|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
3-665 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 1318.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 3 LAADNVLLVEEGRPATAEHPSAGPVYRCKYAKDGLLDLPTDIDSPWQFFSEAVKKYPNEQMLGQRVTTDSKVGPYTWITY 82
Cdd:PLN02861 1 MAETYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 83 KEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTV 162
Cdd:PLN02861 81 KEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 163 SSILSCQKGCSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMGNLDeANLPRKRKTDICTIMYTSGTTGEPKGVI 242
Cdd:PLN02861 161 SSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLD-CELPPKQKTDICTIMYTSGTTGEPKGVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 243 LNNAAISVQVLSIDKMLEVTDRSCDTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGV 322
Cdd:PLN02861 240 LTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 323 PRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSQEEASPRLDRLMFDKIKEALGGRAHMLLSGAAPLPRHV 402
Cdd:PLN02861 320 PRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 403 EEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPEMGYDAFSaDVPRGEICLRGNSMFSG 482
Cdd:PLN02861 400 EEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALS-DVPRGEICLRGNTLFSG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 483 YHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESFLVG 562
Cdd:PLN02861 479 YHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 563 VVVPDRKAIEDWAKlNYQSPNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIERDLITPTFKLKR 642
Cdd:PLN02861 559 VVVPDRQALEDWAA-NNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKR 637
|
650 660
....*....|....*....|...
gi 22330132 643 PQLLQHYKGIVDQLYSEAKRSMA 665
Cdd:PLN02861 638 PQLLKYYKDCIDQLYSEAKGGKA 660
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
75-658 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 861.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGV--DPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEV 152
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 153 SLVFVQEktvssilscqkgcssnlktivsfgevsstqkeeaknqCVSLFSWNEFSLMGNLDEANLPRKRKTDICTIMYTS 232
Cdd:cd05927 81 SIVFCDA-------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 233 GTTGEPKGVILNNAAISVQVLSIDKMLEVTDRsCDTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQ 312
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNK-INPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGfsQEEASPRLDRLMFDKIKEALGGRAHMLL 392
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSG--VVRASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSmVGTVGVPMPTVEARLVSVPEMGYDAFsADVPRGEI 472
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDVPEMNYDAK-DPNPRGEV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 473 CLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWV 551
Cdd:cd05927 359 CIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 552 YGNSFESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIER 631
Cdd:cd05927 439 YGDSLKSFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVEN 518
|
570 580
....*....|....*....|....*..
gi 22330132 632 DLITPTFKLKRPQLLQHYKGIVDQLYS 658
Cdd:cd05927 519 GLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1-665 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 831.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 1 MSLAADNVLLVEEGRPATAEHPSAGPVYRCKYAKDGLLDLPTDIDSPWQFFSEAVKKYPNEQMLGQRVTTDSKVGPYTWI 80
Cdd:PLN02614 1 MSQQKKFIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPNPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEK 160
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 TVSSILSCQKGCSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRKRKTDICTIMYTSGTTGEPKG 240
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 VILNNAAISVQVLSIDKMLEVTDRSCDTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFC 320
Cdd:PLN02614 241 VMISNESIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 321 GVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSQEEASPRLDRLMFDKIKEALGGRAHMLLSGAAPLPR 400
Cdd:PLN02614 321 AVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLAS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 401 HVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPEMGYDAFsADVPRGEICLRGNSMF 480
Cdd:PLN02614 401 HVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDAL-ASTPRGEICIRGKTLF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 481 SGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESFL 560
Cdd:PLN02614 480 SGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 561 VGVVVPDRKAIEDWAKLNYQSpNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIERDLITPTFKL 640
Cdd:PLN02614 560 VAIANPNQQILERWAAENGVS-GDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKK 638
|
650 660
....*....|....*....|....*
gi 22330132 641 KRPQLLQHYKGIVDQLYSEAKRSMA 665
Cdd:PLN02614 639 KRPQLLKYYQSVIDEMYKTTNEKLA 663
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
11-663 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 755.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 11 VEEGRPATAEHPSAGPVYRCKYAKDGLLDLPTDIDSPWQFFSEAVKKYPNEQMLGQRVTTDSKVGPYTWITYKEAHDAAI 90
Cdd:PLN02430 8 VEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYKEVYEEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 91 RIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCQK 170
Cdd:PLN02430 88 QIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 171 GCSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMG--NLDEANLPrkRKTDICTIMYTSGTTGEPKGVILNNAAI 248
Cdd:PLN02430 168 KSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGkeNPSETNPP--KPLDICTIMYTSGTSGDPKGVVLTHEAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 249 SVQVLSIDKMLEVTDRSCDTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDK 328
Cdd:PLN02430 246 ATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFER 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 329 LYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSQEEASPRLDRLMFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRI 408
Cdd:PLN02430 326 IHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 409 IPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPEMGYDAFsADVPRGEICLRGNSMFSGYHKRQD 488
Cdd:PLN02430 406 TSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPL-GEPPRGEICVRGKCLFSGYYKNPE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 489 LTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESFLVGVVVPDR 568
Cdd:PLN02430 485 LTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNE 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 569 KAIEDWAKLN-YQSPndFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLQ 647
Cdd:PLN02430 565 ENTNKWAKDNgFTGS--FEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLK 642
|
650
....*....|....*...
gi 22330132 648 HYKGIVDQLYS--EAKRS 663
Cdd:PLN02430 643 YYQVEIDEMYRklAEKRI 660
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
51-659 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 619.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 51 FSEAVKKYPNEQMLGQRVTTDSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGIT 130
Cdd:PLN02736 50 FVYAVETFRDYKYLGTRIRVDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 131 YVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCQKGCSSnLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMG 210
Cdd:PLN02736 130 SVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPS-VRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 211 NLDEANLPRKRKTDICTIMYTSGTTGEPKGVILN------NAAISVQVLSIDkmlevtdrscdTSDVFFSYLPLAHCYDQ 284
Cdd:PLN02736 209 RSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLThgnliaNVAGSSLSTKFY-----------PSDVHISYLPLAHIYER 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 285 VMEIYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFS 364
Cdd:PLN02736 278 VNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKN 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 365 qeeASPRLDRLMFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTE-SCGGSfTTLAGVFSmVGTVGV 443
Cdd:PLN02736 358 ---PSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTEtSCVIS-GMDEGDNL-SGHVGS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 444 PMPTVEARLVSVPEMGYDAFSADVPRGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:PLN02736 433 PNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 523 FKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYFLDEL 602
Cdd:PLN02736 513 FKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKYEDLKQLCNDPRVRAAVLADM 592
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 22330132 603 NSTAKQYQLKGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLYSE 659
Cdd:PLN02736 593 DAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
49-660 |
3.06e-174 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 509.64 E-value: 3.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNEQMLGQRVTtdskvGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG 128
Cdd:COG1022 15 DLLRRRAARFPDRVALREKED-----GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 129 ITYVPLYDSLGVNAVEFIINHAEVSLVFVQ-EKTVSSILSCQKGCSSnLKTIVSFgevsstqKEEAKNQCVSLFSWNEFS 207
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELPS-LRHIVVL-------DPRGLRDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 208 LMG-NLDEANLPRKRK-----TDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAHC 281
Cdd:COG1022 162 ALGrEVADPAELEARRaavkpDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-----GDRTLSFLPLAHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 282 YDQVMEIYFLSRGSSVGYWRgDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYnyKLGNMRK 361
Cdd:COG1022 237 FERTVSYYALAAGATVAFAE-SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWAL--AVGRRYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 362 GFSQEEASPRL---------DRLMFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRI--IPasnLSQGYGLTESCGGSFTT 430
Cdd:COG1022 314 RARLAGKSPSLllrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRAlgIP---VLEGYGLTETSPVITVN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 431 LAGVFsMVGTVGVPMPTVEARLvsvpemgydafsADvpRGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQE 509
Cdd:COG1022 391 RPGDN-RIGTVGPPLPGVEVKI------------AE--DGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 510 DGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSfESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLC 589
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPYTSYAELA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330132 590 QNLKAQKYF---LDELNStakqyQLKGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLYSEA 660
Cdd:COG1022 535 QDPEVRALIqeeVDRANA-----GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
75-642 |
2.15e-167 |
|
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: 488.65 E-value: 2.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSL 154
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 VFvqektvssilscqkgCSSNlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrKTDICTIMYTSGT 234
Cdd:cd17639 81 IF---------------TDGK----------------------------------------------PDDLACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 235 TGEPKGVILNN----AAISVQVLSIDKMLEVTDRSCdtsdvffSYLPLAHCYDQVMEIYFLSRGSSVGYwrGDIRYLMD- 309
Cdd:cd17639 100 TGNPKGVMLTHgnlvAGIAGLGDRVPELLGPDDRYL-------AYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 310 -------DVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSqeeaSPRLDRLMFDKIKE 382
Cdd:cd17639 171 skrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG----TPLLDELVFKKVRA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 383 ALGGRAHMLLSGAAPLPRHVEEFLRIIPASnLSQGYGLTESCGGSFTTLAGVFSmVGTVGVPMPTVEARLVSVPEMGYDA 462
Cdd:cd17639 247 ALGGRLRYMLSGGAPLSADTQEFLNIVLCP-VIQGYGLTETCAGGTVQDPGDLE-TGRVGPPLPCCEIKLVDWEEGGYST 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 463 FsADVPRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYS 541
Cdd:cd17639 325 D-KPPPRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYR 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 542 RCPLIAQIWVYGNSFESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIH 621
Cdd:cd17639 404 SNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVV 483
|
570 580
....*....|....*....|.
gi 22330132 622 LEPNPFDIERDLITPTFKLKR 642
Cdd:cd17639 484 LLDEEWTPENGLVTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
75-645 |
5.96e-134 |
|
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: 401.20 E-value: 5.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSL 154
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 VFVqektvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmGNLDeanlprkrktDICTIMYTSGT 234
Cdd:cd05907 81 LFV----------------------------------------------------EDPD----------DLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 235 TGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCYDQVMEIYF-LSRGSSVGYWRgDIRYLMDDVQA 313
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLPATEG-----DRHLSFLPLAHVFERRAGLYVpLLAGARIYFAS-SAETLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 314 LKPTVFCGVPRVYDKLYAGIMQKisasglirkklfdfaynyklgnmrkgfsqeeASPRLDRLMFDKikeALGGRAHMLLS 393
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAIKVK-------------------------------AVPGLKRKLFDL---AVGGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 394 GAAPLPRHVEEFLRIIpASNLSQGYGLTESCGGSFTTLAGVFSmVGTVGVPMPTVEARLVsvpemgydafsadvPRGEIC 473
Cdd:cd05907 219 GGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNR-IGTVGKPLPGVEVRIA--------------DDGEIL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 474 LRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVY 552
Cdd:cd05907 283 VRGPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVI 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 553 GNSfESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYFLDELNSTAKqyQLKGFEMLKAIHLEPNPFDIERD 632
Cdd:cd05907 363 GDG-RPFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENG 439
|
570
....*....|...
gi 22330132 633 LITPTFKLKRPQL 645
Cdd:cd05907 440 ELTPTLKLKRPVI 452
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
41-658 |
2.66e-130 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 399.88 E-value: 2.66e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 41 PTDIDSPW-------QFFSEAVKKYPNEQMLGQR--------VTTDSK------VGPYTWITYKEAHDAAIRIGSAIRSR 99
Cdd:PLN02387 47 PELVETPWegattlaALFEQSCKKYSDKRLLGTRklisrefeTSSDGRkfeklhLGEYEWITYGQVFERVCNFASGLVAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 100 GVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCqkgcSSNLKTI 179
Cdd:PLN02387 127 GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDI----SSQLETV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 180 VSF------GEVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRKrkTDICTIMYTSGTTGEPKGVILNNAAISVQVL 253
Cdd:PLN02387 203 KRViymddeGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSP--NDIAVIMYTSGSTGLPKGVMMTHGNIVATVA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 254 SIdkMLEVTDRScdTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYwrGDIRYLMD-----------DVQALKPTVFCGV 322
Cdd:PLN02387 281 GV--MTVVPKLG--KNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 323 PRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSQEEASPRL--DRLMFDKIKEALGGRAHMLLSGAAPLPR 400
Cdd:PLN02387 355 PAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGSWFGAWGLEKLlwDALVFKKIRAVLGGRIRFMLSGGAPLSG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 401 HVEEFLRIIPASNLSQGYGLTESCGGsfttlaGVFS-----MVGTVGVPMPTVEARLVSVPEMGYDAFSADVPRGEICLR 475
Cdd:PLN02387 435 DTQRFINICLGAPIGQGYGLTETCAG------ATFSewddtSVGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 476 GNSMFSGYHKRQDLTDQVL-IDG----WFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIW 550
Cdd:PLN02387 509 GPSVTLGYFKNQEKTDEVYkVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 551 VYGNSFESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIE 630
Cdd:PLN02387 589 VHADPFHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPE 668
|
650 660
....*....|....*....|....*...
gi 22330132 631 RDLITPTFKLKRPQLLQHYKGIVDQLYS 658
Cdd:PLN02387 669 SGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
51-526 |
6.10e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 322.34 E-value: 6.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 51 FSEAVKKYPNeqmlgqrvTTDSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGIT 130
Cdd:pfam00501 1 LERQAARTPD--------KTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 131 YVPLYDSLGVNAVEFIINHAEVSLVFVQE-KTVSSILSC-QKGCSSNLKTIVSFGEVSstqKEEAKNQCVSLFSWnefsl 208
Cdd:pfam00501 73 YVPLNPRLPAEELAYILEDSGAKVLITDDaLKLEELLEAlGKLEVVKLVLVLDRDPVL---KEEPLPEEAKPADV----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 209 mgnlDEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSCDTsDVFFSYLPLAHCYDQVMEI 288
Cdd:pfam00501 145 ----PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPD-DRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 289 YF-LSRGSSVGYWRGDIRY----LMDDVQALKPTVFCGVPRVYDKLYagimqkisasglirkklfdfaynyklgnmrkgf 363
Cdd:pfam00501 220 LGpLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNMLL--------------------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 364 sqeeASPRLDRLMFDKIKealggrahMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFT--TLAGVFSMVGTV 441
Cdd:pfam00501 267 ----EAGAPKRALLSSLR--------LVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTplPLDEDLRSLGSV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 442 GVPMPTVEARLVSVPEMGYdafsadVPR---GEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIID 517
Cdd:pfam00501 335 GRPLPGTEVKIVDDETGEP------VPPgepGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 22330132 518 RKKNIFKLS 526
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
78-659 |
1.33e-93 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 304.21 E-value: 1.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 78 TWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV 157
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 QEKTVSSILSCQKgcSSNLK--TIVSFGEV-SSTQKEEaknqcVSLFSWNEFSLMGNLDEANLPRK---RKTDICTIMYT 231
Cdd:PTZ00216 200 NGKNVPNLLRLMK--SGGMPntTIIYLDSLpASVDTEG-----CRLVAWTDVVAKGHSAGSHHPLNipeNNDDLALIMYT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 232 SGTTGEPKGVILNNAAISVQVLSI-DKMLEVTDRSCDTsDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYwrGDIRYLMD- 309
Cdd:PTZ00216 273 SGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEED-ETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 310 ------DVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGfsqeEASPRLDRLMFDKIKEA 383
Cdd:PTZ00216 350 farphgDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEG----KDTPYWNEKVFSAPRAV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 384 LGGRAHMLLSGAAPLPRHVEEFLRIIPASnLSQGYGLTESCGGSFTTLAGVFSmVGTVGVPMPTVEARLVSVPEmgYDAF 463
Cdd:PTZ00216 426 LGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLE-PNAVGQLLKGVEMKLLDTEE--YKHT 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 464 SADVPRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSR 542
Cdd:PTZ00216 502 DTPEPRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQ 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 543 CPLIAQ--IWVYGNSFESFLVGVVVPDRKAIEDWAKLNyQSPNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAI 620
Cdd:PTZ00216 582 NELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEH-GIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHV 660
|
570 580 590
....*....|....*....|....*....|....*....
gi 22330132 621 HLEPNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLYSE 659
Cdd:PTZ00216 661 RVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
75-643 |
3.47e-81 |
|
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: 264.61 E-value: 3.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSL 154
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 VFVQEktvssilscqkgcSSNlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrktDICTIMYTSGT 234
Cdd:cd17640 81 LVVEN-------------DSD------------------------------------------------DLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 235 TGEPKGVILNNAAISVQVLSIDKML--EVTDRscdtsdvFFSYLPLAHCYDQVMEIYFLSRGSSVGYwrGDIRYLMDDVQ 312
Cdd:cd17640 100 TGNPKGVMLTHANLLHQIRSLSDIVppQPGDR-------FLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAynyklgnmrkgfsqeeasprldrlmfdkikeALGGRAHMLL 392
Cdd:cd17640 171 RVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF-------------------------------LSGGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFLRIIpASNLSQGYGLTE-SCGGSFTTLAGVfsMVGTVGVPMPTVEARLVSvPEMGydafsADVP--- 468
Cdd:cd17640 220 SGGGALPPHVDTFFEAI-GIEVLNGYGLTEtSPVVSARRLKCN--VRGSVGRPLPGTEIKIVD-PEGN-----VVLPpge 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 469 RGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 547
Cdd:cd17640 291 KGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIE 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 548 QIWVYGNSfESFLVGVVVPDRKAIEDWAK-LNYQSPNDFESLCQNLKAQKYFLDELN---STAKQYqlKGFEMLKAIHLE 623
Cdd:cd17640 371 QIMVVGQD-QKRLGALIVPNFEELEKWAKeSGVKLANDRSQLLASKKVLKLYKNEIKdeiSNRPGF--KSFEQIAPFALL 447
|
570 580
....*....|....*....|
gi 22330132 624 PNPFdIERDLITPTFKLKRP 643
Cdd:cd17640 448 EEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
75-642 |
8.38e-72 |
|
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: 241.22 E-value: 8.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSL 154
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 VFVQEktVSSILSCQKGCSSNLKTIvsfgevSSTQKEEAKNQcvslFSWNEFSLMGNLDEANLPRKRKtDICTIMYTSGT 234
Cdd:cd05932 82 LFVGK--LDDWKAMAPGVPEGLISI------SLPPPSAANCQ----YQWDDLIAQHPPLEERPTRFPE-QLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 235 TGEPKGVILN--NAAISVQVLsidkmleVTDRSCDTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQ 312
Cdd:cd05932 149 TGQPKGVMLTfgSFAWAAQAG-------IEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPRVYDKLYAGIMQKISASglirkklfdfaynyKLGNMRKgfsqeeaSPRLDRLMFDKIKEALG-GRAHML 391
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQDKIPQQ--------------KLNLLLK-------IPVVNSLVKRKVLKGLGlDQCRLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 392 LSGAAPLPRHVEEFLRIIpASNLSQGYGLTESCGGSFTTLAGVfSMVGTVGVPMPTVEARLVsvpemgydafsadvPRGE 471
Cdd:cd05932 281 GCGSAPVPPALLEWYRSL-GLNILEAYGMTENFAYSHLNYPGR-DKIGTVGNAGPGVEVRIS--------------EDGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 472 ICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIW 550
Cdd:cd05932 345 ILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVC 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 551 VYGNSFeSFLVGVVVPDRKAIedwAKLNYQSPNDFESLCQNLkaqkyfLDELNSTakqyqLKGFEMLKAIHLEPNPFDIE 630
Cdd:cd05932 425 VIGSGL-PAPLALVVLSEEAR---LRADAFARAELEASLRAH------LARVNST-----LDSHEQLAGIVVVKDPWSID 489
|
570
....*....|..
gi 22330132 631 RDLITPTFKLKR 642
Cdd:cd05932 490 NGILTPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
77-657 |
1.73e-70 |
|
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: 239.95 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 77 YTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIA-MEACMSQGITyVPLYDSLGVNAVEFIINHAEVSLV 155
Cdd:cd05933 6 WHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAaVGAIFAGGIA-VGIYTTNSPEACQYVAETSEANIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 156 FVQ-EKTVSSILSCQKGCSsNLKTIVSFgevsstqKEEAKNQCVSLFSWNEFSLMGNLDE-----ANLPRKRKTDICTIM 229
Cdd:cd05933 85 VVEnQKQLQKILQIQDKLP-HLKAIIQY-------KEPLKEKEPNLYSWDEFMELGRSIPdeqldAIISSQKPNQCCTLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 230 YTSGTTGEPKGVILNNAAISVQVLSIDK---MLEVTDRScdtsDVFFSYLPLAHCYDQVMEIYF-LSRGSSVGYWRGDIR 305
Cdd:cd05933 157 YTSGTTGMPKGVMLSHDNITWTAKAASQhmdLRPATVGQ----ESVVSYLPLSHIAAQILDIWLpIKVGGQVYFAQPDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 306 --YLMDDVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSQEEASPR----LDRLMFDK 379
Cdd:cd05933 233 kgTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLfyrlAKKLVFKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 380 IKEALG-GRAHMLLSGAAPLPRHVEE-FLRI-IPasnLSQGYGLTESCGGSFTTLAGVFSMvGTVGVPMPTVEARLVSVP 456
Cdd:cd05933 313 VRKALGlDRCQKFFTGAAPISRETLEfFLSLnIP---IMELYGMSETSGPHTISNPQAYRL-LSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 457 EMGYdafsadvprGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVEN 535
Cdd:cd05933 389 ADGI---------GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 536 LENTY-SRCPLIAQIWVYGNS--FESFLVGV---VVPDRKAIEDwaKLNYQSPNdfesLCQNLKAQKYFLDEL------- 602
Cdd:cd05933 460 IEDAVkKELPIISNAMLIGDKrkFLSMLLTLkceVNPETGEPLD--ELTEEAIE----FCRKLGSQATRVSEIaggkdpk 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330132 603 --------------NSTAKQYQLKGFEMLkaihlePNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLY 657
Cdd:cd05933 534 vyeaieegikrvnkKAISNAQKIQKWVIL------EKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
48-607 |
2.19e-67 |
|
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: 227.77 E-value: 2.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 48 WQFFSEAVKKYPNEQMLgqrvttdskVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQ 127
Cdd:COG0318 2 ADLLRRAAARHPDRPAL---------VFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 128 GITYVPLYDSLGVNAVEFIINHAEVSLVFVqektvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefs 207
Cdd:COG0318 73 GAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 208 lmgnldeanlprkrktdiCTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCYDQVME 287
Cdd:COG0318 103 ------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPG-----DVVLVALPLFHVFGLTVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 288 IY--FLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYdklyagimqkisaSGLIRKKLFDfayNYKLGNMRkgfsq 365
Cdd:COG0318 160 LLapLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTML-------------ARLLRHPEFA---RYDLSSLR----- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 366 eeasprldrlmfdkikealggrahMLLSGAAPLPRHV-EEFLRIIPAsNLSQGYGLTE-SCGGSFTTLAGVFSMVGTVGV 443
Cdd:COG0318 219 ------------------------LVVSGGAPLPPELlERFEERFGV-RIVEGYGLTEtSPVVTVNPEDPGERRPGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 444 PMPTVEARLVsvpemgyDAFSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKK 520
Cdd:COG0318 274 PLPGVEVRIV-------DEDGRELPPgevGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKK 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 521 NIFKLSqGEYVAVENLENTYSRCPLIAQIWVYGNSFESF---LVGVVVP------DRKAIEDW--AKL-NYQSPNDFEsl 588
Cdd:COG0318 347 DMIISG-GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWgerVVAFVVLrpgaelDAEELRAFlrERLaRYKVPRRVE-- 423
|
570 580
....*....|....*....|.
gi 22330132 589 cqnlkaqkyFLDEL--NSTAK 607
Cdd:COG0318 424 ---------FVDELprTASGK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
80-524 |
1.54e-61 |
|
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: 212.84 E-value: 1.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKGCSSNLKTIvsfgeVSSTQKEEAKNQCVSLFSWNEFSlmgnldEANLPRKR---KTDICTIMYTSGTTG 236
Cdd:cd05911 91 DGLEKVKEAAKELGPKDKII-----VLDDKPDGVLSIEDLLSPTLGEE------DEDLPPPLkdgKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 237 EPKGVILNNAAISVQVLSIDKMLEVTDRScdtSDVFFSYLPLAHCYDQVMEIYFLSRGSSVgYW--RGDIRYLMDDVQAL 314
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFLYGNDGS---NDVILGFLPLYHIYGLFTTLASLLNGATV-IImpKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 315 KPTVFCGVPRvydklyagIMQKISASGLIRKklfdfaynYKLGNMRkgfsqeeasprldrlmfdkikealggrahMLLSG 394
Cdd:cd05911 236 KITFLYLVPP--------IAAALAKSPLLDK--------YDLSSLR-----------------------------VILSG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 395 AAPLPRHVEEFL-RIIPASNLSQGYGLTESCGGSFTTLAGVFSMvGTVGVPMPTVEARLVSVPEM---GYDAfsadvpRG 470
Cdd:cd05911 271 GAPLSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKP-GSVGRLLPNVEAKIVDDDGKdslGPNE------PG 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22330132 471 EICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFK 524
Cdd:cd05911 344 EICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
11-635 |
4.96e-58 |
|
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: 206.15 E-value: 4.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 11 VEEGRPATAEHPSAGpvyrckyaKDGLlDLPTDIDSpwqffseAVKKYPNEQMLGQRVT---TDSKVGPYTW-------- 79
Cdd:cd17632 4 FAAAAPLEAVTEAIR--------RPGL-RLAQIIAT-------VMTGYADRPALGQRATelvTDPATGRTTLrllprfet 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRS-RGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQ 158
Cdd:cd17632 68 ITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 EKTVSSILSCQKGcSSNLKTIVSFG----------EVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRKRKTD--IC 226
Cdd:cd17632 148 AEHLDLAVEAVLE-GGTPPRLVVFDhrpevdahraALESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDdpLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 227 TIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRScdtsDVFFSYLPLAHCYDQVMEIYFLSRGSsVGYW--RGDI 304
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPA----SITLNFMPMSHIAGRISLYGTLARGG-TAYFaaASDM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 305 RYLMDDVQALKPTVFCGVPRVYDKLYagimQKISASgLIRKklfdfaynyklgnMRKGFSQEEASprlDRLMFDKIKEAL 384
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLF----QRYQAE-LDRR-------------SVAGADAETLA---ERVKAELRERVL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 385 GGRAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTEscggsfttlAGVFSMVGTVGVPmPTVEARLVSVPEMGYdaFS 464
Cdd:cd17632 361 GGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE---------AGAVILDGVIVRP-PVLDYKLVDVPELGY--FR 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 465 ADVP--RGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYS 541
Cdd:cd17632 429 TDRPhpRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFA 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 542 RCPLIAQIWVYGNSFESFLVGVVVPDRKAIEDWAKlnyqspndfeslcQNLKAQkyFLDELNSTAKQYQLKGFEMLKAIH 621
Cdd:cd17632 509 ASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDT-------------ARLRAA--LAESLQRIAREAGLQSYEIPRDFL 573
|
650
....*....|....
gi 22330132 622 LEPNPFDIERDLIT 635
Cdd:cd17632 574 IETEPFTIANGLLS 587
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
108-655 |
4.45e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 206.11 E-value: 4.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 108 GIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILsCQKGCSSNLK------TIVS 181
Cdd:PTZ00342 134 GLYGSNSINWLVADLACMLSGVTTLVMHSKFSIDVIVDILNETKLEWLCLDLDLVEGLL-ERKNELPHLKkliildTLIK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 182 FGEV--------------SSTQKEEAKNQCVSLFSWNEFSLMGNLDEA--------------------------NLPRKR 221
Cdd:PTZ00342 213 SKEIninkeeknngsnvnNNGNKNNKEEQKGNDLSNELEDISLGPLEYdkeklekikdlkekakklgisiilfdDMTKNK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 222 KTD----------ICTIMYTSGTTGEPKGVILNNAAISVQVLSIdkmlevtdrsCDTS-------DVFFSYLPLAHCYDQ 284
Cdd:PTZ00342 293 TTNykiqnedpdfITSIVYTSGTSGKPKGVMLSNKNLYNTVVPL----------CKHSifkkynpKTHLSYLPISHIYER 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 285 VMEIYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFS 364
Cdd:PTZ00342 363 VIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFS 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 365 QeeaspRLDRL--MFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSmVGTVG 442
Cdd:PTZ00342 443 K-----FLEGIthISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNN-TESIG 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 443 VPM-PTVEARLVSVPEmgYDAfSADVPRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKK 520
Cdd:PTZ00342 517 GPIsPNTKYKVRTWET--YKA-TDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIVQINKNGSLTFLDRSK 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 521 NIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESFLVGVVVPDR----KAIEDWAKLNYQSPND---FESLCQNLK 593
Cdd:PTZ00342 594 GLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKyllfKCLKDDNMLESTGINEknyLEKLTDETI 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330132 594 AQKYFLD----ELNSTAKQYQLKGFEMLKAIHLEPNPFDIErDLITPTFKLKRPQLLQHYKGIVDQ 655
Cdd:PTZ00342 674 NNNIYVDyvkgKMLEVYKKTNLNRYNIINDIYLTSKVWDTN-NYLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
49-607 |
1.76e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 194.64 E-value: 1.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNeqmlgQRVTTDSKVGpytwITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG 128
Cdd:PRK06187 10 RILRHGARKHPD-----KEAVYFDGRR----TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 129 ITYVPLYDSLGVNAVEFIINHAEVSLVFVqEKTVSSILSCQKGCSSNLKTIVSFGEvssTQKEEAKNQCVSLFSWnefsL 208
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLV-DSEFVPLLAAILPQLPTVRTVIVEGD---GPAAPLAPEVGEYEEL----L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 209 MGNLDEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAHCYD-QVME 287
Cdd:PRK06187 153 AAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR-----DDVYLVIVPMFHVHAwGLPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 288 IYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYdklyagimqkisaSGLIRKKLfdfAYNYKLGNMRkgfsqee 367
Cdd:PRK06187 228 LALMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIW-------------QMLLKAPR---AYFVDFSSLR------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 368 asprldrlmfdkikealggrahMLLSGAAPLPRH-VEEFLRIIPASnLSQGYGLTESCG-GSFTTLA----GVFSMVGTV 441
Cdd:PRK06187 285 ----------------------LVIYGGAALPPAlLREFKEKFGID-LVQGYGMTETSPvVSVLPPEdqlpGQWTKRRSA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 442 GVPMPTVEARLVsvpemgyDAFSADVPR-----GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKII 516
Cdd:PRK06187 342 GRPLPGVEARIV-------DDDGDELPPdggevGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYIT 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 517 DRKKNIFKlSQGEYV-AVEnLENTYSRCPLIAQIWVYG----NSFESFLVGVVV-----PDRKAIEDWAK---LNYQSPN 583
Cdd:PRK06187 415 DRIKDVII-SGGENIyPRE-LEDALYGHPAVAEVAVIGvpdeKWGERPVAVVVLkpgatLDAKELRAFLRgrlAKFKLPK 492
|
570 580
....*....|....*....|....*.
gi 22330132 584 DFeslcqnlkaqkYFLDEL--NSTAK 607
Cdd:PRK06187 493 RI-----------AFVDELprTSVGK 507
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
80-642 |
4.34e-53 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 189.58 E-value: 4.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrktDICTIMYTSGTTGEPK 239
Cdd:cd05914 88 ED--------------------------------------------------------------DVALINYTSGTTGNSK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAH----CYDQVM------EIYFLSRGSSVgywrgdiryLMD 309
Cdd:cd05914 106 GVMLTYRNIVSNVDGVKEVVLLGK-----GDKILSILPLHHiyplTFTLLLpllngaHVVFLDKIPSA---------KII 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 310 DVQALKPTVFCGVPRVYDKLYAGIMQKISasgLIRKKLFDFAYNYKLGNMRKgfsqeeasprlDRLMFDKIKEALGGRAH 389
Cdd:cd05914 172 ALAFAQVTPTLGVPVPLVIEKIFKMDIIP---KLTLKKFKFKLAKKINNRKI-----------RKLAFKKVHEAFGGNIK 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 390 MLLSGAAPLPRHVEEFLRII--PASnlsQGYGLTEScgGSFTTLAGVFSMV-GTVGVPMPTVEARLVSVPEMGYDafsad 466
Cdd:cd05914 238 EFVIGGAKINPDVEEFLRTIgfPYT---IGYGMTET--APIISYSPPNRIRlGSAGKVIDGVEVRIDSPDPATGE----- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 467 vprGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCP- 544
Cdd:cd05914 308 ---GEIIVRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPf 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 545 -LIAQIWVygnsFESFLVGVVVPDRKAIEDWAKLNyqsPNDFESLCQNLkaqkyfLDELNSTAKQY-QLKGFEmlkaIHL 622
Cdd:cd05914 385 vLESLVVV----QEKKLVALAYIDPDFLDVKALKQ---RNIIDAIKWEV------RDKVNQKVPNYkKISKVK----IVK 447
|
570 580
....*....|....*....|
gi 22330132 623 EPNPfdierdlITPTFKLKR 642
Cdd:cd05914 448 EEFE-------KTPKGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
224-607 |
6.45e-52 |
|
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: 182.48 E-value: 6.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHcydqVMEIYFL-----SRGSSVG 298
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEG-----DVFLSTLPLFH----IGGLFGLlgallAGGTVVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 299 YWRGDIRYLMDDVQALKPTVFCGVPRVYDKLyagimqkisasglirkklfdfaynyklgnmrkgfSQEEASPRLDrlmFD 378
Cdd:cd04433 72 LPKFDPEAALELIEREKVTILLGVPTLLARL----------------------------------LKAPESAGYD---LS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 379 KIKealggrahMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMV-GTVGVPMPTVEARLVSvPE 457
Cdd:cd04433 115 SLR--------ALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKpGSVGRPVPGVEVRIVD-PD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 458 MGYDAFSadvPRGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLE 537
Cdd:cd04433 186 GGELPPG---EIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 538 NTYSRCPLIAQIWVYGnsfesflvgvvVPDRKAIED---WAKLNYQSPNDFESLCQNLKAQKY---------FLDEL--N 603
Cdd:cd04433 262 AVLLGHPGVAEAAVVG-----------VPDPEWGERvvaVVVLRPGADLDAEELRAHVRERLApykvprrvvFVDALprT 330
|
....
gi 22330132 604 STAK 607
Cdd:cd04433 331 ASGK 334
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
80-649 |
4.42e-51 |
|
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: 186.47 E-value: 4.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQ- 158
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 EKTVSSILSCQKGCSSnLKTIVSFGEVSSTQKEEAKnqcvsLFSWNEFSLMG--------NLDEANLPRKRKTDICTIMY 230
Cdd:cd17641 92 EEQVDKLLEIADRIPS-VRYVIYCDPRGMRKYDDPR-----LISFEDVVALGraldrrdpGLYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 231 TSGTTGEPKGVILNNAAISVQVLSidkMLEVTDRSCDtsDVFFSYLPLAHCYDQVMEI-YFLSRGSSVGYWRgDIRYLMD 309
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAA---YLAADPLGPG--DEYVSVLPLPWIGEQMYSVgQALVCGFIVNFPE-EPETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 310 DVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYN--YKLGNMRKGFSQEEASPRL-----DRLMFDKIKE 382
Cdd:cd17641 240 DLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRALDRGKRGRPVSLWLRLaswlaDALLFRPLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 383 ALG-GRAHMLLSGAAPLPRHVEEFLRIIpASNLSQGYGLTESCGGSFTTLAGVFSMvGTVGVPMPTVEARLVSVpemgyd 461
Cdd:cd17641 320 RLGfSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVDP-DTVGVPFPGTEVRIDEV------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 462 afsadvprGEICLRGNSMFSGYHKRQDLTDQ-VLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTY 540
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 541 SRCPLIAQIWVYGNSFEsFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYF---LDELNST-AKQYQLKGFEM 616
Cdd:cd17641 464 KFSPYIAEAVVLGAGRP-YLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIrkeVEKVNASlPEAQRIRRFLL 542
|
570 580 590
....*....|....*....|....*....|...
gi 22330132 617 LkaiHLEPNPFDIErdlITPTFKLKRPQLLQHY 649
Cdd:cd17641 543 L---YKELDADDGE---LTRTRKVRRGVIAEKY 569
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
79-522 |
4.84e-51 |
|
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: 183.92 E-value: 4.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 79 WITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVq 158
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 ektvssilscqkgcssnlktIVSFGEVSSTQKeeaknqcvslfswnefslmgnlDEANLPRKRKTDICTIMYTSGTTGEP 238
Cdd:cd05936 103 --------------------AVSFTDLLAAGA----------------------PLGERVALTPEDVAVLQYTSGTTGVP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGVILNNAAISVQVLSIDKMLEVTDRSCDtsdVFFSYLPLAHCYDQ--VMEIYFLSRGSSVGYWRGDIRYLMDDVQALKP 316
Cdd:cd05936 141 KGAMLTHRNLVANALQIKAWLEDLLEGDD---VVLAALPLFHVFGLtvALLLPLALGATIVLIPRFRPIGVLKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 317 TVFCGVPrvydKLYAGIMQkisasglirkklfdfaynyklgnmrkgfsqeeaSPRLDRLMFDKIKEALggrahmllSGAA 396
Cdd:cd05936 218 TIFPGVP----TMYIALLN---------------------------------APEFKKRDFSSLRLCI--------SGGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 397 PLPRHVEEFLRIIPASNLSQGYGLTESC-GGSFTTLAGVfSMVGTVGVPMPTVEARLVsvpemgyDAFSADVPR---GEI 472
Cdd:cd05936 253 PLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGP-RKPGSIGIPLPGTEVKIV-------DDDGEELPPgevGEL 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 22330132 473 CLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:cd05936 325 WVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
80-572 |
2.76e-47 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 172.79 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFvqe 159
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd17631 98 ---------------------------------------------------------------DDLALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIdkmleVTDRSCDTSDVFFSYLPLAHCY-DQVMEIYFLSRGSSVGYWRG-DIRYLMDDVQALKPT 317
Cdd:cd17631 115 GAMLTHRNLLWNAVNA-----LAALDLGPDDVLLVVAPLFHIGgLGVFTLPTLLRGGTVVILRKfDPETVLDLIERHRVT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 318 VFCGVPRVYDklyagimqkisasGLIRKKLFDfayNYKLGNMRKgfsqeeasprldrlmfdkikealggrahmLLSGAAP 397
Cdd:cd17631 190 SFFLVPTMIQ-------------ALLQHPRFA---TTDLSSLRA-----------------------------VIYGGAP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 398 LPrhvEEFLRIIPASN--LSQGYGLTESCGG-SFTTLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVP---RGE 471
Cdd:cd17631 225 MP---ERLLRALQARGvkFVQGYGMTETSPGvTFLSPEDHRRKLGSAGRPVFFVEVRIV-------DPDGREVPpgeVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 472 ICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLIAQIWV 551
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAV 373
|
490 500
....*....|....*....|.
gi 22330132 552 YGnsfesflvgvvVPDRKAIE 572
Cdd:cd17631 374 IG-----------VPDEKWGE 383
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
80-523 |
6.87e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 159.30 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILScQKGCSSNLKTIVSFgevsstQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRkRKTDICTIMYTSGTTGEPK 239
Cdd:PRK07656 111 LFLGVDYS-ATTRLPALEHVVIC------ETEEDDPHTEKMKTFTDFLAAGDPAERAPEV-DPDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILN------NAAISVQVLSI---DKMLEVtdrscdtsdvffsyLPLAH--CYDQVMeIYFLSRGSSV-GYWRGDIRYL 307
Cdd:PRK07656 183 GAMLThrqllsNAADWAEYLGLtegDRYLAA--------------NPFFHvfGYKAGV-NAPLMRGATIlPLPVFDPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 308 MDDVQALKPTVFCGVPRVYDKLYAgimqkisasgLIRKKLFDFAynyklgnmrkgfsqeeaSPRLdrlmfdkikealggr 387
Cdd:PRK07656 248 FRLIETERITVLPGPPTMYNSLLQ----------HPDRSAEDLS-----------------SLRL--------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 388 ahmLLSGAAPLP-RHVEEFLRIIPASNLSQGYGLTESCG-GSFTTLAGVFSMV-GTVGVPMPTVEARLVSvpEMGYDAFS 464
Cdd:PRK07656 286 ---AVTGAASMPvALLERFESELGVDIVLTGYGLSEASGvTTFNRLDDDRKTVaGTIGTAIAGVENKIVN--ELGEEVPV 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 465 ADVprGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIF 523
Cdd:PRK07656 361 GEV--GELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
80-522 |
8.40e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 145.53 E-value: 8.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYV---PLYdslgvNAVE----FIINHAEV 152
Cdd:PRK05605 58 TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLY-----TAHElehpFEDHGARV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 153 slVFVQEKTVSSILSCQKGcsSNLKTIVSFGEVSS-----------------TQKEEAKNQCVSLFSWNEF---SLMGNL 212
Cdd:PRK05605 133 --AIVWDKVAPTVERLRRT--TPLETIVSVNMIAAmpllqrlalrlpipalrKARAALTGPAPGTVPWETLvdaAIGGDG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 213 DEANLPRKRKTDICTIMYTSGTTGEPKGVILN------NAAIS---VQVLSidkmlevtdrscDTSDVFFSYLPLAHCYD 283
Cdd:PRK05605 209 SDVSHPRPTPDDVALILYTSGTTGKPKGAQLThrnlfaNAAQGkawVPGLG------------DGPERVLAALPMFHAYG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 284 QVMEIYF--LSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKlyagIMQKISASGLirkklfdfaynyKLGNMRK 361
Cdd:PRK05605 277 LTLCLTLavSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEK----IAEAAEERGV------------DLSGVRN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 362 GFSqeeasprldrlmfdkikealggrahmllsGAAPLPRHVEEFLRIIPASNLSQGYGLTES----CGGSFTTLAgvfsM 437
Cdd:PRK05605 341 AFS-----------------------------GAMALPVSTVELWEKLTGGLLVEGYGLTETspiiVGNPMSDDR----R 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 438 VGTVGVPMPTVEARLVSvPEmgydAFSADVP---RGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMK 514
Cdd:PRK05605 388 PGYVGVPFPDTEVRIVD-PE----DPDETMPdgeEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIR 462
|
....*...
gi 22330132 515 IIDRKKNI 522
Cdd:PRK05605 463 IVDRIKEL 470
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
78-572 |
1.94e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 143.53 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 78 TWiTYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV 157
Cdd:PRK08316 36 SW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 QEKTVSSILScqkgcSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSWnefsLMGNLDEANLPRKRKTDICTIMYTSGTTGE 237
Cdd:PRK08316 115 DPALAPTAEA-----ALALLPVDTLILSLVLGGREAPGGWLDFADW----AEAGSVAEPDVELADDDLAQILYTSGTESL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 238 PKGVILNNAAISVQVLSIdkmleVTDRSCDTSDVFFSYLPLAHC--YDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQALK 315
Cdd:PRK08316 186 PKGAMLTHRALIAEYVSC-----IVAGDMSADDIPLHALPLYHCaqLDVFLGPYLYVGATNVILDAPDPELILRTIEAER 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 316 PTVFCGVPRVYdklyagimqkISasgLIRKKLFDfayNYKLGNMRKGFSqeeasprldrlmfdkikealggrahmllsGA 395
Cdd:PRK08316 261 ITSFFAPPTVW----------IS---LLRHPDFD---TRDLSSLRKGYY-----------------------------GA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 396 APLPRHV-EEFLRIIPASNLSQGYGLTEscggsFTTLAGVFS------MVGTVGVPMPTVEARLVsvpemgyDAFSADVP 468
Cdd:PRK08316 296 SIMPVEVlKELRERLPGLRFYNCYGQTE-----IAPLATVLGpeehlrRPGSAGRPVLNVETRVV-------DDDGNDVA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 469 R---GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPL 545
Cdd:PRK08316 364 PgevGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASREVEEALYTHPA 442
|
490 500
....*....|....*....|....*..
gi 22330132 546 IAQIWVYGnsfesflvgvvVPDRKAIE 572
Cdd:PRK08316 443 VAEVAVIG-----------LPDPKWIE 458
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
80-607 |
9.48e-36 |
|
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: 140.12 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVD-PGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFvq 158
Cdd:cd05941 12 ITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 ektvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrktDICTIMYTSGTTGEP 238
Cdd:cd05941 90 -----------------------------------------------------------------DPALILYTSGTTGRP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGVILNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAHcydqVMEIYF-----LSRGSSVGYWRGDIRYLMDDVQA 313
Cdd:cd05941 105 KGVVLTHANLAANVRALVDAWRWTE-----DDVLLHVLPLHH----VHGLVNallcpLFAGASVEFLPKFDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 314 LKP-TVFCGVPRVYDKLYAGIMQKISASGLIRKklfdfaynyklgnmrkgfsqeeASPRLDRLMfdkikealggrahmlL 392
Cdd:cd05941 176 MPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARA----------------------AAAERLRLM---------------V 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFLRIIPASNLSQGYGLTE-----SCGgsfttLAGVfSMVGTVGVPMPTVEARLVSvPEMGYDAFSADV 467
Cdd:cd05941 219 SGSAALPVPTLEEWEAITGHTLLERYGMTEigmalSNP-----LDGE-RRPGTVGMPLPGVQARIVD-EETGEPLPRGEV 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 468 prGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKK-NIFKlSQGEYVAVENLENTYSRCPL 545
Cdd:cd05941 292 --GEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPG 368
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330132 546 IAQIWVYGNSFESF---LVGVVVPdRKAIEDWaklnyqspnDFESLCQNLKAQ--KY-------FLDEL--NSTAK 607
Cdd:cd05941 369 VSECAVIGVPDPDWgerVVAVVVL-RAGAAAL---------SLEELKEWAKQRlaPYkrprrliLVDELprNAMGK 434
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
80-524 |
1.97e-35 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 140.45 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILScqkgcsSNLKTIVSfgevsstqkEEAKNqcVSLFSWnefSLMGNLDEANLPRKR--KTDICTIMYTSGTTGE 237
Cdd:cd05904 113 ELAEKLAS------LALPVVLL---------DSAEF--DSLSFS---DLLFEADEAEPPVVVikQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 238 PKGVILNN----AAISVQVLSIDKMLEVtdrscdtSDVFFSYLPLAHCYDQVMEIY-FLSRGSS-VGYWRGDIRYLMDDV 311
Cdd:cd05904 173 SKGVMLTHrnliAMVAQFVAGEGSNSDS-------EDVFLCVLPMFHIYGLSSFALgLLRLGATvVVMPRFDLEELLAAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 312 QALKPTVFCGVPRvydklyagIMQKISASGLIRKklfdfaynYKLGNMRkgfsqeeasprldrlmfdkikealggrahML 391
Cdd:cd05904 246 ERYKVTHLPVVPP--------IVLALVKSPIVDK--------YDLSSLR-----------------------------QI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 392 LSGAAPLPRHVEE-FLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMV--GTVGVPMPTVEARLVSvPEMGydafsADVP 468
Cdd:cd05904 281 MSGAAPLGKELIEaFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAkyGSVGRLVPNVEAKIVD-PETG-----ESLP 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 469 ---RGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFK 524
Cdd:cd05904 355 pnqTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
66-553 |
1.69e-32 |
|
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: 131.98 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 66 QRVTTDSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEF 145
Cdd:cd12119 12 REIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 146 IINHAEVSLVFVqEKTVSSILSCQKGCSSNLKTIVSFGEVSSTQKEEAKNQCvslfSWNEFsLMGNLDEANLPRKRKTDI 225
Cdd:cd12119 92 IINHAEDRVVFV-DRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVL----AYEEL-LAAESPEYDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 226 CTIMYTSGTTGEPKGVILNNAAI---SVQVLSIDKMlevtdrSCDTSDVFFSYLPLAHCY-------------DQVMEIY 289
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLvlhAMAALLTDGL------GLSESDVVLPVVPMFHVNawglpyaaamvgaKLVLPGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 290 FLSRGSsvgywrgdIRYLMDdvqALKPTVFCGVPRVYdklyAGIMQKISASGlirkklfdfaynYKLGNMRKgfsqeeas 369
Cdd:cd12119 240 YLDPAS--------LAELIE---REGVTFAAGVPTVW----QGLLDHLEANG------------RDLSSLRR-------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 370 prldrlmfdkikealggrahMLLSGAAPLPRHVEEFLRIIpaSNLSQGYGLTESCG-GSFTTLAGVFSMVG--------- 439
Cdd:cd12119 285 --------------------VVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETSPlGTVARPPSEHSNLSedeqlalra 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 440 TVGVPMPTVEARLVSV--PEMGYDAFSAdvprGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIID 517
Cdd:cd12119 343 KQGRPVPGVELRIVDDdgRELPWDGKAV----GELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITD 418
|
490 500 510
....*....|....*....|....*....|....*.
gi 22330132 518 RKKNIFKlSQGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:cd12119 419 RSKDVIK-SGGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
80-518 |
5.28e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 131.00 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ------KTVSS---ILSCQKGCSSNLKTIVsfgeVSSTQKEEAKNQCVslfSWNEfsLMGNLDEANLPRKRK-TDICTIM 229
Cdd:COG0365 120 gglrggKVIDLkekVDEALEELPSLEHVIV----VGRTGADVPMEGDL---DWDE--LLAAASAEFEPEPTDaDDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 230 YTSGTTGEPKGVILNNAAISVQVLSIDKM---LEVTDRSCDTSDVFF----SYLplahcydqvmeIYF-LSRGSSVGYWR 301
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKYvldLKPGDVFWCTADIGWatghSYI-----------VYGpLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 302 GDIRY-----LMDDVQALKPTVFCGVPRVYDKLyagimqkisasgliRKKLFDFAYNYKLGNMRKGFSQEEAsprLDRLM 376
Cdd:COG0365 260 GRPDFpdpgrLWELIEKYGVTVFFTAPTAIRAL--------------MKAGDEPLKKYDLSSLRLLGSAGEP---LNPEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 377 FDKIKEALGgrahmllsgaaplprhveefLRIIpasnlsQGYGLTEsCGGSFTTLAGVFSMV-GTVGVPMPTVEARLVsv 455
Cdd:COG0365 323 WEWWYEAVG--------------------VPIV------DGWGQTE-TGGIFISNLPGLPVKpGSMGKPVPGYDVAVV-- 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 456 pemgyDAFSADVPR---GEICLRGN--SMFSGYHKRQDLTDQV---LIDGWFHTGDIGEWQEDGSMKIIDR 518
Cdd:COG0365 374 -----DEDGNPVPPgeeGELVIKGPwpGMFRGYWNDPERYRETyfgRFPGWYRTGDGARRDEDGYFWILGR 439
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-553 |
6.11e-32 |
|
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: 128.56 E-value: 6.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFvqe 159
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd05934 81 ---------------------------------------------------------------VDPASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVIL-NNAAISVQVLSIDKMlEVTDrscdtSDVFFSYLPLAHCYDQVMEIY-FLSRGSSV---------GYWrgdirylm 308
Cdd:cd05934 98 GVVItHANLTFAGYYSARRF-GLGE-----DDVYLTVLPLFHINAQAVSVLaALSVGATLvllprfsasRFW-------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 309 DDVQALKPTVFCGVPRVYDKLYAgimqkisasglirkklfdfaynyklgnmrkgfsqeeASPRLDRlmfdkikealggRA 388
Cdd:cd05934 164 SDVRRYGATVTNYLGAMLSYLLA------------------------------------QPPSPDD------------RA 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 389 HML--LSGAAPLPRHVEEFLRI--IPasnLSQGYGLTESCGGSFTTLaGVFSMVGTVGVPMPTVEARLVsvpemgyDAFS 464
Cdd:cd05934 196 HRLraAYGAPNPPELHEEFEERfgVR---LLEGYGMTETIVGVIGPR-DEPRRPGSIGRPAPGYEVRIV-------DDDG 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 465 ADVPR---GEICLR---GNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLEN 538
Cdd:cd05934 265 QELPAgepGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVER 343
|
490
....*....|....*
gi 22330132 539 TYSRCPLIAQIWVYG 553
Cdd:cd05934 344 AILRHPAVREAAVVA 358
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
81-577 |
1.51e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 129.51 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEK 160
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 TVSS------------ILSCQKGCSSN-----LKTIVSFGevsstqKEEAKNqcvsLFSWNEFSLMGN------LDEANL 217
Cdd:PRK12583 127 FKTSdyhamlqellpgLAEGQPGALACerlpeLRGVVSLA------PAPPPG----FLAWHELQARGEtvsreaLAERQA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 218 PRKRKtDICTIMYTSGTTGEPKGV------ILNNAAISVQVLSidkmLEVTDRSCDTsdvffsyLPLAHCYDQVM-EIYF 290
Cdd:PRK12583 197 SLDRD-DPINIQYTSGTTGFPKGAtlshhnILNNGYFVAESLG----LTEHDRLCVP-------VPLYHCFGMVLaNLGC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 291 LSRGSSVGYWRGDIRYL--MDDVQALKPTVFCGVPRVYdklyagimqkISASGLIRKKLFDfaynykLGNMRKGfsqeea 368
Cdd:PRK12583 265 MTVGACLVYPNEAFDPLatLQAVEEERCTALYGVPTMF----------IAELDHPQRGNFD------LSSLRTG------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 369 sprldrLMfdkikealggrahmllsGAAPLPRHVEEflRIIPASNLSQ---GYGLTESCGGSFTTLAG--VFSMVGTVGV 443
Cdd:PRK12583 323 ------IM-----------------AGAPCPIEVMR--RVMDEMHMAEvqiAYGMTETSPVSLQTTAAddLERRVETVGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 444 PMPTVEARLVsvpemgyDAFSADVPRGEI---CLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRK 519
Cdd:PRK12583 378 TQPHLEVKVV-------DPDGATVPRGEIgelCTRGYSVMKGYWNNPEATAESIDeDGWMHTGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 520 KNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGnsfesflvgvvVPDRKAIED---WAKL 577
Cdd:PRK12583 451 KDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEKYGEEivaWVRL 499
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
54-607 |
1.87e-31 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 129.18 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 54 AVKKYpnEQMLGQRVTTDSKVGpyTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVP 133
Cdd:cd17642 23 AMKRY--ASVPGTIAFTDAHTG--VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 134 LYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCQKGCSSnLKTIVsfgeVSSTQKEEAKNQCvsLFSWNEFSLMGNLD 213
Cdd:cd17642 99 TNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKI-IKTII----ILDSKEDYKGYQC--LYTFITQNLPPGFN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 214 EANLPR---KRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSCDTSdvFFSYLPLAHCYDQVMEIYF 290
Cdd:cd17642 172 EYDFKPpsfDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTA--ILTVIPFHHGFGMFTTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 291 LSRGSSVGYwrgdirylmddvqalkptvfcgVPRVYDKLYAGIMQKISA-SGLIRKKLFDFaynyklgnmrkgFSQeeaS 369
Cdd:cd17642 250 LICGFRVVL----------------------MYKFEEELFLRSLQDYKVqSALLVPTLFAF------------FAK---S 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 370 PRLDRLMFDKIKEalggrahmLLSGAAPLPRHVEEFL-RIIPASNLSQGYGLTESCGGSFTTLAGvFSMVGTVGVPMPTV 448
Cdd:cd17642 293 TLVDKYDLSNLHE--------IASGGAPLSKEVGEAVaKRFKLPGIRQGYGLTETTSAILITPEG-DDKPGAVGKVVPFF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 449 EARLVSvPEMGyDAFSADvPRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLsQ 527
Cdd:cd17642 364 YAKVVD-LDTG-KTLGPN-ERGELCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-K 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 528 GEYVAVENLENTYSRCPLIAQIWVYG----NSFESFLVGVVVPDRKAIEDWAKLNYQSPNdfESLCQNLKAQKYFLDEL- 602
Cdd:cd17642 440 GYQVPPAELESILLQHPKIFDAGVAGipdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ--VSTAKRLRGGVKFVDEVp 517
|
....*.
gi 22330132 603 -NSTAK 607
Cdd:cd17642 518 kGLTGK 523
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
80-522 |
2.05e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 123.22 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYV---PLYDSlgvNAVEFIINHAE----- 151
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTE---RELEYQLHDSGakvil 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 152 -VSLVFVQEKTVSSILSCQKGCSSNLKTIVSFGE---VSSTQKEEAK-----NQCVSLFSWNefSLMGNLDEA-NLPRKR 221
Cdd:PRK06710 127 cLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKnllYPFVQKKQSNlvvkvSESETIHLWN--SVEKEVNTGvEVPCDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 222 KTDICTIMYTSGTTGEPKGVILNNA-AISVQVLSIDKMLEVTDrscdTSDVFFSYLPLAHCYDQ--VMEIYFLSRGSSVG 298
Cdd:PRK06710 205 ENDLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKE----GEEVVLGVLPFFHVYGMtaVMNLSIMQGYKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 299 YWRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKisasglirkklfdfayNYKLGNMRKgfsqeeasprldrlmfd 378
Cdd:PRK06710 281 IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLK----------------EYDISSIRA----------------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 379 kikealggrahmLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVpEM 458
Cdd:PRK06710 328 ------------CISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL-ET 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330132 459 GYDAFSADVprGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:PRK06710 395 GEALPPGEI--GEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
81-576 |
2.13e-29 |
|
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: 121.40 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFvqek 160
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 tvssilscqkgCSSNLK----TIVSFGEVSSTQKEEAknqcvslfswnEFSLMGNLDeanlprkrktDICTIMYTSGTTG 236
Cdd:TIGR01923 77 -----------TDSLLEekdfQADSLDRIEAAGRYET-----------SLSASFNMD----------QIATLMFTSGTTG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 237 EPKGV------ILNNAAISVQVLSIDKmlevtdrscdtSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRyLMDD 310
Cdd:TIGR01923 125 KPKAVphtfrnHYASAVGSKENLGFTE-----------DDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ-LLEM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 311 VQALKPTVFCGVPrvydKLYAGIMQKISASGLIRKKLfdfaynyklgnmrkgfsqeeasprldrlmfdkikeaLGGrahm 390
Cdd:TIGR01923 193 IANERVTHISLVP----TQLNRLLDEGGHNENLRKIL------------------------------------LGG---- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 llsGAAPLPRHVEEFLRIIPasnLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLvSVPEMgydafsadVPRG 470
Cdd:TIGR01923 229 ---SAIPAPLIEEAQQYGLP---IYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKI-KVDNK--------EGHG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 471 EICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIW 550
Cdd:TIGR01923 294 EIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAV 372
|
490 500 510
....*....|....*....|....*....|...
gi 22330132 551 V-------YGNSFESFLVGVVVPDRKAIEDWAK 576
Cdd:TIGR01923 373 VvpkpdaeWGQVPVAYIVSESDISQAKLIAYLT 405
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
54-569 |
1.34e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.48 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 54 AVKKYPNEQMLgqrvttdskVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVP 133
Cdd:PRK06188 21 ALKRYPDRPAL---------VLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 134 LYDSLGVNAVEFIINHAEVS-LVFVQEKTVSSILSCQKGCSSnLKTIVSFGEVsstqkEEAknqcVSLfsWNEFSLMGN- 211
Cdd:PRK06188 92 LHPLGSLDDHAYVLEDAGIStLIVDPAPFVERALALLARVPS-LKHVLTLGPV-----PDG----VDL--LAAAAKFGPa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 212 -LDEANLPrkrkTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRScdtsdvffSYL---PLAHcydqVME 287
Cdd:PRK06188 160 pLVAAALP----PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADP--------RFLmctPLSH----AGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 288 IYFLsrgssVGYWRGDIRYLmddVQALKPTVFCgvpRVYDKlyagimQKISASGLIRKKLfdfaynYKLGNmrkgfsqee 367
Cdd:PRK06188 224 AFFL-----PTLLRGGTVIV---LAKFDPAEVL---RAIEE------QRITATFLVPTMI------YALLD--------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 368 aSPRLDRLMFDKIKealggrahMLLSGAAPL-P-RHVEEFLRIIPAsnLSQGYGLTEsCGGSFTTLA---------GVFs 436
Cdd:PRK06188 272 -HPDLRTRDLSSLE--------TVYYGASPMsPvRLAEAIERFGPI--FAQYYGQTE-APMVITYLRkrdhdpddpKRL- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 437 mvGTVGVPMPTVEARLVsvpemgyDAFSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSM 513
Cdd:PRK06188 339 --TSCGRPTPGLRVALL-------DEDGREVAQgevGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFY 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 22330132 514 KIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGnsfesflvgvvVPDRK 569
Cdd:PRK06188 410 YIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVIG-----------VPDEK 453
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
46-535 |
3.86e-28 |
|
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: 118.56 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 46 SPWQFFSEAVKKYPNeqmlgqRVttdSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACM 125
Cdd:cd12118 5 TPLSFLERAAAVYPD------RT---SIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 126 SQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKtvssilscqkgcssnlktivsfgevsstqkeeaknqcvslFSWNE 205
Cdd:cd12118 76 MAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE----------------------------------------FEYED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 206 FSLMGNLDEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSidkmlEVTDRSCDTSDVFFSYLPLAHC---- 281
Cdd:cd12118 116 LLAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALA-----NILEWEMKQHPVYLWTLPMFHCngwc 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 282 YDQVMeiyFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLyagimqkisasglirkklfdfaynyklGNMRK 361
Cdd:cd12118 191 FPWTV---AAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNML---------------------------ANAPP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 362 gfsqEEASPrldrlmfdkikeaLGGRAHMLLSGAAPLPRHVEEFLRIipASNLSQGYGLTESCGgsfttlagvfsmVGTV 441
Cdd:cd12118 241 ----SDARP-------------LPHRVHVMTAGAPPPAAVLAKMEEL--GFDVTHVYGLTETYG------------PATV 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 442 ----------------------GVPMPTVEARLVSVPEMGydafsADVPR-----GEICLRGNSMFSGYHKRQDLTDQVL 494
Cdd:cd12118 290 cawkpewdelpteerarlkarqGVRYVGLEEVDVLDPETM-----KPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAF 364
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 22330132 495 IDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGE---YVAVEN 535
Cdd:cd12118 365 RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGEnisSVEVEG 407
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
81-609 |
5.57e-28 |
|
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: 117.48 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEk 160
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 tvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnEFslmGNLDEANLPrkrkTDICTIMYTSGTTGEPKG 240
Cdd:cd05903 82 --------------------------------------------RF---RQFDPAAMP----DAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 VILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHC--YDQVMEIYFLSRGSSVgywrgdiryLMDDVQALKptv 318
Cdd:cd05903 111 VMHSHNTLSASIRQYAERLGLGPG-----DVFLVASPMAHQtgFVYGFTLPLLLGAPVV---------LQDIWDPDK--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 319 fcgvprvydklyagIMQKISASGLIrkklFDFAYNYKLGNMRKgfSQEEASPRLDRLMFdkikealggrahmLLSGAAPL 398
Cdd:cd05903 174 --------------ALALMREHGVT----FMMGATPFLTDLLN--AVEEAGEPLSRLRT-------------FVCGGATV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 399 PRHVEEFLRIIPASNLSQGYGLTESCGG-SFTTLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVPR---GEICL 474
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAvTSITPAPEDRRLYTDGRPLPGVEIKVV-------DDTGATLAPgveGELLS 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 475 RGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGN 554
Cdd:cd05903 294 RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAL 372
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 22330132 555 SFESF---LVGVVVPdrkaiEDWAKLnyqspnDFESLCQNLKAQKyfldelnsTAKQY 609
Cdd:cd05903 373 PDERLgerACAVVVT-----KSGALL------TFDELVAYLDRQG--------VAKQY 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-569 |
1.17e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 114.68 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 223 TDICTIMYTSGTTGEPKGV------ILNNAAIsvqvlsIDKMLEVT--DRSCDTsdvffsyLPLAHCYDQVMEIYF-LSR 293
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGAtlthhnIVNNGYF------IGERLGLTeqDRLCIP-------VPLFHCFGSVLGVLAcLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 294 GSSV-----GYwrgDIRYLMDDVQALKPTVFCGVPRVYdklyagimqkISASGLIRKKLFDfaynykLGNMRKGFsqeea 368
Cdd:cd05917 69 GATMvfpspSF---DPLAVLEAIEKEKCTALHGVPTMF----------IAELEHPDFDKFD------LSSLRTGI----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 369 sprldrlmfdkikeaLGGrahmllsgaAPLPRHVEEflRIIPASNLSQ---GYGLTESCGGSFTTLAG--VFSMVGTVGV 443
Cdd:cd05917 125 ---------------MAG---------APCPPELMK--RVIEVMNMKDvtiAYGMTETSPVSTQTRTDdsIEKRVNTVGR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 444 PMPTVEARLVsvpemgyDAFSADVP----RGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDR 518
Cdd:cd05917 179 IMPHTEAKIV-------DPEGGIVPpvgvPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGR 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 22330132 519 KKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGnsfesflvgvvVPDRK 569
Cdd:cd05917 252 IKDMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG-----------VPDER 290
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
80-607 |
1.64e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.88 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSR-GVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQ 158
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 EKTVSSILSCQKgcSSNLKTIVSFGEVSSTQKEEaknqcvslfswnefslMGNLDEANlprkrKTDICTIMYTSGTTGEP 238
Cdd:PRK06839 108 KTFQNMALSMQK--VSYVQRVISITSLKEIEDRK----------------IDNFVEKN-----ESASFIICYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGVILNNAAISVQvlSIDKMLEVTDRSCDTSDVFfsyLPLAHCYDQVMEIY--FLSRGSSVGYWRGDIRYLMDDVQALKP 316
Cdd:PRK06839 165 KGAVLTQENMFWN--ALNNTFAIDLTMHDRSIVL---LPLFHIGGIGLFAFptLFAGGVIIVPRKFEPTKALSMIEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 317 TVFCGVPRVYDKLYAGImqkisasglirkklfDFAynyklgnmrkgfsqeeaSPRLDRLmfdkikealggraHMLLSGAA 396
Cdd:PRK06839 240 TVVMGVPTIHQALINCS---------------KFE-----------------TTNLQSV-------------RWFYNGGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 397 PLP----RHVEEflRIIPasnLSQGYGLTESCGGSFTTLAGVFS-MVGTVGVPMPTVEARLVsvpemgyDAFSADVPRG- 470
Cdd:PRK06839 275 PCPeelmREFID--RGFL---FGQGFGMTETSPTVFMLSEEDARrKVGSIGKPVLFCDYELI-------DENKNKVEVGe 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 471 --EICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQ 548
Cdd:PRK06839 343 vgELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYE 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330132 549 IWVYGNSFE-------SFLV---GVVVPDRKAIEDW-AKL-NYQSPNDFeslcqnlkaqkYFLDEL--NSTAK 607
Cdd:PRK06839 422 VAVVGRQHVkwgeipiAFIVkksSSVLIEKDVIEHCrLFLaKYKIPKEI-----------VFLKELpkNATGK 483
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
75-607 |
4.03e-27 |
|
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: 115.49 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSL 154
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 VFVQEKTVSSilsCQKGCSSNLKTIVSFGEVSSTqkeeaknqCVSLFSWNEFSLMGNLDEANLPRK--RKTDICTIMYTS 232
Cdd:cd05926 90 VLTPKGELGP---ASRAASKLGLAILELALDVGV--------LIRAPSAESLSNLLADKKNAKSEGvpLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 233 GTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscDTSdvfFSYLPLAHCYDQVMEIY--FLSRGSSVGYWRGDIRYLMDD 310
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPD--DRT---LVVMPLFHVHGLVASLLstLAAGGSVVLPPRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 311 VQALKPTVFCGVPRvydklyagIMQKIsasgLIRkklfdfaynyklgnmrkgfSQEEASPRLDRLMFdkIKealggrahm 390
Cdd:cd05926 234 VRDYNATWYTAVPT--------IHQIL----LNR-------------------PEPNPESPPPKLRF--IR--------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 llSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTT-LAGVFSMVGTVGVPmptVEARLVSVPEMGYDAFSADVpr 469
Cdd:cd05926 272 --SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNpLPPGPRKPGSVGKP---VGVEVRILDEDGEILPPGVV-- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 GEICLRGNSMFSGYHKRQDLT-DQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQ 548
Cdd:cd05926 345 GEICLRGPNVTRGYLNNPEANaEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLE 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 549 IWVYGNSFESF---LVGVVVP------DRKAIEDWAKLN---YQSPNDFeslcqnlkaqkYFLDELNSTAK 607
Cdd:cd05926 424 AVAFGVPDEKYgeeVAAAVVLregasvTEEELRAFCRKHlaaFKVPKKV-----------YFVDELPKTAT 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
81-511 |
1.19e-26 |
|
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: 112.74 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSR-GVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCqkgcssnlktivsfgevsstqkeeakNQCVSLFSWNEFSLMGNLDEANLPRKRK--TDICTIMYTSGTTGE 237
Cdd:TIGR01733 81 ALASRLAGL--------------------------VLPVILLDPLELAALDDAPAPPPPDAPSgpDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 238 PKGVILNNAAISVQVLSIDKMLEVtdrscDTSDVFFSYLPLAHcyD-QVMEIYF-LSRGSSV--------GYWRGDIRYL 307
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRYGL-----DPDDRVLQFASLSF--DaSVEEIFGaLLAGATLvvppedeeRDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 308 MDDvqaLKPTVFCGVPRVYDKLyagimqkisasglirkklfdfaynyklgnmrkgfsQEEASPRLDRLmfdkikealggr 387
Cdd:TIGR01733 208 IAE---HPVTVLNLTPSLLALL-----------------------------------AAALPPALASL------------ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 388 AHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTL-----AGVFSMVgTVGVPMPTVEARLVsvpemgyDA 462
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLvdpddAPRESPV-PIGRPLANTRLYVL-------DD 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 463 FSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLIDGWF---------HTGDIGEWQEDG 511
Cdd:TIGR01733 310 DLRPVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRTGDLVRYLPDG 370
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
49-520 |
1.35e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 114.52 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNEQMLgqrVTTDSKvgpYTWiTYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG 128
Cdd:PRK08315 20 QLLDRTAARYPDREAL---VYRDQG---LRW-TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 129 ITYV---PLYDSlgvNAVEFIINHAEVSLVFVQE--KTVS--SIL--------SCQKGCSS-----NLKTIVSFGEVSST 188
Cdd:PRK08315 93 AILVtinPAYRL---SELEYALNQSGCKALIAADgfKDSDyvAMLyelapelaTCEPGQLQsarlpELRRVIFLGDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 189 qkeeaknqcvSLFSWNEFSLMG-NLDEANLPRKRKT----DICTIMYTSGTTGEPKGV------ILNNAaisvqvLSIDK 257
Cdd:PRK08315 170 ----------GMLNFDELLALGrAVDDAELAARQATldpdDPINIQYTSGTTGFPKGAtlthrnILNNG------YFIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 258 MLEVT--DRSCDTsdvffsyLPLAHCYDQVM-EIYFLSRGSSV-----GYwrgDIRYLMDDVQALKPTVFCGVPRVYdkl 329
Cdd:PRK08315 234 AMKLTeeDRLCIP-------VPLYHCFGMVLgNLACVTHGATMvypgeGF---DPLATLAAVEEERCTALYGVPTMF--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 330 yagimqkISASGLIRKKLFDfaynykLGNMRKGfsqeeasprldrLMfdkikealggrahmllsGAAPLPrhVEEFLRII 409
Cdd:PRK08315 301 -------IAELDHPDFARFD------LSSLRTG------------IM-----------------AGSPCP--IEVMKRVI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 410 PASNLSQ---GYGLTESCGGSFTTLAG--VFSMVGTVGVPMPTVEARLVSvPEMGydafsADVPR---GEICLRGNSMFS 481
Cdd:PRK08315 337 DKMHMSEvtiAYGMTETSPVSTQTRTDdpLEKRVTTVGRALPHLEVKIVD-PETG-----ETVPRgeqGELCTRGYSVMK 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 22330132 482 GYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKK 520
Cdd:PRK08315 411 GYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIK 450
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
80-606 |
1.46e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.82 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKgcssnlktiVSFGEVSSTQKEEAKNQcvslfswNEFSLmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:PRK03640 108 DFEAKLIPGIS---------VKFAELMNGPKEEAEIQ-------EEFDL--------------DEVATIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVIL--NN---AAISvQVLSidkmLEVTDRSCdtsdvFFSYLPLAHcydqvmeIYFLS---RgsSVGYwrGDIRYLMDDV 311
Cdd:PRK03640 158 GVIQtyGNhwwSAVG-SALN----LGLTEDDC-----WLAAVPIFH-------ISGLSilmR--SVIY--GMRVVLVEKF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 312 QAlkptvfcgvprvyDKLYAGIMQ-KISASGLIRKKLFDFAYNYKLGNMRKGFsqeeasprldRLMFdkikeaLGGrahm 390
Cdd:PRK03640 217 DA-------------EKINKLLQTgGVTIISVVSTMLQRLLERLGEGTYPSSF----------RCML------LGG---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 llsGAAPLPRHVEEFLRIIPasnLSQGYGLTESCGgSFTTLAGVFSM--VGTVGVPMPTVEARLVsvpEMGYDAFSADVp 468
Cdd:PRK03640 264 ---GPAPKPLLEQCKEKGIP---VYQSYGMTETAS-QIVTLSPEDALtkLGSAGKPLFPCELKIE---KDGVVVPPFEE- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 469 rGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQ 548
Cdd:PRK03640 333 -GEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAE 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330132 549 IWVYGNSFE---SFLVGVVVPDRKAIEDwaklnyqspnDFESLCQN------LKAQKYFLDELNSTA 606
Cdd:PRK03640 411 AGVVGVPDDkwgQVPVAFVVKSGEVTEE----------ELRHFCEEklakykVPKRFYFVEELPRNA 467
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
228-519 |
2.92e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 109.69 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 228 IMYTSGTTGEPKGVILNNAAISVqvlSIDKMLEVTDRSCDtsDVFFSYLPLAHCYDQVMEIY-FLSRGSSV--------- 297
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAA---DLDALAEAWQWTAD--DVLVHGLPLFHVHGLVLGVLgPLRIGNRFvhtgrptpe 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 298 GYWRGdirylmddvQALKPTVFCGVPRVYDKLyagimqkisasglirkklfdfaynyklgnmrkgfSQEEASPRldrlmf 377
Cdd:PRK07787 208 AYAQA---------LSEGGTLYFGVPTVWSRI----------------------------------AADPEAAR------ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 378 dkikeALGGrAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTEscggsftTLAGVFSMV------GTVGVPMPTVEAR 451
Cdd:PRK07787 239 -----ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE-------TLITLSTRAdgerrpGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 452 LVSVP--EMGYDAFSAdvprGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRK 519
Cdd:PRK07787 306 LVDEDggPVPHDGETV----GELQVRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGRE 372
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
78-547 |
1.76e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 108.11 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 78 TWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV 157
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 qEKTVSSILSCQKGCSSNLKTIVsfgeVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRKRKTDICTIMYTSGTTGE 237
Cdd:PRK08162 122 -DTEFAEVAREALALLPGPKPLV----IDVDDPEYPGGRFIGALDYEAFLASGDPDFAWTLPADEWDAIALNYTSGTTGN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 238 PKGVI-------LNnaAISVQVlsidkmlevtdrSCDTSD--VFFSYLPLAHC----YDQVMEIyflSRGSSVGYWRGDI 304
Cdd:PRK08162 197 PKGVVyhhrgayLN--ALSNIL------------AWGMPKhpVYLWTLPMFHCngwcFPWTVAA---RAGTNVCLRKVDP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 305 RYLMDDVQALKPTVFCGVPRVYdklyagimqkisaSGLIrkklfdfaynyklgNMRKGFsqeeasprldrlmfdkiKEAL 384
Cdd:PRK08162 260 KLIFDLIREHGVTHYCGAPIVL-------------SALI--------------NAPAEW-----------------RAGI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 385 GGRAHMLLSGAAPlPRHVEEFLRIIpASNLSQGYGLTESCGGSFT----------TLAGVFSMVGTVGVPMPTVEARLVS 454
Cdd:PRK08162 296 DHPVHAMVAGAAP-PAAVIAKMEEI-GFDLTHVYGLTETYGPATVcawqpewdalPLDERAQLKARQGVRYPLQEGVTVL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 455 VPEMGydafsADVPR-----GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGE 529
Cdd:PRK08162 374 DPDTM-----QPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGE 447
|
490
....*....|....*...
gi 22330132 530 YVAVENLENTYSRCPLIA 547
Cdd:PRK08162 448 NISSIEVEDVLYRHPAVL 465
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
224-537 |
1.81e-24 |
|
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: 107.42 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEvtdrsCDTSDVFFSYLPLAHCYDQVMEIYF-LSRGSSVGYWRG 302
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD-----PNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 303 DIRY-----LMDDVQAlkpTVFCGVPRVYDklyagimqkisasGLIRkklfdFAYNYKLGNMRKGFSQEEAsprLDRLMF 377
Cdd:cd05909 223 PLDYkkipeLIYDKKA---TILLGTPTFLR-------------GYAR-----AAHPEDFSSLRLVVAGAEK---LKDTLR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 378 DKIKEALGGRahmllsgaaplprhveeflriipasnLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPe 457
Cdd:cd05909 279 QEFQEKFGIR--------------------------ILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 458 mGYDAFSADVpRGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLE 537
Cdd:cd05909 332 -THEEVPIGE-GGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIE 408
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-567 |
2.37e-24 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 106.46 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd05930 93 ---------------------------------------------------------------DDLAYVIYTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVTdrscdTSDVFFSYLPLAHcyDQ-VMEIYF-LSRGSSVgYW-----RGDIRYLMDDVQ 312
Cdd:cd05930 110 GVMVEHRGLVNLLLWMQEAYPLT-----PGDRVLQFTSFSF--DVsVWEIFGaLLAGATL-VVlpeevRKDPEALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPRVYdklyagimqkisasglirKKLFDFAYNYKLGNMRkgfsqeeasprldrlmfdkikealggraHMLL 392
Cdd:cd05930 182 EEGITVLHLTPSLL------------------RLLLQELELAALPSLR----------------------------LVLV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGS-FTTLAGVFSMVGTV--GVPMPTVEARLVsvpemgyDAFSADVPR 469
Cdd:cd05930 216 GGEALPPDLVRRWRELLPGARLVNLYGPTEATVDAtYYRVPPDDEEDGRVpiGRPIPNTRVYVL-------DENLRPVPP 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 ---GEICLRGNSMFSGYHKRQDLTDQVLIDGWFH-------TGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENT 539
Cdd:cd05930 289 gvpGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAA 367
|
490 500 510
....*....|....*....|....*....|.
gi 22330132 540 YSRCPLIAQ---IWVYGNSFESFLVGVVVPD 567
Cdd:cd05930 368 LLAHPGVREaavVAREDGDGEKRLVAYVVPD 398
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
80-553 |
3.38e-24 |
|
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: 105.51 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLvfvqe 159
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd05912 77 ---------------------------------------------------------------DDIATIMYTSGTTGKPK 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVTDRSCdtsdvFFSYLPLAHcydqvmeIYFLSrgssvgywrgdirylmddvqALKPTVF 319
Cdd:cd05912 94 GVQQTFGNHWWSAIGSALNLGLTEDDN-----WLCALPLFH-------ISGLS--------------------ILMRSVI 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 320 CGVP-RVYDKlyagimqkisasglirkklFDFAYNYKLGNMRKGFSQEEASPRLDRLMfdkikEALGGRAH-----MLLS 393
Cdd:cd05912 142 YGMTvYLVDK-------------------FDAEQVLHLINSGKVTIISVVPTMLQRLL-----EILGEGYPnnlrcILLG 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 394 GA-APLPRHVEEFLRIIPasnLSQGYGLTESCGgSFTTLAGVFSM--VGTVGVPMPTVEARLVsvpemgyDAFSADVPRG 470
Cdd:cd05912 198 GGpAPKPLLEQCKEKGIP---VYQSYGMTETCS-QIVTLSPEDALnkIGSAGKPLFPVELKIE-------DDGQPPYEVG 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 471 EICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIW 550
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAG 345
|
...
gi 22330132 551 VYG 553
Cdd:cd05912 346 VVG 348
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
79-553 |
1.11e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 104.89 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 79 WiTYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVfvq 158
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 ektvssilscqkgcssnlktivsfgeVSSTQKEEAKNQCVSLFSW-NEFSLMGNLDEANLPRKRktdICTIMYTSGTTGE 237
Cdd:PRK09088 99 --------------------------LGDDAVAAGRTDVEDLAAFiASADALEPADTPSIPPER---VSLILFTSGTSGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 238 PKGVILNNAAISVQVLSIDKMLEVTDRScdtsdVFFSYLPLAHCYDQVMEIY-FLSRGSSVGYWRG-----DIRYLMDdv 311
Cdd:PRK09088 150 PKGVMLSERNLQQTAHNFGVLGRVDAHS-----SFLCDAPMFHIIGLITSVRpVLAVGGSILVSNGfepkrTLGRLGD-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 312 QALKPTVFCGVPRVYDKLYAgimqkisasglirkklfdfaynyklgnmRKGFsqeeASPRLDRLMfdkikealggrahML 391
Cdd:PRK09088 223 PALGITHYFCVPQMAQAFRA----------------------------QPGF----DAAALRHLT-------------AL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 392 LSGAAPlprHVEEFLRI-----IPasnLSQGYGLTEscggsfttlAG-VFSM----------VGTVGVPMPTVEARLVsv 455
Cdd:PRK09088 258 FTGGAP---HAAEDILGwlddgIP---MVDGFGMSE---------AGtVFGMsvdcdvirakAGAAGIPTPTVQTRVV-- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 456 pemgyDAFSADVPRG---EICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYV 531
Cdd:PRK09088 321 -----DDQGNDCPAGvpgELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENV 394
|
490 500
....*....|....*....|..
gi 22330132 532 AVENLENTYSRCPLIAQIWVYG 553
Cdd:PRK09088 395 YPAEIEAVLADHPGIRECAVVG 416
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
80-566 |
1.70e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 103.87 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd05945 97 ---------------------------------------------------------------DDNAYIIFTSGSTGRPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAIsvqVLSIDKMLEVTDRSCDtsDVFFSYLPLAhcYD-QVMEIYF-LSRGSSVgyW------RGDIRYLMDDV 311
Cdd:cd05945 114 GVQISHDNL---VSFTNWMLSDFPLGPG--DVFLNQAPFS--FDlSVMDLYPaLASGATL--VpvprdaTADPKQLFRFL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 312 QALKPTVFCGVPRVydklyagimqkisASGLIRKKLFDfaynyklgnmrkgfsqEEASPRLDrlmfdkikealggraHML 391
Cdd:cd05945 185 AEHGITVWVSTPSF-------------AAMCLLSPTFT----------------PESLPSLR---------------HFL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 392 LSGAaPLP-RHVEEFLRIIPASNLSQGYGLTESCGGSFTT------LAGVFSMvgTVGVPMPtvEARLVSVPEMGYDAFS 464
Cdd:cd05945 221 FCGE-VLPhKTARALQQRFPDARIYNTYGPTEATVAVTYIevtpevLDGYDRL--PIGYAKP--GAKLVILDEDGRPVPP 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 465 ADvpRGEICLRGNSMFSGYHKRQDLTDQVL--IDG--WFHTGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVENLENTY 540
Cdd:cd05945 296 GE--KGELVISGPSVSKGYLNNPEKTAAAFfpDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAAL 372
|
490 500
....*....|....*....|....*....
gi 22330132 541 SRCPLIAQ---IWVYGNSFESFLVGVVVP 566
Cdd:cd05945 373 RQVPGVKEavvVPKYKGEKVTELIAFVVP 401
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
81-546 |
2.18e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.44 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV--- 157
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 --QEKTVSSILSCQKGCSSnLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMGNLDeanlprkrktDICTIMYTSGTT 235
Cdd:PRK06087 131 fkQTRPVDLILPLQNQLPQ-LQQIVGVDKLAPATSSLSLSQIIADYEPLTTAITTHGD----------ELAAVLFTSGTE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 236 GEPKGVILNNAAISVQVLSIDKMLEVTdrscdTSDVFFSYLPLAHC--YDQVMEIYFLSRGSSVgywrgdiryLMDD--- 310
Cdd:PRK06087 200 GLPKGVMLTHNNILASERAYCARLNLT-----WQDVFMMPAPLGHAtgFLHGVTAPFLIGARSV---------LLDIftp 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 311 VQAL------KPTVFCG-VPRVYDKLyagimqkisasglirKKLfdfaynyklgnmrkgfsqEEASPRLDRLMFdkikea 383
Cdd:PRK06087 266 DACLalleqqRCTCMLGaTPFIYDLL---------------NLL------------------EKQPADLSALRF------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 384 lggrahmLLSGAAPLPRHV--EEFLRIIpasNLSQGYGLTESCGGSFTTLAGVFS-MVGTVGVPMPTVEARLVsvpemgy 460
Cdd:PRK06087 307 -------FLCGGTTIPKKVarECQQRGI---KLLSVYGSTESSPHAVVNLDDPLSrFMHTDGYAAAGVEIKVV------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 461 DAFSADVPRG---EICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENL 536
Cdd:PRK06087 370 DEARKTLPPGcegEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREV 448
|
490
....*....|
gi 22330132 537 ENTYSRCPLI 546
Cdd:PRK06087 449 EDILLQHPKI 458
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
80-567 |
3.52e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 104.09 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVqE 159
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT-E 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKGCSSNLKTIVSFGEVSSTqkeeaknqcvSLFSWNEfsLMGNLDEANLPRKRKTDI-CTIMYTSGTTGEP 238
Cdd:PRK07786 122 AALAPVATAVRDIVPLLSTVVVAGGSSDD----------SVLGYED--LLAEAGPAHAPVDIPNDSpALIMYTSGTTGRP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGVILNNAAISVQVLsidkMLEVTDRSCDTSDVFFSYLPLAHCYD-QVMEIYFLSRGSSVGYWRG--DIRYLMDDVQALK 315
Cdd:PRK07786 190 KGAVLTHANLTGQAM----TCLRTNGADINSDVGFVGVPLFHIAGiGSMLPGLLLGAPTVIYPLGafDPGQLLDVLEAEK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 316 PT-VFCgVPRVYdklyagimQKISAsglirkklfdfaynyklgnmrkgfsQEEASPRLDRLmfdkikealggraHMLLSG 394
Cdd:PRK07786 266 VTgIFL-VPAQW--------QAVCA-------------------------EQQARPRDLAL-------------RVLSWG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 395 AAPLPRHV-EEFLRIIPASNLSQGYGLTE----SCggsftTLAG--VFSMVGTVGVPMPTVEARLVsvpemgyDAFSADV 467
Cdd:PRK07786 299 AAPASDTLlRQMAATFPEAQILAAFGQTEmspvTC-----MLLGedAIRKLGSVGKVIPTVAARVV-------DENMNDV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 468 PRG---EICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCP 544
Cdd:PRK07786 367 PVGevgEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHP 445
|
490 500
....*....|....*....|....*.
gi 22330132 545 LIAQIWVYGNSFESF---LVGVVVPD 567
Cdd:PRK07786 446 DIVEVAVIGRADEKWgevPVAVAAVR 471
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
79-577 |
4.57e-23 |
|
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: 102.75 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 79 WITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQ 158
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 EKTVSSILSCQKGcssnlktivsfgevsstqkeeaknqcVSLFSWNEFSLMGNLDEANLPRkrktDICTIMYTSGTTGEP 238
Cdd:cd12116 92 DALPDRLPAGLPV--------------------------LLLALAAAAAAPAAPRTPVSPD----DLAYVIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGVILNNAAISVQVLSI---------DKMLEVTDRSCDTSdVFFSYLPL---AHCydqvmeiYFLSRGSSVgywrgDIRY 306
Cdd:cd12116 142 KGVVVSHRNLVNFLHSMrerlglgpgDRLLAVTTYAFDIS-LLELLLPLlagARV-------VIAPRETQR-----DPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 307 LMDDVQALKPTVfcgvprvydklyagiMQkisasglirkklfdfaynyklgnmrkgfsqeeASPRLDRLMFDkikEALGG 386
Cdd:cd12116 209 LARLIEAHSITV---------------MQ--------------------------------ATPATWRMLLD---AGWQG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 387 RAHM-LLSGAAPLPRHVEEFLrIIPASNLSQGYGLTEscggsfTTLAGVFSMVG------TVGVPMP-----TVEARLVS 454
Cdd:cd12116 239 RAGLtALCGGEALPPDLAARL-LSRVGSLWNLYGPTE------TTIWSTAARVTaaagpiPIGRPLAntqvyVLDAALRP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 455 VPemgydafsADVPrGEICLRGNSMFSGYHKRQDLTDQVLIDG--------WFHTGDIGEWQEDGSMKIIDRKKNIFKLs 526
Cdd:cd12116 312 VP--------PGVP-GELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI- 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 22330132 527 QGEYVAVENLENTYSRCPLIAQ--IWVYGNSFESFLVGVVVPDRKAIEDWAKL 577
Cdd:cd12116 382 RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAAL 434
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
81-537 |
8.16e-23 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 102.75 E-value: 8.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG---ITYVPLYDSLGvnavefIINHAEVS---L 154
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGavtTTANPFYTPAE------IAKQAKASgakL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 VFVQektvssilSCQkgcSSNLKTIVSFGEVSSTQKEEAKNQCVSlfswneFSLMGNLDEANLPRKR--KTDICTIMYTS 232
Cdd:PLN02246 126 IITQ--------SCY---VDKLKGLAEDDGVTVVTIDDPPEGCLH------FSELTQADENELPEVEisPDDVVALPYSS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 233 GTTGEPKGVILNN----AAISVQVLSIDKMLEVTdrscdTSDVFFSYLPLAHCY--DQVMeIYFLSRGSSVGYWRG-DIR 305
Cdd:PLN02246 189 GTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFH-----SDDVILCVLPMFHIYslNSVL-LCGLRVGAAILIMPKfEIG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 306 YLMDDVQALKPTVFCGVPRvydklyagIMQKISASglirkklfDFAYNYKLGNMRkgfsqeeasprldrlmfdkikealg 385
Cdd:PLN02246 263 ALLELIQRHKVTIAPFVPP--------IVLAIAKS--------PVVEKYDLSSIR------------------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 386 grahMLLSGAAPLPRHVEEFLRI-IPASNLSQGYGLTEscggsfttlAG-VFSMV------------GTVGVPMPTVEAR 451
Cdd:PLN02246 302 ----MVLSGAAPLGKELEDAFRAkLPNAVLGQGYGMTE---------AGpVLAMClafakepfpvksGSCGTVVRNAELK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 452 LVSvPEMGyDAFSADVPrGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLsQGEY 530
Cdd:PLN02246 369 IVD-PETG-ASLPRNQP-GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQ 444
|
....*..
gi 22330132 531 VAVENLE 537
Cdd:PLN02246 445 VAPAELE 451
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
80-606 |
1.48e-22 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 101.02 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KtvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnLDeanlprkrktDICTIMYTSGTTGEPK 239
Cdd:cd05935 82 E---------------------------------------------------LD----------DLALIPYTSGTTGLPK 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILN--NAAISVQVLSIDKMLevtdrscDTSDVFFSYLPLAHCYDQV--MEIYFLSRGSSVGYWRGDIRYLMDDVQALK 315
Cdd:cd05935 101 GCMHThfSAAANALQSAVWTGL-------TPSDVILACLPLFHVTGFVgsLNTAVYVGGTYVLMARWDRETALELIEKYK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 316 PTVFCGVPRVYDKLYAgimqkisasglirkklfdfaynyklgnmrkgfsqeeaSPRLDRLMFDKIKealggrahMLLSGA 395
Cdd:cd05935 174 VTFWTNIPTMLVDLLA-------------------------------------TPEFKTRDLSSLK--------VLTGGG 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 396 APLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVgTVGVPMPTVEARLVSvPEMGYDAFSADVprGEICLR 475
Cdd:cd05935 209 APMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQ-CLGIP*FGVDARVID-IETGRELPPNEV--GEIVVR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 476 GNSMFSGYHKRQDLTDQ--VLIDG--WFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQIWV 551
Cdd:cd05935 285 GPQIFKGYWNRPEETEEsfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCV 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 552 Y-------GNSFESFLV------GVVVPDRkaIEDWAK---LNYQSPNDFEslcqnlkaqkyFLDELNSTA 606
Cdd:cd05935 364 IsvpdervGEEVKAFIVlrpeyrGKVTEED--IIEWAReqmAAYKYPREVE-----------FVDELPRSA 421
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
80-553 |
1.71e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 101.50 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KtvssilscqkgcssnLKTIVSFGEVSSTQKEEAKNQCVSLFSwnefslmGNLDEANLPRKRKTDICTIMYTSGTTGEPK 239
Cdd:PRK06145 108 E---------------FDAIVALETPKIVIDAAAQADSRRLAQ-------GGLEIPPQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQvlSIDKMLEVtdrSCDTSDVFFSYLPLAHCYDqvmeiyFLSRGSSVgYWRGDIRYLMDDVQAlkPTVF 319
Cdd:PRK06145 166 GVMHSYGNLHWK--SIDHVIAL---GLTASERLLVVGPLYHVGA------FDLPGIAV-LWVGGTLRIHREFDP--EAVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 320 CGVPRvyDKLYAGIMQKISASGLIrkklfdfaynyklgnmrkgfsqeeASPRLDRLMFDKIKEALGGrahmllsGAAPLP 399
Cdd:PRK06145 232 AAIER--HRLTCAWMAPVMLSRVL------------------------TVPDRDRFDLDSLAWCIGG-------GEKTPE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 400 RHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAG-VFSMVGTVGVPMPTVEARLVSvpemGYDAFSADVPRGEICLRGNS 478
Cdd:PRK06145 279 SRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGrEIEKIGSTGRALAHVEIRIAD----GAGRWLPPNMKGEICMRGPK 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330132 479 MFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:PRK06145 355 VTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
75-520 |
5.05e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 100.43 E-value: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLydslGVNAVEFIINHAEVSL 154
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL----TVPPTYDEPNARLRKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 155 vfvqeKTVSSILScQKGCSSNLKTIVSFgevsSTQKEEAKNQCVSLFSWNEfsLMGNLDEANLPRKRKTDICTIMYTSGT 234
Cdd:cd05906 111 -----RHIWQLLG-SPVVLTDAELVAEF----AGLETLSGLPGIRVLSIEE--LLDTAADHDLPQSRPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 235 TGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCydqvmeiyflsrGSSVGYWRGDIRYLMDDVQAL 314
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQ-----DVFLNWVPLDHV------------GGLVELHLRAVYLGCQQVHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 315 KPTVFCGVPRVYDklyagIMQKISASglirkklFDFAYNYKLGNMRkgfsqeEASPRLDRLMFDkikeaLGGRAHMLLSG 394
Cdd:cd05906 242 TEEILADPLRWLD-----LIDRYRVT-------ITWAPNFAFALLN------DLLEEIEDGTWD-----LSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 395 AAPLPRHVEEFLRII-----PASNLSQGYGLTESCGGSF---------TTLAGVFSmvgTVGVPMPTVEARLVsvpemgy 460
Cdd:cd05906 299 EAVVAKTIRRLLRLLepyglPPDAIRPAFGMTETCSGVIysrsfptydHSQALEFV---SLGRPIPGVSMRIV------- 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330132 461 DAFSADVPRGEIC---LRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGeWQEDGSMKIIDRKK 520
Cdd:cd05906 369 DDEGQLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
218-609 |
1.53e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 98.97 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 218 PRKRKTDICTIMYTSGTTGEPKGVI-LNNAAISvQVLSIDKMLEVTdrscdTSDVFFSYLPLAHcydqvmeiyflsrgsS 296
Cdd:PRK13295 192 LRPGPDDVTQLIYTSGTTGEPKGVMhTANTLMA-NIVPYAERLGLG-----ADDVILMASPMAH---------------Q 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 297 VGYWRGdiryLMDDVQaLKPTVfcgvprvydkLYAGIMQKISASGLIRKK-----------LFDFAYNYKLGNmrkgfsq 365
Cdd:PRK13295 251 TGFMYG----LMMPVM-LGATA----------VLQDIWDPARAAELIRTEgvtftmastpfLTDLTRAVKESG------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 366 eEASPRLDRLmfdkikealggrahmlLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTV-GVP 444
Cdd:PRK13295 309 -RPVSSLRTF----------------LCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTdGCP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 445 MPTVEARLVsvpemgyDAFSADVPRGEI---CLRGNSMFSGYHKRQDLTDqVLIDGWFHTGDIGEWQEDGSMKIIDRKKN 521
Cdd:PRK13295 372 LPGVEVRVV-------DADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKD 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 522 IFkLSQGEYVAVENLENTYSRCPLIAQIWVygnsfesflvgVVVPDRKAIEDWAKLNYQSPN---DFESLCQNLKAQKyf 598
Cdd:PRK13295 444 VI-IRGGENIPVVEIEALLYRHPAIAQVAI-----------VAYPDERLGERACAFVVPRPGqslDFEEMVEFLKAQK-- 509
|
410
....*....|.
gi 22330132 599 ldelnsTAKQY 609
Cdd:PRK13295 510 ------VAKQY 514
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
224-572 |
5.25e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 97.25 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSCDTSDVFFSYLPLAHcydqvmeIYFLSRGSSVGYWRGD 303
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLYH-------IFALTANGLVFMKIGG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 304 IRYLMDD-------VQALKPTVFCGVPRVyDKLYAGIMQkisasglirkklfdfaynyklgnmrkgfsqeeaSPRLDRLM 376
Cdd:PRK08751 282 CNHLISNprdmpgfVKELKKTRFTAFTGV-NTLFNGLLN---------------------------------TPGFDQID 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 377 FDKIKEALGGrahmllsGAApLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEA------ 450
Cdd:PRK08751 328 FSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDAcikdda 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 451 -RLVSVPEMGydafsadvprgEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqG 528
Cdd:PRK08751 400 gTVLAIGEIG-----------ELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-G 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22330132 529 EYVAVENLENTYSRCPLIAQIWVYGnsfesflvgvvVPDRKAIE 572
Cdd:PRK08751 468 FNVYPNEIEDVIAMMPGVLEVAAVG-----------VPDEKSGE 500
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
224-573 |
6.66e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 94.32 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILN------NAAISVQVLSidkmlevtdrsCDTSDVFFSYLPLAHcydqVMEIYFLSRGssv 297
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTaanllaSAAGLHSRLG-----------FGGGDSWLLSLPLYH----VGGLAILVRS--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 298 gYWRGDIRYLMDDVQALKPTVfCGVPRVYDKLYAGIMQKISASGLIRkklfdfaynyklgnmrkgfsqeEASPRLDRLmf 377
Cdd:cd17630 63 -LLAGAELVLLERNQALAEDL-APPGVTHVSLVPTQLQRLLDSGQGP----------------------AALKSLRAV-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 378 dkikealggrahmlLSGAAPLPRH-VEEFL-RIIPasnLSQGYGLTESCGGSFTTLAGVFSMvGTVGVPMPTVEARLVsv 455
Cdd:cd17630 117 --------------LLGGAPIPPElLERAAdRGIP---LYTTYGMTETASQVATKRPDGFGR-GGVGVLLPGRELRIV-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 456 pemgydafsadvPRGEICLRGNSMFSGYHKRQdLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVEN 535
Cdd:cd17630 177 ------------EDGEIWVGGASLAMGYLRGQ-LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEE 242
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 22330132 536 LENTYSRCPLIAQIWVYGNSFESF---LVGVVVPDRKAIED 573
Cdd:cd17630 243 IEAALAAHPAVRDAFVVGVPDEELgqrPVAVIVGRGPADPA 283
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
48-660 |
7.44e-21 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 98.00 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 48 WQffsEAVKKYPNEQMLGQRvttdSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQ 127
Cdd:PTZ00297 433 WE---RSVTRHSTFRCLGQT----SESGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALY 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 128 GITYVPLYDSlgVNAVEFIINHAEVSLVFVQEKTVSSILSCQkgcSSNLKTIV---SFgeVSSTQKEEAKNQCVSLFSWN 204
Cdd:PTZ00297 506 GFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCR---SRKLETVVythSF--YDEDDHAVARDLNITLIPYE 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 205 EFSLMGNLDEANLPRKRKTDICTIMY----TSGTTGEPKGVILNNAAI--SVQVLSIDKMLEVTDRScdTSDVFFSylPL 278
Cdd:PTZ00297 579 FVEQKGRLCPVPLKEHVTTDTVFTYVvdntTSASGDGLAVVRVTHADVlrDISTLVMTGVLPSSFKK--HLMVHFT--PF 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 279 AHCYDQVMEIYFLSRGSSVGywRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLgn 358
Cdd:PTZ00297 655 AMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRS-- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 359 mRKGFSQEEASPRLDRLMFDKIKEALGGRahmllsgaaplprhVEEFlrIIPASNLSQGYGLTES---------CGGSFT 429
Cdd:PTZ00297 731 -RLINIHRRDSSLLRFIFFRATQELLGGC--------------VEKI--VLCVSEESTSFSLLEHisvcyvpclREVFFL 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 430 TLAGVFSMVGTvgvPMPTVEARLVSVPEMgydafSADVPRGEICLRGNSmfsgyHKRqdltdqvlidgwfHTGDI-GEWQ 508
Cdd:PTZ00297 794 PSEGVFCVDGT---PAPSLQVDLEPFDEP-----SDGAGIGQLVLAKKG-----EPR-------------RTLPIaAQWK 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 509 EDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESfLVGVVVPDRKAIE-DWAKLNYQSPNDFES 587
Cdd:PTZ00297 848 RDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGEGGGPA 926
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330132 588 LCQNLK-----AQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLYSEA 660
Cdd:PTZ00297 927 RQLGWTelvayASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDV 1004
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
218-553 |
2.67e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.91 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 218 PRKRKTDICTIMYTSGTTGEPKGVILN--NAAISVQVLSIDKMLEVTDRSCDtsDVFFSYLPLAHCYD-QVMEIYFLSRG 294
Cdd:PLN02574 193 PVIKQDDVAAIMYSSGTTGASKGVVLThrNLIAMVELFVRFEASQYEYPGSD--NVYLAALPMFHIYGlSLFVVGLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 295 SSVGYWRG-DIRYLMDDVQALKPTVFCGVPRVYdklyagimqkisaSGLIRKKlfdfaynyklgnmrKGFSQEeasprld 373
Cdd:PLN02574 271 STIVVMRRfDASDMVKVIDRFKVTHFPVVPPIL-------------MALTKKA--------------KGVCGE------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 374 rlMFDKIKEalggrahmLLSGAAPLPRH-VEEFLRIIPASNLSQGYGLTESCG-GSFTTLAGVFSMVGTVGVPMPTVEAR 451
Cdd:PLN02574 317 --VLKSLKQ--------VSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAvGTRGFNTEKLSKYSSVGLLAPNMQAK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 452 LVsvpEMGYDAFSADVPRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLsQGEY 530
Cdd:PLN02574 387 VV---DWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQ 462
|
330 340
....*....|....*....|...
gi 22330132 531 VAVENLENTYSRCPLIAQIWVYG 553
Cdd:PLN02574 463 IAPADLEAVLISHPEIIDAAVTA 485
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
80-520 |
2.86e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 94.56 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSI--LSCQKGcSSNLKTIVSFGEVSSTqkeEAKNQCVSLFswnefslmgnldeANLPRKRKtDICTIMYTSGTTGE 237
Cdd:PRK07514 109 ANFAWLskIAAAAG-APHVETLDADGTGSLL---EAAAAAPDDF-------------ETVPRGAD-DLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 238 PKGVILN--NAAISVQVLSidKMLEVTDRscdtsDVFFSYLPLAHCYDQ--VMEIYFLSRGSSVGYWRGDirylMDDVQA 313
Cdd:PRK07514 171 SKGAMLShgNLLSNALTLV--DYWRFTPD-----DVLIHALPIFHTHGLfvATNVALLAGASMIFLPKFD----PDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 314 LKP--TVFCGVPRVYDKLYAgimqkisasglirkklfdfaynyklgnmrkgfsqeeaSPRLDRlmfdkikEALggrAHML 391
Cdd:PRK07514 240 LMPraTVMMGVPTFYTRLLQ-------------------------------------EPRLTR-------EAA---AHMR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 392 L--SGAAPL--PRHVEEFLR----IIpasnlsQGYGLTESCGGSFTTLAGVfSMVGTVGVPMPTVEARLVSvPEMGydaf 463
Cdd:PRK07514 273 LfiSGSAPLlaETHREFQERtghaIL------ERYGMTETNMNTSNPYDGE-RRAGTVGFPLPGVSLRVTD-PETG---- 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330132 464 sADVPRGEIC---LRGNSMFSGYHK-----RQDLTDqvliDGWFHTGDIGEWQEDGSMKIIDRKK 520
Cdd:PRK07514 341 -AELPPGEIGmieVKGPNVFKGYWRmpektAEEFRA----DGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
80-553 |
3.31e-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: 93.68 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KtvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrktDICTIMYTSGTTGEPK 239
Cdd:cd05919 91 D---------------------------------------------------------------DIAYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVI--LNNAAISVQVLSIDKM-LEVTDRSCDTSDVFFSYlPLAHCYdqvmeIYFLSRGSSV---GYWRgDIRYLMDDVQA 313
Cdd:cd05919 108 GVMhaHRDPLLFADAMAREALgLTPGDRVFSSAKMFFGY-GLGNSL-----WFPLAVGASAvlnPGWP-TAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 314 LKPTVFCGVPRVYdklyagimqkisasglirkklfdfaynyklGNMRKGFSQEEASPRLDRLMFdkikealggrahmllS 393
Cdd:cd05919 181 FRPTVLYGVPTFY------------------------------ANLLDSCAGSPDALRSLRLCV---------------S 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 394 GAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSmVGTVGVPMPTVEARLVSvpEMGYDAfSADVPrGEIC 473
Cdd:cd05919 216 AGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWR-LGSTGRPVPGYEIRLVD--EEGHTI-PPGEE-GDLL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 474 LRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:cd05919 291 VRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVA 369
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
74-606 |
5.10e-20 |
|
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: 93.97 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 74 VGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVS 153
Cdd:cd05959 24 IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 154 LVFVQEKTVSSILSCQKGCSSNLKTIVsfgeVSSTQKEEAKnqcvslFSWNEFSLMGNLDEANLPRKRKTDICTIMYTSG 233
Cdd:cd05959 104 VVVVSGELAPVLAAALTKSEHTLVVLI----VSGGAGPEAG------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 234 TTGEPKGVI-LNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAHCYDQVMEIYF-LSRGSSVgywrgdirYLM--- 308
Cdd:cd05959 174 STGRPKGVVhLHADIYWTAELYARNVLGIRE-----DDVCFSAAKLFFAYGLGNSLTFpLSVGATT--------VLMper 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 309 -------DDVQALKPTVFCGVPrvydKLYAGIMqkisasglirkklfdfaynyklgnmrkgfsqeeASPRLDRLMFDKIK 381
Cdd:cd05959 241 ptpaavfKRIRRYRPTVFFGVP----TLYAAML---------------------------------AAPNLPSRDLSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 382 ealggrahMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVfSMVGTVGVPMPTVEARLVSvpEMGYD 461
Cdd:cd05959 284 --------LCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGR-VRYGTTGKPVPGYEVELRD--EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 462 AfsADVPRGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTYS 541
Cdd:cd05959 353 V--ADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALV 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330132 542 RCPLIAQIWVYGNSFESFL---VGVVVPdRKAIEDWAKLnyqsPNDFESLCQN-LKAQKY-----FLDELNSTA 606
Cdd:cd05959 430 QHPAVLEAAVVGVEDEDGLtkpKAFVVL-RPGYEDSEAL----EEELKEFVKDrLAPYKYprwivFVDELPKTA 498
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
78-606 |
7.48e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 93.67 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 78 TWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV 157
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 QEKTVSSILSCQKGCSSnLKTIVSFGEVSSTQKEEAknqcvslFSWNEF-SLMGNLDEANLprkRKTDICTIMYTSGTTG 236
Cdd:PRK06155 125 EAALLAALEAADPGDLP-LPAVWLLDAPASVSVPAG-------WSTAPLpPLDAPAPAAAV---QPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 237 EPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAH-----CYDQVM----EIYFLSRGSSVGYWrgdiryl 307
Cdd:PRK06155 194 PSKGVCCPHAQFYWWGRNSAEDLEIGAD-----DVLYTTLPLFHtnalnAFFQALlagaTYVLEPRFSASGFW------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 308 mDDVQALKPTVFcgvprvydklyagimqkisasglirkklfdfaynYKLGNMRKGFSQEEASPRldrlmfdkikealgGR 387
Cdd:PRK06155 262 -PAVRRHGATVT----------------------------------YLLGAMVSILLSQPARES--------------DR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 388 AHML---LSGAAPLPRHVEEFLRIipASNLSQGYGLTES---CGGSFTTLAGvfsmvGTVGVPMPTVEARLVSvpEMGyD 461
Cdd:PRK06155 293 AHRVrvaLGPGVPAALHAAFRERF--GVDLLDGYGSTETnfvIAVTHGSQRP-----GSMGRLAPGFEARVVD--EHD-Q 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 462 AFSADVPrGEICLRGN---SMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLEN 538
Cdd:PRK06155 363 ELPDGEP-GELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQ 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 539 TYSRCPLIAQIWVYGNSFE----SFLVGVVVPDRKAIEDWAKLNYQSPN----------DFES---LCQNLKAQKYFLDE 601
Cdd:PRK06155 441 VLLSHPAVAAAAVFPVPSElgedEVMAAVVLRDGTALEPVALVRHCEPRlayfavpryvEFVAalpKTENGKVQKFVLRE 520
|
....*
gi 22330132 602 LNSTA 606
Cdd:PRK06155 521 QGVTA 525
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
224-572 |
1.85e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 92.39 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSCDTSDVFFSY--LPLAHcydqvmeIYFLSRGSSVGYWR 301
Cdd:PRK07059 205 DVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDQLNFVcaLPLYH-------IFALTVCGLLGMRT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 302 G----------DIRYLMDDVQALKPTVFCGVprvyDKLYAGIMQkisasglirkklfdfaynyklgnmrkgfsqeeaSPR 371
Cdd:PRK07059 278 GgrnilipnprDIPGFIKELKKYQVHIFPAV----NTLYNALLN---------------------------------NPD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 372 LDRLMFDKIKEALGGrahmllsGAApLPRHVEEFLRIIPASNLSQGYGLTES----CGGSFTTlaGVFSmvGTVGVPMPT 447
Cdd:PRK07059 321 FDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSETspvaTCNPVDA--TEFS--GTIGLPLPS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 448 VEarlVSVpemgYDAFSADVPRG---EICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIF 523
Cdd:PRK07059 389 TE---VSI----RDDDGNDLPLGepgEICIRGPQVMAGYWNRPDETAKVMTaDGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 22330132 524 KLSqGEYVAVENLENTYSRCPLIaqiwvygnsFESFLVGvvVPDRKAIE 572
Cdd:PRK07059 462 LVS-GFNVYPNEIEEVVASHPGV---------LEVAAVG--VPDEHSGE 498
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
224-522 |
2.12e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.01 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIdkMLEVTDRSCDtsDVFFSYLPLAHCYD--QVMEIYFLSRGSSVGYWR 301
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDIL--QKEGLNWVVG--DVTYLPLPATHIGGlwWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 302 GDIRYLMDDVQALKPTVFCGVPRVYDKLYagimqkisasglirkklfdfaynyklgNMRKGFSQEeaSPRLDRLMFdkik 381
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLV---------------------------SELKSANAT--VPSLRLIGY---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 382 ealggrahmllSGAAPLPRHVEEFLrIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPemGYD 461
Cdd:cd17635 125 -----------GGSRAIAADVRFIE-ATGLTNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATD--GIA 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 462 AFSADvpRGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:cd17635 191 GPSAS--FGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSES 249
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
75-660 |
2.80e-19 |
|
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: 91.72 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 75 GPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEF-----IINH 149
Cdd:cd05921 21 GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLaklkhLFEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 150 AEVSLVFVQEKTVSSilscqkgcsSNLKTIVSFG-EVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEAnLPRKRKTDICTI 228
Cdd:cd05921 101 LKPGLVFAQDAAPFA---------RALAAIFPLGtPLVVSRNAVAGRGAISFAELAATPPTAAVDAA-FAAVGPDTVAKF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 229 MYTSGTTGEPKGVILNNAAISvqvLSIDKMLEVTDRSCDTSDVFFSYLPLAHcydqvmeiyflSRGSSVGY----WRGDI 304
Cdd:cd05921 171 LFTSGSTGLPKAVINTQRMLC---ANQAMLEQTYPFFGEEPPVLVDWLPWNH-----------TFGGNHNFnlvlYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 305 RYL-------------MDDVQALKPTVFCGVPRVYDKLyAGIMQKISAsglIRKKLFDfaynyklgnmrkgfsqeeaspr 371
Cdd:cd05921 237 LYIddgkpmpggfeetLRNLREISPTVYFNVPAGWEML-VAALEKDEA---LRRRFFK---------------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 372 ldrlmfdkikealggRAHMLLSGAAPLPRHVEEFL---------RIIPasnLSQGYGLTEScGGSFTTLAGVFSMVGTVG 442
Cdd:cd05921 291 ---------------RLKLMFYAGAGLSQDVWDRLqalavatvgERIP---MMAGLGATET-APTATFTHWPTERSGLIG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 443 VPMPTVEARLvsVPEMGydafsadvpRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMK---IID- 517
Cdd:cd05921 352 LPAPGTELKL--VPSGG---------KYEVRVKGPNVTPGYWRQPELTAQAFDeEGFYCLGDAAKLADPDDPAkglVFDg 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 518 RKKNIFKLSQGEYVAVENLEN-TYSRC-PLIAQIWVYGNSFEsFLVGVVVPDRKAIEdwaKLNYQSPNDFESLCQNLKAQ 595
Cdd:cd05921 421 RVAEDFKLASGTWVSVGPLRArAVAACaPLVHDAVVAGEDRA-EVGALVFPDLLACR---RLVGLQEASDAEVLRHAKVR 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330132 596 KYFLDELNSTAKQYQLKGFEMLKAIHLEpNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLYSEA 660
Cdd:cd05921 497 AAFRDRLAALNGEATGSSSRIARALLLD-EPPSIDKGEITDKGYINQRAVLERRAALVERLYADT 560
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
224-605 |
3.36e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 91.75 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLevTDRSCDTSDVFFSYLPLAHCYDQVMEIYFLsrgssvgywrgd 303
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALM--GSNLNEGCEILIAPLPLYHIYAFTFHCMAM------------ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 304 irYLMDDVQALKPTvfcgvPRVYDKLYAgIMQKISASGLIrkklfdfaynyKLGNMRKGFSQEEASPRLDrlmFDKIKea 383
Cdd:PRK05677 274 --MLIGNHNILISN-----PRDLPAMVK-ELGKWKFSGFV-----------GLNTLFVALCNNEAFRKLD---FSALK-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 384 lggrahMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTE-SCGGSFTTLAGVfsMVGTVGVPMPTVEARLVsvpemgyDA 462
Cdd:PRK05677 330 ------LTLSGGMALQLATAERWKEVTGCAICEGYGMTEtSPVVSVNPSQAI--QVGTIGIPVPSTLCKVI-------DD 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 463 FSADVPRGEI---CLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLEN 538
Cdd:PRK05677 395 DGNELPLGEVgelCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELED 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330132 539 TYSRCPLIAQIWVYG----NSFESFLVGVVVP-----DRKAIEDWAKLN---YQSPNDFEslcqnlkaqkyFLDELNST 605
Cdd:PRK05677 474 VLAALPGVLQCAAIGvpdeKSGEAIKVFVVVKpgetlTKEQVMEHMRANltgYKVPKAVE-----------FRDELPTT 541
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
49-569 |
5.22e-19 |
|
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: 90.34 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNEQMLGQRVTTdskvgpytwITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG 128
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRS---------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 129 ITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTvssilscqKGCSSNLKTIVSFGEVSSTQKEEAKNQCVSlfswnefsl 208
Cdd:cd12117 72 AAYVPLDPELPAERLAFMLADAGAKVLLTDRSL--------AGRAGGLEVAVVIDEALDAGPAGNPAVPVS--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 209 mgnldeanlprkrKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSiDKMLEVTDRscdtsDVFFSYLPLAhcYDQVM-E 287
Cdd:cd12117 135 -------------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPD-----DRVLQTSPLA--FDASTfE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 288 IY--FLSRGSSVGYWRG---DIRYLMDDVQALKPTVfcgvprvydklyagiMQKISAsglirkkLFdfaynyklgnmrkg 362
Cdd:cd12117 194 IWgaLLNGARLVLAPKGtllDPDALGALIAEEGVTV---------------LWLTAA-------LF-------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 363 fsqeeasprldRLMFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTEScggsfTTLAGVFSMV---- 438
Cdd:cd12117 238 -----------NQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEN-----TTFTTSHVVTelde 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 439 --GTV--GVPMPTVEARLVsvpemgyDAFSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLI-----DG--WFHTGDI 504
Cdd:cd12117 302 vaGSIpiGRPIANTRVYVL-------DEDGRPVPPgvpGELYVGGDGLALGYLNRPALTAERFVadpfgPGerLYRTGDL 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330132 505 GEWQEDGSMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIAQIWVY---GNSFESFLVGVVVPDRK 569
Cdd:cd12117 375 ARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVVVvreDAGGDKRLVAYVVAEGA 441
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
40-537 |
1.03e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 90.04 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 40 LPTDIDSPwQFFSEAVKKYPNEQMLGQRVTTDSkvgpytwITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWII 119
Cdd:PLN02330 24 VPDKLTLP-DFVLQDAELYADKVAFVEAVTGKA-------VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 120 AMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVfvqektVSSILSCQKGCSSNLKTIVsFGEVSStqkEEAKNqcvs 199
Cdd:PLN02330 96 VALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI------VTNDTNYGKVKGLGLPVIV-LGEEKI---EGAVN---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 200 lfsWNEFSLMGNL--DEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSidKMLEVTDRSCDTSdVFFSYLP 277
Cdd:PLN02330 162 ---WKELLEAADRagDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCS--SLFSVGPEMIGQV-VTLGLIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 278 LAHCYDqVMEIYFLS---RGSSVGYWRGDIRYLmddvqalkptvfcgvprvydkLYAGIMQKISASGLIRKKLFDFAYNy 354
Cdd:PLN02330 236 FFHIYG-ITGICCATlrnKGKVVVMSRFELRTF---------------------LNALITQEVSFAPIVPPIILNLVKN- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 355 klgnmrkgfsqeeasPRLDRLMFDKIKealggrAHMLLSGAAPL-PRHVEEFLRIIPASNLSQGYGLTE-SC----GGSF 428
Cdd:PLN02330 293 ---------------PIVEEFDLSKLK------LQAIMTAAAPLaPELLTAFEAKFPGVQVQEAYGLTEhSCitltHGDP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 429 TTLAGVfSMVGTVGVPMPTVEARLVSvPEMGYdAFSADVPrGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEW 507
Cdd:PLN02330 352 EKGHGI-AKKNSVGFILPNLEVKFID-PDTGR-SLPKNTP-GELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYI 427
|
490 500 510
....*....|....*....|....*....|
gi 22330132 508 QEDGSMKIIDRKKNIFKLsQGEYVAVENLE 537
Cdd:PLN02330 428 DDDGDIFIVDRIKELIKY-KGFQVAPAELE 456
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
59-533 |
1.98e-18 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 89.17 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 59 PNEQMLGQRVTTdskvGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSL 138
Cdd:PRK08180 53 PDRVFLAERGAD----GGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 139 GVNAVEF-----IINHAEVSLVFVQEKTV--SSILSCqkgcssnlktIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMGN 211
Cdd:PRK08180 129 SLVSQDFgklrhVLELLTPGLVFADDGAAfaRALAAV----------VPADVEVVAVRGAVPGRAATPFAALLATPPTAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 212 LDEANlPRKRKTDICTIMYTSGTTGEPKGVILNNAAI-SVQVLsidkMLEVTDRSCDTSDVFFSYLPLAHCYdqvmeiyf 290
Cdd:PRK08180 199 VDAAH-AAVGPDTIAKFLFTSGSTGLPKAVINTHRMLcANQQM----LAQTFPFLAEEPPVLVDWLPWNHTF-------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 291 lsrGSS-----VGYWRGDIrYLmDD-----------VQALK---PTVFCGVPRVYDKLyAGIMQKISAsglIRKKLFdfa 351
Cdd:PRK08180 266 ---GGNhnlgiVLYNGGTL-YI-DDgkptpggfdetLRNLReisPTVYFNVPKGWEML-VPALERDAA---LRRRFF--- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 352 ynyklgnmrkgfsqeeasprldrlmfdkikealgGRAHMLLSGAAPLPRHVEEFL----------RIIpasnLSQGYGLT 421
Cdd:PRK08180 334 ----------------------------------SRLKLLFYAGAALSQDVWDRLdrvaeatcgeRIR----MMTGLGMT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 422 EScGGSFTTLAGVFSMVGTVGVPMPTVEARLvsVPEMGydafsadvpRGEICLRGNSMFSGYHKRQDLTDQVLID-GWFH 500
Cdd:PRK08180 376 ET-APSATFTTGPLSRAGNIGLPAPGCEVKL--VPVGG---------KLEVRVKGPNVTPGYWRAPELTAEAFDEeGYYR 443
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 22330132 501 TGDIGEWQE----------DGsmkiidRKKNIFKLSQGEYVAV 533
Cdd:PRK08180 444 SGDAVRFVDpadperglmfDG------RIAEDFKLSSGTWVSV 480
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
224-553 |
2.88e-18 |
|
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: 86.40 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNaaisVQVLSIDK----MLEVT--DRSCDTSDVFFSYLPLAHCydqvmeIYFLSRGSSV 297
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAH----RQTLRAAAawadCADLTedDRYLIINPFFHTFGYKAGI------VACLLTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 298 -GYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKisasglirkklfdfayNYKLGNMRKGfsqeeasprldrlm 376
Cdd:cd17638 71 vPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRK----------------KFDLSSLRAA-------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 377 fdkikealggrahmlLSGAAPLPRHVEEFLRI-IPASNLSQGYGLTES-----C--GGSFTTLAGvfsmvgTVGVPMPTV 448
Cdd:cd17638 121 ---------------VTGAATVPVELVRRMRSeLGFETVLTAYGLTEAgvatmCrpGDDAETVAT------TCGRACPGF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 449 EARLVSvpemgydafsadvpRGEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQ 527
Cdd:cd17638 180 EVRIAD--------------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY-IVG 244
|
330 340
....*....|....*....|....*.
gi 22330132 528 GEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:cd17638 245 GFNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
215-595 |
6.40e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 88.44 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 215 ANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCYDQVMEIYF-LSR 293
Cdd:PRK08633 774 LYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRND-----DVILSSLPFFHSFGLTVTLWLpLLE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 294 GSSVgywrgdirylmddVQALKPTVFCGVPRVYDKLYAGIMqkISASGLIRkklfdfAYnyklgnMRkgfsqeeaSPRLD 373
Cdd:PRK08633 849 GIKV-------------VYHPDPTDALGIAKLVAKHRATIL--LGTPTFLR------LY------LR--------NKKLH 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 374 RLMFDKIkealggraHMLLSGAAPLPRHV-EEF-----LRIIpasnlsQGYGLTES------------CGGsftTLAGVF 435
Cdd:PRK08633 894 PLMFASL--------RLVVAGAEKLKPEVaDAFeekfgIRIL------EGYGATETspvasvnlpdvlAAD---FKRQTG 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 436 SMVGTVGVPMPTVEARLVSvPEMGydafsADVPRGE---ICLRGNSMFSGYHKRQDLTDQVLID----GWFHTGDIGEWQ 508
Cdd:PRK08633 957 SKEGSVGMPLPGVAVRIVD-PETF-----EELPPGEdglILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLD 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 509 EDGSMKIIDRKKNIFKLSqGEYV---AVENlentysrcpLIAQIwvYGNSFESFLVgVVVPDRKAIEDWAKLNYQSPNDF 585
Cdd:PRK08633 1031 EDGFLTITDRYSRFAKIG-GEMVplgAVEE---------ELAKA--LGGEEVVFAV-TAVPDEKKGEKLVVLHTCGAEDV 1097
|
410
....*....|
gi 22330132 586 ESLCQNLKAQ 595
Cdd:PRK08633 1098 EELKRAIKES 1107
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
394-526 |
2.65e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.49 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 394 GAAPLPRHVEEFLRIIPASNLSQGYGLTEScggSFTTLAGVFSMV---GTVGVPMPTVEARLVsvpemgyDAFSADVP-- 468
Cdd:PRK08974 333 GGMAVQQAVAERWVKLTGQYLLEGYGLTEC---SPLVSVNPYDLDyysGSIGLPVPSTEIKLV-------DDDGNEVPpg 402
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 22330132 469 -RGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLS 526
Cdd:PRK08974 403 ePGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVS 461
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
39-520 |
3.11e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 85.78 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 39 DLPtdiDSPWQFFSEAVKKYPNEQMLGQRVTTDSKVGPYTWiTYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWI 118
Cdd:PRK07529 22 DLP---ASTYELLSRAAARHPDAPALSFLLDADPLDRPETW-TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 119 IAMEACMSQGITyVPLYDSLGVNAVEFIINHAEVSLVF---------VQEKTVSSILSCqkgcsSNLKTIVSF------- 182
Cdd:PRK07529 98 FALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVtlgpfpgtdIWQKVAEVLAAL-----PELRTVVEVdlarylp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 183 GEVSSTQKEEAKNQCVSLFSWNEfsLMGNLDEANL---PRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKML 259
Cdd:PRK07529 172 GPKRLAVPLIRRKAHARILDFDA--ELARQPGDRLfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 260 EVTDrscdtSDVFFSYLPLAH---CYDQVMEIyfLSRGSSV------GYwRGD--IRYLMDDVQALKPTVFCGVPRVYdk 328
Cdd:PRK07529 250 GLGP-----GDTVFCGLPLFHvnaLLVTGLAP--LARGAHVvlatpqGY-RGPgvIANFWKIVERYRINFLSGVPTVY-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 329 lyAGIMQKISASglirkklfdfaynYKLGNMRKGFSqeeasprldrlmfdkikealggrahmllsGAAPLPRHV-EEF-- 405
Cdd:PRK07529 320 --AALLQVPVDG-------------HDISSLRYALC-----------------------------GAAPLPVEVfRRFea 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 406 ---LRIIpasnlsQGYGLTE-SCGGSFTTLAGVfSMVGTVGVPMPTVEARLVSVPEMGydAFSADVPR---GEICLRGNS 478
Cdd:PRK07529 356 atgVRIV------EGYGLTEaTCVSSVNPPDGE-RRIGSVGLRLPYQRVRVVILDDAG--RYLRDCAVdevGVLCIAGPN 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 22330132 479 MFSGY---HKRQDLtdqVLIDGWFHTGDIGEWQEDGSMKIIDRKK 520
Cdd:PRK07529 427 VFSGYleaAHNKGL---WLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
399-569 |
1.58e-16 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 81.16 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 399 PRHVEEFLRIIPASNLSqGYGLTESCGgsFTTLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVPR---GEICLR 475
Cdd:cd17637 125 PETIQRFEETTGATFWS-LYGQTETSG--LVTLSPYRERPGSAGRPGPLVRVRIV-------DDNDRPVPAgetGEIVVR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 476 GNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRK--KNIFKlSQGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:cd17637 195 GPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPAIAEVCVIG 273
|
170
....*....|....*.
gi 22330132 554 nsfesflvgvvVPDRK 569
Cdd:cd17637 274 -----------VPDPK 278
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
77-551 |
2.24e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.58 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 77 YTWI-TYKEAHdaaiRIGSAIRSRGVDPGHCCGIYGANCPewiiameaCMSQGITYVPLYDSLgVNAVE---------FI 146
Cdd:PLN02479 46 YTWAqTYQRCR----RLASALAKRSIGPGSTVAVIAPNIP--------AMYEAHFGVPMAGAV-VNCVNirlnaptiaFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 147 INHAEVSLVFVQEKTVS------SILSCQKGCSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRK 220
Cdd:PLN02479 113 LEHSKSEVVMVDQEFFTlaeealKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGAIEYEKFLETGDPEFAWKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 221 RKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRScdtsdVFFSYLPLAHC----YDQVMEIYFlsrGSS 296
Cdd:PLN02479 193 DEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGA-----VYLWTLPMFHCngwcFTWTLAALC---GTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 297 VGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLyagimqkISASglirkklfdfaynyklgnmrkgfsQEEASPRLDRLM 376
Cdd:PLN02479 265 ICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTI-------VNAP------------------------KSETILPLPRVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 377 fdkikealggraHMLLSGAAPLPRHVeeFLRIIPASNLSQGYGLTESCGGSfttlagvfsmvgTV--------GVPmPTV 448
Cdd:PLN02479 314 ------------HVMTAGAAPPPSVL--FAMSEKGFRVTHTYGLSETYGPS------------TVcawkpewdSLP-PEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 449 EARLVSVPEMGYDAFS----------ADVPR-----GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSM 513
Cdd:PLN02479 367 QARLNARQGVRYIGLEgldvvdtktmKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYI 446
|
490 500 510
....*....|....*....|....*....|....*...
gi 22330132 514 KIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWV 551
Cdd:PLN02479 447 EIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASV 483
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
65-553 |
2.43e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 82.49 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 65 GQRVTTDSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVE 144
Cdd:PRK06018 25 NREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 145 FIINHAEVSLVFVqEKTVSSILSCQKGCSSNLKTIVSFGEVSSTQKEEAKN---------QCVSLFSWNEFslmgnlDEA 215
Cdd:PRK06018 105 WIINHAEDRVVIT-DLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNavayeewiaEADGDFAWKTF------DEN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 216 NlprkrktdICTIMYTSGTTGEPKGVILNNAAISVQVLsIDKMLEVTDRSCdtSDVFFSYLPLAHC-------------Y 282
Cdd:PRK06018 178 T--------AAGMCYTSGTTGDPKGVLYSHRSNVLHAL-MANNGDALGTSA--ADTMLPVVPLFHAnswgiafsapsmgT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 283 DQVMEIYFLSrGSSVgywrgdirYLMDDVQalKPTVFCGVPRVYDKLyagiMQKISASGLirkKLfdfaynyklgnmrkg 362
Cdd:PRK06018 247 KLVMPGAKLD-GASV--------YELLDTE--KVTFTAGVPTVWLML----LQYMEKEGL---KL--------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 363 fsqeeasPRLDrlmfdkikealggrahMLLSGAAPLPRH-VEEFLRIipASNLSQGYGLTEScggsfttlagvfSMVGTV 441
Cdd:PRK06018 294 -------PHLK----------------MVVCGGSAMPRSmIKAFEDM--GVEVRHAWGMTEM------------SPLGTL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 442 GV-PMP----TVEARLVSVPEMGYDAFS----------ADVPR-----GEICLRGNSMFSGYHKRQD-LTDQvliDGWFH 500
Cdd:PRK06018 337 AAlKPPfsklPGDARLDVLQKQGYPPFGvemkitddagKELPWdgktfGRLKVRGPAVAAAYYRVDGeILDD---DGFFD 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 22330132 501 TGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
46-538 |
2.72e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 46 SPWQFFSEAVKKYPNEQmlgqrvttdSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACM 125
Cdd:PLN03102 15 TPITFLKRASECYPNRT---------SIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 126 SQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQ---EKTVSSILSCQKGCSSNLKTIVSF-GEVSSTQK---EEAKNQCV 198
Cdd:PLN03102 86 MAGAVLNPINTRLDATSIAAILRHAKPKILFVDrsfEPLAREVLHLLSSEDSNLNLPVIFiHEIDFPKRpssEELDYECL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 199 SLFSWNEFSLMGNLdeanLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIdkmleVTDRSCDTSDVFFSYLPL 278
Cdd:PLN03102 166 IQRGEPTPSLVARM----FRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSA-----IIGWEMGTCPVYLWTLPM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 279 AHCYDQVMEIYFLSRG-SSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGimqkisasglirkklfdfaynyklg 357
Cdd:PLN03102 237 FHCNGWTFTWGTAARGgTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG------------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 358 nmrkgfSQEEASPRldrlmfdkikealGGRAHMLLSGAAPLPRHVEEFLRIipASNLSQGYGLTESCGG----------- 426
Cdd:PLN03102 292 ------NSLDLSPR-------------SGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPvlfcewqdewn 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 427 --------SFTTLAGVfSMVGTVGVPMPTVEArLVSVPEMGYDAfsadvprGEICLRGNSMFSGYHKRQDLTDQVLIDGW 498
Cdd:PLN03102 351 rlpenqqmELKARQGV-SILGLADVDVKNKET-QESVPRDGKTM-------GEIVIKGSSIMKGYLKNPKATSEAFKHGW 421
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 22330132 499 FHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLEN 538
Cdd:PLN03102 422 LNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVEN 460
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
393-572 |
3.33e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 82.18 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVP---R 469
Cdd:PRK12492 340 SGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVI-------DDDGNELPlgeR 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 GEICLRGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQ 548
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFNVYPNEIEDVVMAHPKVAN 491
|
170 180
....*....|....*....|....
gi 22330132 549 IWVYGnsfesflvgvvVPDRKAIE 572
Cdd:PRK12492 492 CAAIG-----------VPDERSGE 504
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
81-553 |
4.56e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 81.65 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEK 160
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 TVSSILSCQKGCSSNLKTIVsfgeVSSTQKEEAKNqcVSLFSWNEFSLMGNLDEAnlPRKRKTDICTIMYTSGTTGEPKG 240
Cdd:PRK08008 119 FYPMYRQIQQEDATPLRHIC----LTRVALPADDG--VSSFTQLKAQQPATLCYA--PPLSTDDTAEILFTSGTTSRPKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 VILNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAHCYDQ---VMEIY-------FLSRGSSVGYWRgdirylmdD 310
Cdd:PRK08008 191 VVITHYNLRFAGYYSAWQCALRD-----DDVYLTVMPAFHIDCQctaAMAAFsagatfvLLEKYSARAFWG--------Q 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 311 VQALKPTVFCGVPRVYDKLyagIMQKISAsglirkklfdfaynyklgnmrkgfsqEEASPRLDRLMF-----DKIKEALG 385
Cdd:PRK08008 258 VCKYRATITECIPMMIRTL---MVQPPSA--------------------------NDRQHCLREVMFylnlsDQEKDAFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 386 GRAHMllsgaaplprhveeflriipasNLSQGYGLTEScggsfttlagvfsMVGTVGVPmPTVEARLVSV--PEMGYDAF 463
Cdd:PRK08008 309 ERFGV----------------------RLLTSYGMTET-------------IVGIIGDR-PGDKRRWPSIgrPGFCYEAE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 464 SAD-----VPR---GEICLRG---NSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYV 531
Cdd:PRK08008 353 IRDdhnrpLPAgeiGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENV 431
|
490 500
....*....|....*....|..
gi 22330132 532 AVENLENTYSRCPLIAQIWVYG 553
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVG 453
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
80-512 |
8.79e-16 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 81.44 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSIlscqkgcssnlktivsfgevsstqkEEAKNQCVSLfswnEFSLMGNLDEANLPRKRK-TDICTIMYTSGTTGEP 238
Cdd:COG1020 582 ALAARL-------------------------PELGVPVLAL----DALALAAEPATNPPVPVTpDDLAYVIYTSGSTGRP 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGV------ILNNAAISVQVLSI---DKMLEVTDRSCDTS--DVFfsyLPLAH--CydqvmeIYFLSRGssvgyWRGDIR 305
Cdd:COG1020 633 KGVmvehraLVNLLAWMQRRYGLgpgDRVLQFASLSFDASvwEIF---GALLSgaT------LVLAPPE-----ARRDPA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 306 YLMDDVQALKPTVFCGVPRVYDKLyagimqkisasglirkklfdfaynyklgnmrkgfsQEEASPRLDRLmfdkikealg 385
Cdd:COG1020 699 ALAELLARHRVTVLNLTPSLLRAL-----------------------------------LDAAPEALPSL---------- 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 386 grAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGS-FTTLAGVFSMVGTV--GVPMPTVEARLVsvpemgyDA 462
Cdd:COG1020 734 --RLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDStYYEVTPPDADGGSVpiGRPIANTRVYVL-------DA 804
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330132 463 FSADVP---RGEICLRGNSMFSGYHKRQDLTDQVLIDG--------WFHTGDIGEWQEDGS 512
Cdd:COG1020 805 HLQPVPvgvPGELYIGGAGLARGYLNRPELTAERFVADpfgfpgarLYRTGDLARWLPDGN 865
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-539 |
1.51e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 79.41 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 213 DEANLPRKR--KTDICTIMYTSGTTGEPKGV------ILNNAAISVQVLSIDKmlevtdrscdtSDVFFSYLPLAHCYD- 283
Cdd:cd05922 105 ARASAPAHEvsHEDLALLLYTSGSTGSPKLVrlshqnLLANARSIAEYLGITA-----------DDRALTVLPLSYDYGl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 284 QVMEIYFLSRGSSVGYWRGDI-RYLMDDVQALKPTVFCGVPrvydklyagimqkisasglirkklfdfaYNYKLgnmrkg 362
Cdd:cd05922 174 SVLNTHLLRGATLVLTNDGVLdDAFWEDLREHGATGLAGVP----------------------------STYAM------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 363 fsqeeasprLDRLMFDKIKEAlggRAHMLLSGAAPLPRH-VEEFLRIIPASNLSQGYGLTEsCGGSFTTLAG--VFSMVG 439
Cdd:cd05922 220 ---------LTRLGFDPAKLP---SLRYLTQAGGRLPQEtIARLRELLPGAQVYVMYGQTE-ATRRMTYLPPerILEKPG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 440 TVGVPMPtvEARLVSVPEMGYDAFSADVprGEICLRGNSMFSGYHKR-QDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDR 518
Cdd:cd05922 287 SIGLAIP--GGEFEILDDDGTPTPPGEP--GEIVHRGPNVMKGYWNDpPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGR 362
|
330 340
....*....|....*....|.
gi 22330132 519 KKNIFKLSqGEYVAVENLENT 539
Cdd:cd05922 363 RDRMIKLF-GNRISPTEIEAA 382
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
50-536 |
1.63e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.09 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 50 FFSEAVKKYPNEQMLGQRvttDSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGI 129
Cdd:PRK12582 54 LLAKWAAEAPDRPWLAQR---EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 130 TYVPL---YD--SLGVNAVEFIINHAEVSLVFVQE--------KTVS----SILSCQKGCSSNlkTIVSFGEVSSTQKEE 192
Cdd:PRK12582 131 PAAPVspaYSlmSHDHAKLKHLFDLVKPRVVFAQSgapfaralAALDlldvTVVHVTGPGEGI--ASIAFADLAATPPTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 193 AKNQCVslfswnefslmgnldEANLPRKrktdICTIMYTSGTTGEPKGVILNNAAISVQvlsIDKMLEVTDRSCDTS-DV 271
Cdd:PRK12582 209 AVAAAI---------------AAITPDT----VAKYLFTSGSTGMPKAVINTQRMMCAN---IAMQEQLRPREPDPPpPV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 272 FFSYLPLAHCYdqvmeiyflsrGSSVGY----WRGDIRYLmDD-----------VQALK---PTVFCGVPRVYDKLyAGI 333
Cdd:PRK12582 267 SLDWMPWNHTM-----------GGNANFngllWGGGTLYI-DDgkplpgmfeetIRNLReisPTVYGNVPAGYAML-AEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 334 MQKISAsglIRKKLFDfaynyKLGNMRKGfsqeeaSPRLDRLMFDKIkEALGGRAhmllSGaaplprhveeflRIIPasn 413
Cdd:PRK12582 334 MEKDDA---LRRSFFK-----NLRLMAYG------GATLSDDLYERM-QALAVRT----TG------------HRIP--- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 414 LSQGYGLTEScGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPEmgydafsadvpRGEICLRGNSMFSGYHKRQDLTDQV 493
Cdd:PRK12582 380 FYTGYGATET-APTTTGTHWDTERVGLIGLPLPGVELKLAPVGD-----------KYEVRVKGPNVTPGYHKDPELTAAA 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 22330132 494 LI-DGWFHTGDIGEW--QEDGSMKII--DRKKNIFKLSQGEYVAVENL 536
Cdd:PRK12582 448 FDeEGFYRLGDAARFvdPDDPEKGLIfdGRVAEDFKLSTGTWVSVGTL 495
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
40-586 |
2.67e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 79.23 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 40 LPTDIDSP----WQFFSEAVKKYPNE---QMLGQRvttdskvgpytwITYKEAHDAAIRIGSAIRSR-GVDPGHCCGIYG 111
Cdd:PRK08314 1 LPKSLTLPetslFHNLEVSARRYPDKtaiVFYGRA------------ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 112 ANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCQKG-------CSSNLKTIVSFGE 184
Cdd:PRK08314 69 QNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNlrlrhviVAQYSDYLPAEPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 185 VS-----STQKEEAKNQCVSLFSWNEfslmgNLDEANLPRKRKT---DICTIMYTSGTTGEPKGVILNNAAISVQVLSid 256
Cdd:PRK08314 149 IAvpawlRAEPPLQALAPGGVVAWKE-----ALAAGLAPPPHTAgpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVG-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 257 kmlEVTDRSCDTSDVFFSYLPLAHCYDQV--ME--IYflsRGSSVgywrgdirYLMddvqalkptvfcgvPRvYDKLYAG 332
Cdd:PRK08314 222 ---SVLWSNSTPESVVLAVLPLFHVTGMVhsMNapIY---AGATV--------VLM--------------PR-WDREAAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 333 --I-MQKISASGLIRKKLFDFAynyklgnmrkgfsqeeASPRLDRLMFDKIKeALGGrahmllsGAAPLPRHVEEFLRII 409
Cdd:PRK08314 273 rlIeRYRVTHWTNIPTMVVDFL----------------ASPGLAERDLSSLR-YIGG-------GGAAMPEAVAERLKEL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 410 PASNLSQGYGLTEscggsftTLAGVFS------MVGTVGVPMPTVEARLVSvPEMGydafsADVPR---GEICLRGNSMF 480
Cdd:PRK08314 329 TGLDYVEGYGLTE-------TMAQTHSnppdrpKLQCLGIPTFGVDARVID-PETL-----EELPPgevGEIVVHGPQVF 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 481 SGYHKRQDLTDQVLI--DG--WFHTGDIGEWQEDGSMKIIDRKKNI-----FKLSQGEyvaVENLenTYsRCPLIAQIWV 551
Cdd:PRK08314 396 KGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMinasgFKVWPAE---VENL--LY-KHPAIQEACV 469
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 22330132 552 Y-------GNSFESFLV------GVVVPDRkaIEDWAKLN---YQSPNDFE 586
Cdd:PRK08314 470 IatpdprrGETVKAVVVlrpearGKTTEEE--IIAWAREHmaaYKYPRIVE 518
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
80-577 |
4.99e-15 |
|
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: 78.29 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKGCSSnLKTIVSFGEVSSTQKEEAKNQCVSlfsWNEfsLMGNLDEANLPRKRKTDICTIMYTSGTTGEPK 239
Cdd:TIGR03098 106 ERLDLLHPALPGCHD-LRTLIIVGDPAHASEGHPGEEPAS---WPK--LLALGDADPPHPVIDSDMAAILYTSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVTdrscdTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYwrgdIRYLM--DDVQALKP- 316
Cdd:TIGR03098 180 GVVLSHRNLVAGAQSVATYLENR-----PDDRLLAVLPLSFDYGFNQLTTAFYVGATVVL----HDYLLprDVLKALEKh 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 317 --TVFCGVPrvydKLYAgimqkisasglirkKLFDFAYnyklgnmrkgfsQEEASPRLDRLMfdkikeALGGRahmllsg 394
Cdd:TIGR03098 251 giTGLAAVP----PLWA--------------QLAQLDW------------PESAAPSLRYLT------NSGGA------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 395 aapLPRHVEEFLR-IIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSvpEMGYDAfsADVPRGEIC 473
Cdd:TIGR03098 288 ---MPRATLSRLRsFLPNARLFLMYGLTEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLR--EDGSEC--APGEEGELV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 474 LRGNSMFSGYHKRQDLT-----------DQVLIDG---WfhTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENT 539
Cdd:TIGR03098 361 HRGALVAMGYWNDPEKTaerfrplppfpGELHLPElavW--SGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEV 437
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 22330132 540 YSRCPLIAQIWVYGNSFESF---LVGVVVPDRKAIEDWAKL 577
Cdd:TIGR03098 438 AYATGLVAEAVAFGVPDPTLgqaIVLVVTPPGGEELDRAAL 478
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
81-526 |
5.46e-15 |
|
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: 77.76 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEK 160
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 tvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrktDICTIMYTSGTTGEPKG 240
Cdd:cd05972 82 ---------------------------------------------------------------DPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 VILNNAA----ISVQVLSIDkmLEVTDRSCDTSD------VFFSYL-PLAHcydqvmeiyflsrGSSV---GYWRGDIRY 306
Cdd:cd05972 99 VLHTHSYplghIPTAAYWLG--LRPDDIHWNIADpgwakgAWSSFFgPWLL-------------GATVfvyEGPRFDAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 307 LMDDVQALKPTVFCGVPRVYDKLyagIMQKISAsglirkklfdfaynYKLGNMRKGFSQEEAsprLDRLMFDKIKEALGg 386
Cdd:cd05972 164 ILELLERYGVTSFCGPPTAYRML---IKQDLSS--------------YKFSHLRLVVSAGEP---LNPEVIEWWRAATG- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 387 rahmllsgaapLPRHveeflriipasnlsQGYGLTEScggsfTTLAGVFSMV----GTVGVPMPtvearlvsvpemGYDA 462
Cdd:cd05972 223 -----------LPIR--------------DGYGQTET-----GLTVGNFPDMpvkpGSMGRPTP------------GYDV 260
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330132 463 FSAD-----VPRGE---ICLRGN--SMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLS 526
Cdd:cd05972 261 AIIDddgreLPPGEegdIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
220-577 |
7.70e-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: 77.53 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 220 KRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVtdrscDTSDVFFSYLPLAHcyDQVMEIYFLSrgssvGY 299
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW-----KTKDRILSWMPLTH--DMGLIAFHLA-----PL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 300 WRGDIRYLMddvqalkPT-VFCGVPRVYdklyagiMQKISASGLIRKKLFDFAYNYklgnmrkgfsqeeaspRLDRLMFD 378
Cdd:cd05908 171 IAGMNQYLM-------PTrLFIRRPILW-------LKKASEHKATIVSSPNFGYKY----------------FLKTLKPE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 379 KIKEALGGRAHMLLSGAAP-LPRHVEEFLRIIPASNLSQG-----YGLTE-SCGGSFTTLAGVFSMVG------TVGVPM 445
Cdd:cd05908 221 KANDWDLSSIRMILNGAEPiDYELCHEFLDHMSKYGLKRNailpvYGLAEaSVGASLPKAQSPFKTITlgrrhvTHGEPE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 446 PTV---EARLVSVPEMGYDAFSADVpR--------------GEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGeW 507
Cdd:cd05908 301 PEVdkkDSECLTFVEVGKPIDETDI-RicdednkilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLG-F 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330132 508 QEDGSMKIIDRKKN-IFKLSQGEY------VAVENLENTYSRcplIAQIWVYGNSFESFLVGVVVPDRKAIEDWAKL 577
Cdd:cd05908 379 IRNGRLVITGREKDiIFVNGQNVYphdierIAEELEGVELGR---VVACGVNNSNTRNEEIFCFIEHRKSEDDFYPL 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-522 |
8.41e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 76.37 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCYDQVMEIYF-LSRGSSVGY--- 299
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPD-----DVLLCGLPLFHVNGSVVTLLTpLASGAHVVLagp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 300 --WRGdiRYLMDD----VQALKPTVFCGVPRVYdklyAGIMQKisasglirkklfdfAYNYKLGNMRKGFSqeeasprld 373
Cdd:cd05944 78 agYRN--PGLFDNfwklVERYRITSLSTVPTVY----AALLQV--------------PVNADISSLRFAMS--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 374 rlmfdkikealggrahmllsGAAPLPrhVEEFLRIIPASNLS--QGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEAR 451
Cdd:cd05944 129 --------------------GAAPLP--VELRARFEDATGLPvvEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVR 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330132 452 LVSVPEMGYDAFSADVPR-GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:cd05944 187 IKVLDGVGRLLRDCAPDEvGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
79-523 |
2.06e-14 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 76.51 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 79 WITYKEAHDAAIRIGSAIRSRGvDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEfiinhaevslvfvq 158
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAE-------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 ekTVSSILscqkgCSSNLKTIVSFGEVSSTQKEEAKNQC-VSLFSWNEFSLMGNLDEANL--PRKRKTDICTIMYTSGTT 235
Cdd:cd05931 89 --RLAAIL-----ADAGPRVVLTTAAALAAVRAFAASRPaAGTPRLLVVDLLPDTSAADWppPSPDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 236 GEPKGVILNNAAISVQVLSIDKMLEvtdrsCDTSDVFFSYLPLAHcyDqvmeiyflsrgssvgywrgdirylMDDVQALK 315
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQIRRAYG-----LDPGDVVVSWLPLYH--D------------------------MGLIGGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 316 PTVFCGVPRVYdklyagimqkISASGLIRKKLF----------------DFAYNYKLgnmRKGfsQEEASPRLDrLmfdk 379
Cdd:cd05931 211 TPLYSGGPSVL----------MSPAAFLRRPLRwlrlisryratisaapNFAYDLCV---RRV--RDEDLEGLD-L---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 380 ikealgGRAHMLLSGAAP-----LPRHVEEFLRI-IPASNLSQGYGLTESC----------GGSFTTLAGVFSMVGTVGV 443
Cdd:cd05931 271 ------SSWRVALNGAEPvrpatLRRFAEAFAPFgFRPEAFRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRAVAV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 444 PMPTVEAR-LVSV--PEMGYDAFSAD------VPR---GEICLRGNSMFSGYHKRQDLTDQVLI-------DGWFHTGDI 504
Cdd:cd05931 345 AADDPAAReLVSCgrPLPDQEVRIVDpetgreLPDgevGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDL 424
|
490 500
....*....|....*....|....*.
gi 22330132 505 GEWQED-----GSMK--IIDRKKNIF 523
Cdd:cd05931 425 GFLHDGelyitGRLKdlIIVRGRNHY 450
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
65-538 |
3.09e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 75.97 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 65 GQRVTTDSKVGpyTW-------ITYKEAHDAAIRIGSAIRSR-GVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYD 136
Cdd:PRK05620 19 GSTVHGDTTVT--TWggaeqeqTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 137 SLGVNAVEFIINHAEVSLVFVQEKTVSSILSCQKGCSSnLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFsLMGNLDEAN 216
Cdd:PRK05620 97 QLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPC-VRAVVFIGPSDADSAAAHMPEGIKVYSYEAL-LDGRSTVYD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 217 LPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSidkmLEVTDRSCDTSDV-FFSYLPLAHcydqvmeiyFLSRGS 295
Cdd:PRK05620 175 WPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLS----LRTTDSLAVTHGEsFLCCVPIYH---------VLSWGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 296 SVGYWRGDIRYLMDD-----------VQALKPTVFCGVPRVYDKLYAGIMQKisasglirkklfdfaynyklgnmrkgfs 364
Cdd:PRK05620 242 PLAAFMSGTPLVFPGpdlsaptlakiIATAMPRVAHGVPTLWIQLMVHYLKN---------------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 365 qeeaSPRldRLMFDKIkealggrahmlLSGAAPLPRHV----EEFLRIipasNLSQGYGLTEScggsfttlagvfSMVGT 440
Cdd:PRK05620 294 ----PPE--RMSLQEI-----------YVGGSAVPPILikawEERYGV----DVVHVWGMTET------------SPVGT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 441 VGVPMPTV--EARL---VS-----------VPEMGYDAFSADVPRGEICLRGN------------------SMFSGyHKR 486
Cdd:PRK05620 341 VARPPSGVsgEARWayrVSqgrfpasleyrIVNDGQVMESTDRNEGEIQVRGNwvtasyyhspteegggaaSTFRG-EDV 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 22330132 487 QDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLEN 538
Cdd:PRK05620 420 EDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLEN 470
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
80-577 |
6.89e-14 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 74.43 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQe 159
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrKTDICTIMYTSGTTGEPK 239
Cdd:cd17650 92 --------------------------------------------------------------PEDLAYVIYTSGTTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVTDRSCD-------TSDVFFSYLPLAHCYDQVMeiYFLSRGSsvgywRGDIRYLMDDVQ 312
Cdd:cd17650 110 GVMVEHRNVAHAAHAWRREYELDSFPVRllqmasfSFDVFAGDFARSLLNGGTL--VICPDEV-----KLDPAALYDLIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPrvydKLYAGIMQKISASGLirkklfdfaynyklgnmrkgfsqeeaspRLDRLmfdkikealggRAHMLL 392
Cdd:cd17650 183 KSRITLMESTP----ALIRPVMAYVYRNGL----------------------------DLSAM-----------RLLIVG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGS--FTTLAGVFSMVGTV--GVPMPT-----VEARLVSVPEMGYdaf 463
Cdd:cd17650 220 SDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDStyYEEGRDPLGDSANVpiGRPLPNtamyvLDERLQPQPVGVA--- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 464 sadvprGEICLRGNSMFSGYHKRQDLTDQVLIDGWF-------HTGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVENL 536
Cdd:cd17650 297 ------GELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEI 369
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 22330132 537 ENTYSRCPLIAQIWV---YGNSFESFLVGVVVPDRKAieDWAKL 577
Cdd:cd17650 370 ESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAEL 411
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
389-551 |
9.87e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 73.75 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 389 HMLLSGAAplprhveeflriIPASnLSQ-----------GYGLTEScgGSfTTLAGVFSMVGTVGVPMPTVEARLVSvpe 457
Cdd:PRK09029 244 AVLLGGAA------------IPVE-LTEqaeqqgircwcGYGLTEM--AS-TVCAKRADGLAGVGSPLPGREVKLVD--- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 458 mgydafsadvprGEICLRGNSMFSGYH---KRQDLTDQvliDGWFHTGDIGEWQeDGSMKIIDRKKNIFkLSQGEYVAVE 534
Cdd:PRK09029 305 ------------GEIWLRGASLALGYWrqgQLVPLVND---EGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPE 367
|
170
....*....|....*..
gi 22330132 535 NLENTYSRCPLIAQIWV 551
Cdd:PRK09029 368 EIERVINQHPLVQQVFV 384
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
80-526 |
1.10e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 74.31 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKGCSsnLKTI--VSFGEV-----------SSTQKEEAKNQCVSLFSwnefSLMGNLDEANLPRKRKTDIC 226
Cdd:PRK06178 139 QLAPVVEQVRAETS--LRHVivTSLADVlpaeptlplpdSLRAPRLAAAGAIDLLP----ALRACTAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 227 TIMYTSGTTGEPKGVI----------LNNAAISVQVlsidkmlevtdrscDTSDVFFSYLPLahcydqvmeiyFLSRGSS 296
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEhtqrdmvytaAAAYAVAVVG--------------GEDSVFLSFLPE-----------FWIAGEN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 297 VGYwrgdirylmddvqaLKPtVFCGVPRV----YDKLyaGIMQKISasglirkklfdfayNYKLGNMR---KGFSQEEAS 369
Cdd:PRK06178 268 FGL--------------LFP-LFSGATLVllarWDAV--AFMAAVE--------------RYRVTRTVmlvDNAVELMDH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 370 PRLDRLMFDKIKEAlggrahMLLSGAAPLPRHVEEFLRIIPASNLSQG-YGLTES--CGgSFTT--LAGVFSMVGT---V 441
Cdd:PRK06178 317 PRFAEYDLSSLRQV------RVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTEThtCD-TFTAgfQDDDFDLLSQpvfV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 442 GVPMPTVEARLVSVpEMGydafsADVP---RGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDR 518
Cdd:PRK06178 390 GLPVPGTEFKICDF-ETG-----ELLPlgaEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGR 463
|
....*...
gi 22330132 519 KKNIFKLS 526
Cdd:PRK06178 464 RKEMLKVN 471
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
224-645 |
1.53e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 73.68 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISVQvlSIDKMLEVtdrSCDTSDVFFSYLPLAH------CYDQVMeiyflSRGSSV 297
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVQ--SLAKIAIV---GYGEDDVYLHTAPLCHigglssALAMLM-----VGACHV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 298 GYWRGDIRYLMDDVQALKPTVFCGVPrvydklyaGIMQKISAsgLIRKKLFDFAYNYklgnMRKgfsqeeasprldrlmf 377
Cdd:PLN02860 243 LLPKFDAKAALQAIKQHNVTSMITVP--------AMMADLIS--LTRKSMTWKVFPS----VRK---------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 378 dkikealggrahmLLSGAAPLP-RHVEEFLRIIPASNLSQGYGLTESCGG-SFTTL-------------------AGVFS 436
Cdd:PLN02860 293 -------------ILNGGGSLSsRLLPDAKKLFPNAKLFSAYGMTEACSSlTFMTLhdptlespkqtlqtvnqtkSSSVH 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 437 M-VGT-VGVPMPTVEARLvsvpemGYDAFSADvprGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSM 513
Cdd:PLN02860 360 QpQGVcVGKPAPHVELKI------GLDESSRV---GRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKAGNL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 514 KIIDRKKNIFKlSQGEYVAVENLENTYSRCPLIAQIWVYGNSfESFLVGVVVPDRKAIEDWAKLNYQSPNDFES--LCQn 591
Cdd:PLN02860 431 WLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGVP-DSRLTEMVVACVRLRDGWIWSDNEKENAKKNltLSS- 507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 22330132 592 lkaqkyflDELNSTAKQYQLKGFEMLKAIHLEPNPFDierdlITPTFKLKRPQL 645
Cdd:PLN02860 508 --------ETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-567 |
2.39e-13 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 72.34 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVfvqe 159
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanLPRKRKTDICTIMYTSGTTGEPK 239
Cdd:cd17653 99 ---------------------------------------------------------LTTDSPDDLAYIIFTSGSTGIPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVT--DRSCDTSDVFFSYlplahCYDQVMEIyfLSRGSSVgYWRGDIRYLMDDVQALkpT 317
Cdd:cd17653 122 GVMVPHRGVLNYVSQPPARLDVGpgSRVAQVLSIAFDA-----CIGEIFST--LCNGGTL-VLADPSDPFAHVARTV--D 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 318 VFCGVPrvydklyaGIMQKISASGLirkklfdfaynyklgnmrkgfsqeeasPRLDRLmfdkikealggrahmLLSGAAP 397
Cdd:cd17653 192 ALMSTP--------SILSTLSPQDF---------------------------PNLKTI---------------FLGGEAV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 398 LPRHVEEFLriiPASNLSQGYGLTE-SCGGSFT-TLAGVFSmvgTVGVPMPTVEARLVsvpemgyDAFSADVP---RGEI 472
Cdd:cd17653 222 PPSLLDRWS---PGRRLYNAYGPTEcTISSTMTeLLPGQPV---TIGKPIPNSTCYIL-------DADLQPVPegvVGEI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 473 CLRGNSMFSGYHKRQDLT-DQVLIDGWFH------TGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVENLENT-YSRCP 544
Cdd:cd17653 289 CISGVQVARGYLGNPALTaSKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVvLQSQP 367
|
490 500
....*....|....*....|...
gi 22330132 545 LIAQiwVYGNSFESFLVGVVVPD 567
Cdd:cd17653 368 EVTQ--AAAIVVNGRLVAFVTPE 388
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
80-526 |
2.48e-13 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 72.91 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVF-VQ 158
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVaIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 EKTVSS-ILSCQKGCSSNLKTIVSFGEVSStqkeeaknqcvslfSWNEF-SLMGNLDEANLPRKRKT-----DICTIMYT 231
Cdd:cd05970 128 EDNIPEeIEKAAPECPSKPKLVWVGDPVPE--------------GWIDFrKLIKNASPDFERPTANSypcgeDILLVYFS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 232 SGTTGEPKGVILNNAAISVQVLSID--KMLEVTDRSCDTSDVFFSYLPLAHCYDQVMEiyflsrGSSV---GYWRGDIRY 306
Cdd:cd05970 194 SGTTGMPKMVEHDFTYPLGHIVTAKywQNVREGGLHLTVADTGWGKAVWGKIYGQWIA------GAAVfvyDYDKFDPKA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 307 LMDDVQALKPTVFCGVPRVYdklyagimqkisaSGLIRKKLFDfaynYKLGNMRKGFSQEEAsprLDRLMFDKIKEALGg 386
Cdd:cd05970 268 LLEKLSKYGVTTFCAPPTIY-------------RFLIREDLSR----YDLSSLRYCTTAGEA---LNPEVFNTFKEKTG- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 387 rahmllsgaaplprhveeflriipaSNLSQGYGLTEsCGGSFTTLAGVFSMVGTVGVPMPTVEARLvsvpeMGYDAFSAD 466
Cdd:cd05970 327 -------------------------IKLMEGFGQTE-TTLTIATFPWMEPKPGSMGKPAPGYEIDL-----IDREGRSCE 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330132 467 V-PRGEICLRGNS-----MFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLS 526
Cdd:cd05970 376 AgEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
376-567 |
3.09e-13 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 71.18 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 376 MFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRIIPASNLSQ---GYGLTEscGGSFTTLAGV-FSMVGTVGVPMPTVEAR 451
Cdd:cd17636 98 TIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRkpgGYGQTE--VMGLATFAALgGGAIGGAGRPSPLVQVR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 452 LVsvpemgyDAFSADVPRG---EICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlsqg 528
Cdd:cd17636 176 IL-------DEDGREVPDGevgEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK---- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22330132 529 eyVAVENL-----ENTYSRCPLIAQIWVYGnsfesflvgvvVPD 567
Cdd:cd17636 245 --SGAENIypaevERCLRQHPAVADAAVIG-----------VPD 275
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
80-570 |
3.92e-13 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 72.23 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVssilsCQKGCSSNLKTIVSFGEVSSTQKEEAknqcvslfswnefSLMGNLDEANLPRKRKT-------DICTIMYTS 232
Cdd:PRK05852 124 DGP-----HDRAEPTTRWWPLTVNVGGDSGPSGG-------------TLSVHLDAATEPTPATStpeglrpDDAMIMFTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 233 GTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCYDQVMEIY-FLSRGSSV---GYWRGDIRYLM 308
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSVRAIITGYRLSPR-----DATVAVMPLYHGHGLIAALLaTLASGGAVllpARGRFSAHTFW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 309 DDVQALKPTVFCGVPRVYdklyagimqkisasglirkklfdfaynyklgnmrkgfsqeeasprldRLMFDKIKEALGGRA 388
Cdd:PRK05852 261 DDIKAVGATWYTAVPTIH-----------------------------------------------QILLERAATEPSGRK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 389 HMLL----SGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSM----VGTVGVPMPTVEARLVSVPEMGY 460
Cdd:PRK05852 294 PAALrfirSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQtenpVVSTGLVGRSTGAQIRIVGSDGL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 461 DAFSADVprGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTY 540
Cdd:PRK05852 374 PLPAGAV--GEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVL 450
|
490 500 510
....*....|....*....|....*....|...
gi 22330132 541 SRCPLIAQIWVYGNSFESF---LVGVVVPDRKA 570
Cdd:PRK05852 451 ASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESA 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
80-606 |
1.33e-12 |
|
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: 70.62 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQ- 158
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 159 --EKTVSSILScqKGCSSNLKTIVSFGEVSSTqkeeaknqcvslfswnefslmGNLDEAnlPRKRKTDICTIMYTSGTTG 236
Cdd:cd05923 109 daQVMDAIFQS--GVRVLALSDLVGLGEPESA---------------------GPLIED--PPREPEQPAFVFYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 237 EPKGVILNNAAISVQVLSidkMLEVTDRSCDTSDVFFSYLPLAHCydqvmeIYFlsRGSSVGYWRGDIRYLM----DDVQ 312
Cdd:cd05923 164 LPKGAVIPQRAAESRVLF---MSTQAGLRHGRHNVVLGLMPLYHV------IGF--FAVLVAALALDGTYVVveefDPAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALK------PTVFCGVPRVYDKLYAgimqkisasglirkklfdfaynyklgnmrkgfSQEEASPRLDRLmfdkikealgg 386
Cdd:cd05923 233 ALKlieqerVTSLFATPTHLDALAA--------------------------------AAEFAGLKLSSL----------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 387 rAHMLLSGAA---PLPRHVEEFLRIiPASNLsqgYGLTEScggsFTTLAGVFSMVGTVGVPMPTVEARLVSVPEmGYDAF 463
Cdd:cd05923 270 -RHVTFAGATmpdAVLERVNQHLPG-EKVNI---YGTTEA----MNSLYMRDARTGTEMRPGFFSEVRIVRIGG-SPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 464 SADVPRGEIC--LRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYS 541
Cdd:cd05923 340 LANGEEGELIvaAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLS 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330132 542 RCPLIAQIWVYGNSFESF---LVGVVVPDRKAIedwaklnyqSPNDFESLCQ-----NLKAQK--YFLDELNSTA 606
Cdd:cd05923 419 RHPGVTEVVVIGVADERWgqsVTACVVPREGTL---------SADELDQFCRaselaDFKRPRryFFLDELPKNA 484
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
80-577 |
1.60e-12 |
|
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: 70.03 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVfvqe 159
Cdd:cd17643 13 LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnLDEANlprkrktDICTIMYTSGTTGEPK 239
Cdd:cd17643 89 ----------------------------------------------------LTDPD-------DLAYVIYTSGSTGRPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISvqvlsidKMLEVTDR--SCDTSDV---FFSYlplahCYD-QVMEIY-FLSRGSS---VGYW-RGDIRYLM 308
Cdd:cd17643 110 GVVVSHANVL-------ALFAATQRwfGFNEDDVwtlFHSY-----AFDfSVWEIWgALLHGGRlvvVPYEvARSPEDFA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 309 DDVQALKPTVFCGVPrvydklyagimqkiSAsglirkklfdFaynykLGNMRKGFSQEEASPRLdRLMFdkikeaLGGRA 388
Cdd:cd17643 178 RLLRDEGVTVLNQTP--------------SA----------F-----YQLVEAADRDGRDPLAL-RYVI------FGGEA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 389 hmLLsgAAPLPRHVEEFlrIIPASNLSQGYGLTESCggSFTT--------LAGvfSMVGTVGVPMPTVEARLVsvpemgy 460
Cdd:cd17643 222 --LE--AAMLRPWAGRF--GLDRPQLVNMYGITETT--VHVTfrpldaadLPA--AAASPIGRPLPGLRVYVL------- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 461 DAFSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLIDGWF--------HTGDIGEWQEDGSMKIIDR-----KKNIFK 524
Cdd:cd17643 285 DADGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmyRTGDLARRLPDGELEYLGRadeqvKIRGFR 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 22330132 525 LSQGEyvavenLENTYSRCPLIAQIWVYGNSFE---SFLVGVVVPDRKAIEDWAKL 577
Cdd:cd17643 365 IELGE------IEAALATHPSVRDAAVIVREDEpgdTRLVAYVVADDGAAADIAEL 414
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
49-518 |
1.70e-12 |
|
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: 70.05 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNEQMLgqrVTTDSKvgpytwITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG 128
Cdd:cd17655 1 ELFEEQAEKTPDHTAV---VFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 129 ITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCqkgcssnlktivsfGEVSSTQKEEAKNQcvslfswnefsl 208
Cdd:cd17655 72 GAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAFI--------------GLIDLLDEDTIYHE------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 209 mgnlDEANLPRKRK-TDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVtdrscDTSDVFFSYLPLAhcYD-QVM 286
Cdd:cd17655 126 ----ESENLEPVSKsDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ-----GEHLRVALFASIS--FDaSVT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 287 EIYF-LSRGSSVgywrgdirYLMDDVQALKPTVFCgvpRVYDKLYAGIMqKISASGLirkKLFDFAynyklgnmrkgfsq 365
Cdd:cd17655 195 EIFAsLLSGNTL--------YIVRKETVLDGQALT---QYIRQNRITII-DLTPAHL---KLLDAA-------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 366 eeasprlDRLMFDKIKealggraHMLLSGAAPLPRHVEEFLRIIPAS-NLSQGYGLTESCGGSFTTLAGVfSMVGTVGVP 444
Cdd:cd17655 246 -------DDSEGLSLK-------HLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVDASIYQYEP-ETDQQVSVP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 445 M--PTVEARLVSVpemgyDAFSADVP---RGEICLRGNSMFSGYHKRQDLTDQVLIDGWF-------HTGDIGEWQEDGS 512
Cdd:cd17655 311 IgkPLGNTRIYIL-----DQYGRPQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermyRTGDLARWLPDGN 385
|
....*.
gi 22330132 513 MKIIDR 518
Cdd:cd17655 386 IEFLGR 391
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
81-606 |
1.30e-11 |
|
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: 67.12 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVD-PGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd05958 12 TYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALCAH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd05958 92 ALTAS----------------------------------------------------------DDICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 G-------VILNNAAISVQVLSidkmLEVTDRSCDTSDVFFSYlplahCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQ 312
Cdd:cd05958 114 AtmhfhrdPLASADRYAVNVLR----LREDDRFVGSPPLAFTF-----GLGGVLLFPFGVGASGVLLEEATPDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPrvydKLYAGIMQKISASGlirkklfdfaynYKLGNMRKGFSQEEASPrldRLMFDKIKEALGgrahmll 392
Cdd:cd05958 185 RYKPTVLFTAP----TAYRAMLAHPDAAG------------PDLSSLRKCVSAGEALP---AALHRAWKEATG------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 sgaaplprhveeflriIPasnLSQGYGLTESCgGSFTTLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVPRGEI 472
Cdd:cd05958 239 ----------------IP---IIDGIGSTEMF-HIFISARPGDARPGATGKPVPGYEAKVV-------DDEGNPVPDGTI 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 473 ---CLRGNsmfSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLIAQ 548
Cdd:cd05958 292 grlAVRGP---TGCRYLADKRQRTYVqGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAE 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330132 549 IWVYGNSFESFLVGV---------VVPDR---KAIEDWAKLN---YQSPNDFEslcqnlkaqkyFLDELNSTA 606
Cdd:cd05958 368 CAVVGHPDESRGVVVkafvvlrpgVIPGPvlaRELQDHAKAHiapYKYPRAIE-----------FVTELPRTA 429
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
49-569 |
1.65e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 66.99 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNEQML--GQRVttdskvgpYTWITYKEAHDAairIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMS 126
Cdd:PRK07470 11 HFLRQAARRFPDRIALvwGDRS--------WTWREIDARVDA---LAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 127 QGITYVPlydslgvnaVEFIINHAEVSlvFVQEKTVSSILSCQ----------KGCSSNLKTIVSFGEVSSTQKEEAknq 196
Cdd:PRK07470 80 LGAVWVP---------TNFRQTPDEVA--YLAEASGARAMICHadfpehaaavRAASPDLTHVVAIGGARAGLDYEA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 197 cvslfswnefslmgnLDEANLPRKRKT------DICTIMYTSGTTGEPKgvilnnAAisvqVLSIDKM-LEVTDRSCD-- 267
Cdd:PRK07470 146 ---------------LVARHLGARVANaavdhdDPCWFFFTSGTTGRPK------AA----VLTHGQMaFVITNHLADlm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 268 ----TSDVFFSYLPLAHcydqvmeiyflsrGSSvgywrgdIRYLMDDVQALKpTVFCGVPRvydklyagiMQKISASGLI 343
Cdd:PRK07470 201 pgttEQDASLVVAPLSH-------------GAG-------IHQLCQVARGAA-TVLLPSER---------FDPAEVWALV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 344 RKklfdfaynYKLGNMrkgFsqeeASPRLDRLMFDKikEALGGRAHMLLS----GAAPLPRHVEEFLRIIPASNLSQGYG 419
Cdd:PRK07470 251 ER--------HRVTNL---F----TVPTILKMLVEH--PAVDRYDHSSLRyviyAGAPMYRADQKRALAKLGKVLVQYFG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 420 LTEsCGGSFTTLA--------GVFSMVGTVGVPMPTVEarlVSVpemgYDAFSADVP---RGEICLRGNSMFSGYHKRQD 488
Cdd:PRK07470 314 LGE-VTGNITVLPpalhdaedGPDARIGTCGFERTGME---VQI----QDDEGRELPpgeTGEICVIGPAVFAGYYNNPE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 489 LTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGnsfesflvgvvVPDR 568
Cdd:PRK07470 386 ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPDP 453
|
.
gi 22330132 569 K 569
Cdd:PRK07470 454 V 454
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
217-540 |
1.73e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 67.68 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 217 LPRKRKTDICTIMYTSGTTGEPKGV------ILNNAAisvQVLS-IDkmlevtdrsCDTSDVFFSYLPLAHCYdqvmeiy 289
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVvlshrnLLANRA---QVAArID---------FSPEDKVFNALPVFHSF------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 290 flsrGSSVGywrgdirylmddvqALKPTVFcGVPrVYdkLYAG------IMQKISASG---LIRKKLF-----DFAYNYK 355
Cdd:PRK06814 848 ----GLTGG--------------LVLPLLS-GVK-VF--LYPSplhyriIPELIYDTNatiLFGTDTFlngyaRYAHPYD 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 356 LGNMRKGFSQEEasprldrlmfdKIKEAlggrahmllsgaaplPRHV--EEF-LRIIpasnlsQGYGLTESCGG-SFTTl 431
Cdd:PRK06814 906 FRSLRYVFAGAE-----------KVKEE---------------TRQTwmEKFgIRIL------EGYGVTETAPViALNT- 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 432 aGVFSMVGTVGVPMPTVEARLVSVP--EMGydafsadvprGEICLRGNSMFSGYHKrqdlTD-----QVLIDGWFHTGDI 504
Cdd:PRK06814 953 -PMHNKAGTVGRLLPGIEYRLEPVPgiDEG----------GRLFVRGPNVMLGYLR----AEnpgvlEPPADGWYDTGDI 1017
|
330 340 350
....*....|....*....|....*....|....*....
gi 22330132 505 GEWQEDGSMKIIDRKKNIFKLSqGEYV---AVENLENTY 540
Cdd:PRK06814 1018 VTIDEEGFITIKGRAKRFAKIA-GEMIslaAVEELAAEL 1055
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
80-570 |
2.52e-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: 66.53 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilSCQKGCSSNLKTIVSFGEVSSTQKEEAKnqcvslfswnefslmgnldeanlPRKRKTDICTIMYTSGTTGEPK 239
Cdd:cd12114 93 -------PDAQLDVAVFDVLILDLDALAAPAPPPP-----------------------VDVAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVT--DR-------SCDTS--DVFFSylplahcydqvmeiyfLSRGSSV----GYWRGDI 304
Cdd:cd12114 143 GVMISHRAALNTILDINRRFAVGpdDRvlalsslSFDLSvyDIFGA----------------LSAGATLvlpdEARRRDP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 305 RYLMDDVQALKPTVFCGVPRVYDKL--YAGimqkiSASGLIRkklfdfaynyklgnmrkgfsqeeaSPRLDRLMFDKIKE 382
Cdd:cd12114 207 AHWAELIERHGVTLWNSVPALLEMLldVLE-----AAQALLP------------------------SLRLVLLSGDWIPL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 383 ALGGRAHMLLSGAaplprhveeflRIIpasnlsqgyglteSCGGSftTLAGVFSMVGTVGvpmpTVEARLVSVPeMGY-- 460
Cdd:cd12114 258 DLPARLRALAPDA-----------RLI-------------SLGGA--TEASIWSIYHPID----EVPPDWRSIP-YGRpl 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 461 --------DAFSADVP---RGEICLRGNSMFSGYHKRQDLTDQVLID-----GWFHTGDIGEWQEDGSMKIIDRKKNIFK 524
Cdd:cd12114 307 anqryrvlDPRGRDCPdwvPGELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 22330132 525 LsQGEYVAVENLENTYSRCPLIAQ--IWVYGNSFESFLVGVVVPDRKA 570
Cdd:cd12114 387 V-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
391-606 |
3.74e-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: 64.73 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 LLSGAAPLPRHVEEFLR-IIPASNLSQGYGLTEScggSFTT--LAGVFSMVGTVGVPMPTVEARLVSvpemgydafSADV 467
Cdd:cd17633 115 IFSSGQKLFESTKKKLKnIFPKANLIEFYGTSEL---SFITynFNQESRPPNSVGRPFPNVEIEIRN---------ADGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 468 PRGEICLRGNSMFSGYHKRQDLTDqvliDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIA 547
Cdd:cd17633 183 EIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIE 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330132 548 QIWVYGNSFESF---LVGVVVPDrkaiedwaKLNYQSPNDFesLCQNLKAQK-----YFLDELNSTA 606
Cdd:cd17633 258 EAIVVGIPDARFgeiAVALYSGD--------KLTYKQLKRF--LKQKLSRYEipkkiIFVDSLPYTS 314
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
81-553 |
4.55e-11 |
|
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: 65.60 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEK 160
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 tvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanLPRKR-KTDICTIMYTSGTTGEPK 239
Cdd:cd05969 82 --------------------------------------------------------LYERTdPEDPTLLHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSI---------DKMLEVTDRSCDTSDVFFSYLPLAH-CYDQVMEIYFlsrgsSVGYWRGDIrylmd 309
Cdd:cd05969 106 GVLHVHDAMIFYYFTGkyvldlhpdDIYWCTADPGWVTGTVYGIWAPWLNgVTNVVYEGRF-----DAESWYGII----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 310 dvQALKPTVFCGVPrvydklyagimqkiSASGLIRKKLFDFAYNYKLGNMRkgFSQEEASPrldrLMFDKIK---EALGG 386
Cdd:cd05969 176 --ERVKVTVWYTAP--------------TAIRMLMKEGDELARKYDLSSLR--FIHSVGEP----LNPEAIRwgmEVFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 387 RAHmllsgaaplprhveeflriipasnlsQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVS-----VP--EMG 459
Cdd:cd05969 234 PIH--------------------------DTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDengneLPpgTKG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 460 YDAFSADVPrgeiclrgnSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENT 539
Cdd:cd05969 288 ILALKPGWP---------SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESA 357
|
490
....*....|....
gi 22330132 540 YSRCPLIAQIWVYG 553
Cdd:cd05969 358 LMEHPAVAEAGVIG 371
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
80-250 |
5.70e-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: 65.68 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVssilscQKGCSSNLKTIVS---FGEVSSTQKEEAKNQCVSLFSWNE------FSLMGNLDEANLP-RKRKTDICTIM 229
Cdd:cd17634 165 GGV------RAGRSVPLKKNVDdalNPNVTSVEHVIVLKRTGSDIDWQEgrdlwwRDLIAKASPEHQPeAMNAEDPLFIL 238
|
170 180
....*....|....*....|.
gi 22330132 230 YTSGTTGEPKGVILNNAAISV 250
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLV 259
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
215-537 |
9.38e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.12 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 215 ANLPRKrKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscdtsDVFFSYLPLAHCYDQVMEIYF-LSR 293
Cdd:PRK08043 358 AQVKQQ-PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPN-----DRFMSALPLFHSFGLTVGLFTpLLT 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 294 GSSVGYWRGDIRYLMddvqalkptvfcgVPR-VYDKlyagimqkiSASGLIRKKLF-----DFAYNYKLGNMRKGFS-QE 366
Cdd:PRK08043 432 GAEVFLYPSPLHYRI-------------VPElVYDR---------NCTVLFGTSTFlgnyaRFANPYDFARLRYVVAgAE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 367 EASPRLDRLMFDKIKealggrahmllsgaaplprhveefLRIIpasnlsQGYGLTEsCggsfttlAGVFSM-------VG 439
Cdd:PRK08043 490 KLQESTKQLWQDKFG------------------------LRIL------EGYGVTE-C-------APVVSInvpmaakPG 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 440 TVGVPMPTVEARLVSVP--EMGydafsadvprGEICLRGNSMFSGYHKRQ----------DLTDQVLIDGWFHTGDIGEW 507
Cdd:PRK08043 532 TVGRILPGMDARLLSVPgiEQG----------GRLQLKGPNIMNGYLRVEkpgvlevptaENARGEMERGWYDTGDIVRF 601
|
330 340 350
....*....|....*....|....*....|
gi 22330132 508 QEDGSMKIIDRKKNIFKLSqGEYVAVENLE 537
Cdd:PRK08043 602 DEQGFVQIQGRAKRFAKIA-GEMVSLEMVE 630
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
78-242 |
1.49e-10 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 64.05 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 78 TWiTYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV 157
Cdd:cd05968 91 TL-TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 QEKTVssilscQKGCSSNLKTIVsfgevsstqkEEAKNQCVSL--------------------FSWNEFSlmgnldEANL 217
Cdd:cd05968 170 ADGFT------RRGREVNLKEEA----------DKACAQCPTVekvvvvrhlgndftpakgrdLSYDEEK------ETAG 227
|
170 180
....*....|....*....|....*...
gi 22330132 218 PRKRKT---DICTIMYTSGTTGEPKGVI 242
Cdd:cd05968 228 DGAERTeseDPLMIIYTSGTTGKPKGTV 255
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
80-577 |
1.76e-10 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 63.90 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgEVSSTQKEEAknqcVSLFSWNEFSLMGNLDEANLPRKRKTDICTIMYTSGTTGEPK 239
Cdd:cd17651 101 ------------------------ALAGELAVEL----VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVT--DRSCDTSDVFFSYlplahcydQVMEIY-FLSRGSSV----GYWRGDIRYLMDDV- 311
Cdd:cd17651 153 GVVMPHRSLANLVAWQARASSLGpgARTLQFAGLGFDV--------SVQEIFsTLCAGATLvlppEEVRTDPPALAAWLd 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 312 -----QALKPTVFcgvprvydklyagiMQKISASGLirkklfdfaynyklgnmrkgfSQEEASPRLdrlmfdkikealgg 386
Cdd:cd17651 225 eqrisRVFLPTVA--------------LRALAEHGR---------------------PLGVRLAAL-------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 387 rAHMLLSG-AAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSM---VGTVGVPMPTVEARLVsvpemgyDA 462
Cdd:cd17651 256 -RYLLTGGeQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpaPPPIGRPIDNTRVYVL-------DA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 463 FSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLIDGWF-------HTGDIGEWQEDGSMKIIDR-----KKNIFKLSQ 527
Cdd:cd17651 328 ALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRaddqvKIRGFRIEL 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 22330132 528 GEyvavenLENTYSRCPLIAQIWVYG---NSFESFLVGVVVPDRKAIEDWAKL 577
Cdd:cd17651 408 GE------IEAALARHPGVREAVVLAredRPGEKRLVAYVVGDPEAPVDAAEL 454
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
80-241 |
2.51e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 63.38 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK04813 28 LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKGCSSNLKTIVSFGEVSStqkeeaKNQCVSlfswnefslmGNldeanlprkrktDICTIMYTSGTTGEPK 239
Cdd:PRK04813 108 ELPLEILGIPVITLDELKDIFATGNPYD------FDHAVK----------GD------------DNYYIIFTSGTTGKPK 159
|
..
gi 22330132 240 GV 241
Cdd:PRK04813 160 GV 161
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
224-522 |
4.07e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 62.71 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAIsvqVLSIDKMLEVTDRSCDTsDVFFSYLPLAHcyDQVMeIYFLSrgssVGYWRGd 303
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNL---YANAEAMFVAAEFDVET-DVMVSWLPLFH--DMGM-VGFLT----VPMYFG- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 304 irylmddVQALK--PTVFCGVPRVYDKL---YAGIMqkISASGlirkklfdFAYNYKLGNMRKGfsQEEASPRLDRLMFd 378
Cdd:PRK07768 221 -------AELVKvtPMDFLRDPLLWAELiskYRGTM--TAAPN--------FAYALLARRLRRQ--AKPGAFDLSSLRF- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 379 kikealggrahmLLSGAAPL-PRHVEEFLR-----------IIPAsnlsqgYGLTEscggsfTTLAGVFSMVG------- 439
Cdd:PRK07768 281 ------------ALNGAEPIdPADVEDLLDagarfglrpeaILPA------YGMAE------ATLAVSFSPCGaglvvde 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 440 ------------------------TVGVPMPTVEARLVSvpemgyDAFSADVPR--GEICLRGNSMFSGYHKRQDLTDQV 493
Cdd:PRK07768 337 vdadllaalrravpatkgntrrlaTLGPPLPGLEVRVVD------EDGQVLPPRgvGVIELRGESVTPGYLTMDGFIPAQ 410
|
330 340
....*....|....*....|....*....
gi 22330132 494 LIDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:PRK07768 411 DADGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-580 |
4.28e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 37 LLDLPT--DIDSPWQFFSEAvkkYPNEQMLGQRVTTDSKVGPYTW--------ITYKEAHDAAIRIGSAIRSRGVDPGHC 106
Cdd:PRK12316 1979 LLDAGErqRILADWDRTPEA---YPRGPGVHQRIAEQAARAPEAIavvfgdqhLSYAELDSRANRLAHRLRARGVGPEVR 2055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 107 CGIYGANCPEWIIAMEACMSQGITYVPLyDslgvnavefiINHAEVSLVFVQEKTVSSILSCQKGCSSNLKTIVSFGEVS 186
Cdd:PRK12316 2056 VAIAAERSFELVVALLAVLKAGGAYVPL-D----------PNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLP 2124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 187 STQKEEaknqcvslfsWNEFSlmgnlDEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSC 266
Cdd:PRK12316 2125 LDRDAE----------WADYP-----DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADC 2189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 267 DTSDVFFSylplahcYDQVMEIYF--LSRGSSVgywrgdiryLMDDVQALKPtvfcgvprvyDKLYAGIMQKisasGLir 344
Cdd:PRK12316 2190 ELQFMSFS-------FDGAHEQWFhpLLNGARV---------LIRDDELWDP----------EQLYDEMERH----GV-- 2237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 345 kKLFDFAYNYkLGNMRKGFSQEEASPRLDRLMFdkikealGGRAhmlLSGAAplprhVEEFLRIIPASNLSQGYGLTESC 424
Cdd:PRK12316 2238 -TILDFPPVY-LQQLAEHAERDGRPPAVRVYCF-------GGEA---VPAAS-----LRLAWEALRPVYLFNGYGPTEAV 2300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 425 GGSFTTLAGVFSMVGTVGVPMPT-VEARLVSVPEMGYDAFSADVPrGEICLRGNSMFSGYHKRQDLTDQVLIDGWF---- 499
Cdd:PRK12316 2301 VTPLLWKCRPQDPCGAAYVPIGRaLGNRRAYILDADLNLLAPGMA-GELYLGGEGLARGYLNRPGLTAERFVPDPFsasg 2379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 500 ----HTGDIGEWQEDGSMKIIDR-----KKNIFKLSQGEYVAvENLENTYSR-CPLIAQIWVYGNSfesfLVGVVVPDRK 569
Cdd:PRK12316 2380 erlyRTGDLARYRADGVVEYLGRidhqvKIRGFRIELGEIEA-RLQAHPAVReAVVVAQDGASGKQ----LVAYVVPDDA 2454
|
570
....*....|.
gi 22330132 570 AIEDWAKLNYQ 580
Cdd:PRK12316 2455 AEDLLAELRAW 2465
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
80-568 |
7.85e-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: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSIlscqkgcssnlktivsfgevsstqkeeAKNQCVSLFSWNEFSLMGNLDEANLPRKrkTDICTIMYTSGTTGEPK 239
Cdd:cd17646 104 DLAARL---------------------------PAGGDVALLGDEALAAPPATPPLVPPRP--DNLAYVIYTSGSTGRPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSI---------DKMLEVTDRSCDTSdvffsylplahcydqVMEIYF-LSRGSSV------GywRGD 303
Cdd:cd17646 155 GVMVTHAGIVNRLLWMqdeyplgpgDRVLQKTPLSFDVS---------------VWELFWpLVAGARLvvarpgG--HRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 304 IRYLMDDVQALKPTVFCGVPrvydklyagimqkisasglirkklfdfaynyklgNMRKGFSQEEASPRLDRLMfdkikea 383
Cdd:cd17646 218 PAYLAALIREHGVTTCHFVP----------------------------------SMLRVFLAEPAAGSCASLR------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 384 lggraHMLLSGAAPLPRHVEEFLRIIPASnLSQGYGLTESCGGSftTLAGVFSMVGT----VGVPMPTVEARLVsvpemg 459
Cdd:cd17646 257 -----RVFCSGEALPPELAARFLALPGAE-LHNLYGPTEAAIDV--THWPVRGPAETpsvpIGRPVPNTRLYVL------ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 460 yDAFSADVPRG---EICLRGNSMFSGYHKRQDLTDQVLIDGWF-------HTGDIGEWQEDGSMKIIDRKKNIFKLsQGE 529
Cdd:cd17646 323 -DDALRPVPVGvpgELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKI-RGF 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 22330132 530 YVAVENLENTYSRCPLIAQIWVY---GNSFESFLVGVVVPDR 568
Cdd:cd17646 401 RVEPGEIEAALAAHPAVTHAVVVaraAPAGAARLVGYVVPAA 442
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
80-570 |
7.90e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCqkgcsSNLKTIVSFGEVSSTQKEEAKNQCVslfswnefslmgNLDEANLprkrktdiCTIMYTSGTTGEPK 239
Cdd:PRK12467 618 HLLAQLPVP-----AGLRSLCLDEPADLLCGYSGHNPEV------------ALDPDNL--------AYVIYTSGSTGQPK 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAIS---------VQVLSIDKMLEVTDRSCDTSdvffsylplahcydqVMEIYF-LSRGSSVgywrgdirYLMD 309
Cdd:PRK12467 673 GVAISHGALAnyvcviaerLQLAADDSMLMVSTFAFDLG---------------VTELFGaLASGATL--------HLLP 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 310 DVQALKPtvfcgvprvyDKLYAGImqkisasglirkklfdfaynyklgnMRKGFSQEEASP-RLDRLMFDKIKEALGGRA 388
Cdd:PRK12467 730 PDCARDA----------EAFAALM-------------------------ADQGVTVLKIVPsHLQALLQASRVALPRPQR 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 389 HMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFT---TLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSA 465
Cdd:PRK12467 775 ALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTyelSDEERDFGNVPIGQPLANLGLYIL-------DHYLN 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 466 DVP---RGEICLRGNSMFSGYHKRQDLT------DQVLIDG--WFHTGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVE 534
Cdd:PRK12467 848 PVPvgvVGELYIGGAGLARGYHRRPALTaerfvpDPFGADGgrLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELG 926
|
490 500 510
....*....|....*....|....*....|....*...
gi 22330132 535 NLENTYSRCPLI--AQIWVYGNSFESFLVGVVVPDRKA 570
Cdd:PRK12467 927 EIEARLLAQPGVreAVVLAQPGDAGLQLVAYLVPAAVA 964
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
81-553 |
1.10e-09 |
|
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: 60.91 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVqek 160
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 tvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnlDEANlprkrktDICTIMYTSGTTGEPKG 240
Cdd:cd05971 85 ----------------------------------------------------DGSD-------DPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 vILNNAAISVQVLSIDKM-LEVTDRscdTSDVFFSYLPLAhcydqvmeiyflsrgssvgyWRGDiryLMDdvqALKPTVF 319
Cdd:cd05971 106 -ALHAHRVLLGHLPGVQFpFNLFPR---DGDLYWTPADWA--------------------WIGG---LLD---VLLPSLY 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 320 CGVPRVydklyAGIMQKISAsglirKKLFDFAYNYKLGN----------MRKGFSQEEASPRLDRLMFDKiKEALGGRah 389
Cdd:cd05971 156 FGVPVL-----AHRMTKFDP-----KAALDLMSRYGVTTaflpptalkmMRQQGEQLKHAQVKLRAIATG-GESLGEE-- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 390 MLLSGAAPLPRHVEEFlriipasnlsqgYGLTEsCGGSFTTLAGVFSMV-GTVGVPMPTVEARLVsvpemgyDAFSADVP 468
Cdd:cd05971 223 LLGWAREQFGVEVNEF------------YGQTE-CNLVIGNCSALFPIKpGSMGKPIPGHRVAIV-------DDNGTPLP 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 469 ---RGEICLR--GNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLENTYSRC 543
Cdd:cd05971 283 pgeVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKH 361
|
490
....*....|
gi 22330132 544 PLIAQIWVYG 553
Cdd:cd05971 362 PAVLMAAVVG 371
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
80-645 |
1.15e-09 |
|
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: 60.83 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGityvplydslgvnAVEFIINHaevslvfvqe 159
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIG-------------AVAALINY---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevssTQKEEAKNQCVSLFSwnefslmgnldeanlPRKRKTDICTIMYTSGTTGEPK 239
Cdd:cd05940 61 ----------------------------NLRGESLAHCLNVSS---------------AKHLVVDAALYIYTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNN-----AAISVQVLSIDKmlevtdrscdTSDVFFSYLPLAH------CYDQV----MEIYFLSRGSSVGYWrgdi 304
Cdd:cd05940 98 AAIISHrrawrGGAFFAGSGGAL----------PSDVLYTCLPLYHstalivGWSAClasgATLVIRKKFSASNFW---- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 305 rylmDDVQALKPTVF----------CGVPRV-YDKlyAGIMQKISASGLirkklfdfaynyklgnmrkgfsqeeaspRLD 373
Cdd:cd05940 164 ----DDIRKYQATIFqyigelcrylLNQPPKpTER--KHKVRMIFGNGL----------------------------RPD 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 374 rlMFDKIKEALGgrahmllsgaapLPRhVEEFlriipasnlsqgYGLTEsCGGSFTTLAGVFSMVGTVGVPMPTV-EARL 452
Cdd:cd05940 210 --IWEEFKERFG------------VPR-IAEF------------YAATE-GNSGFINFFGKPGAIGRNPSLLRKVaPLAL 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 453 VSV------PEMGYDAFSADVPRGE----IC-LRGNSMFSGYHKRQDLTDQVLI------DGWFHTGDIGEWQEDGSMKI 515
Cdd:cd05940 262 VKYdlesgePIRDAEGRCIKVPRGEpgllISrINPLEPFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYF 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 516 IDRKKNIFKLsQGEYVAVENLENTYSRCPLIAQIWVYgnsfesflvGVVVPDRKAIEDWAKLNYQSPNDFeslcqNLKA- 594
Cdd:cd05940 342 VDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVY---------GVQVPGTDGRAGMAAIVLQPNEEF-----DLSAl 406
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 22330132 595 QKYFLDELNSTAKQYQLKgfeMLKAIHlepnpfdierdlITPTFKLKRPQL 645
Cdd:cd05940 407 AAHLEKNLPGYARPLFLR---LQPEME------------ITGTFKQQKVDL 442
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
51-553 |
1.26e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 61.43 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 51 FSEAVKKYPNEQML---GQRvttdskvgpytwITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQ 127
Cdd:PRK08279 43 FEEAAARHPDRPALlfeDQS------------ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 128 GITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCqKGCSSNLKTIVSFGEVSSTQKEEAKN--QCVSLFSwne 205
Cdd:PRK08279 111 GAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEA-RADLARPPRLWVAGGDTLDDPEGYEDlaAAAAGAP--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 206 fslmgnldEANLP-RKRKT--DICTIMYTSGTTGEPKGVILNNAaisvQVLsidKMLEVTDRSCDT--SDVFFSYLPLAH 280
Cdd:PRK08279 187 --------TTNPAsRSGVTakDTAFYIYTSGTTGLPKAAVMSHM----RWL---KAMGGFGGLLRLtpDDVLYCCLPLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 281 ------CYDQVmeiyfLSRGSSV---------GYWrgdirylmDDVQALKPTVFCgvprvydklYAGimqkisasGLIRk 345
Cdd:PRK08279 252 ntggtvAWSSV-----LAAGATLalrrkfsasRFW--------DDVRRYRATAFQ---------YIG--------ELCR- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 346 klfdfaynYKLgnmrkgfsQEEASP-----RLdRLMF---------DKIKEALGgrahmllsgaapLPRHVEeflriipa 411
Cdd:PRK08279 301 --------YLL--------NQPPKPtdrdhRL-RLMIgnglrpdiwDEFQQRFG------------IPRILE-------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 412 snlsqGYGLTEsCGGSFTTlagVFSMVGTVG-VPMPTVE-ARLVSV------PEMGYDAFSADVPRGEICL-----RGNS 478
Cdd:PRK08279 344 -----FYAASE-GNVGFIN---VFNFDGTVGrVPLWLAHpYAIVKYdvdtgePVRDADGRCIKVKPGEVGLligriTDRG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 479 MFSGYHKRQDlTDQVLI-------DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIAQIWV 551
Cdd:PRK08279 415 PFDGYTDPEA-SEKKILrdvfkkgDAWFNTGDLMRDDGFGHAQFVDRLGDTFRW-KGENVATTEVENALSGFPGVEEAVV 492
|
..
gi 22330132 552 YG 553
Cdd:PRK08279 493 YG 494
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
80-525 |
4.16e-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: 59.25 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQe 159
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrKTDICTIMYTSGTTGEPK 239
Cdd:cd12115 104 --------------------------------------------------------------PDDLAYVIYTSGSTGRPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVIL--NNAAISVQ----VLSIDKM---LEVTDRSCDTSdVFFSYLPLAHcydqvmeiyflsrGSSVgywrgdirYLMDD 310
Cdd:cd12115 122 GVAIehRNAAAFLQwaaaAFSAEELagvLASTSICFDLS-VFELFGPLAT-------------GGKV--------VLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 311 VQAL-------KPTVFCGVPRVYDKLyagimqkisasglirkklfdfaynyklgnmrkgfsqeeasprldrLMFDKIKEA 383
Cdd:cd12115 180 VLALpdlpaaaEVTLINTVPSAAAEL---------------------------------------------LRHDALPAS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 384 LggRAhMLLSGaAPLPRH-VEEFLRIIPASNLSQGYGLTEScggsfTTLAgVFSMVG-------TVGVPMPTVEARLVsv 455
Cdd:cd12115 215 V--RV-VNLAG-EPLPRDlVQRLYARLQVERVVNLYGPSED-----TTYS-TVAPVPpgasgevSIGRPLANTQAYVL-- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 456 pemgyDAFSADVP---RGEICLRGNSMFSGYHKRQDLTDQVLIDGWFH-------TGDIGEWQEDGSMKIIDRKKNIFKL 525
Cdd:cd12115 283 -----DRALQPVPlgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQVKV 357
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
78-553 |
5.81e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 58.98 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 78 TWiTYKEAHDAAIRIGSAIRS-RGVDPGHCCGIYGANCPEWIIAMEACMSQGityvplydslgvnAVEFIINHAEVSLVF 156
Cdd:cd05937 5 TW-TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIG-------------AAPAFINYNLSGDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 157 VQektvssilsCQKgcSSNLKTIVSfgevsstqkeeaknqcvslfswnefslmgnlDEAnlprkrktDICTIMYTSGTTG 236
Cdd:cd05937 71 IH---------CLK--LSGSRFVIV-------------------------------DPD--------DPAILIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 237 EPKGVILNNAAISVQVLSIDKMLEVTDrscdtSDVFFSYLPLAHCYDQVM-EIYFLSRGSSVGYWRG-DIRYLMDDVQAL 314
Cdd:cd05937 101 LPKAAAISWRRTLVTSNLLSHDLNLKN-----GDRTYTCMPLYHGTAAFLgACNCLMSGGTLALSRKfSASQFWKDVRDS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 315 KPTVFcgvprvydkLYAGIMQKISASGLIRKKlfDFAYNYKL--GNmrkGFSQEeasprldrlMFDKIKEALGgrahmll 392
Cdd:cd05937 176 GATII---------QYVGELCRYLLSTPPSPY--DRDHKVRVawGN---GLRPD---------IWERFRERFN------- 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 sgaapLPRhVEEFlriipasnlsqgYGLTESCGGSFTTLAGVFSmVGTVG----------------VPMPTVEARLVSVP 456
Cdd:cd05937 226 -----VPE-IGEF------------YAATEGVFALTNHNVGDFG-AGAIGhhglirrwkfenqvvlVKMDPETDDPIRDP 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 457 EMGydaFSADVPR---GEICLRGN----SMFSGYHKRQDLTDQVLI-------DGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:cd05937 287 KTG---FCVRAPVgepGEMLGRVPfknrEAFQGYLHNEDATESKLVrdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510
....*....|....*....|....*....|.
gi 22330132 523 FKLsQGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:cd05937 364 FRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
46-559 |
7.81e-09 |
|
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: 58.60 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 46 SPWQFFSEAVkkypneQMLGQRVTTDSKvgpYTWityKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACM 125
Cdd:cd05915 3 RAAALFGRKE------VVSRLHTGEVHR---TTY---AEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 126 SQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQektvSSILSCQKGCSSNLKTIvsfgevSSTQKEEAKNQcvslfSWNE 205
Cdd:cd05915 71 GMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD----PNLLPLVEAIRGELKTV------QHFVVMDEKAP-----EGYL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 206 FSLMGNldeANLPRKRKTDIC---TIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSCDtsdVFFSYLPLAHCY 282
Cdd:cd05915 136 AYEEAL---GEEADPVRVPERaacGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD---VVLPVVPMFHVN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 283 DQVMEIYFLSRGSSVGYWR--GDIRYLMDDVQALKPTVFCGVPRVYDKLyagimqkISASGLIRKklfdfAYNYKLGNMR 360
Cdd:cd05915 210 AWCLPYAATLVGAKQVLPGprLDPASLVELFDGEGVTFTAGVPTVWLAL-------ADYLESTGH-----RLKTLRRLVV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 361 KGFSQEEASPRLDRLMFDKIKEALG-------GRAHMLLSGAAPLPRhvEEFLRIIPASNLSQgygltescggsfttlag 433
Cdd:cd05915 278 GGSAAPRSLIARFERMGVEVRQGYGltetspvVVQNFVKSHLESLSE--EEKLTLKAKTGLPI----------------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 434 vfsMVGTVGVPMPTVearlVSVPemgYDAFSADVprgeICLRGNSMFSGYHKRQDLTD-QVLIDGWFHTGDIGEWQEDGS 512
Cdd:cd05915 339 ---PLVRLRVADEEG----RPVP---KDGKALGE----VQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGY 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 22330132 513 MKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQIWVYGNSFESF 559
Cdd:cd05915 405 VEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKEAAVVAIPHPKW 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
80-519 |
9.13e-09 |
|
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: 58.32 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVqe 159
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvSSIlscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeanlprkrkTDICTIMYTSGTTGEPK 239
Cdd:cd05918 103 ---SSP---------------------------------------------------------SDAAYVIFTSGSTGKPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAISVQVLSIDKMLEVTDrscdTSDVF-FSylplAHCYD-QVMEIYF-LSRGSSVGYWRGDIRylMDD----VQ 312
Cdd:cd05918 123 GVVIEHRALSTSALAHGRALGLTS----ESRVLqFA----SYTFDvSILEIFTtLAAGGCLCIPSEEDR--LNDlagfIN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 313 ALKPTVFCGVPrvydklyagimqkiSASGLIRKKLFdfaynyklgnmrkgfsqeeasPRLDRLMfdkikealggrahmlL 392
Cdd:cd05918 193 RLRVTWAFLTP--------------SVARLLDPEDV---------------------PSLRTLV---------------L 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 393 SGAAPLPRHVEEFlriipAS--NLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVeARLVsvpemgyDAFSAD--VP 468
Cdd:cd05918 223 GGEALTQSDVDTW-----ADrvRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVV-------DPDNHDrlVP 289
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330132 469 R---GEICLRGNSMFSGYHKRQDLTDQVLIDG--W------------FHTGDIGEWQEDGSMKIIDRK 519
Cdd:cd05918 290 IgavGELLIEGPILARGYLNDPEKTAAAFIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRK 357
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
216-538 |
1.23e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.90 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 216 NLPRKRKTDICTIMYTSGTTGEPKGVILNNAAisvqvlsidkmLEVTDRSC------DTSDVFFSYLPLAHCYdqvmeiy 289
Cdd:PRK06334 176 GVSDKDPEDVAVILFTSGTEKLPKGVPLTHAN-----------LLANQRAClkffspKEDDVMMSFLPPFHAY------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 290 flsrgssvGYwrgdirylmdDVQALKPtVFCGVPRV--YDKLYAgimQKISAsgLIRKKLFDFA------YNYKLGNMRK 361
Cdd:PRK06334 238 --------GF----------NSCTLFP-LLSGVPVVfaYNPLYP---KKIVE--MIDEAKVTFLgstpvfFDYILKTAKK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 362 gfsQEEASPRLdRLMF---DKIKEALggrahmllsgaaplprhVEEFLRIIPASNLSQGYGLTEsCGgSFTTLAGVFS-- 436
Cdd:PRK06334 294 ---QESCLPSL-RFVViggDAFKDSL-----------------YQEALKTFPHIQLRQGYGTTE-CS-PVITINTVNSpk 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 437 MVGTVGVPMPTVEARLVSvpemgyDAFSADVPRGE---ICLRGNSMFSGYHKRQDLTDQVLIDG--WFHTGDIGEWQEDG 511
Cdd:PRK06334 351 HESCVGMPIRGMDVLIVS------EETKVPVSSGEtglVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHG 424
|
330 340
....*....|....*....|....*..
gi 22330132 512 SMKIIDRKKNIFKLSqGEYVAVENLEN 538
Cdd:PRK06334 425 ELFLKGRLSRFVKIG-AEMVSLEALES 450
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
80-241 |
2.25e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 57.20 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGIT-------YVP-----LYDSLGVNAVefiI 147
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVpvnvnyrYVEdelryLLDDSDAVAL---V 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 148 NHAEVSLVF--VQEKTvssilscqkgcsSNLKTIVSFGEVSStqkEEAKNQCVSLfswneFSLMGNLDEANLPRKRKTDI 225
Cdd:PRK07798 106 YEREFAPRVaeVLPRL------------PKLRTLVVVEDGSG---NDLLPGAVDY-----EDALAAGSPERDFGERSPDD 165
|
170
....*....|....*.
gi 22330132 226 CTIMYTSGTTGEPKGV 241
Cdd:PRK07798 166 LYLLYTGGTTGMPKGV 181
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
470-538 |
2.28e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 57.02 E-value: 2.28e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330132 470 GEICLRGNSMFSGYHKRQDltdQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKlSQGEYVAVENLEN 538
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIEN 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
359-607 |
3.62e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 56.31 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 359 MRKGFSQEEASPRLDR----------LMFDKIKEA-------LGGRAHMLL--SGAAPLPRHVEEFL-RIIPAsnLSQGY 418
Cdd:PRK13382 267 TRRRFDPEATLDLIDRhratglavvpVMFDRIMDLpaevrnrYSGRSLRFAaaSGSRMRPDVVIAFMdQFGDV--IYNNY 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 419 GLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVPRGE---ICLRGNSMFSGYHKRqdlTDQVLI 495
Cdd:PRK13382 345 NATEAGMIATATPADLRAAPDTAGRPAEGTEIRIL-------DQDFREVPTGEvgtIFVRNDTQFDGYTSG---STKDFH 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 496 DGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESF---LVGVVVPDRKAIE 572
Cdd:PRK13382 415 DGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYgqrLAAFVVLKPGASA 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22330132 573 DWAKL---------NYQSPNDFEslcqnlkaqkyFLDEL--NSTAK 607
Cdd:PRK13382 494 TPETLkqhvrdnlaNYKVPRDIV-----------VLDELprGATGK 528
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
49-242 |
4.18e-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: 56.51 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPnEQMLGQRVTTD------SKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPG-HCCGiYGANCPEWIIAM 121
Cdd:cd05943 63 RWFPGARLNYA-ENLLRHADADDpaaiyaAEDGERTEVTWAELRRRVARLAAALRALGVKPGdRVAG-YLPNIPEAVVAM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 122 EACMSQGITYV---PLY------DSLG---------VNAVEF---IINHAEVslvfvqektvssILSCQKGCSSNLKTIV 180
Cdd:cd05943 141 LATASIGAIWSscsPDFgvpgvlDRFGqiepkvlfaVDAYTYngkRHDVREK------------VAELVKGLPSLLAVVV 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330132 181 SFGEVSSTQKEEAKNQCVSlfSWNEFSLMGNLDEANLPRKRKTDICTIMYTSGTTGEPKGVI 242
Cdd:cd05943 209 VPYTVAAGQPDLSKIAKAL--TLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIV 268
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
80-250 |
7.92e-08 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 55.40 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVfvqe 159
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktVSSILSCQKGCSSNLKTIVSfgevssTQKEEAKNQCVSLFSWNEFSLM-------GNLDEANLPRKRK---------T 223
Cdd:cd05967 159 --VTASCGIEPGKVVPYKPLLD------KALELSGHKPHHVLVLNRPQVPadltkpgRDLDWSELLAKAEpvdcvpvaaT 230
|
170 180
....*....|....*....|....*..
gi 22330132 224 DICTIMYTSGTTGEPKGVILNNAAISV 250
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAV 257
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
80-565 |
8.47e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.40 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 ktvssilSCQKGCSSNLKTIVSFGEVSSTQKEEAknqcvslfswNEFSLMGNLDE-ANLPRKRKTDICTIMYTSGTTGEP 238
Cdd:PRK05857 122 -------GSKMASSAVPEALHSIPVIAVDIAAVT----------RESEHSLDAASlAGNADQGSEDPLAMIFTSGTTGEP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 239 KGVILNNA---AISvQVLSIDKMLEVTDRSCDTSdvfFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQALK 315
Cdd:PRK05857 185 KAVLLANRtffAVP-DILQKEGLNWVTWVVGETT---YSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 316 PTVFCGVPRVYDKLyagimqkisasglirkklfdfAYNYKLGNMrkgfsqeeASPRLdRLMfdkikeALGGRahmllsga 395
Cdd:PRK05857 261 VATTCLVPTLLSKL---------------------VSELKSANA--------TVPSL-RLV------GYGGS-------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 396 aplpRHVEEFLRIIPASNL--SQGYGLTES-CGG-SFTTLAGVFSMV--GTVGVPMPTVEARLVsvPEMGYDAFSADVPR 469
Cdd:PRK05857 297 ----RAIAADVRFIEATGVrtAQVYGLSETgCTAlCLPTDDGSIVKIeaGAVGRPYPGVDVYLA--ATDGIGPTAPGAGP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 ----GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPL 545
Cdd:PRK05857 371 sasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIAEGVSG 449
|
490 500
....*....|....*....|..
gi 22330132 546 IAQIWVYGNSFESF--LVGVVV 565
Cdd:PRK05857 450 VREAACYEIPDEEFgaLVGLAV 471
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
80-567 |
8.82e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 55.07 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRgVDPGHCC--GIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFV 157
Cdd:PRK07867 29 TSWREHIRGSAARAAALRAR-LDPTRPPhvGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 158 QEKTVSSILSCQKGcssnlktiVSFGEVSSTQkeeaknqcvslfsWNEfSLMGNLD-EANLPRKRKTDICTIMYTSGTTG 236
Cdd:PRK07867 108 ESAHAELLDGLDPG--------VRVINVDSPA-------------WAD-ELAAHRDaEPPFRVADPDDLFMLIFTSGTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 237 EPKGVILNNAAISVQVLSIDKMLEVTdrscdTSDVFFSYLPLAHcydqvmeiyflsrGSSVgywrgdirylmddVQALKP 316
Cdd:PRK07867 166 DPKAVRCTHRKVASAGVMLAQRFGLG-----PDDVCYVSMPLFH-------------SNAV-------------MAGWAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 317 TVFCGvprvydklyAGIM--QKISASGL---IRKklFDFAY-NYkLGnmrKGFSQEEASPRLD-------RLMFdkikea 383
Cdd:PRK07867 215 ALAAG---------ASIAlrRKFSASGFlpdVRR--YGATYaNY-VG---KPLSYVLATPERPddadnplRIVY------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 384 lggrahmllsGAAPLPRHVEEFLRIIPASnLSQGYGLTEScGGSFTTLAGVFSmvGTVGVPMPTVEarlVSVPEMG---- 459
Cdd:PRK07867 274 ----------GNEGAPGDIARFARRFGCV-VVDGFGSTEG-GVAITRTPDTPP--GALGPLPPGVA---IVDPDTGtecp 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 460 ------YDAFSADVPRGEIC-LRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVA 532
Cdd:PRK07867 337 paedadGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD-GENLG 415
|
490 500 510
....*....|....*....|....*....|....*
gi 22330132 533 VENLENTYSRCPLIAQIWVYGnsfesflvgvvVPD 567
Cdd:PRK07867 416 TAPIERILLRYPDATEVAVYA-----------VPD 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
397-551 |
9.82e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 54.88 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 397 PLPRHVEEFLRIIPASNLSQGYGLTEScggsfTTLA----GVFSMVGTVGVPMPTVEARLVsvpemgyDAFSADVPRGEI 472
Cdd:cd05974 211 PLNPEVIEQVRRAWGLTIRDGYGQTET-----TALVgnspGQPVKAGSMGRPLPGYRVALL-------DPDGAPATEGEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 473 CL-----RGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVEnLENTYSRCPLIA 547
Cdd:cd05974 279 ALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE-LESVLIEHPAVA 357
|
....
gi 22330132 548 QIWV 551
Cdd:cd05974 358 EAAV 361
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
80-569 |
1.52e-07 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 54.40 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSIlscqkgcSSNLKTIVSfgEVSSTQKEEAKNqcvslfswneFSLMGNLDeanlprkrktDICTIMYTSGTTGEPK 239
Cdd:cd17656 94 HLKSKL-------SFNKSTILL--EDPSISQEDTSN----------IDYINNSD----------DLLYIIYTSGTTGKPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 240 GVILNNAAIS---------VQVLSIDKMLEVTDRSCDTsdvffsylplahCYDQVMEIyfLSRGSSVGYWRGDIRylmdd 310
Cdd:cd17656 145 GVQLEHKNMVnllhferekTNINFSDKVLQFATCSFDV------------CYQEIFST--LLSGGTLYIIREETK----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 311 vqalkptvfcgvpRVYDKLYAGImqkisASGLIRKKLFDFAYnyklgnMRKGFSQEEASPRLdrlmFDKIKEALGGRAHM 390
Cdd:cd17656 206 -------------RDVEQLFDLV-----KRHNIEVVFLPVAF------LKFIFSEREFINRF----PTCVKHIITAGEQL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 LLSgaaplprhvEEFLRIIPASNLSqgygLTESCGGSFTTLAGVFSMVGTVGVP-MPTVEARLVSVPEMGYDAFSADVPR 469
Cdd:cd17656 258 VIT---------NEFKEMLHEHNVH----LHNHYGPSETHVVTTYTINPEAEIPeLPPIGKPISNTWIYILDQEQQLQPQ 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 G---EICLRGNSMFSGYHKRQDLTDQVLIDGWF-------HTGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVENLENT 539
Cdd:cd17656 325 GivgELYISGASVARGYLNRQELTAEKFFPDPFdpnermyRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQ 403
|
490 500 510
....*....|....*....|....*....|...
gi 22330132 540 YSRCPLIAQ--IWVYGNSF-ESFLVGVVVPDRK 569
Cdd:cd17656 404 LLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
394-522 |
1.57e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 54.32 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 394 GAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPtvEARLVSVPEMGYDAFSADVprGEIC 473
Cdd:PRK12406 279 AAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAP--GAELRFVDEDGRPLPQGEI--GEIY 354
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 22330132 474 LR--GNSMFSgYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:PRK12406 355 SRiaGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDM 404
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
82-522 |
1.64e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 54.24 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 82 YKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIInhaevslvfvqeKT 161
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYI------------AQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 162 VSSILScqkgcSSNLKTIVSFGEVSSTQKEEAKNQ-CVSLFSWNEFSLMGNLDeANLPRKRKTDICTIMYTSGTTGEPKG 240
Cdd:PRK09192 120 LRGMLA-----SAQPAAIITPDELLPWVNEATHGNpLLHVLSHAWFKALPEAD-VALPRPTPDDIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 VILNNAAI--SVQVLSIDKM-LEVTDRsCdtsdvfFSYLPLAHcyDQVMEIYFLS---RGSSVGYwrgdirylmddvqaL 314
Cdd:PRK09192 194 VIITHRALmaNLRAISHDGLkVRPGDR-C------VSWLPFYH--DMGLVGFLLTpvaTQLSVDY--------------L 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 315 KPTVFCGVPRVYDKLYAGIMQKISASGlirkklfdfAYNYKLGnMRKGFSQEEASprLD----RLmfdkikEALGG---R 387
Cdd:PRK09192 251 PTRDFARRPLQWLDLISRNRGTISYSP---------PFGYELC-ARRVNSKDLAE--LDlscwRV------AGIGAdmiR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 388 AHMLLSGA---APLPRHVEEFLriipASnlsqgYGLTEScggsftTLAGVFSMVGTvGVPMPTVEARLVS---------- 454
Cdd:PRK09192 313 PDVLHQFAeafAPAGFDDKAFM----PS-----YGLAEA------TLAVSFSPLGS-GIVVEEVDRDRLEyqgkavapga 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 455 --------------VPEMGY---DAFSADVPR---GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGeWQEDGSMK 514
Cdd:PRK09192 377 etrrvrtfvncgkaLPGHEIeirNEAGMPLPErvvGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLG-YLLDGYLY 455
|
....*...
gi 22330132 515 IIDRKKNI 522
Cdd:PRK09192 456 ITGRAKDL 463
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
418-607 |
9.73e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 51.85 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 418 YGLTEScggSFTTLAGVFSMV---GTVGVPMPTVEARLvsvpemgYDAFSADVPRGE---ICLRGNSMFSGYhkrQDLTD 491
Cdd:PRK07788 355 YGSTEV---AFATIATPEDLAeapGTVGRPPKGVTVKI-------LDENGNEVPRGVvgrIFVGNGFPFEGY---TDGRD 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 492 QVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESF---LVGVVVP-- 566
Cdd:PRK07788 422 KQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFgqrLRAFVVKap 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22330132 567 ----DRKAIEDWAKLN---YQSPNDFeslcqnlkaqkYFLDEL--NSTAK 607
Cdd:PRK07788 501 gaalDEDAIKDYVRDNlarYKVPRDV-----------VFLDELprNPTGK 539
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
231-523 |
1.42e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 51.31 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 231 TSGTTGEPKGVILNNAAisvqVLS-IDKMLEVTDRSCDtSDVFFSYLPLAHcyDqvMEIYFLSRGSSVG--YWrgdiryl 307
Cdd:PRK05851 160 TAGSTGTPRTAILSPGA----VLSnLRGLNARVGLDAA-TDVGCSWLPLYH--D--MGLAFLLTAALAGapLW------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 308 mddvqaLKPT-VFCGVPRVYdklyagiMQKISASGLIRKKLFDFAYNY--KLGnmrkgfsqeeasprldrlmfDKIKEAL 384
Cdd:PRK05851 224 ------LAPTtAFSASPFRW-------LSWLSDSRATLTAAPNFAYNLigKYA--------------------RRVSDVD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 385 GGRAHMLLSGAAPLprHVEEFLRIIPA--------SNLSQGYGLTES--------CG-----GSFTTLAGVFSMVGTV-G 442
Cdd:PRK05851 271 LGALRVALNGGEPV--DCDGFERFATAmapfgfdaGAAAPSYGLAEStcavtvpvPGiglrvDEVTTDDGSGARRHAVlG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 443 VPMPTVEARlVSVPEMGYDAFSADVprGEICLRGNSMFSGYHKRQDLTDqvliDGWFHTGDIGeWQEDGSMKIIDRKK-- 520
Cdd:PRK05851 349 NPIPGMEVR-ISPGDGAAGVAGREI--GEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLG-YLVDGGLVVCGRAKel 420
|
....*....
gi 22330132 521 ------NIF 523
Cdd:PRK05851 421 itvagrNIF 429
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
81-518 |
1.77e-06 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 50.83 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 81 TYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEK 160
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTHHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 161 tvssilscqkgcssnlktivsfgevsstqkeeaknqcvslfswnefslmgnldeANLprkrktdiCTIMYTSGTTGEPKG 240
Cdd:cd17649 94 ------------------------------------------------------RQL--------AYVIYTSGSTGTPKG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 241 VILNNAAISVQVLSIDKMLEVTdrscdTSDVFFSYLPLAhcYDQVMEIYF--LSRGSSVgywrgdiryLMDDVQALKPTv 318
Cdd:cd17649 112 VAVSHGPLAAHCQATAERYGLT-----PGDRELQFASFN--FDGAHEQLLppLICGACV---------VLRPDELWASA- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 319 fcgvprvyDKLYAGIM-QKISASGLIRKKLFDFAynyklgnmrkgfsqEEASPRLDRLMfdkikealgGRAHMLLSGAAP 397
Cdd:cd17649 175 --------DELAEMVReLGVTVLDLPPAYLQQLA--------------EEADRTGDGRP---------PSLRLYIFGGEA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 398 LPrhVEEFLRIIPAS-NLSQGYGLTESC-------GGSFTTLAGVFSMVGTvgvPMPTVEARLVsvpemgyDAFSADVPR 469
Cdd:cd17649 224 LS--PELLRRWLKAPvRLFNAYGPTEATvtplvwkCEAGAARAGASMPIGR---PLGGRSAYIL-------DADLNPVPV 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 ---GEICLRGNSMFSGYHKRQDLTDQVLIDG--------WFHTGDIGEWQEDGSMKIIDR 518
Cdd:cd17649 292 gvtGELYIGGEGLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGR 351
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-519 |
2.62e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 50.29 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVSSILSCQKGCSSNLKTIVSFGEVSStqkeeaknqcvslfSWNEFslmgnldEANLPRKRKTDI------CTIMYTSG 233
Cdd:PRK08276 92 ALADTAAELAAELPAGVPLLLVVAGPVP--------------GFRSY-------EEALAAQPDTPIadetagADMLYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 234 TTGEPKGVI--LNNAAISvQVLSIDKMLEVTDRSCDTSDVFFSYLPLAHcydqvmeiyflsrgSSVGYWRGDirylmddV 311
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPD-EAPGMMLALLGFGMYGGPDSVYLSPAPLYH--------------TAPLRFGMS-------A 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 312 QALKPTVFcgvprvydklyagIMQKISASG---LIRKklfdfaynYKLGNmrkgfSQ-------------EEASPRLD-- 373
Cdd:PRK08276 209 LALGGTVV-------------VMEKFDAEEalaLIER--------YRVTH-----SQlvptmfvrmlklpEEVRARYDvs 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 374 --RLMfdkikealggrahmlLSGAAPLPRHVEEflRII----PAsnLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPmpt 447
Cdd:PRK08276 263 slRVA---------------IHAAAPCPVEVKR--AMIdwwgPI--IHEYYASSEGGGVTVITSEDWLAHPGSVGKA--- 320
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330132 448 VEARLVSVPEMGydafsADVPRGEICL----RGNSMFSgYHKRQDLTDQVLID-GWFHTGDIGEWQEDGSMKIIDRK 519
Cdd:PRK08276 321 VLGEVRILDEDG-----NELPPGEIGTvyfeMDGYPFE-YHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRK 391
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
49-577 |
3.65e-06 |
|
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: 49.74 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 49 QFFSEAVKKYPNEQMLgqrVTTDSKvgpytwITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQG 128
Cdd:cd17644 4 QLFEEQVERTPDAVAV---VFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 129 ITYVPLYDSLGVNAVEFIINHAEVSLVFvqektvssilscqkgcssnlktivsfgevssTQKEeaknqcvslfswnefsl 208
Cdd:cd17644 75 GAYVPLDPNYPQERLTYILEDAQISVLL-------------------------------TQPE----------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 209 mgnldeaNLprkrktdiCTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRscDTSDVFFSYlplahCYD-QVME 287
Cdd:cd17644 107 -------NL--------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS--DRVLQFASI-----AFDvAAEE 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 288 IY--FLSRGSSV---GYWRGDIRYLMDDVQALKPTVFcGVPRVYDKLYAGIMQKISASGLirkklfdfaynyklgnmrkg 362
Cdd:cd17644 165 IYvtLLSGATLVlrpEEMRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIDLP-------------------- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 363 fsqeeASPRLdrlmfdkikealggrahMLLSGAAPLPRHVEEFLRII-PASNLSQGYGLTES------CGGSFTTLAGVF 435
Cdd:cd17644 224 -----SSLRL-----------------VIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEAtiaatvCRLTQLTERNIT 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 436 SMvgTVGVPMPTVEARLVsvpemgyDAFSADVP---RGEICLRGNSMFSGYHKRQDLTDQVLIDGWFH---------TGD 503
Cdd:cd17644 282 SV--PIGRPIANTQVYIL-------DENLQPVPvgvPGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGD 352
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330132 504 IGEWQEDGSMKIIDR-----KKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNsfeSFLVGVVVPDRKAIEDWAKL 577
Cdd:cd17644 353 LARYLPDGNIEYLGRidnqvKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGN---KRLVAYIVPHYEESPSTVEL 428
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
438-568 |
4.83e-06 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 49.76 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 438 VGTVGVPM-PTVEARLVsvpemgyDAFSADVPRGEI---CLRGNSMFSGYHK-----RQDLTDqvliDGWFHTGDIGEWQ 508
Cdd:COG1021 352 LTTQGRPIsPDDEVRIV-------DEDGNPVPPGEVgelLTRGPYTIRGYYRapehnARAFTP----DGFYRTGDLVRRT 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330132 509 EDGSMKIIDRKKNifklsQ----GEYVAVENLENTYSRCPLIAQiwvygnsfesflVGVV-VPDR 568
Cdd:COG1021 421 PDGYLVVEGRAKD-----QinrgGEKIAAEEVENLLLAHPAVHD------------AAVVaMPDE 468
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
414-584 |
7.06e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 49.22 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 414 LSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLvsvpemgYDAFSADV-PR--GEICLRGNSMFSGYhkrQDLT 490
Cdd:PRK13383 320 LYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRI-------LDRNNRPVgPRvtGRIFVGGELAGTRY---TDGG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 491 DQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESF---LVGVVVP- 566
Cdd:PRK13383 390 GKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAVADNAVIGVPDERFghrLAAFVVLh 468
|
170 180
....*....|....*....|....*.
gi 22330132 567 -----DRKAIEDWAK---LNYQSPND 584
Cdd:PRK13383 469 pgsgvDAAQLRDYLKdrvSRFEQPRD 494
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
80-567 |
2.03e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 47.82 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVplydslGVNA------VEFIINHAEVS 153
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI------AVNTryrsheVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 154 LVFVQEK----TVSSILS-CQKGCSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSwneFSLMGNLdEANLPRKRKTDICTI 228
Cdd:PRK06164 110 WLVVWPGfkgiDFAAILAaVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFA---LPDPAPP-AAAGERAADPDAGAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 229 MYT-SGTTGEPKGVILNNAAIsvqvlsidkmlevtdrscdtsdvffsylpLAHCyDQVMEIYFLSRGSSVgywrgdiryl 307
Cdd:PRK06164 186 LFTtSGTTSGPKLVLHRQATL-----------------------------LRHA-RAIARAYGYDPGAVL---------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 308 mddvQALKPtvFCGVPRvydklYAGIMQKISASG-LIRKKLFDFAYNYKLgnMRK-----GFSQEEasprldrlMFDKIK 381
Cdd:PRK06164 226 ----LAALP--FCGVFG-----FSTLLGALAGGApLVCEPVFDAARTARA--LRRhrvthTFGNDE--------MLRRIL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 382 EALGGRAHM----LLSGAAPLPRhveefLRIIPASNLSQGYGLTESCGGSfttlaGVFSMV--GTV-----------GVP 444
Cdd:PRK06164 285 DTAGERADFpsarLFGFASFAPA-----LGELAALARARGVPLTGLYGSS-----EVQALValQPAtdpvsvrieggGRP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 445 M-PTVEARLVSvPEMGydAFSADVPRGEICLRGNSMFSGYHKRQDLTDQVLI-DGWFHTGDIGEWQEDGSMKIIDRKKNI 522
Cdd:PRK06164 355 AsPEARVRARD-PQDG--ALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDS 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 22330132 523 FKLSqGEYVAVENLENTYSRCPLIAQIWVYGNSFESFLVGV--VVPD 567
Cdd:PRK06164 432 LRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVafVIPT 477
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
399-567 |
3.49e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 46.94 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 399 PRHVEEFLRIIPASnLSQGYGLTEscGGSFTTLAGVFSmVGTVGVPMPTVE----ARLVSVPEMGYDA----FSADVPRG 470
Cdd:PRK13388 277 PRDIAEFSRRFGCQ-VEDGYGSSE--GAVIVVREPGTP-PGSIGRGAPGVAiynpETLTECAVARFDAhgalLNADEAIG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 471 EIC-LRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQI 549
Cdd:PRK13388 353 ELVnTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRV 431
|
170
....*....|....*...
gi 22330132 550 WVYGnsfesflvgvvVPD 567
Cdd:PRK13388 432 AVYA-----------VPD 438
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
382-577 |
6.65e-05 |
|
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: 45.71 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 382 EALGGRAHMLLSGAAPLPRHVEeflRIIPASNLSQGYGLTESCGGSftTLAGVFSMVGTV--GVPMPTV-----EARLVS 454
Cdd:cd17652 201 DDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCA--TMAGPLPGGGVPpiGRPVPGTrvyvlDARLRP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 455 VPemgydafsADVPrGEICLRGNSMFSGYHKRQDLTDQVLIDGWF--------HTGDIGEWQEDGSMKIIDRKKNIFKLs 526
Cdd:cd17652 276 VP--------PGVP-GELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmyRTGDLARWRADGQLEFLGRADDQVKI- 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22330132 527 QGEYVAVENLENTYSRCPLIAQ--IWVYGN-SFESFLVGVVVPDRKAIEDWAKL 577
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEavVVVRDDrPGDKRLVAYVVPAPGAAPTAAEL 399
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
392-569 |
3.34e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 43.50 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 392 LSGAAPLPRHVEEF---LRIipasNLSQGYGLTESCGGSfttlagVFSmvgtvGVPMPTVEARlvsvpemgydafsadVP 468
Cdd:PRK07824 157 LVGGGPAPAPVLDAaaaAGI----NVVRTYGMSETSGGC------VYD-----GVPLDGVRVR---------------VE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 469 RGEICLRGNSMFSGYhKRQDLTDQVLIDGWFHTGDIGEWqEDGSMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLIAQ 548
Cdd:PRK07824 207 DGRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGAL-DDGVLTVLGRADDAIS-TGGLTVLPQVVEAALATHPAVAD 283
|
170 180
....*....|....*....|.
gi 22330132 549 IWVYGnsfesflvgvvVPDRK 569
Cdd:PRK07824 284 CAVFG-----------LPDDR 293
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
391-577 |
4.46e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 43.22 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 LLSGAAPLPRHVEEFLRII--PASNLSQGYGLTE-----SCGGS--FTTLAGVFS-MVGT-VGVPMPTVEARLVSVPEMG 459
Cdd:cd05910 204 VLSAGAPVPIALAARLRKMlsDEAEILTPYGATEalpvsSIGSRelLATTTAATSgGAGTcVGRPIPGVRVRIIEIDDEP 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 460 YDAFSAD--VPR---GEICLRGNSMFSGYHKRQDLTDQVLIDG-----WFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGE 529
Cdd:cd05910 284 IAEWDDTleLPRgeiGEITVTGPTVTPTYVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGT 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22330132 530 Y--VAVENLENTY---SRCPLIAqiwvYGNSFESFLVGVVVPDRKAIEDWAKL 577
Cdd:cd05910 364 LytEPVERVFNTHpgvRRSALVG----VGKPGCQLPVLCVEPLPGTITPRARL 412
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
418-553 |
1.25e-03 |
|
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: 41.98 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 418 YGLTESCGGSFTTLAGVFSMVGTVGVPmptVEARLVSVPEMGydafsADVPR---GEICLRGNSMFSgYHKRQDLT-DQV 493
Cdd:cd05929 276 YGGTEGQGLTIINGEEWLTHPGSVGRA---VLGKVHILDEDG-----NEVPPgeiGEVYFANGPGFE-YTNDPEKTaAAR 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 494 LIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQIWVYG 553
Cdd:cd05929 347 NEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG 405
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
440-548 |
1.38e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 41.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 440 TVGVPM-PTVEARLVsvpemgyDAFSADVPRGEICL---RGNSMFSGYHKRQDLTDQVL-IDGWFHTGDIGEWQEDGSMK 514
Cdd:PRK10946 354 TQGRPMsPDDEVWVA-------DADGNPLPQGEVGRlmtRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYIT 426
|
90 100 110
....*....|....*....|....*....|....*...
gi 22330132 515 IIDRKKNifklsQ----GEYVAVENLENTYSRCPLIAQ 548
Cdd:PRK10946 427 VVGREKD-----QinrgGEKIAAEEIENLLLRHPAVIH 459
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
438-548 |
1.67e-03 |
|
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: 41.54 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 438 VGTVGVPM-PTVEARLVsvpemgyDAFSADVPRGEI---CLRGNSMFSGY-----HKRQDLTDqvliDGWFHTGDIGEWQ 508
Cdd:cd05920 307 IHTQGRPMsPDDEIRVV-------DEEGNPVPPGEEgelLTRGPYTIRGYyrapeHNARAFTP----DGFYRTGDLVRRT 375
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 22330132 509 EDGSMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIAQ 548
Cdd:cd05920 376 PDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPAVHD 414
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
80-241 |
2.27e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.28 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 80 ITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQE 159
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 160 KTVssilscQKGCSSNLKTIVsfgevsstqkEEAKNQCVSL--------------------FSWNEfsLMGNldeanlpr 219
Cdd:PRK00174 179 EGV------RGGKPIPLKANV----------DEALANCPSVekvivvrrtggdvdwvegrdLWWHE--LVAG-------- 232
|
170 180 190
....*....|....*....|....*....|...
gi 22330132 220 krKTDICT-----------IMYTSGTTGEPKGV 241
Cdd:PRK00174 233 --ASDECEpepmdaedplfILYTSGSTGKPKGV 263
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
213-248 |
3.18e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 40.80 E-value: 3.18e-03
10 20 30
....*....|....*....|....*....|....*.
gi 22330132 213 DEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAI 248
Cdd:PRK10252 588 GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
223-280 |
3.57e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 40.35 E-value: 3.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 22330132 223 TDICTIMYTSGTTGEPKGVILNNaaisVQVLSIDKMLEVtdRSCDTSDVFFSYLPLAH 280
Cdd:cd05938 144 KSPALYIYTSGTTGLPKAARISH----LRVLQCSGFLSL--CGVTADDVIYITLPLYH 195
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
470-553 |
5.44e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 39.76 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 GEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAQI 549
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEI 412
|
....
gi 22330132 550 WVYG 553
Cdd:PRK07638 413 VVIG 416
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
391-553 |
5.92e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.59 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 391 LLSGAAPLPRHVEE--FLRIipasNLSQGYGLTESCGGSFTTLAGVFSMVGT-VGVPMPTVEARLVSVPemgydafsadv 467
Cdd:PRK07445 236 LLGGAPAWPSLLEQarQLQL----RLAPTYGMTETASQIATLKPDDFLAGNNsSGQVLPHAQITIPANQ----------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 468 pRGEICLRGNSMFSGYHkrQDLTDQvliDGWFHTGDIGEWQEDGSMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIA 547
Cdd:PRK07445 301 -TGNITIQAQSLALGYY--PQILDS---QGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQ 373
|
....*.
gi 22330132 548 QIWVYG 553
Cdd:PRK07445 374 DVCVLG 379
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
470-576 |
6.25e-03 |
|
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: 39.46 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330132 470 GEICLRGNSMFSGYHKRQDLTDQVLI-------DGWFHTGDIGEWQEDGSMKIIDRKKNIFKLsQGEYVAVENLENTYSR 542
Cdd:cd17645 289 GELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMN 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 22330132 543 CPLI---AQIWVYGNSFESFLVGVVVP----DRKAIEDWAK 576
Cdd:cd17645 368 HPLIelaAVLAKEDADGRKYLVAYVTApeeiPHEELREWLK 408
|
|
| |
