTSGTSGDPKGVVLTH---QAVATFVVGMDIFMDQfedkmthdDVYLSFLPLAHILDRMneeyffrKGASVGYYHG 299
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHrraWRGGAFFAGSGGALPS--------DVLYTCLPLYHSTALI-------VGWSACLASG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 300 DLNVLR---------DDIQELKPT----------YLAGVPRV-FERIHegiqkalqelnpRRRLIF-NALykhklawmnr 358
Cdd:cd05940 149 ATLVIRkkfsasnfwDDIRKYQATifqyigelcrYLLNQPPKpTERKH------------KVRMIFgNGL---------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 359 gyshsKASPMADFIAFRKIrdklggrirllvsggaplsPEIEEFlrvtcccfvvqgYGLTEtlGGTAL----GFPdemcm 434
Cdd:cd05940 207 -----RPDIWEEFKERFGV-------------------PRIAEF------------YAATE--GNSGFinffGKP----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 435 lGTVG-----IPAVYNeIRLEEVAEMGYDPLgENPAGeICIR------GQCM--------FSGYYKNPELTE----EVIK 491
Cdd:cd05940 244 -GAIGrnpslLRKVAP-LALVKYDLESGEPI-RDAEG-RCIKvprgepGLLIsrinplepFDGYTDPAATEKkilrDVFK 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 492 DG--WFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLENIFGQNSVVQDIWVYGdsfksmlvaVVVPNPE 565
Cdd:cd05940 320 KGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG---------VQVPGTD 385
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
213-563 |
1.00e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.92 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 213 ETNPPKAF---NICTIMYTSGTSGDPKGVVLTHQAVATFVVGMdifmdQFEDKMTHDDVYLSFLPLAhiLDRMNEEYFFR 289
Cdd:PRK12467 1708 DSNPAVNLapqNLAYVIYTSGSTGRPKGAGNRHGALVNRLCAT-----QEAYQLSAADVVLQFTSFA--FDVSVWELFWP 1780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 290 --KGASV----GYYHGDLNVLRDDIQELKPTYLAGVPRVFERIhegIQKALQELNPR--RRLIFNAlykhklawmnrgys 361
Cdd:PRK12467 1781 liNGARLviapPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQL---LQMDEQVEHPLslRRVVCGG-------------- 1843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 362 hsKASPMAdfiAFRKIRDKLGGRirllvsggaplspeieeflrvtcccFVVQGYGLTETlggtalgfpdemcmlgtvGIP 441
Cdd:PRK12467 1844 --EALEVE---ALRPWLERLPDT-------------------------GLFNLYGPTET------------------AVD 1875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 442 AVYNEIRLEEVAEMGYDPLGE--------------NP-----AGEICIRGQCMFSGYYKNPELT-EEVIKDGW------- 494
Cdd:PRK12467 1876 VTHWTCRRKDLEGRDSVPIGQpianlstyildaslNPvpigvAGELYLGGVGLARGYLNRPALTaERFVADPFgtvgsrl 1955
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065806855 495 FHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEHLE-NIFGQNSVVQDIWVYGD-SFKSMLVAVVVPN 563
Cdd:PRK12467 1956 YRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEaRLREQGGVREAVVIAQDgANGKQLVAYVVPT 2025
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
225-272 |
1.12e-04 |
|
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: 44.99 E-value: 1.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVAT-FVVGMDIFmdqfedKMTHDDVYLSF 272
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHANVLAlFAATQRWF------GFNEDDVWTLF 140
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
78-242 |
1.85e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.79 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAA--------------------------HTLICVPL 131
Cdd:PRK03584 116 SWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASlgaiwsscspdfgvqgvldrfgqiepKVLIAVDG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 132 YdTLGSGAVDYIVEHAEIdfvfvqdtkIKGLlepdckcaKRLKAIVSFTNVSDELSHKASEigvKTYSWLDFLHMGREKP 211
Cdd:PRK03584 196 Y-RYGGKAFDRRAKVAEL---------RAAL--------PSLEHVVVVPYLGPAAAAAALP---GALLWEDFLAPAEAAE 254
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2065806855 212 EETNpPKAFN--ICtIMYTSGTSGDPK-------GVVLTH 242
Cdd:PRK03584 255 LEFE-PVPFDhpLW-ILYSSGTTGLPKcivhghgGILLEH 292
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
78-238 |
4.10e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 43.40 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 78 TYKEVYEEVLQIGSALRAVGAEPGCRVGIYGINCPQWIIAMEACAAHTLICVPLYDTLGSGAVDYIVEHAEIDFVFVQDT 157
Cdd:PRK10524 86 TFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 158 -----KI---KGLLEPDCKCAKRLKAIVSFTNVSDELSHKASEIGVKtYSWLDFLHMGREKP----EETNPPkafnicTI 225
Cdd:PRK10524 166 gsrggKVvpyKPLLDEAIALAQHKPRHVLLVDRGLAPMARVAGRDVD-YATLRAQHLGARVPvewlESNEPS------YI 238
|
170
....*....|...
gi 2065806855 226 MYTSGTSGDPKGV 238
Cdd:PRK10524 239 LYTSGTTGKPKGV 251
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
88-277 |
5.33e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.19 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 88 QIGSALRAVGAE------PGCRVGIYginCPQ---WIIAMEACAAHTLICVPLYDTLGSGavdyiveHAEidfvfvqdtk 158
Cdd:PRK12476 73 QLGVRLRAVGARlqqvagPGDRVAIL---APQgidYVAGFFAAIKAGTIAVPLFAPELPG-------HAE---------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 159 ikgllepdckcakRLKAIVSFTNVSDELSHKASEIGVKtyswlDFL--HMGREKPE---------------ETNPPKAFN 221
Cdd:PRK12476 133 -------------RLDTALRDAEPTVVLTTTAAAEAVE-----GFLrnLPRLRRPRviaidaipdsagesfVPVELDTDD 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2065806855 222 ICTIMYTSGTSGDPKGVVLTHQAVATFVVGMDIFMDQFeDKMTHDdvyLSFLPLAH 277
Cdd:PRK12476 195 VSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLL-DRNTHG---VSWLPLYH 246
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
225-562 |
7.02e-04 |
|
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: 42.46 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 225 IMYTSGTSGDPKGVVLTHQAVATFvvgmdifmdqfedkmthddvylsflpLAHILDRMNEEYFfrkGASVGYYHGDLNVL 304
Cdd:cd17656 133 IIYTSGTTGKPKGVQLEHKNMVNL--------------------------LHFEREKTNINFS---DKVLQFATCSFDVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 305 rddIQELKPTYLAGvpRVFERIHEGIQKALQELnprrrliFNALYKHKLawmnrgyshSKASPMADFIAF----RKIRDK 380
Cdd:cd17656 184 ---YQEIFSTLLSG--GTLYIIREETKRDVEQL-------FDLVKRHNI---------EVVFLPVAFLKFifseREFINR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 381 LGGRIRLLVSGGAPL--SPEIEEFLRvTCCCFVVQGYGLTETLGGTALGF--PDEMCMLGTVGIPAVYNEIRLEEvAEMG 456
Cdd:cd17656 243 FPTCVKHIITAGEQLviTNEFKEMLH-EHNVHLHNHYGPSETHVVTTYTInpEAEIPELPPIGKPISNTWIYILD-QEQQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 457 YDPLGEnpAGEICIRGQCMFSGYYKNPELT-EEVIKDGW------FHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVAL 529
Cdd:cd17656 321 LQPQGI--VGELYISGASVARGYLNRQELTaEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIEL 397
|
330 340 350
....*....|....*....|....*....|....*.
gi 2065806855 530 EHLENIFGQNSVVQD--IWVYGDSF-KSMLVAVVVP 562
Cdd:cd17656 398 GEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVM 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
221-518 |
7.35e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 221 NICTIMYTSGTSGDPKGVVLTHqavATFVVGMDIFMDQFEDKMTHDDVYLSFLPLAHILDRMneeyffrkgasvgyyhGD 300
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSH---GNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLI----------------GG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 301 LnvlrddiqeLKPTYlAGVPRVFerihegiqkalqeLNPRRRLifnalyKHKLAWMnRGYSH--SKASPMADFiAFRKIR 378
Cdd:PRK05691 228 L---------LQPIF-SGVPCVL-------------MSPAYFL------ERPLRWL-EAISEygGTISGGPDF-AYRLCS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 379 DKLG---------GRIRLLVSGGAPLSPE-IEEFL-RVTCCCFVVQG----YGLTE-TL---------GGTALGF----- 428
Cdd:PRK05691 277 ERVSesalerldlSRWRVAYSGSEPIRQDsLERFAeKFAACGFDPDSffasYGLAEaTLfvsggrrgqGIPALELdaeal 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065806855 429 ------PDEMCMLGTVGIPAVYNEIRLEEVAEMgyDPLGENPAGEICIRGQCMFSGYYKNPELTEE--VIKDG--WFHTG 498
Cdd:PRK05691 357 arnraePGTGSVLMSCGRSQPGHAVLIVDPQSL--EVLGDNRVGEIWASGPSIAHGYWRNPEASAKtfVEHDGrtWLRTG 434
|
330 340
....*....|....*....|....*..
gi 2065806855 499 DI-----GEILPNGVLK--IIDRKKNL 518
Cdd:PRK05691 435 DLgflrdGELFVTGRLKdmLIVRGHNL 461
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
462-519 |
5.89e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 39.93 E-value: 5.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065806855 462 ENPA---GEICIRGQCMFSGYYKNPELTEEV-----------IKDG-WFHTGDIGEILpNGVLKIIDRKKNLI 519
Cdd:PRK05850 391 ECPAgtvGEIWVHGDNVAAGYWQKPEETERTfgatlvdpspgTPEGpWLRTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| |
