|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
56-555 |
0e+00 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 903.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 56 SYPALSAQAAREPAAFWGPLARDtLLWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVQKSPESVALIWERDEPG 135
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 136 TEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVV 215
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 216 ITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHM-GDLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTS 294
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 295 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWET 374
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 375 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAP 454
Cdd:cd05966 321 VEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 455 RPSEegAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 534
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNEVEG-EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGA 477
|
490 500
....*....|....*....|.
gi 1622839332 535 HRTEGGYYQITGRMDDVINIS 555
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVS 498
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
51-555 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 902.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 51 ASQPGSYPALSAQAAREPAAFWGPLARDTLLWDTPYHTVWDCDFSTgKIGWFLGGQLNVSVNCLDQHVQKSPESVALIWE 130
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 131 RDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDA 210
Cdd:TIGR02188 80 GDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 211 KCKVVITFNQGLRGGRVMELKKIVDEAVKHCP-TVQHVLVAHRTDNKV-HMGD-LDIPLEQEMAKEDPVCAPESMGSEDV 287
Cdd:TIGR02188 160 GAKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVEgRDVWWHDLMAKASAYCEPEPMDSEDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 288 LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPN 367
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 368 AGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTET 447
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 448 GGICIAPRPSeeGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGY 527
Cdd:TIGR02188 400 GGIMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGY 477
|
490 500
....*....|....*....|....*...
gi 1622839332 528 YFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:TIGR02188 478 YFTGDGARRDKDGYIWITGRVDDVINVS 505
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
57-555 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 801.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 57 YPALSAQAAREPAAFWGPLARDtLLWDTPYHTVWDCDfsTGKIGWFLGGQLNVSVNCLDQHVQKSPESVALIWERDEPGT 136
Cdd:PRK00174 19 YKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIWEGDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 TFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGD-LDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSG 295
Cdd:PRK00174 176 TADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEgRDLWWHELVAGASDECEPEPMDAEDPLFILYTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETV 375
Cdd:PRK00174 256 STGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 376 ERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPR 455
Cdd:PRK00174 336 DKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 456 PseeGA-EILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 534
Cdd:PRK00174 416 P---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEG-GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGA 491
|
490 500
....*....|....*....|.
gi 1622839332 535 HRTEGGYYQITGRMDDVINIS 555
Cdd:PRK00174 492 RRDEDGYYWITGRVDDVLNVS 512
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
101-555 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 652.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 101 WFLGGQLNVSVNCLDQHVQKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAA 180
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 181 MLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMG 260
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 261 DlDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWIT 340
Cdd:COG0365 161 G-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 341 GHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN 420
Cdd:COG0365 240 GHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 421 CEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQ 500
Cdd:COG0365 320 PEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVIKG 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 501 AWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:COG0365 393 PWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS 447
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
41-555 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 551.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 41 PSGSAPAVAAASQPGSYPALSAQAAREPAAFWGPLArDTLLWDTPYHTVWDC----DFSTG--KIGWFLGGQLNVSVNCL 114
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQK-SPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PLN02654 95 DRNVEAgNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKIVDEA----------VKHCPTVQHVLVAHRTDNKVHMGDlD 263
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-D 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 264 IPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHS 343
Cdd:PLN02654 254 VWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 344 YVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEA 423
Cdd:PLN02654 334 YVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 424 WEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPseeGAEIL-PGMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAW 502
Cdd:PLN02654 414 WRWFFNVVGDSRCPISDTWWQTETGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSW 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 503 PGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:PLN02654 490 PGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 542
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
63-555 |
0e+00 |
|
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: 539.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 63 QAAREPAAFWGPLARDtLLWDTPYHTVWDCDFSTGK--IGWFLGGQLNVSVNCLDQHVQKSPESVALIWERDEpGTEVR- 139
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFN 219
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 QGLRGGRVMELKKIVDEAVK-HCPTVQHVLVAHRTDNKVH-MGDLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGST 297
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 298 GMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVER 377
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 378 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPS 457
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 458 EEgaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRT 537
Cdd:cd17634 405 AI--ELKAGSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRD 481
|
490
....*....|....*...
gi 1622839332 538 EGGYYQITGRMDDVINIS 555
Cdd:cd17634 482 EDGYYWITGRSDDVINVA 499
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
57-555 |
2.26e-151 |
|
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: 448.69 E-value: 2.26e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 57 YPALSAQAAREPAAFWGPLARdTLLWDTPYHTVWDCDfSTGKIGWFLGGQLNVSVNCLDQHVQKS-PESVALIWERDEPG 135
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 136 TEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVV 215
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 216 ITFNQGLRGGRVMELKKIVDEAVK---HCPtvQHVLVAHRTDNKVHMGD--LDIPLEQEMAKEDPV-CAPesMGSEDVLF 289
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALElsgHKP--HHVLVLNRPQVPADLTKpgRDLDWSELLAKAEPVdCVP--VAATDPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 290 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV-YPNA 368
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 369 GRYWETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTE 446
Cdd:cd05967 315 GAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 447 TGGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAYP 525
Cdd:cd05967 392 TGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFP 470
|
490 500 510
....*....|....*....|....*....|
gi 1622839332 526 GYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05967 471 GYYDTGDAGYKDEDGYLFIMGRTDDVINVA 500
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
56-555 |
2.17e-136 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 410.49 E-value: 2.17e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 56 SYPALSAQAAREPAAFWGPLARdTLLWDTPYHTVwdCDFSTGKIG-WFLGGQLNVSVNCLDQHVQKSPESVALIWERDEP 134
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR-RIDWQTPFTQV--LDYSNPPFArWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:PRK10524 80 DEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 215 VITFNQGLRGGRVMELKKIVDEAV---KHCPtvQHVLVAHR---TDNKVHMGDLDIPLEQEmAKEDPVCAPESMGSEDVL 288
Cdd:PRK10524 160 IVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVDRglaPMARVAGRDVDYATLRA-QHLGARVPVEWLESNEPS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 289 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNA 368
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 369 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG 448
Cdd:PRK10524 317 GIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP---VIDNYWQTETG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 449 GICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAY-PG 526
Cdd:PRK10524 394 WPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQ 473
|
490 500
....*....|....*....|....*....
gi 1622839332 527 YYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:PRK10524 474 VYSTFDWGIRDADGYYFILGRTDDVINVA 502
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
55-576 |
6.30e-129 |
|
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: 390.70 E-value: 6.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 55 GSYPALSAQAAREPAAFWGPLARDTLLW--DTPYHTVwdcDFSTGK--IGWFLGGQLNVSVNCLDQHVQKSPESVALIWE 130
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIEwyEPPYQTL---DLSGGKpwAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 131 rDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDA 210
Cdd:cd05968 84 -GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 211 KCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKV--HMGDlDIPLEQEMAKEDPvcAPESMGSEDVL 288
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFtpAKGR-DLSYDEEKETAGD--GAERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 289 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNA 368
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 369 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTE-T 447
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 448 GGI--CIAPRPSEEGA--EILPGMAmrpffgivPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQRFVDAYFKA 523
Cdd:cd05968 399 GGIlgNVLIKPIKPSSfnGPVPGMK--------ADVLDESGKPARPE--VGELVLLAPWPGMTRGFWRDEDRYLETYWSR 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 524 YPGYYFTGDGAHRTEGGYYQITGRMDDVINISNTlQIGGLFREAIRNS-GDLLE 576
Cdd:cd05968 469 FDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGK-RVGPAEIESVLNAhPAVLE 521
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
101-555 |
1.84e-108 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 336.48 E-value: 1.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 101 WFLGGQLNVSVNCLDQHVqKSP--ESVALIWERdePGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAV 178
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 179 AAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGLRggrvmelKKIVDEavkhCPTVQHVLVahrTDNKVH 258
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD----LPSLKHVLL---VGEDVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 259 MGDLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQagyllYAALTH----KLVFDHRPGDIFGCVA 334
Cdd:PRK04319 179 EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NAMLQHyqtgKYVLDLHEDDVYWCTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 335 DIGWITGHSYVVYGPLCNGATSVLFESTpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 414
Cdd:PRK04319 254 DPGWVTGTSYGIFAPWLNGATNVIDGGR---FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 415 VGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEegaEILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSG 494
Cdd:PRK04319 331 VGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAM---DIKPGSMGKPLPGIEAAIVDDQGNELP-PNRMG 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 495 ALCISQAWPGMARTIYGDHQRFvDAYFKayPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:PRK04319 404 NLAIKKGWPSMMRGIWNNPEKY-ESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS 461
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
114-555 |
3.61e-103 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 317.72 E-value: 3.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNQglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDnkvhMGDLDIPLEQEMAKE 273
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLV----FDHRPGDIFGCVADIGWITGHSYVVYGP 349
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 350 LCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHR 429
Cdd:pfam00501 223 LLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 430 VVGdsrCTLVDTWWQTETGGICIAPRPsEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTI 509
Cdd:pfam00501 300 LFG---GALVNGYGLTETTGVVTTPLP-LDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839332 510 YGDHQRFVDAYFKayPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:pfam00501 374 LNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
141-555 |
8.04e-90 |
|
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: 284.01 E-value: 8.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQ 220
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 221 glrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipLEQEMAKEDPvcapesmgsedvLFMLYTSGSTGMP 300
Cdd:cd05969 82 ---------------------------------------------LYERTDPEDP------------TLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 301 KGIVHTQAGYLLYAaLTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKI 380
Cdd:cd05969 105 KGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 381 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeG 460
Cdd:cd05969 181 TVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP---C 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 461 AEILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRFvDAYFKAypGYYFTGDGAHRTEGG 540
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELP-PGTKGILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDG 330
|
410
....*....|....*
gi 1622839332 541 YYQITGRMDDVINIS 555
Cdd:cd05969 331 YFWFVGRADDIIKTS 345
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
141-555 |
7.40e-69 |
|
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: 228.76 E-value: 7.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnq 220
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 221 glrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmGSEDVLFMLYTSGSTGMP 300
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 301 KGIVHTqAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNagRYWETVERLKI 380
Cdd:cd05972 97 KGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 381 NQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETgGICIAPRPseeG 460
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTET-GLTVGNFP---D 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 461 AEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAHRTEGG 540
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTGDRAYRDEDG 319
|
410
....*....|....*
gi 1622839332 541 YYQITGRMDDVINIS 555
Cdd:cd05972 320 YFWFVGRADDIIKSS 334
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
55-553 |
1.23e-62 |
|
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: 217.52 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 55 GSYPALSAQAAREPAAFWgplardTLLWD---TPYHTVWDCDFSTGKI----GWFLGGQLNVSVNCLDQHVQksPESVAL 127
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLLRHADA--DDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 128 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRI 207
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 208 NDAKCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDIP----LEQEMAKE-DPVCAPESM 282
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 283 GSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVvyGPLCNGATSVLFEST 362
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 363 PVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTW 442
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 443 WQTETGG--IC--------IAP-RPSEEGAEILpGMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMARTIYG 511
Cdd:cd05943 399 LASISGGtdIIscfvggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWN 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1622839332 512 DH--QRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd05943 468 DPdgSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLN 511
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
114-555 |
4.00e-62 |
|
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: 211.59 E-value: 4.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemake 273
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 dpvcapesmgsedvlFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNG 353
Cdd:COG0318 104 ---------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGd 433
Cdd:COG0318 168 ATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 434 srCTLVDTWWQTETGGICIAPRpsEEGAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD- 512
Cdd:COG0318 241 --VRIVEGYGLTETSPVVTVNP--EDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPGEVGEIVVRG--PNVMKGYWNDp 313
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839332 513 ---HQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:COG0318 314 eatAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
55-553 |
5.38e-60 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 210.81 E-value: 5.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 55 GSYPALSAQAAREPAAFWgplardTLLWD-------TPYHTVWDcdfSTGKIG--WFLGGQLNVSVNCLDQHvqkSPESV 125
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 126 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAG 205
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 206 RINDAKCKVVITFNqGLR-GGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLD--IPLEQEMAK-EDPVCAPES 281
Cdd:PRK03584 181 RFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIF----GCvadiGWITgHSYVVYGPLCnGATSV 357
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 358 LFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrct 437
Cdd:PRK03584 334 LYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA---- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 438 lvDTWWQTETGG--IC---IAprpseeGAEILP-----------GMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQA 501
Cdd:PRK03584 410 --DVWLASISGGtdICscfVG------GNPLLPvyrgeiqcrglGMAVEAW--------DEDGRPVVG--EVGELVCTKP 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 502 WPGMArtIY----GDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:PRK03584 472 FPSMP--LGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLN 525
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
52-555 |
7.87e-59 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 207.29 E-value: 7.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 52 SQPGSYPALSAQAAREPAAFWGPLARDTLLWDTPYHTVwdcdFSTGKI--GWFLGGQLNVSVNCLDQHVqKSP---ESVA 126
Cdd:PTZ00237 5 SDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKV----YSGDEIypDWFKGGELNTCYNVLDIHV-KNPlkrDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 127 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGR 206
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 207 INDAKCKVVITFNQGLRGGRVMELKKIVDEAV---KHCPTvqHVLVAHRTD-------NKVHmgdlDIPL-------EQE 269
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIelsTFKPS--NVITLFRNDitsesdlKKIE----TIPTipntlswYDE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 270 MAK-----EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSY 344
Cdd:PTZ00237 234 IKKikennQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 345 VvYGPLCNGATSVLFESTPVYPNAGR--YWETVERLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPI 419
Cdd:PTZ00237 314 L-YGSLSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 420 NCEAWEWLHRVVGdSRCTLVdtWWQTETGG---ICIAPRPSEEGAEILPGmamrPFfgIVPVLMDEKGSVVeGSNVSGAL 496
Cdd:PTZ00237 393 EESIPEYIENKLK-IKSSRG--YGQTEIGItylYCYGHINIPYNATGVPS----IF--IKPSILSEDGKEL-NVNEIGEV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 497 CISQAWP-GMARTIYGDHQRFvDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:PTZ00237 463 AFKLPMPpSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKIS 521
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
286-555 |
1.26e-48 |
|
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: 172.08 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDhRPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFEStpvy 365
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL-TEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 366 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT 445
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 446 ETGGICIAPRPSEEgaEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDayfkaYP 525
Cdd:cd04433 150 ETGGTVATGPPDDD--ARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVD-----ED 221
|
250 260 270
....*....|....*....|....*....|
gi 1622839332 526 GYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
108-555 |
2.16e-45 |
|
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: 168.06 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 108 NVSVNCLDQHVQKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARI 187
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWC-DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 188 GAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGlrggrvmELKKIVDEAVKHCPTVQhVLVahrtdnKVHMGDLD--IP 265
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECPSKP-KLV------WVGDPVPEgwID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 266 LEQEMAKEDPV----CAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAgYLLYAALTHKLVFDHRPGDIFGCVADIGWITG 341
Cdd:cd05970 162 FRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 342 HSYVVYGPLCNGATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINC 421
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 422 EAWEWLHRVVGDSrctLVDTWWQTETGgICIAPRPseeGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNvSGALCI--S 499
Cdd:cd05970 316 EVFNTFKEKTGIK---LMEGFGQTETT-LTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 500 QAWP-GMARTIYGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05970 388 KGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
136-552 |
8.03e-44 |
|
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: 162.77 E-value: 8.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 136 TEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVV 215
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 216 ITFNQGLrggrvmelkKIVDEAVKHCPTVQHV-LVAHRTDNKVHMGDLDIPLEQEMAKEDPVCAPEsmGSEDVLFMLYTS 294
Cdd:cd05911 87 FTDPDGL---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 295 GSTGMPKGivhtqagyllyAALTHK-LVFDH-----------RPGDIFGCVADIGWITGHSYVVYGPLCnGATSVLFESt 362
Cdd:cd05911 156 GTTGLPKG-----------VCLSHRnLIANLsqvqtflygndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 363 pvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTW 442
Cdd:cd05911 223 ---FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 443 WQTETGGICIAPRPSEEGAE----ILPGMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS--QAWPG-------MARTI 509
Cdd:cd05911 296 GMTETGGILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyynnpeaTKETF 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622839332 510 YGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:cd05911 368 DED-------------GWLHTGDIGYFDEDGYLYIVDRKKELI 397
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
140-577 |
5.26e-41 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 153.83 E-value: 5.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglrggrvmelkkivDEAVKHcptvqhvlvahrtdnkvhmgDLDipleqemakedpvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05973 79 ---------------DAANRH--------------------KLD---------------------SDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 300 PKGIVHTQAGYLLYAALTHKLVfDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgryWETVERLK 379
Cdd:cd05973 103 PKGVPVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 380 INQFYGAPTAVRLLLKYGdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETgGICIA-----P 454
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTEL-GMVLAnhhalE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 455 RPSEEGAE--ILPGMAmrpffgiVPVLMDEKGSVVEGsnVSGALCISQA-WPGMArtiYGDHQRFVDAYFKAypGYYFTG 531
Cdd:cd05973 254 HPVHAGSAgrAMPGWR-------VAVLDDDGDELGPG--EPGRLAIDIAnSPLMW---FRGYQLPDTPAIDG--GYYLTG 319
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839332 532 DGAHRTEGGYYQITGRMDDVInISNTLQIGGLFREAIrnsgdLLEH 577
Cdd:cd05973 320 DTVEFDPDGSFSFIGRADDVI-TMSGYRIGPFDVESA-----LIEH 359
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
106-555 |
3.74e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 153.03 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 106 QLNVSvNCLDQHVQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACA 185
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 186 RIGAV-HTV-IFagFSAASLAGRINDAKCKVVItFNQglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDNKVHmGDLD 263
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS--------EFVPLLAAILPQLPTVRTVIVEGDGPAAPL-APEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 264 IPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDI-------FGCVAdI 336
Cdd:PRK06187 146 GEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA-WLKLSRDDVylvivpmFHVHA-W 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 337 GWItghsyvvYGPLCNGATSVL---FESTPVypnagryWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLG 413
Cdd:PRK06187 224 GLP-------YLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFSSLRLVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 414 SVGEPIN---CEAWEWLHrvvgdsRCTLVDTWWQTETGGI--CIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVE 488
Cdd:PRK06187 288 YGGAALPpalLREFKEKF------GIDLVQGYGMTETSPVvsVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELP 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 489 GSNVS-GALCISQAWpgMARTIYGDHQRFVDAYfkaYPGYYFTGDGAHRTEGGYYQITGRMDDVI-----NIS 555
Cdd:PRK06187 362 PDGGEvGEIIVRGPW--LMQGYWNRPEATAETI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIisggeNIY 429
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
108-561 |
4.56e-38 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 147.61 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 108 NVSVNCLDQHVQKS-----PESVALIWERDEpGTEVRITYRELLETTCRLANTLKrhGVC---RGDCVAIYMPVSPLAVA 179
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGK-GDEVKWSFRELGSLSRKAANVLS--GACglqRGDRVAVILPRVPEWWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 180 AMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPTVQ-HVLVAHRTDNkvh 258
Cdd:cd05928 83 VNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKtKLLVSEKSRD--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 259 mGDLDIPLEQEMAKEDPVCApeSMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGW 338
Cdd:cd05928 151 -GWLNFKELLNEASTEHHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 339 ITGHSYVVYGPLCNGATsVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEP 418
Cdd:cd05928 228 IKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 419 INCEAWE-WLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPGMAMRPFFGIVPVLMDEKGSVV-EGSNVSGAL 496
Cdd:cd05928 303 LNPEVLEkWKAQTGLD----IYEGYGQTETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEGDIGI 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 497 CISQAWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINiSNTLQIG 561
Cdd:cd05928 375 RVKPIRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVIN-SSGYRIG 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
114-555 |
2.82e-37 |
|
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: 143.52 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVItfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemake 273
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 dpvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNG 353
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinceAWEWLHRVVGD 433
Cdd:cd17631 166 GTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 434 SRCTLVDTWWQTETG-GICIAPRpseEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTIYGD 512
Cdd:cd17631 236 RGVKFVQGYGMTETSpGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVPP-GEVGEIVVRG--PHVMAGYWNR 309
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622839332 513 HQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVInIS 555
Cdd:cd17631 310 PEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMI-IS 348
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
139-555 |
3.54e-37 |
|
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: 144.43 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 NqglrggrvmELKKIVDEAV-KHCPTVQHVLVA--HRTDNKVHMgdldipLEQEMAKEDPVCAPESMGSEDVLFMLYTSG 295
Cdd:cd05959 109 G---------ELAPVLAAALtKSEHTLVVLIVSggAGPEAGALL------LAELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETV 375
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 376 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVgdsrCTLVDTWWQTETGGICIAP 454
Cdd:cd05959 251 RRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGErWKARFG----LDILDGIGSTEMLHIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 455 RPSeegaEILPGMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQawPGMArTIYGdHQRfvDAYFKAYPGYYF-TGDG 533
Cdd:cd05959 325 RPG----RVRYGTTGKPVPGYEVELRDEDGGDVADG-EPGELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTrTGDK 393
|
410 420
....*....|....*....|..
gi 1622839332 534 AHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05959 394 YVRDDDGFYTYAGRADDMLKVS 415
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
122-554 |
1.57e-35 |
|
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: 138.81 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapes 281
Cdd:cd05930 75 RLAYILEDSGAKLVLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 mGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFES 361
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 362 TPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDT 441
Cdd:cd05930 168 EVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 442 WWQTETGGICIA---PRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGDH----Q 514
Cdd:cd05930 241 YGPTEATVDATYyrvPPDDEEDGRVPIG---RPIPNTRVYVLDENLRPV-PPGVPGELYIGGA--GLARGYLNRPeltaE 314
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622839332 515 RFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd05930 315 RFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKI 354
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
56-554 |
1.63e-35 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 142.14 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 56 SYPALSAQAAREPAAFWgPLARDTL--LWDTPYHTVWDCDFSTGKIG-WFLGGQLNVSVNCLDQHVQKSPESVALIWeRD 132
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW-SIVLDELslVFSVPPRCILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAIIW-RD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 133 EPGTEV---RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRIND 209
Cdd:PLN03052 199 EGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 210 AKCKVVITFNQGLRGGRVMELKKIVDEAvkHCPTVQhVLVAHRTDNKVHMGDLDIPLEQEMAKEDPVCAPES-----MGS 284
Cdd:PLN03052 279 SKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEykaveQPV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 285 EDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALT--HklvFDHRPGDIFGCVADIGWITGHsYVVYGPLCNGATSVLFEST 362
Cdd:PLN03052 356 EAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLALYNGS 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 363 PVYPNAGRYwetVERLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgdSRCT 437
Cdd:PLN03052 432 PLGRGFAKF---VQDAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWLM-----SRAG 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 438 ---LVDTWWQTETGGICIAP---RPSEEGAEILPGMAMRPFfgivpvLMDEKGSVVEgSNVSG----ALCisqawPGM-- 505
Cdd:PLN03052 497 ykpIIEYCGGTELGGGFVTGsllQPQAFAAFSTPAMGCKLF------ILDDSGNPYP-DDAPCtgelALF-----PLMfg 564
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 506 --ARTIYGDHQrfvDAYFKAYPGYYFT-----GDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PLN03052 565 asSTLLNADHY---KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNL 617
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
140-555 |
2.81e-34 |
|
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: 134.90 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmGSEDVLFMLYTSGSTGM 299
Cdd:cd05919 89 ---------------------------------------------------------------SADDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 300 PKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADI--GWITGHSyvVYGPLCNGATSVLFestPVYPNAGRYWETVER 377
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 378 LKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPS 457
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 458 eegaEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI--SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAH 535
Cdd:cd05919 256 ----AWRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVrgPSAAVGYWNNPEKSRATFNG-------GWYRTGDKFC 323
|
410 420
....*....|....*....|
gi 1622839332 536 RTEGGYYQITGRMDDVINIS 555
Cdd:cd05919 324 RDADGWYTHAGRADDMLKVG 343
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
141-554 |
1.46e-31 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 126.61 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 141 TYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFn 219
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 QGLRGGRVMELKKIVDEAvkhcptvqhvlvahrtdnkvhmgDLDIPLEQEMAKEDPVCAPEsmGSEDVLFMLYTSGSTGM 299
Cdd:TIGR01733 80 SALASRLAGLVLPVILLD-----------------------PLELAALDDAPAPPPPDAPS--GPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 300 PKGIVHTQAGyLLYAALTHKLVFDHRPGDIfgcvadigWITGHSYV-------VYGPLCNGATSVLFESTPVYPNAGRYW 372
Cdd:TIGR01733 135 PKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 373 ETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICI 452
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTVWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 453 A---PRPSEEGAEILP-GmamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDAYFKAY 524
Cdd:TIGR01733 279 AtlvDPDDAPRESPVPiG---RPLANTRLYVLDDDLRPV-PVGVVGELYIGG--PGVARGYLNRpeltAERFVPDPFAGG 352
|
410 420 430
....*....|....*....|....*....|..
gi 1622839332 525 PGY--YFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:TIGR01733 353 DGArlYRTGDLVRYLPDGNLEFLGRIDDQVKI 384
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
171-554 |
3.07e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 121.46 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 171 MPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTV-----Q 245
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVlpaagE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 246 HVLVAHRTDNKVHMGDLDIPLEQEMAKEDPVcAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHR 325
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 326 PGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYwetVERLKINQFYGAPTAVRLLLKYGDAWVKKYD 405
Cdd:PLN03051 159 PGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 406 RSSLRTLGSVGEPINCEAWEWLHRVVGDSRcTLVDTWWQTETGGICIAPRPSEEGAeilPGMAMRPFFGIVPVLMDEKG- 484
Cdd:PLN03051 235 WSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQA---PGAFSTASLGTRFVLLNDNGv 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839332 485 SVVEGSNVSGALCISQAWPGMA-RTIYGDHQRfvdAYFKAYPGYYFT-------GDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PLN03051 311 PYPDDQPCVGEVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNL 385
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
135-555 |
6.83e-29 |
|
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: 119.46 E-value: 6.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 215 VITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDpvcapesmGSEDVLFMLYTS 294
Cdd:cd05971 82 LVT--------------------------------------------------------D--------GSDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 295 GSTGMPKGIVHTQA---GYLLYAALTHKLVfdHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnaGRY 371
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDP--KAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 372 WETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG--- 448
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFGVE---VNEFYGQTECNlvi 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 449 GICIAPRPseegaeILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYY 528
Cdd:cd05971 249 GNCSALFP------IKPGSMGKPIPGHRVAIVDDNGTPLP-PGEVGEIAVELPDPVAFLG-YWNNPSATEKKMAG--DWL 318
|
410 420
....*....|....*....|....*..
gi 1622839332 529 FTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
114-330 |
5.79e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 118.28 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNQGLrggrvmeLKKiVDEAVKHCPTVQHVLVAhrtDNKVHMGDLD-IPLEQEMAK 272
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVL---DPRGLRDDPRlLSLDELLAL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 273 EDPVCAPE-------SMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIF 330
Cdd:COG1022 164 GREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRT 227
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
128-552 |
8.86e-28 |
|
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: 116.96 E-value: 8.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 128 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV-HTvIFAGFSAASLAGR 206
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT-INPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 207 INDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPTVQHVLV-AHRTDNKVHMGDLDIPLEQEMAKEDPVCAPESMGSE 285
Cdd:cd12119 93 INHAEDRVVFVDR---------DFLPLLEAIAPRLPTVEHVVVmTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLVFDHRPGDIFGCVADI----GW-------ITGHSYVVYGPLCNG 353
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVGAKLVLPGPYLDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINCEAWEWLHrv 430
Cdd:cd12119 244 ASLA---------------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 431 vgdsrctlVDT---WWQTETGGICIAPRPSEEGAEILPGMAM-------RPFFGIVPVLMDEKGSVVEGSNVS-GALCIS 499
Cdd:cd12119 305 --------VRVihaWGMTETSPLGTVARPPSEHSNLSEDEQLalrakqgRPVPGVELRIVDDDGRELPWDGKAvGELQVR 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 500 QAWpgMARTIYGDHQR----FVDAYFKaypgyyfTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:cd12119 377 GPW--VTKSYYKNDEEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVI 424
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
114-550 |
4.07e-27 |
|
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: 116.88 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvQHVLVAHRTDNKVHMGDLDIPLEQEMAKE 273
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLT---------------------------QSALAARLPELGVPVLALDALALAAEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPVCAPesmGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhrPGDIFGCVADIG-----WitghsyVVY 347
Cdd:COG1020 609 NPPVPV---TPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSfdasvW------EIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 348 GPLCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINCEAWEWL 427
Cdd:COG1020 678 GALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 428 HRVVGDsrCTLVDTWWQTETGGICIA--PRPSEEGAEILP-GmamRPFFGIVPVLMDEKGSVV-EGsnVSGALCIsqAWP 503
Cdd:COG1020 752 RARLPG--ARLVNLYGPTETTVDSTYyeVTPPDADGGSVPiG---RPIANTRVYVLDAHLQPVpVG--VPGELYI--GGA 822
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 504 GMARTIYGDH----QRFVDAYFkAYPG--YYFTGDGAHRTEGGYYQITGRMDD 550
Cdd:COG1020 823 GLARGYLNRPeltaERFVADPF-GFPGarLYRTGDLARWLPDGNLEFLGRADD 874
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
139-555 |
4.11e-27 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 114.94 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 NqglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDNkvhmGDLDipLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTG 298
Cdd:TIGR02262 110 G---------ALLPVIKAALGKSPHLEHRVVVGRPEA----GEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 299 MPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETVERL 378
Cdd:TIGR02262 175 MPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 379 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVVGDsrctLVDTWWQTETGGICIAPRPS 457
Cdd:TIGR02262 252 QPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTEMLHIFLSNLPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 458 eegaEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRT 537
Cdd:TIGR02262 326 ----DVRYGTSGKPVPGYRLRLVGDGGQDV-ADGEPGELLISG---PSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRN 395
|
410
....*....|....*...
gi 1622839332 538 EGGYYQITGRMDDVINIS 555
Cdd:TIGR02262 396 DDGSYTYAGRTDDMLKVS 413
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
114-552 |
5.57e-27 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 115.15 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVI---TFnqglrggRVMELKKIVDEAVKHCPTVQHVLVAHrTDNKVHMGDLDIPLEQEM 270
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVvpkTF-------RGFDHAAMARRLRPELPALRHVVVVG-GDGADSFEALLITPAWEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 271 AKEDP-VCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQ----AGYLLYAALthklvFDHRPGDIFGCVADIGWITGHSYV 345
Cdd:PRK13295 182 EPDAPaILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 VYGPLCNGATSVLFEStpvypnagryWETVERLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEP 418
Cdd:PRK13295 257 LMMPVMLGATAVLQDI----------WDPARAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 419 INCEAWEWLHRVVGdsrCTLVDTWWQTETGGIC-IAPRPSEEGAEI-----LPGMAMRpffgIV-----PVLMDEKGS-V 486
Cdd:PRK13295 324 IPGALVERARAALG---AKIVSAWGMTENGAVTlTKLDDPDERASTtdgcpLPGVEVR----VVdadgaPLPAGQIGRlQ 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 487 VEG-SNVSGALcisqAWPGMARTiygdhqrfvDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK13295 397 VRGcSNFGGYL----KRPQLNGT---------DA-----DGWFDTGDLARIDADGYIRISGRSKDVI 445
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
118-554 |
1.29e-26 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 112.73 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITFnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmGDldipleqemakedpvc 277
Cdd:cd05945 75 SPAERIREILDAAKPALLIAD-----------------------------------------GD---------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 apesmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIgwitghS-----YVVYGPLCN 352
Cdd:cd05945 98 --------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 353 GATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINCEAWEWLHRVVG 432
Cdd:cd05945 163 GATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 433 DSRctLVDTWWQTETGGICIAPRPSEE---GAEILP-GmamRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMART 508
Cdd:cd05945 240 DAR--IYNTYGPTEATVAVTYIEVTPEvldGYDRLPiG---YAKPGAKLVILDEDGRPVPP-GEKGELVISG--PSVSKG 311
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622839332 509 iYGDHQRFVDAYFKAYPGY--YFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd05945 312 -YLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
114-553 |
2.69e-26 |
|
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: 112.93 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtV 193
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFS--AASLAGRINDAKCKVVITfnqgLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVhmgDLDIPLEQEMA 271
Cdd:COG1021 103 VFALPAhrRAEISHFAEQSEAVAYII----PDRHRGFDYRALARELQAEVPSLRHVLVVGDAGEFT---SLDALLAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 272 KEDPVCAPEsmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDhrPGDIFGCVADIgwitGHSY-----V 345
Cdd:COG1021 176 LSEPRPDPD-----DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICgLD--ADTVYLAALPA----AHNFplsspG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GS-------- 414
Cdd:COG1021 245 VLGVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLqvgGAklspelar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 415 -VGEPINCeaweWLHRVVG------------DSRCTLVDTwwQtetGgiciapRPSEEGAEILpgmamrpffgIVpvlmD 481
Cdd:COG1021 319 rVRPALGC----TLQQVFGmaeglvnytrldDPEEVILTT--Q---G------RPISPDDEVR----------IV----D 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 482 EKGS-VVEGSnvSGALcisqawpgMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAHRTEGGYYQITGR 547
Cdd:COG1021 370 EDGNpVPPGE--VGEL--------LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGR 430
|
....*.
gi 1622839332 548 MDDVIN 553
Cdd:COG1021 431 AKDQIN 436
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
115-560 |
1.42e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.55 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWerdePGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITFNQGLrggrvmelkKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDIPLEQEMAkeD 274
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPA--T 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 PVcAPESMGSEdvlfMLYTSGSTGMPKGI--------VHTQAGYLlyaALTHKLvFDHRPGDIFGCVADIGwitgHSyvv 346
Cdd:PRK13391 149 PI-ADESLGTD----MLYSSGTTGRPKGIkrplpeqpPDTPLPLT---AFLQRL-WGFRSDMVYLSPAPLY----HS--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 347 yGPL--CN-----GATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPi 419
Cdd:PRK13391 213 -APQraVMlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAP- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 420 nCEAwewlhrvvgDSRCTLVDtWW---------QTETGGICiAPRPSEEGAEilPGMAMRPFFGIVPVLMDekgsvvegs 490
Cdd:PRK13391 287 -CPP---------QVKEQMID-WWgpiiheyyaATEGLGFT-ACDSEEWLAH--PGTVGRAMFGDLHILDD--------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 491 nvSGALCIsqawPGMARTIYGDHQR-FVdaYFK----------AYPGYYFTGDGAHRTEGGYYQITGRMDDVInISNTLQ 559
Cdd:PRK13391 344 --DGAELP----PGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVN 414
|
.
gi 1622839332 560 I 560
Cdd:PRK13391 415 I 415
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-554 |
1.57e-25 |
|
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: 109.98 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITfnQGLRGGRVMELKKIVdeavkhcptvqhvlvahrtdnkvhmgDLDIPLEQEMAKED 274
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAV--------------------------VIDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 PVCApesmGSEDVLFMLYTSGSTGMPKGIVHTQAGYLlyaalthKLVFDHR-----PGDIFGCVADIGWiTGHSYVVYGP 349
Cdd:cd12117 130 AVPV----SPDDLAYVMYTSGSTGRPKGVAVTHRGVV-------RLVKNTNyvtlgPDDRVLQTSPLAF-DASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 350 LCNGATSVLFE-STPVYPNAGRywETVERLKINQFY--------------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 414
Cdd:cd12117 198 LLNGARLVLAPkGTLLDPDALG--ALIAEEGVTVLWltaalfnqladedpECFAGLRELLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 415 vGEPINCeawewlhrvVGDSRCTLVDTWWQTetggiciaPRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVEgSNVSG 494
Cdd:cd12117 276 -LRLVNG---------YGPTENTTFTTSHVV--------TELDEVAGSIPIG---RPIANTRVYVLDEDGRPVP-PGVPG 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 495 ALCISQAwpGMARTIYGD----HQRFVDAYFKayPG--YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd12117 334 ELYVGGD--GLALGYLNRpaltAERFVADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
138-552 |
1.52e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 108.12 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 138 VRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAgFSAASLAGRINDAKCKVVIT 217
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPL-LEPEQIAELLRAAGAKVLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 218 fnqgLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTD--------------NKVHMGDLDipLEQEMAKE--DPVCAPES 281
Cdd:PRK07529 136 ----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARylpgpkrlavplirRKAHARILD--FDAELARQpgDRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGD----------IFGCVAdigwitghsyVVYGPLC 351
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV----------TGLAPLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 352 NGATSVLfeSTPV-YPNAG---RYWETVERLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRTLGSVGEPINCEAWEWL 427
Cdd:PRK07529 279 RGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 428 HRVVGdsrCTLVDTWWQTE-TGGICIAPR--PSEEGA--EILPGMAMRpffgIVPVlmDEKGSVVEGSNVS--GALCISQ 500
Cdd:PRK07529 354 EAATG---VRIVEGYGLTEaTCVSSVNPPdgERRIGSvgLRLPYQRVR----VVIL--DDAGRYLRDCAVDevGVLCIAG 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 501 A--WPGMARtiyGDHQRfvDAYFkaYPGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK07529 425 PnvFSGYLE---AAHNK--GLWL--EDGWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
114-555 |
2.67e-24 |
|
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: 106.11 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVI---TFNQGLRGGRVMELKKIVDEavkhcptvqhvlvahrtdnkvhmgdldipleqem 270
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIvavSFTDLLAAGAPLGERVALTP---------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 271 akedpvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHK--LVFDHRPGDIFGCVADIGWITGHSYVVYG 348
Cdd:cd05936 125 --------------EDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:cd05936 190 PLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 429 RVVGdsrCTLVDTWWQTETGGIcIAPRPSEEgaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCIS--QAWPGma 506
Cdd:cd05936 264 ELTG---VPIVEGYGLTETSPV-VAVNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEV-GELWVRgpQVMKG-- 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 507 rtiYGDH-----QRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05936 335 ---YWNRpeetaEAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVG 378
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
116-555 |
2.68e-24 |
|
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: 106.27 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 116 QHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 196 AGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqHVLVAHRTDNKVHMGDLDIPLEQEMAKEDP 275
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLT----------------------------HPALAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 276 VCAPESMGseDVLFMLYTSGSTGMPKGIV--HTQAGYLLYAaltHKLVFDHRPGDIFGCVADIGWITGHSYvVYGPLCNG 353
Cdd:cd17651 129 PDPALDAD--DLAYVIYTSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQE-IFSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAW--EWLHRVV 431
Cdd:cd17651 203 ATLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTEDlrEFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 432 GdsrCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCIsqAWPGMARTIYG 511
Cdd:cd17651 280 G---LRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPP-GVPGELYI--GGAGLARGYLN 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622839332 512 D----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd17651 354 RpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIR 401
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
122-554 |
1.07e-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: 104.30 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALiweRDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd12116 1 PDATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivDEAvkhcptvqhvlvahrTDNKVHMGDLDIPLEQEMAKEDPVCAPES 281
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFdhRPGDIFGCVADIGW-ITGHSyvVYGPLCNGATSVLF 359
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGL--GPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 360 ESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdaWvkkYDRSSLRTL-GsvGEPinceawewLHRVVGDSRCTL 438
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAG--W---QGRAGLTALcG--GEA--------LPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 439 VDTWWQ----TETGGICIAPRPSEEGAEILPGmamRPFFGIVPVLMDEKG-SVVEGsnVSGALCIsqAWPGMARTIYGD- 512
Cdd:cd12116 263 VGSLWNlygpTETTIWSTAARVTAAAGPIPIG---RPLANTQVYVLDAALrPVPPG--VPGELYI--GGDGVAQGYLGRp 335
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1622839332 513 ---HQRFVDAYFkAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd12116 336 altAERFVPDPF-AGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKI 381
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-415 |
1.35e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 104.74 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 119 QKSPESVALIWErdepGTEvrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 198
Cdd:PRK06178 44 RERPQRPAIIFY----GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 199 SAASLAGRINDAKCKVVITFNQglrggrvmeLKKIVdEAVKHCPTVQHVLVAHRTD-----------------NKVHMGD 261
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQ---------LAPVV-EQVRAETSLRHVIVTSLADvlpaeptlplpdslrapRLAAAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 262 LDI-PLEQEMAKEDPVCAPESmgseDVLFML-YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWI 339
Cdd:PRK06178 188 IDLlPALRACTAPVPLPPPAL----DALAALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWI 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 340 TGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSV 415
Cdd:PRK06178 264 AGENFGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVV 333
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
114-552 |
2.80e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 103.45 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK07656 11 LARAARRFGDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFnQGLRGgrvmelkkiVDEAVKHC-PTVQHVlVAHRTDNKVHMGDLDIPLEQEMAK 272
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVL-GLFLG---------VDYSATTRlPALEHV-VICETEEDDPHTEKMKTFTDFLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 273 EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHKLvfDHRPGD----------IFGCVAdiGWIT 340
Cdd:PRK07656 154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMltHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 341 ghsyvvygPLCNGATsVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPIn 420
Cdd:PRK07656 229 --------PLMRGAT-ILPL--PVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 421 ceAWEWLHRVVGDSRCTLVDTWWQ-TETGGI-CIAPRpsEEGAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI 498
Cdd:PRK07656 294 --PVALLERFESELGVDIVLTGYGlSEASGVtTFNRL--DDDRKTVAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLV 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 499 S-----QAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK07656 369 RgpnvmKGYYDDpeatAAAIDAD-------------GWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
139-553 |
2.03e-22 |
|
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: 100.15 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 nqglrggrvmelkkivdeavkhcPTVqhvlvaHRTDNKVHMGDldipleqemakedpvcapesmgseDVLFMLYTSGSTG 298
Cdd:cd05903 80 -----------------------PER------FRQFDPAAMPD------------------------AVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 299 MPKGIVHTqAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 378
Cdd:cd05903 107 EPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 379 KINQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPINC----EAWEWLHRVVgdsrctlVDTWWQTETGGICI 452
Cdd:cd05903 182 GVTFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVPRslarRAAELLGAKV-------CSAYGSTECPGAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 453 APRPSEEGAEIlpGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMartIYGDHQRfVDAYFKAYP-GYYFTG 531
Cdd:cd05903 251 SITPAPEDRRL--YTDGRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSV---FLGYLDR-PDLTADAAPeGWFRTG 321
|
410 420
....*....|....*....|..
gi 1622839332 532 DGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIII 343
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
118-410 |
5.26e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 99.62 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK08316 21 ARRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITfNQGLRGgrvmelkkIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDIpleQEMAKEDPVC 277
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLV-DPALAP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 APE-SMGSEDVLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVfdhrpgdifGCVADIGWITG----------HS--- 343
Cdd:PRK08316 163 EPDvELADDDLAQILYTSGTESLPKGAMLT------HRALIAEYV---------SCIVAGDMSADdiplhalplyHCaql 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839332 344 YVVYGP-LCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR 410
Cdd:PRK08316 228 DVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR 289
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
122-552 |
6.57e-22 |
|
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: 99.23 E-value: 6.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITFNQG---LRGG--RVMelkkIVDEAVKHCptvqhvlvahrtdnkVHMGDLDIPleqemAKEDPV 276
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaekLASLalPVV----LLDSAEFDS---------------LSFSDLLFE-----ADEAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 277 CAPEsMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHRPGDIFGCVADIGWITGHSYVVYGPLCNGAT 355
Cdd:cd05904 151 PVVV-IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGAT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 356 SVlfestpVYP--NAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGD 433
Cdd:cd05904 230 VV------VMPrfDLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 434 SRctLVDTWWQTETGGICIAPRPSEEGAE-------ILPGMAMRpffgIVpvlmDEKGSVVEGSNVSGALCISQawPGM- 505
Cdd:cd05904 302 VD--LGQGYGMTESTGVVAMCFAPEKDRAkygsvgrLVPNVEAK----IV----DPETGESLPPNQTGELWIRG--PSIm 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 506 ----------ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:cd05904 370 kgylnnpeatAATIDKE-------------GWLHTGDLCYIDEDGYLFIVDRLKELI 413
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
137-577 |
6.66e-22 |
|
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: 98.70 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCR-GDCVAIYMPVSPLAVAAMLACARIGAVhtvifagfsaaslagrindakCKVV 215
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 216 ITFnqgLRGGrvmELKKIVDEAvkhcpTVQHVLVAHRTdnkvhmgdldipleqemakedpvcapesMGSEDVLFMLYTSG 295
Cdd:cd05958 67 MPL---LRPK---ELAYILDKA-----RITVALCAHAL----------------------------TASDDICILAFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 375
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 376 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPR 455
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 456 PSeegaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQawPGMARTIYGDHQRfvdAYFKAypGYYFTGDGAH 535
Cdd:cd05958 259 PG----DARPGATGKPVPGYEAKVVDDEGNPVPDGTI-GRLAVRG--PTGCRYLADKRQR---TYVQG--GWNITGDTYS 326
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622839332 536 RTEGGYYQITGRMDDVInisntlQIGGLFREAIRNSGDLLEH 577
Cdd:cd05958 327 RDPDGYFRHQGRSDDMI------VSGGYNIAPPEVEDVLLQH 362
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
118-553 |
8.24e-22 |
|
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: 98.74 E-value: 8.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd05923 11 ASRAPDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRI-NDAKCKVVITFNQG------LRGGRVMELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDIPLEQEM 270
Cdd:cd05923 87 LKAAELAELIeRGEMTAAVIAVDAQvmdaifQSGVRVLALSDLVG--------------------------LGEPESAGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 271 AKEDPVCAPESMGsedvlFMLYTSGSTGMPKGIVHTQAgyllyAALTHKLVFDHRPGDIFGC------VADIGWITGHSY 344
Cdd:cd05923 141 LIEDPPREPEQPA-----FVFYTSGTTGLPKGAVIPQR-----AAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 345 VVYGPLCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAW 424
Cdd:cd05923 211 VLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 425 EWLHRVVGDSRctlVDTWWQTETGGICIAPRPSeegaeilPGMAMRPFFG----IVPVL--MDEKGSVVEGSNVSGALCI 498
Cdd:cd05923 285 ERVNQHLPGEK---VNIYGTTEAMNSLYMRDAR-------TGTEMRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAA 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 499 SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd05923 355 DAAFTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMII 402
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
140-556 |
1.38e-21 |
|
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: 97.64 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINdakckvvitfn 219
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglRGGRVMelkKIVDEAVKhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgSEDVLFMLYTSGSTGM 299
Cdd:cd05974 70 ---RGGAVY---AAVDENTH--------------------------------------------ADDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 300 PKGIVHTQAGYLLyAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVypNAGRYWETVERLK 379
Cdd:cd05974 100 PKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 380 INQFYGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGIcIAPRPsee 459
Cdd:cd05974 177 VTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP--- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 460 GAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsgALCISQAWP-GMARTIYGDHQRFVDAYfkaYPGYYFTGDGAHRTE 538
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGAPATEGEV--ALDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDE 320
|
410
....*....|....*...
gi 1622839332 539 GGYYQITGRMDDVINISN 556
Cdd:cd05974 321 DGYLTYVGRADDVFKSSD 338
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-555 |
3.82e-21 |
|
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: 96.21 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 nqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDPVCapesmgsedvlfMLYTSGSTG 298
Cdd:cd05934 82 -------------------------------------------------------DPAS------------ILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 299 MPKGIVHTQAgYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 378
Cdd:cd05934 95 PPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 379 KINQFYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPS 457
Cdd:cd05934 170 GATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 458 EEGaeilPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWP-GMARTIYGDHqrfvDAYFKAYP-GYYFTGDGAH 535
Cdd:cd05934 242 PRR----PGSIGRPAPGYEVRIVDDDGQELP-AGEPGELVIRGLRGwGFFKGYYNMP----EATAEAMRnGWFHTGDLGY 312
|
410 420
....*....|....*....|....*
gi 1622839332 536 RTEGGYYQITGRMDDVI-----NIS 555
Cdd:cd05934 313 RDADGFFYFVDRKKDMIrrrgeNIS 337
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
114-333 |
1.32e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 95.71 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITfnqglrGGrvmELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDipLEQeMAKE 273
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIV------GE---ELVEAFEEARADLARPPRLWVAGGDTLDDPEGYED--LAA-AAAG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 274 DPVCAPESMGS---EDVLFMLYTSGSTGMPKGIVHTQAGYLLY----AALThklvfDHRPGDIFGCV 333
Cdd:PRK08279 185 APTTNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAmggfGGLL-----RLTPDDVLYCC 246
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
122-553 |
3.93e-20 |
|
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: 93.53 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd05926 1 PDAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglRGGRVMElkkiVDEAVKHcPTVQHVLVAHRTDNKVHMGDLDiPLEQEMAKEDPVCAPES 281
Cdd:cd05926 77 EFEFYLADLGSKLVLT-----PKGELGP----ASRAASK-LGLAILELALDVGVLIRAPSAE-SLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGYLL---YAALTHKLVfdhrPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL 358
Cdd:cd05926 146 PLPDDLALILHTSGTTGRPKGVPLTHRNLAAsatNITNTYKLT----PDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 359 festPVYPNAGRYWETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGdsrCT 437
Cdd:cd05926 222 ----PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFG---AP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 438 LVDTWWQTETGG------ICIAPRPseegaeilPGMAMRPfFGIVPVLMDEKGSVVEgSNVSGALCISQawPGMARTIYG 511
Cdd:cd05926 293 VLEAYGMTEAAHqmtsnpLPPGPRK--------PGSVGKP-VGVEVRILDEDGEILP-PGVVGEICLRG--PNVTRGYLN 360
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622839332 512 DHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd05926 361 NPEANAEAAFKD--GWFRTGDLGYLDADGYLFLTGRIKELIN 400
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
122-494 |
9.67e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 92.64 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVItFNQGLrGGRVMELKkivDEavkhCPTVQHVL-VAHRTDNKVHMGdlDIPLEQEMAKEDPVCAPE 280
Cdd:PRK07798 91 ELRYLLDDSDAVALV-YEREF-APRVAEVL---PR----LPKLRTLVvVEDGSGNDLLPG--AVDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 281 SmGSEDVLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLvfDHRPG----DIFGCVADIGWITGHSYVVYGPLCNGAT- 355
Cdd:PRK07798 160 E-RSPDDLYLLYTGGTTGMPKGVMWRQED--IFRVLLGGR--DFATGepieDEEELAKRAAAGPGMRRFPAPPLMHGAGq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 356 -----------SVLFESTPVYpNAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGS 414
Cdd:PRK07798 235 waafaalfsgqTVVLLPDVRF-DADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 415 VGEPINCEAWEWLHRVVGDSrcTLVDTWWQTETG--GICIAPRPSEEGAeilpgmamRPFFGIVP--VLMDEKGSVVE-G 489
Cdd:PRK07798 304 GGALFSPSVKEALLELLPNV--VLTDSIGSSETGfgGSGTVAKGAVHTG--------GPRFTIGPrtVVLDEDGNPVEpG 373
|
....*
gi 1622839332 490 SNVSG 494
Cdd:PRK07798 374 SGEIG 378
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
115-554 |
1.75e-19 |
|
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: 91.22 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALiwerdePGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVItfnqglrggrvmelkkivdeavkhCPTVQHvlvahrtdnkvhmgdldipleqemaked 274
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLL------------------------TTDSPD---------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 pvcapesmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIGW--ITGhsyVVYGPLCN 352
Cdd:cd17653 106 -----------DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 353 GATSVLfeSTPVYPnagryWETVERlKINQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPINCE-AWEWLHRVV 431
Cdd:cd17653 171 GGTLVL--ADPSDP-----FAHVAR-TVDALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEAVPPSlLDRWSPGRR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 432 -----GDSRCTLVDTWWQTETGgiciapRPSEEGAEIlPGMAMRpffgivpvLMDE-KGSVVEGsnVSGALCISQawPGM 505
Cdd:cd17653 235 lynayGPTECTISSTMTELLPG------QPVTIGKPI-PNSTCY--------ILDAdLQPVPEG--VVGEICISG--VQV 295
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 506 ARTIYGDHQRFVDAY--FKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17653 296 ARGYLGNPALTASKFvpDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKV 348
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
114-413 |
6.20e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 90.19 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVItFNQGLRGgrvMELKKIVDEAVKHC-PTVQHVLVAHRTDNKV---HMGDLDIPLEQE 269
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLV-VWPGFKG---IDFAAILAAVPPDAlPPLRAIAVVDDAADATpapAPGARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 270 MAKEDPVCAPESmGSEDVLFMLY-TSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDIFGCVADIGWITGHSYVVyG 348
Cdd:PRK06164 166 DPAPPAAAGERA-ADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-G 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 349 PLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLG 413
Cdd:PRK06164 243 ALAGGAPLVCE---PVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFG 300
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
114-554 |
2.10e-18 |
|
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: 88.10 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERdepgteVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITfnQGLRGGRvmelkkIVDEAVKhcPTVQHVLVAHRTDnkvhmgdldipleqemAKE 273
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLT--TADLAAR------LPAGGDV--ALLGDEALAAPPA----------------TPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPVCAPesmgsEDVLFMLYTSGSTGMPKGIVHTQAG---YLLYaaLTHKlvFDHRPGDIFGCVADIGWITGhSYVVYGPL 350
Cdd:cd17646 132 LVPPRP-----DNLAYVIYTSGSTGRPKGVMVTHAGivnRLLW--MQDE--YPLGPGDRVLQKTPLSFDVS-VWELFWPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 351 CNGATSVLFEstpvyPNAGR---YW-ETVERLKINQFYGAPTAVRLLLkygdAWVKKYDRSSLRTLGSVGEPINCEAWEW 426
Cdd:cd17646 202 VAGARLVVAR-----PGGHRdpaYLaALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 427 LHRVVGdsrCTLVDTWWQTETgGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMA 506
Cdd:cd17646 273 FLALPG---AELHNLYGPTEA-AIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVP-VGVPGELYL--GGVQLA 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 507 RTIYG----DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17646 346 RGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
122-555 |
3.34e-18 |
|
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: 87.36 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDPvcapes 281
Cdd:cd17643 75 RIAFILADSGPSLLLT--------------------------------------------------------DP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 mgsEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHRpgDIfgcvadigWITGHSYV-------VYGPLCNG 353
Cdd:cd17643 93 ---DDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFNED--DV--------WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATSVLFES----TPVypnagRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINCEAWE-W 426
Cdd:cd17643 160 GRLVVVPYevarSPE-----DFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRpW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 427 LHRvVGDSRCTLVDTWWQTETggiCIAPRPSEEGAEILPGMAM----RPFFGIVPVLMDEKGSVVEGSnVSGALCISQaw 502
Cdd:cd17643 231 AGR-FGLDRPQLVNMYGITET---TVHVTFRPLDAADLPAAAAspigRPLPGLRVYVLDADGRPVPPG-VVGELYVSG-- 303
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839332 503 PGMARTIYG----DHQRFVDAYFKAyPG--YYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd17643 304 AGVARGYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIR 361
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
140-568 |
3.49e-18 |
|
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: 87.27 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakEDPvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05907 84 -----------------------------------------------------EDP---------DDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 300 PKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnagrywETVERLK 379
Cdd:cd05907 102 PKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL------DDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 380 INQFYGAPtavRLLLK-YGDAWVKK--------YDR---SSLRTLGSVGEPINCEAWEWLHRvVGdsrCTLVDTWWQTET 447
Cdd:cd05907 175 PTVFLAVP---RVWEKvYAAIKVKAvpglkrklFDLavgGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 448 GGICIAPRPsEEGAEILPGMAMRPffgiVPVLMDEKGSVVegsnVSGalcisqawPGMARTIYGDHQRFVDAYFKayPGY 527
Cdd:cd05907 248 SAVVTLNPP-GDNRIGTVGKPLPG----VEVRIADDGEIL----VRG--------PNVMLGYYKNPEATAEALDA--DGW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 528 YFTGDGAHRTEGGYYQITGRMDDVI------NIS-----NTLQIGGLFREAI 568
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIitsggkNISpepieNALKASPLISQAV 360
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
139-419 |
3.83e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 87.71 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRH-GVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIT 217
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 218 fnqglrggrVMELKKIVDEAVKHCPtVQHVLVAHRTD-------NKVH------------MGDLDIPLEQEMAKEDPVcA 278
Cdd:PRK08314 115 ---------GSELAPKVAPAVGNLR-LRHVIVAQYSDylpaepeIAVPawlraepplqalAPGGVVAWKEALAAGLAP-P 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 279 PESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL 358
Cdd:PRK08314 184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 359 F-----EStpvypnAGRyweTVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPI 419
Cdd:PRK08314 263 MprwdrEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAM 317
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
122-554 |
4.24e-18 |
|
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: 87.14 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17650 1 PDAIAVSDA------TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDPvcapes 281
Cdd:cd17650 75 RLQYMLEDSGAKLLLT--------------------------------------------------------QP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 mgsEDVLFMLYTSGSTGMPKGIVHTQAGYL--------LY--AALTHKLV------FDHRPGDIfgCVAdigwitghsyv 345
Cdd:cd17650 93 ---EDLAYVIYTSGTTGKPKGVMVEHRNVAhaahawrrEYelDSFPVRLLqmasfsFDVFAGDF--ARS----------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 vygpLCNGATSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPIncEA 423
Cdd:cd17650 157 ----LLNGGTLVICPDEVKL-DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 424 WEWLHRVVGdSRCTLVDTWWQTETggiCIAPRPSEEGAEILPGMAM----RPFFGIVPVLMDEKGSVVEgSNVSGALCIS 499
Cdd:cd17650 228 FKTLAARFG-QGMRIINSYGVTEA---TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQP-VGVAGELYIG 302
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839332 500 QAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17650 303 GA--GVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKI 359
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
116-422 |
7.34e-18 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 86.91 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 116 QHVQKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVcRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 196 A---GFSAASLAGRINDAKCKVVITfNQGLRGGrvmelkkiVDEAVKHCPTVQHVLVAHrTDNKvhmgDLDIPleqemak 272
Cdd:cd05931 80 PptpGRHAERLAAILADAGPRVVLT-TAAALAA--------VRAFAASRPAAGTPRLLV-VDLL----PDTSA------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 273 eDPVCAPeSMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFG----CVADIGWITGhsyvVYG 348
Cdd:cd05931 139 -ADWPPP-SPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCNGATSVLFEstpvyPNA-----GRYWETVERLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPINC 421
Cdd:cd05931 212 PLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVRP 285
|
.
gi 1622839332 422 E 422
Cdd:cd05931 286 A 286
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
122-554 |
1.35e-17 |
|
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: 85.50 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17649 1 PDAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvQHvlvahrtdnkvhmgdldipleqemakedpvcaPES 281
Cdd:cd17649 75 RLRYMLEDSGAGLLLT---------------------------HH--------------------------------PRQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 MGsedvlFMLYTSGSTGMPKGIVHTQagyllyAALTH-----KLVFDHRPGDIFGCVADIGWITGHSYvVYGPLCNGAtS 356
Cdd:cd17649 96 LA-----YVIYTSGSTGTPKGVAVSH------GPLAAhcqatAERYGLTPGDRELQFASFNFDGAHEQ-LLPPLICGA-C 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 357 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCE-AWEWLhrvvgDSR 435
Cdd:cd17649 163 VVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRWL-----KAP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 436 CTLVDTWWQTE---TGGICIAPRPSEEGAEILP-GmamRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG 511
Cdd:cd17649 237 VRLFNAYGPTEatvTPLVWKCEAGAARAGASMPiG---RPLGGRSAYILDADLNPVP-VGVTGELYI--GGEGLARGYLG 310
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622839332 512 ----DHQRFV-DAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17649 311 rpelTAERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKI 358
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
120-328 |
2.73e-17 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 84.83 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 120 KSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 199
Cdd:TIGR03098 12 RLPDATALVH------HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 200 AASLAGRINDAKCKVVITFNQGLRggrvmelkkIVDEAVKHCPTVQHVLvahRTDNKVHMGDLDIPLE----QEMAKEDP 275
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLD---------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEEpaswPKLLALGD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 276 VCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLvfDHRPGD 328
Cdd:TIGR03098 154 ADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAqSVATYL--ENRPDD 205
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
139-330 |
4.02e-17 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 84.01 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 nqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgDLDIPLEQEMAKEDPVCAPesMGSEDVLFMLYTSGSTG 298
Cdd:cd05939 82 ------------------------------------------NLLDPLLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTG 117
|
170 180 190
....*....|....*....|....*....|..
gi 1622839332 299 MPKGIVHTQAGYLLYAALTHKlVFDHRPGDIF 330
Cdd:cd05939 118 LPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVV 148
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
141-419 |
4.65e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 84.26 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnQ 220
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT--Q 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 221 GLRGGRVMELkkivdeavKHCPTVQHVLVAHRTDNKVHMGDLdipleqeMAKEDPVCAPESMGSEDVLFMLYTSGSTGMP 300
Cdd:PLN02246 130 SCYVDKLKGL--------AEDDGVTVVTIDDPPEGCLHFSEL-------TQADENELPEVEISPDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 301 KGIVhtqagyllyaaLTHK-LV-------------FDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL---FEstp 363
Cdd:PLN02246 195 KGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpkFE--- 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 364 vypnAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPI 419
Cdd:PLN02246 261 ----IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPL 310
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
135-485 |
5.34e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 83.80 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 215 VITfnqglrGGRVMELkkiVDEAVKHCPT-VQHVLVAHrtdnkvhmGDLD--IPLEQEMAKEDPV-CAPESMGSEdvlfM 290
Cdd:PRK08276 87 LIV------SAALADT---AAELAAELPAgVPLLLVVA--------GPVPgfRSYEEALAAQPDTpIADETAGAD----M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 291 LYTSGSTGMPKGIVhtqagyllyAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGA-------------TSV 357
Cdd:PRK08276 146 LYSSGTTGRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 358 LFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP----INCEAWEWLHRVVgd 433
Cdd:PRK08276 217 VMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPcpveVKRAMIDWWGPII-- 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 434 srctlVDTWWQTETGGICIAprPSEEGAEiLPGMAMRPFFGIVPVLmDEKGS 485
Cdd:PRK08276 291 -----HEYYASSEGGGVTVI--TSEDWLA-HPGSVGKAVLGEVRIL-DEDGN 333
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
116-557 |
7.51e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 83.64 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 116 QHVQKSPESVALIwerDEPGTevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 196 AGFSAASLAGRINDAKCKVVIT---FNQGLRGGRVMELKKIVdeavkhcPTVQHVLVAhrtdNKVHMGDLDIPLEQEMAK 272
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlFKQTRPVDLILPLQNQL-------PQLQQIVGV----DKLAPATSSLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 273 EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLL----YAALTHkLVFDhrpgDIFGCVADIGWITGHSYVVYG 348
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINC----EAW 424
Cdd:PRK06087 250 PFLIGARSVLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIPKkvarECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 425 EwlHRVVgdsrctLVDTWWQTETggiciAPR---PSEEGAEILPGMAMRPFFGI-VPVLMDEKGSV---VEGSNVSGAlc 497
Cdd:PRK06087 324 Q--RGIK------LLSVYGSTES-----SPHavvNLDDPLSRFMHTDGYAAAGVeIKVVDEARKTLppgCEGEEASRG-- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839332 498 isqawPGMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVI-----NISNT 557
Cdd:PRK06087 389 -----PNVFMGYLDEPEltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIvrggeNISSR 446
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
119-463 |
3.27e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.87 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 119 QKSPESVALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKivdEAVKHCPTVqhvlvahrtDNKVHMG--DLDiPLEQEMAK 272
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK---PSVRRLVTV---------GGRLLWGgtTLA-TLLRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 273 EDPVCAPesMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLlyAALTH-KLVFDHRPGDIfgcvaDIgwitgHSY---VVYG 348
Cdd:PRK09274 164 APFPMAD--LAPDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEAlREDYGIEPGEI-----DL-----PTFplfALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCnGATSVLFESTPVYP---NAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWE 425
Cdd:PRK09274 230 PAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839332 426 WLHRVVGD--------------------SRCTLVDTWWQTETG-GICIApRPSeEGAEI 463
Cdd:PRK09274 307 RFRAMLPPdaeiltpygatealpissieSREILFATRAATDNGaGICVG-RPV-DGVEV 363
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
114-552 |
6.62e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 80.59 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNqglrGGRVMELKKIVDEAVKHCPTVQHVLVAH----RTDNKVHMGDLDIP---L 266
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD----AFKTSDYHAMLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 267 EQEMAKEDPVCAPE-------SMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDHrpgdifgcvadiGWI 339
Cdd:PRK12583 176 WHELQARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKG-----------ATLSHHNILNN------------GYF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 340 TGHS---------------YVVYGPLCNGATSVLFESTPVYPN----AGRYWETVERLKINQFYGAPTAVRLLLKYGDaw 400
Cdd:PRK12583 233 VAESlgltehdrlcvpvplYHCFGMVLANLGCMTVGACLVYPNeafdPLATLQAVEEERCTALYGVPTMFIAELDHPQ-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 401 VKKYDRSSLRTLGSVGEPinCEAwEWLHRVVGDSRCTLVD-TWWQTETGGICIA-------PRPSEEGAEILPGMAMRpf 472
Cdd:PRK12583 311 RGNFDLSSLRTGIMAGAP--CPI-EVMRRVMDEMHMAEVQiAYGMTETSPVSLQttaaddlERRVETVGRTQPHLEVK-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 473 fgivpvLMDEKGSVVEGSNVsGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQ 543
Cdd:PRK12583 386 ------VVDPDGATVPRGEI-GELCtrgysVMKGYWNNpeatAESIDED-------------GWMHTGDLATMDEQGYVR 445
|
....*....
gi 1622839332 544 ITGRMDDVI 552
Cdd:PRK12583 446 IVGRSKDMI 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-554 |
1.62e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.77 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK12316 518 EEQVERTPEAPALAF------GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDIPLEQEMAKED 274
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLS--------------------------QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 PvcAPE-SMGSEDVLFMLYTSGSTGMPKGIVHTqagyllYAALTHKL-----VFDHRPGDIFGCVADIGWITGHsYVVYG 348
Cdd:PRK12316 646 E--NPGtELNPENLAYVIYTSGSTGKPKGAGNR------HRALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSV-WEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLH 428
Cdd:PRK12316 717 PLMSGARLVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEAL---PADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 429 RVVGD-SRCTLVDTWWQTE-TGGICIAPRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMA 506
Cdd:PRK12316 789 QVFAKlPQAGLYNLYGPTEaAIDVTHWTCVEEGGDSVPIG---RPIANLACYILDANLEPVP-VGVLGELYLAGR--GLA 862
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 507 RTIYG----DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK12316 863 RGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 914
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
57-113 |
1.86e-15 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 70.58 E-value: 1.86e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 57 YPALSAQAAREPAAFWGPLARDtLLWDTPYHTVWDCDFStGKIGWFLGGQLNVSVNC 113
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
118-554 |
2.59e-15 |
|
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: 78.51 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd12115 9 AARTPDAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvc 277
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 apesmGSEDVLFMLYTSGSTGMPKG--IVHTQAGYLLYAALthklvfDHRPGDIFGCVADIGWITGHSYV--VYGPLCNG 353
Cdd:cd12115 103 -----DPDDLAYVIYTSGSTGRPKGvaIEHRNAAAFLQWAA------AAFSAEELAGVLASTSICFDLSVfeLFGPLATG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATSVLFESTPVYPNAGRYWETVerlKINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLH----- 428
Cdd:cd12115 172 GKVVLADNVLALPDLPAAAEVT---LINT---VPSAAAELLRHDAL------PASVRVVNLAGEPLPRDLVQRLYarlqv 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 429 -RVV---GDSRctlvDTWWQTetggicIAPRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpG 504
Cdd:cd12115 240 eRVVnlyGPSE----DTTYST------VAPVPPGASGEVSIG---RPLANTQAYVLDRALQPV-PLGVPGELYIGGA--G 303
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 505 MARTIYGD----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd12115 304 VARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKV 357
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
114-553 |
3.53e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 78.39 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNQGLRGGRvmelkkivDEAVKHCPtvqhVLVAHRTDNKVHMGDLDIPLEQEMAKE 273
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRA--------EPTTRWWP----LTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPVCAPESMGSEDVLFMlYTSGSTGMPKGIVHTQAGyllYAALTHKLVFDHRPGDIFGCVADIGWITGHSYV--VYGPLC 351
Cdd:PRK05852 166 PATSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 352 NGATSVLfestpvyPNAGR-----YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEW 426
Cdd:PRK05852 242 SGGAVLL-------PARGRfsahtFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 427 LHRVVG--------------DSRCTLVDTWWQTETGGICIAPRPSEEGAEIlpgMAMRPFFGIVPVlmDEKGSV-VEGSN 491
Cdd:PRK05852 315 LQTEFAapvvcafgmteathQVTTTQIEGIGQTENPVVSTGLVGRSTGAQI---RIVGSDGLPLPA--GAVGEVwLRGTT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 492 VsgalcisqawpgmARTIYGD----HQRFVDAYFKaypgyyfTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:PRK05852 390 V-------------VRGYLGDptitAANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELIN 435
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
139-555 |
4.39e-15 |
|
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: 77.52 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 NqglrggrvmELkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGSTG 298
Cdd:cd05935 81 S---------EL------------------------------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 299 MPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF-----ESTPvypnagrywE 373
Cdd:cd05935 98 LPKGCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL---------E 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 374 TVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETggicIA 453
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTET----MS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 454 P-------RPSEEGAEIlpgmamrPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAYPG 526
Cdd:cd05935 239 QthtnpplRPKLQCLGI-------P*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIKGR 309
|
410 420 430
....*....|....*....|....*....|
gi 1622839332 527 YYF-TGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05935 310 RFFrTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
116-552 |
9.31e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 77.27 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 116 QHVQKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIympvspLA------VAAMLACARIGA 189
Cdd:PRK07788 57 HAARRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 190 VHTVIFAGFSAASLAGRINDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPTVqHVLVAHrTDNKVHMGDLDIPLEQE 269
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAAREGVKALVYDD---------EFTDLLSALPPDLGRL-RAWGGN-PDDDEPSGSTDETLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 270 MAKED--PVCAPESMGSedvlFMLYTSGSTGMPKGIVHTQAGYLLYAAlthkLVFDHRP---GDIFGCVADIGWITGHSY 344
Cdd:PRK07788 194 IAGSStaPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLA----GLLSRVPfraGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 345 VVYGpLCNGATSVL---FestpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINC 421
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 422 EAWEWLHRVVGDSRCTLvdtWWQTETGGICIApRPSEegAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQA 501
Cdd:PRK07788 338 ELATRALEAFGPVLYNL---YGSTEVAFATIA-TPED--LAEAPGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNG 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 502 WPgMARTIYGDHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK07788 411 FP-FEGYTDGRDKQIID-------GLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
122-358 |
1.48e-14 |
|
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: 76.16 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd12114 1 PDATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvQHVLVAHRTDNkvhmGDLDIPLEQEMAKEDPVCAPES 281
Cdd:cd12114 75 RREAILADAGARLVLT---------------------------DGPDAQLDVAV----FDVLILDLDALAAPAPPPPVDV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 mGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhrPGDIFGCVA----DIGwitghSYVVYGPLCNGATS 356
Cdd:cd12114 124 -APDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATL 195
|
..
gi 1622839332 357 VL 358
Cdd:cd12114 196 VL 197
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
114-552 |
3.03e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 75.45 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNqglrggrvMELKKIVDeaVKHCPTVQHVLVAHRTD------------------- 254
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLD--------LVFPRVTN--VQSATKIEHVIVTRIADflpfpknllypfvqkkqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 255 -----NKVHMGDLDIPLEQEM-AKEDPVCAPESmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGD 328
Cdd:PRK06710 174 lvvkvSESETIHLWNSVEKEVnTGVEVPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 329 --IFGcVADIGWITGHSYVVYGPLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDR 406
Cdd:PRK06710 250 evVLG-VLPFFHVYGMTAVMNLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 407 SSLRTLGSVGEPINCEAWEWLHRVVG-----------DSRCTLVDTWWQTETGGICIAPRPSEEG--AEILPGMAMRPff 473
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETVTGgklvegyglteSSPVTHSNFLWEKRVPGSIGVPWPDTEAmiMSLETGEALPP-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 474 givpvlmDEKGSVVegsnVSGALCISQAW--PGMARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDV 551
Cdd:PRK06710 401 -------GEIGEIV----VKGPQIMKGYWnkPEETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
.
gi 1622839332 552 I 552
Cdd:PRK06710 457 I 457
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
120-329 |
4.62e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 74.91 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 120 KSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 199
Cdd:PRK07514 14 ADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 200 AASLAGRINDAKCKVVItfnqgLRGGRVMELKKIvdeAVKHcpTVQHV--LVAHRTDnkvhmgdldiPLEQEMAKEDPVC 277
Cdd:PRK07514 89 LAELDYFIGDAEPALVV-----CDPANFAWLSKI---AAAA--GAPHVetLDADGTG----------SLLEAAAAAPDDF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 278 APESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDI 329
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSH-GNLLSNALTLVDYWRFTPDDV 199
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
112-550 |
1.18e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 73.54 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 112 NCLDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVH 191
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 192 TVIFAGFSAASLAGRINDAKCKVVI---TFNQGLRGGRVMELK---KIVDEAVKHCPTVQHVLVAHRtDNKVHMGDLDip 265
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchaDFPEHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 266 leqemaKEDPvcapesmgsedvLFMLYTSGSTGMPKGIV--HTQAGYLlyaaLTHKLVfDHRPGdifgcvadigwITGH- 342
Cdd:PRK07470 162 ------HDDP------------CWFFFTSGTTGRPKAAVltHGQMAFV----ITNHLA-DLMPG-----------TTEQd 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 343 -SYVVyGPL---------CN---GATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSL 409
Cdd:PRK07470 208 aSLVV-APLshgagihqlCQvarGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 410 RTLGSVGEPINCEAWEWLHRVVGDsrcTLVDTWWQTE-TGGICIAPRP---SEEGAEILPGMAMRPFFGIVPVLMDEKGS 485
Cdd:PRK07470 283 RYVIYAGAPMYRADQKRALAKLGK---VLVQYFGLGEvTGNITVLPPAlhdAEDGPDARIGTCGFERTGMEVQIQDDEGR 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 486 VVeGSNVSGALCISqawpGMArtIYGDHQRFVDAYFKAYPGYYF-TGDGAHRTEGGYYQITGRMDD 550
Cdd:PRK07470 360 EL-PPGETGEICVI----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASD 418
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
132-547 |
2.21e-13 |
|
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: 72.75 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 132 DEPGTEVriTYRELLETTCRLANTLKRhGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIfaGFSAASLAGR--IND 209
Cdd:cd05909 2 DTLGTSL--TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVML--NYTAGLRELRacIKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 210 AKCKVVITFNQGLRGGRVMELKKIVDEAvkhcptvqHVLVAHRTDNKVHMGD-------LDIPLEQEMAKEDPVCAPesm 282
Cdd:cd05909 77 AGIKTVLTSKQFIEKLKLHHLFDVEYDA--------RIVYLEDLRAKISKADkckaflaGKFPPKWLLRIFGVAPVQ--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 283 gSEDVLFMLYTSGSTGMPKGIVHTQAGYL--LYAALTHklvFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfe 360
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 361 stpvYPNAGRYW---ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVGEPINC---EAWEWLHRVVgds 434
Cdd:cd05909 220 ----HPNPLDYKkipELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGIR--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 435 rctLVDTWWQTETG---GICIAPRPSEEGA--EILPGMAMR--PFFGIVPVLMDEKGSV-VEGSNV-SGALcisqAWPGM 505
Cdd:cd05909 289 ---ILEGYGTTECSpviSVNTPQSPNKEGTvgRPLPGMEVKivSVETHEEVPIGEGGLLlVRGPNVmLGYL----NEPEL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622839332 506 ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGR 547
Cdd:cd05909 362 TSFAFGD-------------GWYDTGDIGKIDGEGFLTITGR 390
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
136-552 |
4.48e-13 |
|
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: 71.79 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 136 TEVRITYRELLETTCRLANTLKRHG--------VCRGDCVAIYMPvsplavaaMLACARIGAVHTVIFAGFSAASLAGRI 207
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGlkqndriaVCSENSLQFFLP--------VIAGLFIGVGVAPTNDIYNERELDHSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 208 NDAKCKVVITFNQGLRggRVMELKKIVdeavkhcPTVQHVLVahrTDNKVHMGDLDiPLEQEMAKEDPVC-------APE 280
Cdd:cd17642 113 NISKPTIVFCSKKGLQ--KVLNVQKKL-------KIIKTIII---LDSKEDYKGYQ-CLYTFITQNLPPGfneydfkPPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 281 SMGSEDVLFMLYTSGSTGMPKGIvhtqagyllyaALTHKLV---FDHRPGDIFGC-----VADIGWITGHS----YVVYG 348
Cdd:cd17642 180 FDRDEQVALIMNSSGSTGLPKGV-----------QLTHKNIvarFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCNGATSVL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINCEAWE 425
Cdd:cd17642 249 YLICGFRVVLmykFEEE-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 426 WLHRVVGDSrcTLVDTWWQTE-TGGICIAP----RPSEEGaeilpgmAMRPFFGIVPVLMDEKGSVveGSNVSGALCISQ 500
Cdd:cd17642 320 AVAKRFKLP--GIRQGYGLTEtTSAILITPegddKPGAVG-------KVVPFFYAKVVDLDTGKTL--GPNERGELCVKG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 501 awPGMARTIYGDHQRFVDAYFKayPGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:cd17642 389 --PMIMKGYVNNPEATKALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKSLI 436
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-308 |
5.19e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 71.73 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 111 VNCLDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV 190
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 191 HTVIFAGFSAASLAGRINDAKCKVVITfnQGLRGGRVMELKKIVdeavkhcPTVQHVLVA-HRTDNKVhmgdldIPLEQE 269
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALAPVATAVRDIV-------PLLSTVVVAgGSSDDSV------LGYEDL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622839332 270 MAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQA 308
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHA 197
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
122-311 |
7.22e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.13 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPtVQHVLVAHRTDNK----VHMGDLDipLEQEMAKEDPVC 277
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDT---------EFAEVAREALALLP-GPKPLVIDVDDPEypggRFIGALD--YEAFLASGDPDF 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622839332 278 APESMGSE-DVLFMLYTSGSTGMPKGIV-HTQAGYL 311
Cdd:PRK08162 174 AWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL 209
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
116-430 |
7.70e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 70.65 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 116 QHVQKSPESVAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakED 274
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLT-------------------------------------------------------SS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 PvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQAGYLLyAALTHKLVFDHRPGD--------IFG-CVADIgwitghsyv 345
Cdd:cd05918 105 P---------SDAAYVIFTSGSTGKPKGVVIEHRALST-SALAHGRALGLTSESrvlqfasyTFDvSILEI--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 vYGPLCNGAT------SVLFESTPvypnagrywETVERLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVG 416
Cdd:cd05918 166 -FTTLAAGGClcipseEDRLNDLA---------GFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGG 224
|
330
....*....|....*
gi 1622839332 417 EPINCEAWE-WLHRV 430
Cdd:cd05918 225 EALTQSDVDtWADRV 239
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
131-552 |
3.04e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.01 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 131 RDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV-HTVIFAGFsAASLAGRIND 209
Cdd:PRK06018 31 RSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 210 AKCKVVI---TFnqglrggrVMELKKIVDeavkHCPTVQHVLVAhrTDnKVHMGDLDIP----LEQEMAKEDPVCAPESM 282
Cdd:PRK06018 110 AEDRVVItdlTF--------VPILEKIAD----KLPSVERYVVL--TD-AAHMPQTTLKnavaYEEWIAEADGDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 283 GSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlvfdhrpGDIFGCVA-DI-----------GW-------ITGHS 343
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANN-------GDALGTSAaDTmlpvvplfhanSWgiafsapSMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 344 YVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPincea 423
Cdd:PRK06018 248 LVMPGAKLDGAS--------VY-------ELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 424 wEWLHRVVGDSRCTLVDTWWQTET---GGICIAPRPSEEgaeiLPG--------MAMRPFFGIVPVLMDEKG-SVVEGSN 491
Cdd:PRK06018 308 -RSMIKAFEDMGVEVRHAWGMTEMsplGTLAALKPPFSK----LPGdarldvlqKQGYPPFGVEMKITDDAGkELPWDGK 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 492 VSGALCISQawPGMARTIYGDHQRFVDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK06018 383 TFGRLKVRG--PAVAAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVI 436
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
114-553 |
3.68e-12 |
|
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: 68.51 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtV 193
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAgfsaaslagrindakckvvitfnqgLRGGRVMELKKIVD--EAVkhcptvqhVLVAHRTdnkvHMGDLDIPLEQEMA 271
Cdd:cd05920 93 VLA-------------------------LPSHRRSELSAFCAhaEAV--------AYIVPDR----HAGFDHRALARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 272 KEDPvcapesmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHRpgDIFGCVADIgwitGHSYV----- 345
Cdd:cd05920 136 ESIP----------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLDQD--TVYLAVLPA----AHNFPlacpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE 425
Cdd:cd05920 200 VLGTLLAGGRVVLAPD----PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 426 WLHRVVGdsrCTLVDTWWQTEtGGICIApRPSEEGAEIL--PGMAMRPFFGIVPVlmDEKGSVVeGSNVSGALcisqawp 503
Cdd:cd05920 274 RVPPVLG---CTLQQVFGMAE-GLLNYT-RLDDPDEVIIhtQGRPMSPDDEIRVV--DEEGNPV-PPGEEGEL------- 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 504 gMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd05920 339 -LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRIKDQIN 391
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
118-554 |
4.79e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.42 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK12467 522 ARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITFNQGLRGGRVmelkkivdeavkhCPTVQHVLVahrtdnkvhmgDLDIPLEQEMAKEDPvc 277
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------------PAGLRSLCL-----------DEPADLLCGYSGHNP-- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 aPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIGWITGHsYVVYGPLCNGATSV 357
Cdd:PRK12467 650 -EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALASGATLH 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 358 LFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLHRVVGDS-RC 436
Cdd:PRK12467 727 LLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEAL---QVDLLARVRALGpGA 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 437 TLVDTWWQTETGGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARtiyGDHQR- 515
Cdd:PRK12467 799 RLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGA--GLAR---GYHRRp 872
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839332 516 ------FVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK12467 873 altaerFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKI 918
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
112-306 |
5.66e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 68.07 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 112 NCLDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVH 191
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFEEKK------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 192 TVIFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivDEAVKHcptvqhvlvAHRTDNKVHMGDLdipleQEMA 271
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLIT-----------------DDDFEA---------KLIPGISVKFAEL-----MNGP 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622839332 272 KEDPVcaPESMGSED-VLFMLYTSGSTGMPKGIVHT 306
Cdd:PRK03640 129 KEEAE--IQEEFDLDeVATIMYTSGTTGKPKGVIQT 162
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-319 |
5.66e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 68.30 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITFNqGLRGGRVME-LKKIVDEaVKHC----------PTVQHVLvahRTDNKVHMGDL 262
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVAmLYELAPE-LATCepgqlqsarlPELRRVI---FLGDEKHPGML 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 263 DIPLEQEMAKEDPVCAPESMGSE----DVLFMLYTSGSTGMPKGivhtqagyllyAALTHK 319
Cdd:PRK08315 173 NFDELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKG-----------ATLTHR 222
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
139-560 |
6.83e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 67.80 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYM----PVSPLAVAAMlacaRIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMrndfAFFEAAYAAM----RLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 215 VITFNQGLRGgrvmeLKKIVDEAVK--HCPTVQHVLVAHRTDN---KVHMGDLDipLEQEMAKEDPVCAPESMGSEDvlf 289
Cdd:PRK12406 87 LIAHADLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISPallTPPAGAID--WEGWLAQQEPYDGPPVPQPQS--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 290 MLYTSGSTGMPKGIVHtqagyllyAALT--HKLVFDHRPGDIFgcvadiGWITGHSYVVYGPlcngatsvLFESTP-VYP 366
Cdd:PRK12406 157 MIYTSGTTGHPKGVRR--------AAPTpeQAAAAEQMRALIY------GLKPGIRALLTGP--------LYHSAPnAYG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 367 -NAGRYWET---------------VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAwewlhrv 430
Cdd:PRK12406 215 lRAGRLGGVlvlqprfdpeellqlIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAP--CPA------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 431 vgDSRCTLVDtWW---------QTETGGICIAprpSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISqa 501
Cdd:PRK12406 286 --DVKRAMIE-WWgpviyeyygSTESGAVTFA---TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI-- 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839332 502 wPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVInISNTLQI 560
Cdd:PRK12406 358 -AGNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNI 412
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
111-318 |
1.04e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 67.33 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 111 VNCLDQHVQKSPESVALiwerDEPGTEvrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV 190
Cdd:PRK05605 35 VDLYDNAVARFGDRPAL----DFFGAT--TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 191 ---HTVIfagFSAASLAGRINDAKCKVVITFN------QGLRGGrvMELKKIVD-EAVKHCPTVQHVLV------AHRTD 254
Cdd:PRK05605 109 vveHNPL---YTAHELEHPFEDHGARVAIVWDkvaptvERLRRT--TPLETIVSvNMIAAMPLLQRLALrlpipaLRKAR 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839332 255 NKVHMGDLD-IPLEQ----EMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTH 318
Cdd:PRK05605 184 AALTGPAPGtVPWETlvdaAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKG-----------AQLTH 241
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
118-554 |
1.23e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK12316 4561 ARMTPDAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITFNQGLRGGRVmelkkivdeavkhcPTVQHVLVAHRTDNKVHMGDLDiPLEQEMAkedpvc 277
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRLPI--------------PDGLASLALDRDEDWEGFPAHD-PAVRLHP------ 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 apesmgsEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHK--LVFDHRPGDIFGCVADIGWITGHSYV-------VYG 348
Cdd:PRK12316 4694 -------DNLAYVIYTSGSTGRPKG-----------VAVSHGslVNHLHATGERYELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 349 PLCNGAtSVLFESTPVYPNAGRYWETVE-RLKINQFygAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPIN----CEA 423
Cdd:PRK12316 4756 PLINGA-SVVIRDDSLWDPERLYAEIHEhRVTVLVF--PPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAqasyDLA 4829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 424 WE-----WLHRVVGDSRCTLVDTWWQTETGGICiaprpseeGAEILPgmAMRPFFGIVPVLMDEKGSV----VEGSNVSG 494
Cdd:PRK12316 4830 WRalkpvYLFNGYGPTETTVTVLLWKARDGDAC--------GAAYMP--IGTPLGNRSGYVLDGQLNPlpvgVAGELYLG 4899
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 495 ALCISQAW---PGMARtiygdhQRFVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK12316 4900 GEGVARGYlerPALTA------ERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKI 4957
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-554 |
1.24e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK12316 3064 EEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptVQHVLVAHRTDNKVHMGDldiPLEQEMAKED 274
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLS--------------------------QSHLRLPLAQGVQVLDLD---RGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 PvcaPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIGWiTGHSYVVYGPLCNGA 354
Cdd:PRK12316 3189 P---AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 355 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGepincEAWEWLHRVVGDS 434
Cdd:PRK12316 3264 RVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA----HRCTSLKRIVCGG-----EALPADLQQQVFA 3333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 435 RCTLVDTWWQTETGGICIAPRPSEEGAEILPgmAMRPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMARtiyGDHQ 514
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAVP--IGRPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR---GYHN 3405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1622839332 515 -------RFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK12316 3406 rpgltaeRFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKI 3452
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
118-554 |
1.25e-11 |
|
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: 66.97 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd17655 7 AEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITfnqglrggrvmelkkivDEAVKHcptvqhvlvahrtdNKVHMGDLDIpLEQEMAKEDPV- 276
Cdd:cd17655 81 YPEERIQYILEDSGADILLT-----------------QSHLQP--------------PIAFIGLIDL-LDEDTIYHEESe 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 277 -CAPESmGSEDVLFMLYTSGSTGMPKGIVHTQAG-------------------YLLYAALThklvFDHRPGDIFGCVadi 336
Cdd:cd17655 129 nLEPVS-KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankviyqgehlrVALFASIS----FDASVTEIFASL--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 337 gwITGHSYVVYG--PLCNGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLlkygdAWVKKYDRSSLRTLGS 414
Cdd:cd17655 201 --LSGNTLYIVRkeTVLDGQALT---------------QYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 415 VGEPINCE-AWEWLHRVvgDSRCTLVDTWWQTETggiCIaprpseeGAEILPGMAMRPFFGIVPV----------LMDEK 483
Cdd:cd17655 259 GGEALSTElAKKIIELF--GTNPTITNAYGPTET---TV-------DASIYQYEPETDQQVSVPIgkplgntriyILDQY 326
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 484 GSVV-EGsnVSGALCISQAwpGMARTiYGDH-----QRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17655 327 GRPQpVG--VAGELYIGGE--GVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKI 398
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
114-549 |
1.95e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDakCKVVITFNQGLRGGRVmelkkivdeavkhcPTVQHVLVahrtdnkvhmgdldIPLEQEMAKE 273
Cdd:PRK05691 1211 LDPDYPAERLAYMLAD--SGVELLLTQSHLLERL--------------PQAEGVSA--------------IALDSLHLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPVCAPE-SMGSEDVLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVFDHRP-----GDIFGCVADIGWITGhSYVVY 347
Cdd:PRK05691 1261 WPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNT------HAALAERLQWMQATyalddSDVLMQKAPISFDVS-VWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 348 GPLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE-- 425
Cdd:PRK05691 1334 WPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA----AACTSLRRLFSGGEALPAELRNrv 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 426 -------WLHRVVGDSRCTLVDTWWQtetggiCIAprpsEEGAEILPGmamRPFFGIVPVLMDEKGSVVEGSnVSGALCI 498
Cdd:PRK05691 1409 lqrlpqvQLHNRYGPTETAINVTHWQ------CQA----EDGERSPIG---RPLGNVLCRVLDAELNLLPPG-VAGELCI 1474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 499 SQAwpGMARTIYG----DHQRFV-DAYFKAYPGYYFTGDGAHRTEGGYYQITGRMD 549
Cdd:PRK05691 1475 GGA--GLARGYLGrpalTAERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLD 1528
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
122-552 |
2.08e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.55 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK06188 26 PDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVItFNQGLRGGRVMELkkivdeaVKHCPTVQHVLVahrtdnkvhMGDLDI--PLEQEMAKEDPVCAP 279
Cdd:PRK06188 100 DHAYVLEDAGISTLI-VDPAPFVERALAL-------LARVPSLKHVLT---------LGPVPDgvDLLAAAAKFGPAPLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 280 ESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALthklvfdhrpgdifgCVADIGWITGHSYVVYGPLCNGAtsvlf 359
Cdd:PRK06188 163 AAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI---------------QLAEWEWPADPRFLMCTPLSHAG----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 360 eSTPVYP--------------NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN----C 421
Cdd:PRK06188 223 -GAFFLPtllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSpvrlA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 422 EAwewlHRVVGDsrcTLVDTWWQTETgGICIAPRPSEEGAEILPGM---AMRPFFGIVPVLMDEKGSVVEGSNVsGALCI 498
Cdd:PRK06188 300 EA----IERFGP---IFAQYYGQTEA-PMVITYLRKRDHDPDDPKRltsCGRPTPGLRVALLDEDGREVAQGEV-GEICV 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 499 SQawPGMArtiygdhqrfvDAYFKAyP---------GYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK06188 371 RG--PLVM-----------DGYWNR-PeetaeafrdGWLHTGDVAREDEDGFYYIVDRKKDMI 419
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-567 |
2.14e-11 |
|
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: 66.31 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 149 TCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF----AGFSAASLAGRINDAKCKVVITfnqglrg 224
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVLA------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 225 grVMELKKIVDEAVKHCPTVQHVLvahRTDNKVHMGDlDIPlEQEMAKEDPVCapesmgsedvlfMLYTSGSTGMPKGIV 304
Cdd:cd05922 76 --DAGAADRLRDALPASPDPGTVL---DADGIRAARA-SAP-AHEVSHEDLAL------------LLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 305 --HTQagyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfESTPVYPNAgrYWETVERLKINQ 382
Cdd:cd05922 137 lsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 383 FYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTE-TGGICIAPrPSEEGA 461
Cdd:cd05922 210 LAGVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEaTRRMTYLP-PERILE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 462 EilPGMAMRPFFGIVPVLMDEKGS----------VVEGSNVSGALCISQAWPGMARtiygdhqRFVDAyfkaypgyYFTG 531
Cdd:cd05922 284 K--PGSIGLAIPGGEFEILDDDGTptppgepgeiVHRGPNVMKGYWNDPPYRRKEG-------RGGGV--------LHTG 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839332 532 DGAHRTEGGYYQITGRMDDVI----------NISNTLQIGGLFREA 567
Cdd:cd05922 347 DLARRDEDGFLFIVGRRDRMIklfgnrisptEIEAAARSIGLIIEA 392
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
121-554 |
2.16e-11 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 66.34 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 121 SPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 200
Cdd:cd17656 1 TPDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 201 ASLAGRINDAKCKVVITFNqglrggrvmelkkivdeavkHCPTVQhvlvahrTDNKVHMgDLDIPLEqemAKEDPVCAPE 280
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQR--------------------HLKSKL-------SFNKSTI-LLEDPSI---SQEDTSNIDY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 281 SMGSEDVLFMLYTSGSTGMPKGIV--HTQAGYLLyaalthKLVFDHRPGDIFGCVADigwITGHSYVV-----YGPLCNG 353
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL------HFEREKTNINFSDKVLQ---FATCSFDVcyqeiFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 AT------------SVLFE-------STPVYPNAgrYWETV--ERLKINQFygaPTAVRLLLKYGDAWVkkydrsslrtl 412
Cdd:cd17656 195 GTlyiireetkrdvEQLFDlvkrhniEVVFLPVA--FLKFIfsEREFINRF---PTCVKHIITAGEQLV----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 413 gsvgepINCEAWEWLHRvvgdSRCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAmRPFFGIVPVLMDEKGSVVEgSNV 492
Cdd:cd17656 259 ------ITNEFKEMLHE----HNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIG-KPISNTWIYILDQEQQLQP-QGI 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 493 SGALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17656 327 VGELYISGA--SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKI 390
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-549 |
2.40e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITfnqglrGGRVMElkkivdeavkHCPTVQHVLVAhrtdnkvhmgDLDIPLEQEMAKE 273
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT------QAHLLE----------QLPAPAGDTAL----------TLDRLDLNGYSEN 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPvcAPESMGsEDVLFMLYTSGSTGMPKGI--------VHTQAGYLLYAALTHKLVFDHRPGDIFGCVADigwitghsyv 345
Cdd:PRK12467 3229 NP--STRVMG-ENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSFDGAQER---------- 3295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 VYGPLCNGATSVLfestpvypNAGRYW---ETV-----ERLKINQFygAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGE 417
Cdd:PRK12467 3296 FLWTLICGGCLVV--------RDNDLWdpeELWqaihaHRISIACF--PPAYLQQFAEDAGG----ADCASLDIYVFGGE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 418 PINCEAWEWLHRVV---------GDSRCTLVDTWWQTETGGICIAP-----RP-SEEGAEILPGmAMRPffgiVPVlmde 482
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDAVCEAPyapigRPvAGRSIYVLDG-QLNP----VPV---- 3432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 483 kgsvvegsNVSGALCIsqAWPGMARtiyGDHQ-------RFVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMD 549
Cdd:PRK12467 3433 --------GVAGELYI--GGVGLAR---GYHQrpsltaeRFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRID 3494
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
116-552 |
2.52e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.19 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 116 QHVQKSPESVALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 196 AGFSAASLAgRINDAKCKVVITFNqglRGGRVmelkkivdeAVKHCPTVQHVLVAHRTDNKVHMGDLDIPLEQEMAKEDP 275
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPAAALVA---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 276 vcapeSMGSEDVLFMLYTSGSTGMPKGIvhtqagyLLyaalthklvfdhrPGDIFGCVADI---------GWITGHSyvV 346
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAV-------LL-------------ANRTFFAVPDIlqkeglnwvTWVVGET--T 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 347 YGPLcnGATSVlfestpvypnAGRYW----------------------ETVERLKINQFYGAPTAVRLL---LKYGDAwv 401
Cdd:PRK05857 218 YSPL--PATHI----------GGLWWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLvseLKSANA-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 402 kkyDRSSLRTLGSVGEPInceawewlhrVVGDSR---CTLVDT---WWQTETG--GICIaPRPSEEGAEILPGMAMRPFF 473
Cdd:PRK05857 284 ---TVPSLRLVGYGGSRA----------IAADVRfieATGVRTaqvYGLSETGctALCL-PTDDGSIVKIEAGAVGRPYP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 474 GIVPVLMDEKGSVVEGSNVSGALCISQAW---PGMARTIYGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDD 550
Cdd:PRK05857 350 GVDVYLAATDGIGPTAPGAGPSASFGTLWiksPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSE 426
|
..
gi 1622839332 551 VI 552
Cdd:PRK05857 427 MI 428
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
124-360 |
3.75e-11 |
|
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: 65.94 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 124 SVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAAS 202
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 203 LAGRINDAKCKVVITfnqglrggrVMELKKIVDEAVKHCPTVQHVLV-AHRTDNKVHMGDLDIPLEQEMAKEDPV----- 276
Cdd:cd17632 132 LAPILAETEPRLLAV---------SAEHLDLAVEAVLEGGTPPRLVVfDHRPEVDAHRAALESARERLAAVGIPVttltl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 277 -------------CAPESmgSEDVLFML-YTSGSTGMPKGIVHT--------------QAGYLLYAALTHKLVFDHRPGD 328
Cdd:cd17632 203 iavrgrdlppaplFRPEP--DDDPLALLiYTSGSTGTPKGAMYTerlvatfwlkvssiQDIRPPASITLNFMPMSHIAGR 280
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622839332 329 IfgcvadigwitghsyVVYGPLCNGAT---------SVLFE 360
Cdd:cd17632 281 I---------------SLYGTLARGGTayfaaasdmSTLFD 306
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
132-554 |
1.15e-10 |
|
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: 64.23 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 132 DEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAK 211
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 212 cKVVITFNQGL---RGGRVMELKKIVDEAVkhcptvqhvlvahrtdnkvHMGDLDIPLEQEMAKEDPVCAPESmGSEDVL 288
Cdd:cd05906 112 -HIWQLLGSPVvltDAELVAEFAGLETLSG-------------------LPGIRVLSIEELLDTAADHDLPQS-RPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 289 FMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFgcvadIGW-----ITGHSYVVYGPLCNGATSVLFESTP 363
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 364 VYPNAGRYWETVERLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLV 439
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLL--EPYGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 440 DT-----WWQTETGGICI------APRPSEE------GAEIlPGMAMRpffgivpvLMDEKGSVVEGSNVsGALCISqaw 502
Cdd:cd05906 320 PDairpaFGMTETCSGVIysrsfpTYDHSQAlefvslGRPI-PGVSMR--------IVDDEGQLLPEGEV-GRLQVR--- 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839332 503 pGMARTiygdhqrfvdayfkayPGYY---------FTGDGAHRT------EGGYYQITGRMDDVINI 554
Cdd:cd05906 387 -GPVVT----------------KGYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIV 436
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
137-406 |
1.15e-10 |
|
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: 63.86 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 tfnqglrggrvmelkkiVDEAvkhcptvqhvlvaHRTDNKVHMGDLDIPLEQEMAKEDPVCapesmgsedvlfMLYTSGS 296
Cdd:cd12118 107 -----------------VDRE-------------FEYEDLLAEGDPDFEWIPPADEWDPIA------------LNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 297 TGMPKGIVHTQAG-YL--LYAALTHKLvfDHRPG-----DIFGCVadiGWItghsyVVYGPLCNGATSVLFESTpvypNA 368
Cdd:cd12118 145 TGRPKGVVYHHRGaYLnaLANILEWEM--KQHPVylwtlPMFHCN---GWC-----FPWTVAAVGGTNVCLRKV----DA 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622839332 369 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDR 406
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH 248
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
115-557 |
1.22e-10 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 63.93 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK08008 14 DDLADVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKivdeavKHCPtvQHVLVAhRTDNKVHMGDLDipLEQEMAKED 274
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQED------ATPL--RHICLT-RVALPADDGVSS--FTQLKAQQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 P-VCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQ-----AGYllYAALTHKLVFDHR-----PG---DiFGCVADIGWIT 340
Cdd:PRK08008 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDDDVyltvmPAfhiD-CQCTAAMAAFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 341 GhsyvvygplcnGATSVLFEStpvYpNAGRYWETVERLKINQFYGAPTAVR-LLLKYGDAWvkkyDRS-SLRTLG----- 413
Cdd:PRK08008 239 A-----------GATFVLLEK---Y-SARAFWGQVCKYRATITECIPMMIRtLMVQPPSAN----DRQhCLREVMfylnl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 414 SVGEPincEAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRPSEEgaEILPGMAmRPFFGIVPVLMDEKGSVVEgSNVS 493
Cdd:PRK08008 300 SDQEK---DAFEERFGV------RLLTSYGMTETIVGIIGDRPGDK--RRWPSIG-RPGFCYEAEIRDDHNRPLP-AGEI 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 494 GALCIsQAWPGmaRTIYGDHQRFVDAYFKAYP--GYYFTGDGAHRTEGGYYQITGRMDDVI-----NISNT 557
Cdd:PRK08008 367 GEICI-KGVPG--KTIFKEYYLDPKATAKVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIkrggeNVSCV 434
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
285-552 |
1.27e-10 |
|
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: 63.07 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 285 EDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH----------RPGDI----------FGCVADIGWITGHsy 344
Cdd:cd05917 2 DDVINIQFTSGTTGSPKG-----------ATLTHHNIVNNgyfigerlglTEQDRlcipvplfhcFGSVLGVLACLTH-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 345 vvygplcnGATSVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAW 424
Cdd:cd05917 69 --------GATMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 425 EWLHRVVGDSRCTLVdtWWQTETGGICIAPR---PSEEGAE----ILPGMAMRpffgivpvLMDEKGSVVEGSNVSGALC 497
Cdd:cd05917 136 KRVIEVMNMKDVTIA--YGMTETSPVSTQTRtddSIEKRVNtvgrIMPHTEAK--------IVDPEGGIVPPVGVPGELC 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 498 ISQAwpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:cd05917 206 IRGY--SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMI 256
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
114-308 |
1.28e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 64.68 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkiVDEavkhcptvqhvlVAHRTDNkvhmGDLDIPLEQEMAKE 273
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLIT----------------TAD------------QLPRFAD----VPDLTSLCYNAPLA 585
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622839332 274 DPVCAPESMGS-EDVLFMLYTSGSTGMPKGIVHTQA 308
Cdd:PRK10252 586 PQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQT 621
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
139-369 |
2.23e-10 |
|
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: 63.14 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIfagfsaaslagrindakckvvitf 218
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 NQGLRGgrvmelkkivdEAVKHCPTV---QHVLVahrtdnkvhmgdldipleqemakedpvcapesmgseDVLFMLYTSG 295
Cdd:cd05940 59 NYNLRG-----------ESLAHCLNVssaKHLVV------------------------------------DAALYIYTSG 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 296 STGMPKGivhtqagyllyAALTHklvfdHRpgdifgcvadigWITGhSYVVYGPLCNGATSVLFESTPVYPNAG 369
Cdd:cd05940 92 TTGLPKA-----------AIISH-----RR------------AWRG-GAFFAGSGGALPSDVLYTCLPLYHSTA 136
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
139-335 |
3.62e-10 |
|
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: 62.69 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRH-GVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIT 217
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 218 fnqglrggrVMELKKIVDEAvkhCPTVQ----HVLVAHRTDNKVHMGDLDIPLEQemAKEDPVcaPESMGSEdVLFM--- 290
Cdd:cd05938 85 ---------APELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVISLLDKVDA--ASDEPV--PASLRAH-VTIKspa 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622839332 291 --LYTSGSTGMPKGIVHTQAGYLLYAALTHklvfdhrpgdIFGCVAD 335
Cdd:cd05938 148 lyIYTSGTTGLPKAARISHLRVLQCSGFLS----------LCGVTAD 184
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
114-553 |
7.23e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 61.54 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQksPESVALIW-ERdepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMP-VSPLAVaAMLACARIGAVh 191
Cdd:PRK10946 31 LTRHAA--SDAIAVICgER-------QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYI-TFFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 192 tVIFAGFSAASL-----AGRINDAkckVVItfnqGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRtdnkvhmgDLDIPL 266
Cdd:PRK10946 100 -PVNALFSHQRSelnayASQIEPA---LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLND--------DGEHSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 267 EQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYlLYAAlthklvfdHRPGDIFGCVADIGWI----TGH 342
Cdd:PRK10946 164 DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDY-YYSV--------RRSVEICGFTPQTRYLcalpAAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 343 SYVVYGPlcnGATSVLFESTPVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLgSVG-- 416
Cdd:PRK10946 235 NYPMSSP---GALGVFLAGGTVVlapdPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL-QVGga 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 417 -----------EPINCEawewLHRVVGDSRcTLV------DTWWQT-ETGGiciapRPSEEGAEIlpgmamrpffGIVpv 478
Cdd:PRK10946 311 rlsetlarripAELGCQ----LQQVFGMAE-GLVnytrldDSDERIfTTQG-----RPMSPDDEV----------WVA-- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 479 lmDEKGS-VVEGSnvSGALcisqawpgMAR---TIYG-----DHQRFVdayFKAyPGYYFTGDGAHRTEGGYYQITGRMD 549
Cdd:PRK10946 369 --DADGNpLPQGE--VGRL--------MTRgpyTFRGyykspQHNASA---FDA-NGFYCSGDLVSIDPDGYITVVGREK 432
|
....
gi 1622839332 550 DVIN 553
Cdd:PRK10946 433 DQIN 436
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
117-552 |
8.11e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 61.44 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 117 HVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFA 196
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 197 GFSAASLAGRINDAKCKVVitfnqglrggrvmelkkIVDEAVKHCPTVQH---VLVAHRTDNKVHMGDLDIPleqemake 273
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLL-----------------LVDEEFDAIVALETpkiVIDAAAQADSRRLAQGGLE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 dpvCAPESMGSEDVLF-MLYTSGSTGMPKGIVHTqagyllYAALTHKlVFDHrpgdifgcVADIGWITGHSYVVYGPLCN 352
Cdd:PRK06145 140 ---IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHS------YGNLHWK-SIDH--------VIALGLTASERLLVVGPLYH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 353 -GA-----TSVL-----------FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWvkKYDRSSLRTLGSV 415
Cdd:PRK06145 202 vGAfdlpgIAVLwvggtlrihreFDPEAVL-------AAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 416 GEPINCEAWEWLHRVVGDSRctLVDTWWQTETggiCIAPRPSEEGAEILP-GMAMRPFFGIVPVLMDEKGSVVEgSNVSG 494
Cdd:PRK06145 273 GEKTPESRIRDFTRVFTRAR--YIDAYGLTET---CSGDTLMEAGREIEKiGSTGRALAHVEIRIADGAGRWLP-PNMKG 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839332 495 ALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK06145 347 EICMRG--PKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMI 399
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
140-359 |
1.06e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 61.15 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglRGGRVMELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDIPLEQE----MAKEDPVCAPESMGS----------E 285
Cdd:PTZ00216 200 ---NGKNVPNLLRLMKSGGMPNTTI------------IYLDSLPASVDTEgcrlVAWTDVVAKGHSAGShhplnipennD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839332 286 DVLFMLYTSGSTGMPKGIVHTQaGYLLYAALThklvFDHRPGDIFGCVADigwitGHSYVVYGPLCN----GATSVLF 359
Cdd:PTZ00216 265 DLALIMYTSGTTGDPKGVMHTH-GSLTAGILA----LEDRLNDLIGPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
140-330 |
1.32e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.90 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFN 219
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 QglrggrvmELKKIVDEAvKHCPTVQHVLVAHRTDNKVHMGDLD--------IPLEQEMAKEDPVcAPESMGSEDVLFML 291
Cdd:PLN02387 187 K--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGssnwtvssFSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622839332 292 YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIF 330
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
140-388 |
1.39e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 60.82 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfN 219
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 QGLR----GGRVMELKKIVDEAVKHCPTvqhvlvahrtdnkvhmgDLDIpleqemakedpvcapesMGSEDVLFMLYTSG 295
Cdd:PRK06060 110 DALRdrfqPSRVAEAAELMSEAARVAPG-----------------GYEP-----------------MGGDALAYATYTSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfESTPVYPNAGRYWETv 375
Cdd:PRK06060 156 TTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
250
....*....|...
gi 1622839332 376 eRLKINQFYGAPT 388
Cdd:PRK06060 234 -RFGPSVLYGVPN 245
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-552 |
1.47e-09 |
|
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: 59.80 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 284 SEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGAtSVLFESTP 363
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 364 VYPNAGRY---WETVERLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLV 439
Cdd:cd05944 79 GYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVELRARFEDATG---LPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 440 DTWWQTETggICIAPRPSEEGAEILPGMAMR-PFFGIVPVLMDEKGSVVE--GSNVSGALCIsqAWPGMAR-TIYGDHQR 515
Cdd:cd05944 151 EGYGLTEA--TCLVAVNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRdcAPDEVGEICV--AGPGVFGgYLYTEGNK 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622839332 516 FVDayfkAYPGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:cd05944 227 NAF----VADGWLNTGDLGRLDADGYLFITGRAKDLI 259
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
118-554 |
5.05e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.59 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK12316 2013 AARAPEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 198 FSAASLAGRINDAKCKVVITfnqglrggrvmelKKIVDEAVKhCPTVQHVLvahrtdnkvhmgDLDIPLEQEmakEDPVC 277
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT-------------QRHLLERLP-LPAGVARL------------PLDRDAEWA---DYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 APE-SMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDifgCVADIGWIT--GHSYVVYGPLCNGA 354
Cdd:PRK12316 2138 APAvQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 355 tSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDS 434
Cdd:PRK12316 2214 -RVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 435 RctLVDTWWQTETggiCIAPRPSEEGAEILPGMAMRPffgIVPVLMDEKGSVVEGS------NVSGALCISQAwpGMART 508
Cdd:PRK12316 2289 Y--LFNGYGPTEA---VVTPLLWKCRPQDPCGAAYVP---IGRALGNRRAYILDADlnllapGMAGELYLGGE--GLARG 2358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 509 IYG----DHQRFVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK12316 2359 YLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
139-552 |
7.26e-09 |
|
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: 58.07 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTL-KRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIt 217
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 218 fnqglrggrvmelkkivDEAVkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsedvlfMLYTSGST 297
Cdd:cd05941 90 -----------------DPAL---------------------------------------------------ILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 298 GMPKGIVHTQAGylLYA---ALTHKLVFdhRPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlFESTPvYPNAGRYWET 374
Cdd:cd05941 102 GRPKGVVLTHAN--LAAnvrALVDAWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGAS---VEFLP-KFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 375 VERLKINQFYGAPTAVRLLLKYGDAWVKKYD---RSSLRTL-----GSVGEPINC-EAWEWL--HRvvgdsrctLVDTWW 443
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQYYEAHFTDPQfarAAAAERLrlmvsGSAALPVPTlEEWEAItgHT--------LLERYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 444 QTETGGICIAP-----RPSEEGAEiLPGMAMRpffgivpVLMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQRFVD 518
Cdd:cd05941 246 MTEIGMALSNPldgerRPGTVGMP-LPGVQAR-------IVDEETGEPLPRGEV-GEIQV--RGPSVFKEYWNKPEATKE 314
|
410 420 430
....*....|....*....|....*....|....*
gi 1622839332 519 AyFKAyPGYYFTGDGAHRTEGGYYQITGRM-DDVI 552
Cdd:cd05941 315 E-FTD-DGWFKTGDLGVVDEDGYYWILGRSsVDII 347
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
122-554 |
7.28e-09 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 58.03 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17652 1 PDAPAVVFG------DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 202 SLAGRINDAKCKVVITFnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapes 281
Cdd:cd17652 75 RIAYMLADARPALLLTT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 282 mgSEDVLFMLYTSGSTGMPKGIV--HTQAGYLLYAALTHklvFDHRPGDifgCVADIGWITGHSYV--VYGPLCNGATSV 357
Cdd:cd17652 92 --PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGS---RVLQFASPSFDASVweLLMALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 358 LFESTPVYPNAGrYWETVERLKINQFYGAPTAVrlllkygdAWVKKYDRSSLRTLGSVGEPINCE---AWEWLHRVV--- 431
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAAL--------AALPPDDLPDLRTLVVAGEACPAElvdRWAPGRRMInay 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 432 GDSRCTLVDTWwqtetggiciaprpseegAEILPGMAM----RPFFGI-VPVLMDEKGSVVEGsnVSGALCIsqAWPGMA 506
Cdd:cd17652 235 GPTETTVCATM------------------AGPLPGGGVppigRPVPGTrVYVLDARLRPVPPG--VPGELYI--AGAGLA 292
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 507 RTiYGDH-----QRFVDAYFKAyPG--YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17652 293 RG-YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKI 345
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-554 |
7.48e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.02 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK12467 1580 IEDQAAATPEAVALVF------GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 194 IFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDipLEQEMAKE 273
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT--------------------------QSHLQARLPLPDGLRSLVLD--QEDDWLEG 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 274 DPVCAPES-MGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH--RPGDIFGCVADIGWITGHSYV----- 345
Cdd:PRK12467 1706 YSDSNPAVnLAPQNLAYVIYTSGSTGRPKG-----------AGNRHGALVNRlcATQEAYQLSAADVVLQFTSFAfdvsv 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 346 --VYGPLCNGAtSVLFESTPVYPNAGRYWETVERLKI----------NQF------YGAPTAVRLLLKYGDAWVKKYDRS 407
Cdd:PRK12467 1775 weLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRP 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 408 SLRTLGSVGepinceawewLHRVVGDSRCTLVDTWWQtetggiciAPRPSEEGAEILPgmamrpffgIVPVLMDEKGSVV 487
Cdd:PRK12467 1854 WLERLPDTG----------LFNLYGPTETAVDVTHWT--------CRRKDLEGRDSVP---------IGQPIANLSTYIL 1906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 488 EGS------NVSGALCISQAwpGMARtiyGDH-------QRFVDAYFkAYPG--YYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK12467 1907 DASlnpvpiGVAGELYLGGV--GLAR---GYLnrpaltaERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQV 1980
|
..
gi 1622839332 553 NI 554
Cdd:PRK12467 1981 KI 1982
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
139-552 |
1.01e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 57.79 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIympvspLA------VAAMLACARIGAV-HTV---IFAgfsaASLAGRIN 208
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTInprLFP----EQIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 209 DAKCKVV---ITFnqglrggrvmelKKIVDEAVKHCPTVQHVLVAhrTDnKVHMGDLDIPL---EQEMAKEDPVCAPESM 282
Cdd:PRK07008 109 HAEDRYVlfdLTF------------LPLVDALAPQCPNVKGWVAM--TD-AAHLPAGSTPLlcyETLVGAQDGDYDWPRF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 283 GSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYA---ALThklvfdhrpgDIFGCVA-DI-----------GW-------IT 340
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHRSTVLHAygaALP----------DAMGLSArDAvlpvvpmfhvnAWglpysapLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 341 GHSYVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSL-RTL--GSVGE 417
Cdd:PRK07008 244 GAKLVLPGPDLDGKS--------LY-------ELIEAERVTFSAGVPTVWLGLLNHMREAGLRF--STLrRTVigGSACP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 418 PINCEAWEwlhrvvGDSRCTLVDTWWQTET---GGICI-----APRPSEEGAEILPGMAmRPFFGIVPVLMDEKGSvveg 489
Cdd:PRK07008 307 PAMIRTFE------DEYGVEVIHAWGMTEMsplGTLCKlkwkhSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGR---- 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839332 490 snvsgalciSQAWPGMArtiYGD-HQR---FVDAYFK--AYP---GYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK07008 376 ---------ELPWDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVI 435
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
137-556 |
2.19e-08 |
|
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: 56.68 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 TfnqglrggrvmelkkivdeavkhcptvqhvlvahrTDNkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGS 296
Cdd:cd05914 85 V-----------------------------------SDE-----------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 297 TGMPKGIVHTQAG----------YLLYAALTHKLVFdhRP-GDIFGCVADIgwitghsyvVYgPLCNGATSVLFESTP-- 363
Cdd:cd05914 101 TGNSKGVMLTYRNivsnvdgvkeVVLLGKGDKILSI--LPlHHIYPLTFTL---------LL-PLLNGAHVVFLDKIPsa 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 364 ---------VYPNAG--RYWETVERLK---INQFYGAPTAVRLLLKYGDAWVKKYDRSSL--------RTLGSVGEPINC 421
Cdd:cd05914 169 kiialafaqVTPTLGvpVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 422 EAWEWLHRVvgdsRCTLVDTWWQTETGGICIAPRPSEE----GAEILPGMAMRPFfgiVPVLMDEKGS-VVEGSNVsgal 496
Cdd:cd05914 249 DVEEFLRTI----GFPYTIGYGMTETAPIISYSPPNRIrlgsAGKVIDGVEVRID---SPDPATGEGEiIVRGPNV---- 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 497 cisqawpgMaRTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINISN 556
Cdd:cd05914 318 --------M-KGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIVLSS 366
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
178-424 |
3.28e-08 |
|
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: 56.23 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 178 VAAMLACA---RIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnqglrggrvmELKKIVDEAVKHCPTVQHVLVAhrTD 254
Cdd:cd05929 33 AAAAEGVWiadGVYIYLINSILTVFAAAAAWKCGACPAYKSSR-----------APRAEACAIIEIKAAALVCGLF--TG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 255 NKVHMGDLDIPLEQEMAKEDPVcAPESMGSEdvlfMLYTSGSTGMPKGIvhtqagyllyaalthKLVFDHRPGD---IFG 331
Cdd:cd05929 100 GGALDGLEDYEAAEGGSPETPI-EDEAAGWK----MLYSGGTTGRPKGI---------------KRGLPGGPPDndtLMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 332 CVADIGWITGHSYVVYGPL-------------CNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGD 398
Cdd:cd05929 160 AALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTLVLMEKF----DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPE 235
|
250 260
....*....|....*....|....*.
gi 1622839332 399 AWVKKYDRSSLRTLGSVGEPinCEAW 424
Cdd:cd05929 236 AVRNAYDLSSLKRVIHAAAP--CPPW 259
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
113-307 |
3.36e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.43 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 113 CLDQHVQKSPESVALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSP----LAVAAMLACARIG 188
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 189 AVHtvifagfSAASLAGRiNDAKCKVVItfnQGLRGGRVmelkkIVDEAVKHCPTVQHVLVAHR---TDNKVHMGDLDIP 265
Cdd:PRK08180 123 PVS-------PAYSLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAATP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622839332 266 LEQEMAKEDPVCAPESM---GSEDVLFMLYTSGSTGMPKGIVHTQ 307
Cdd:PRK08180 187 FAALLATPPTAAVDAAHaavGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
140-355 |
4.32e-08 |
|
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: 55.89 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFN 219
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 QglrgGRVMELKKIVDEAvkhcPTVQHVLVA-------HRTDNKVHMGDLdIPLEQEMAKEDPVCAPESMGS---EDVLF 289
Cdd:cd17641 92 E----EQVDKLLEIADRI----PSVRYVIYCdprgmrkYDDPRLISFEDV-VALGRALDRRDPGLYEREVAAgkgEDVAV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 290 MLYTSGSTGMPKGIVhTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGAT 355
Cdd:cd17641 163 LCTTSGTTGKPKLAM-LSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFI 227
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
115-554 |
5.62e-08 |
|
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: 55.52 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITfnQGlrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemaked 274
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT--QP----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 pvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPgDIFGCVADIGWITGhSYVVYGPLCNGA 354
Cdd:cd17644 106 ----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 355 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINCEAWEWLHRVVGDs 434
Cdd:cd17644 174 TLVL-RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 435 RCTLVDTWWQTE---TGGICIAPRPSEEGA-EILPGmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIY 510
Cdd:cd17644 251 FIQLINVYGPTEatiAATVCRLTQLTERNItSVPIG---RPIANTQVYILDENLQPVP-VGVPGELHIGGV--GLARGYL 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622839332 511 G----DHQRFVDAYFKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17644 325 NrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKI 374
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
139-307 |
1.01e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 54.81 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 nqglrggrvmelkkivDEAVKhcptvqhvlvAHRTDnkvhMGDLDIpLEQEMAKEDPVCAPeSMGSEDVLFMLYTSGSTG 298
Cdd:PRK09088 101 ----------------DDAVA----------AGRTD----VEDLAA-FIASADALEPADTP-SIPPERVSLILFTSGTSG 148
|
....*....
gi 1622839332 299 MPKGIVHTQ 307
Cdd:PRK09088 149 QPKGVMLSE 157
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
286-553 |
2.36e-07 |
|
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: 52.72 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVfdhrpgdifGCVADIGW--------ITGHSYVVYGPLCNGATSV 357
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---------GFGGGDSWllslplyhVGGLAILVRSLLAGAELVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 358 LFESTPVYPNAGRYWETVERLkinqfygAPTAVRLLLKYG--DAWVKkydrsSLRTLGSVGEPINCEawewLHRVVGDSR 435
Cdd:cd17630 72 LERNQALAEDLAPPGVTHVSL-------VPTQLQRLLDSGqgPAALK-----SLRAVLLGGAPIPPE----LLERAADRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 436 CTLVDTWWQTETGGICIAPRPSEEGA----EILPGMAMRpffgivpvlmdekgsVVEGsnvsGALCISQAWPGMARTIYG 511
Cdd:cd17630 136 IPLYTTYGMTETASQVATKRPDGFGRggvgVLLPGRELR---------------IVED----GEIWVGGASLAMGYLRGQ 196
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622839332 512 DHQRFVDayfkayPGYYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd17630 197 LVPEFNE------DGWFTTKDLGELHADGRLTVLGRADNMII 232
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-553 |
3.10e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.77 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 284 SEDVLFMLYTSGSTGMPKGIVHTQA---GYLLYAALTHKLVFDhrPGDIFGCVADIGwiTGHSYVVYGPLCNGA------ 354
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFT--PSEDAHKAAAAA--AGTVMFPAPPLMHGTgswtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 355 TSVLFESTPVYP----NAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPIN 420
Cdd:cd05924 78 GGLLGGQTVVLPddrfDPEEVWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 421 CEAWEWLHRVVGDSrcTLVDTWWQTETGGICIApRPSEEGAEilpgmaMRPFFGIVP--VLMDEKGSVVE-GSNVSGALc 497
Cdd:cd05924 148 PEVKQGLLELVPNI--TLVDAFGSSETGFTGSG-HSAGSGPE------TGPFTRANPdtVVLDDDGRVVPpGSGGVGWI- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839332 498 isqAWPG-MARTIYGDHQRfVDAYFKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVIN 553
Cdd:cd05924 218 ---ARRGhIPLGYYGDEAK-TAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCIN 272
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
119-552 |
5.65e-07 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 52.45 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 119 QKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 198
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 199 SAASLAGRINDAKCKVVItFNQglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDNKV-HMGDLDIPLEQEmakedpvc 277
Cdd:PRK13382 128 AGPALAEVVTREGVDTVI-YDE--------EFSATVDRALADCPQATRIVAWTDEDHDLtVEVLIAAHAGQR-------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 aPESMGSEDVLFMLyTSGSTGMPKGIVHTQAGyllyAALTHKLVFDHRPgdifgcvadigWITGHSYVVYGPL------C 351
Cdd:PRK13382 191 -PEPTGRKGRVILL-TSGTTGTPKGARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMfhawgfS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 352 NGATSVLFESTPVYPNAGRYWETVERLKINQFYG---APTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:PRK13382 254 QLVLAASLACTIVTRRRFDPEATLDLIDRHRATGlavVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 429 RVVGDsrcTLVDTWWQTETGGICIApRPSEEGAEilPGMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMART 508
Cdd:PRK13382 334 DQFGD---VIYNNYNATEAGMIATA-TPADLRAA--PDTAGRPAEGTEIRILDQDFREVP--------------TGEVGT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622839332 509 IYGDHQRFVDAYFKA-----YPGYYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK13382 394 IFVRNDTQFDGYTSGstkdfHDGFMASGDVGYLDENGRLFVVGRDDEMI 442
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
140-306 |
1.37e-06 |
|
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: 51.06 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtDNKvhmgdldipleqemakedpvcapesmgSEDVLFMLYTSGSTGM 299
Cdd:cd17639 84 ----------------------------------DGK---------------------------PDDLACIMYTSGSTGN 102
|
....*..
gi 1622839332 300 PKGIVHT 306
Cdd:cd17639 103 PKGVMLT 109
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
119-311 |
1.51e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 50.64 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 119 QKSPESVALIwERDEpgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtVIFagf 198
Cdd:PRK09029 14 QVRPQAIALR-LNDE-----VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR--VLP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 199 saaslagrINDAKCkvvitfnqglrggrVMELKKIVDEAvkhcpTVQHVLVAHRTDNkvhMGDLDIPLEQEMAKEDPVC- 277
Cdd:PRK09029 83 --------LNPQLP--------------QPLLEELLPSL-----TLDFALVLEGENT---FSALTSLHLQLVEGAHAVAw 132
|
170 180 190
....*....|....*....|....*....|....
gi 1622839332 278 APESMGSedvlfMLYTSGSTGMPKGIVHTQAGYL 311
Cdd:PRK09029 133 QPQRLAT-----MTLTSGSTGLPKAAVHTAQAHL 161
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
135-387 |
2.05e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 50.61 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAkcKV 214
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA--EV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 215 VITFNQglrGGRVMELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDIPLEQEMAKEDPVCAP----ESMGS------ 284
Cdd:PLN02861 151 SIAFVQ---ESKISSILSCLPKCSSNLKTI------------VSFGDVSSEQKEEAEELGVSCFSweefSLMGSldcelp 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 285 ----EDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFdhrpgdifgcVADIGWITGHSYVVYGPLCNGATSVLfE 360
Cdd:PLN02861 216 pkqkTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLAHVYDQVI-E 284
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622839332 361 STPVYPNAG-RYW--------ETVERLKINQFYGAP 387
Cdd:PLN02861 285 TYCISKGASiGFWqgdirylmEDVQALKPTIFCGVP 320
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
137-395 |
2.08e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 50.79 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 TFNqglrggrvmELKKIVDEAVKHCPTVQH-----VLVAHRTDNKVHMGDLDIPLEQEMAKEDPvcAPESMGS------- 284
Cdd:PLN03102 117 VDR---------SFEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 285 EDVLFMLYTSGSTGMPKGIVHTQAGYLLyAALThklvfdhrpgdifgcvADIGWITGHSYVVYGPL----CN-------- 352
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYL-STLS----------------AIIGWEMGTCPVYLWTLpmfhCNgwtftwgt 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622839332 353 ---GATSVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLK 395
Cdd:PLN03102 249 aarGGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK 290
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
137-556 |
2.52e-06 |
|
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: 50.05 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 TFNqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmGSEDVLFMLYTSGS 296
Cdd:cd17640 83 VEN---------------------------------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 297 TGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIgWitgHSY---VVYGPLCNGAtSVLFESTPVYPN------ 367
Cdd:cd17640 100 TGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAYTSIRTLKDdlkrvk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 368 ------AGRYWETVERLKINQFYGAPTAVRLLLKYgdawvkkydrssLRTLGSVGEPINCeawewlhrvvGDSRCTLVDT 441
Cdd:cd17640 174 phyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGISG----------GGALPPHVDT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 442 WWQ------------TETGGICIAPRPSeegaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALcisqawpgMARti 509
Cdd:cd17640 232 FFEaigievlngyglTETSPVVSARRLK----CNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIV--------WVR-- 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839332 510 yGDHqrFVDAYFK---------AYPGYYFTGDGAHRTEGGYYQITGRMDDVINISN 556
Cdd:cd17640 298 -GPQ--VMKGYYKnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSN 350
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
140-555 |
2.57e-06 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 50.40 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 tfnqglrggrVME-LKKIVDEAVKHCPtVQHVLVAhrtdnkvHMGDL----------------------DIP----LEQE 269
Cdd:PRK07059 126 ----------VLEnFATTVQQVLAKTA-VKHVVVA-------SMGDLlgfkghivnfvvrrvkkmvpawSLPghvrFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 270 MAK-EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYL---LYAALTHKLVFDHRPGD---IFGCVADIgwitgh 342
Cdd:PRK07059 188 LAEgARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPL------ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 343 sYVVYGPLCN-------GATSVLFestpvyPN----AGRYWEtVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR- 410
Cdd:PRK07059 262 -YHIFALTVCgllgmrtGGRNILI------PNprdiPGFIKE-LKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 411 TLG---SVGEPInceAWEWLHRvvgdSRCTLVDTWWQTETGGICIA--------------PRPSEEgaeilpgMAMRpff 473
Cdd:PRK07059 332 ANGggmAVQRPV---AERWLEM----TGCPITEGYGLSETSPVATCnpvdatefsgtiglPLPSTE-------VSIR--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 474 givpvlmDEKGSVVEGSNVsGALCIS--QAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQI 544
Cdd:PRK07059 395 -------DDDGNDLPLGEP-GEICIRgpQVMAGywnrpdeTAKVMTAD-------------GFFRTGDVGVMDERGYTKI 453
|
490
....*....|.
gi 1622839332 545 TGRMDDVINIS 555
Cdd:PRK07059 454 VDRKKDMILVS 464
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
286-551 |
2.80e-06 |
|
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: 49.42 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 286 DVLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHklVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlfestp 363
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMcaHRQT-LRAAAAWAD--CADLTEDDRYLIINPFFHTFGYKAGIVACLLTGAT-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 364 VYPNA----GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrcTLV 439
Cdd:cd17638 70 VVPVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE--TVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 440 DTWWQTETGGICIApRPSEEgAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNV-SGALCISQAwpgMARTIYGDhqrfvd 518
Cdd:cd17638 146 TAYGLTEAGVATMC-RPGDD-AETVATTCGRACPGFEVRIADDGEVLVRGYNVmQGYLDDPEA---TAEAIDAD------ 214
|
250 260 270
....*....|....*....|....*....|...
gi 1622839332 519 ayfkaypGYYFTGDGAHRTEGGYYQITGRMDDV 551
Cdd:cd17638 215 -------GWLHTGDVGELDERGYLRITDRLKDM 240
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-433 |
2.92e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.77 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVItf 218
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 219 nqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdlDIPLeqemakedpvcapesmgSEDVLFMLYTSGSTG 298
Cdd:cd05910 80 --------------------------------------------GIPK-----------------ADEPAAILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 299 MPKGIVHTQAgylLYAALTHKL--VFDHRPGDI----FGCVAdigwitghsyvVYGPLCnGATSVLFESTPVYP---NAG 369
Cdd:cd05910 99 TPKGVVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQ 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 370 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD 433
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSD 225
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
115-554 |
4.49e-06 |
|
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: 49.48 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 115 DQHVQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemaked 274
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 275 pvcapesmGSEDVLFMLYTSGSTGMPKGI-VHTQAgyLLYAALTHKLVFDHRPGDIFGCVADIGWiTGHSYVVYGPLCNG 353
Cdd:cd17645 102 --------NPDDLAYVIYTSGSTGLPKGVmIEHHN--LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 354 ATsvlfesTPVYPNAGRYweTVERLkiNQFYGAPTAVRLLLKYGDA-WVKKYDRSSLRTLGSVGEPINceawewlhrVVG 432
Cdd:cd17645 171 AA------LHVVPSERRL--DLDAL--NDYFNQEGITISFLPTGAAeQFMQLDNQSLRVLLTGGDKLK---------KIE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 433 DSRCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAMRPffgiVPVLMDEKGSVVEGSNVSGALCIsqAWPGMARTIYG- 511
Cdd:cd17645 232 RKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDN----TRVYILDEALQLQPIGVAGELCI--AGEGLARGYLNr 305
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839332 512 ---DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:cd17645 306 pelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
135-555 |
4.51e-06 |
|
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: 49.39 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMP------VSPLAVaaMLAcariGAVHTVIFAGFSAASLAGRIN 208
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 209 DAKCKVVITfnqglrgGRV---MELKKIVDEAVKHCPTVQH-VLVAHRT-DNKVHMGDldiPLEqemakEDPVCAPESMG 283
Cdd:cd05932 76 HSESKALFV-------GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 284 SedvlfMLYTSGSTGMPKGIVHTQA--GYLLYAALTHklvFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFES 361
Cdd:cd05932 141 T-----LIYTSGTTGQPKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 362 TPVYPnagrywETVERLKINQFYGAPtavRLLLK-----YGDAWVKKYDR-------SSL--------------RTLGSV 415
Cdd:cd05932 213 LDTFV------EDVQRARPTLFFSVP---RLWTKfqqgvQDKIPQQKLNLllkipvvNSLvkrkvlkglgldqcRLAGCG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 416 GEPINCEAWEWLHRVVGDsrctLVDTWWQTETGGICIAPRP--SEEG--AEILPGMAMRpffgivpvlMDEKGSVVEGSn 491
Cdd:cd05932 284 SAPVPPALLEWYRSLGLN----ILEAYGMTENFAYSHLNYPgrDKIGtvGNAGPGVEVR---------ISEDGEILVRS- 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839332 492 vsgalcisqawPGMARTIYGDHQRFVDAyFKAyPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:cd05932 350 -----------PALMMGYYKDPEATAEA-FTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTS 400
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
133-301 |
6.59e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 48.84 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 133 EPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIY--MPV--SPLAVAAMLACARIGAVHT----VIFAGFSAASLA 204
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVWAEDTLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 205 gRINDAKCKVVITfnqglrGGRVMELKKIVDEAvkhcpTVQHVLVAhrtdnkvhmgdldipleqEMAKEDPVcAPESMGS 284
Cdd:PRK07768 103 -VIGMIGAKAVVV------GEPFLAAAPVLEEK-----GIRVLTVA------------------DLLAADPI-DPVETGE 151
|
170
....*....|....*..
gi 1622839332 285 EDVLFMLYTSGSTGMPK 301
Cdd:PRK07768 152 DDLALMQLTSGSTGSPK 168
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
133-304 |
1.13e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 48.48 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 133 EPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKC 212
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 213 KVVITFNQglrggRVMELKKIVDEAVKHCPTVQHV---------------LVAHRTDNKVHMGD---LDIPLEQEmaked 274
Cdd:PLN02614 153 SIVFVEEK-----KISELFKTCPNSTEYMKTVVSFggvsreqkeeaetfgLVIYAWDEFLKLGEgkqYDLPIKKK----- 222
|
170 180 190
....*....|....*....|....*....|
gi 1622839332 275 pvcapesmgsEDVLFMLYTSGSTGMPKGIV 304
Cdd:PLN02614 223 ----------SDICTIMYTSGTTGDPKGVM 242
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
138-330 |
1.27e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 47.92 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 138 VRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIT 217
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 218 ----FNQGLRGGRVMELKKivDEAVKhcPTVQHVLVAHRTDNKV---HMGDLDIPLEQEMAKEDPVCAPESMGSE-DVLF 289
Cdd:PLN02479 124 dqefFTLAEEALKILAEKK--KSSFK--PPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADEwQSIA 199
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622839332 290 MLYTSGSTGMPKGIV-HTQAGYLLyaALTHKLVFDHRPGDIF 330
Cdd:PLN02479 200 LGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVY 239
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
137-404 |
1.45e-05 |
|
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: 47.81 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 217 TFNqglrggrvmELKKIVDEAVKhcptvqhvLVAHRTDNKVHMGDLDiPLEQEMAKEDPVCAPESMGSE-DVLFMLYTSG 295
Cdd:cd05915 102 FDP---------NLLPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 296 STGMPKGIVHTQAG-YLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEstpvYPNAGRYWET 374
Cdd:cd05915 164 TTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVEL 239
|
250 260 270
....*....|....*....|....*....|
gi 1622839332 375 VERLKINQFYGAPTAVRLLLKYGDAWVKKY 404
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRL 269
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
122-217 |
7.36e-05 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 45.47 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGD-CVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 200
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90
....*....|....*..
gi 1622839332 201 ASLAGRINDAKCKVVIT 217
Cdd:cd17648 75 ERIQFILEDTGARVVIT 91
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
141-302 |
8.80e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 45.12 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 141 TYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVitfn 219
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 220 qglrggrvmelkkIVDEavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05937 83 -------------IVDP------------------------------------------------DDPAILIYTSGTTGL 101
|
...
gi 1622839332 300 PKG 302
Cdd:cd05937 102 PKA 104
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
261-554 |
1.85e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 44.25 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 261 DLDIPLEQEMAKEDPVCAPES-MGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKlvFDHRPGDIFGCVADIgw 338
Cdd:PRK13388 125 DVDTPAYAELVAAAGALTPHReVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPL-- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 339 itGHSYVVY---GP-LCNGATSVLfestPVYPNAGRYWETVerlkinQFYGAP--TAVRLLLKYGDAWVKKYDRS--SLR 410
Cdd:PRK13388 201 --FHSNAVMagwAPaVASGAAVAL----PAKFSASGFLDDV------RRYGATyfNYVGKPLAYILATPERPDDAdnPLR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 411 -TLGSVGEPINCEawEWLHRVvgdsRCTLVDTWWQTETGGICIAPRPSEEGAeilpgmAMRPFFGIV-----------PV 478
Cdd:PRK13388 269 vAFGNEASPRDIA--EFSRRF----GCQVEDGYGSSEGAVIVVREPGTPPGS------IGRGAPGVAiynpetltecaVA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 479 LMDEKGSVVEGSNVSGALcISQAWPGMARTIYGDH----QRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK13388 337 RFDAHGALLNADEAIGEL-VNTAGAGFFEGYYNNPeataERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRV 408
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
142-328 |
2.28e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 44.23 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 142 YRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHT-----VIFAGFSA--ASLAGRINDAKCKV 214
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 215 VITfnqglrggrVMELKKIVDEAVKHCPTVqhvlvahrtdnkvhmgdLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTS 294
Cdd:PRK09192 132 IIT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSS 185
|
170 180 190
....*....|....*....|....*....|....*
gi 1622839332 295 GSTGMPKGIVHTQ-AGYLLYAALTHKLVfDHRPGD 328
Cdd:PRK09192 186 GSTRFPRGVIITHrALMANLRAISHDGL-KVRPGD 219
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
140-214 |
5.46e-04 |
|
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: 42.72 E-value: 5.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839332 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
114-309 |
1.15e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 41.65 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 114 LDQHVQKSPESVA---LIWERDEPGTEVRITYRELLETTCRLANTLKRHgVCRGDCVAIYMPVSPLAVAAMLACARIGAV 190
Cdd:PRK12476 40 IERNIANVGDTVAyryLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 191 HTVIFA----GfSAASLAGRINDAKCKVVITfnqglrggrvmelkkivDEAVKhcPTVQHVLVAHRTDNKVHMGDLD-IP 265
Cdd:PRK12476 119 AVPLFApelpG-HAERLDTALRDAEPTVVLT-----------------TTAAA--EAVEGFLRNLPRLRRPRVIAIDaIP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622839332 266 leqEMAKEDPVCAPesMGSEDVLFMLYTSGSTGMPKG--IVHTQAG 309
Cdd:PRK12476 179 ---DSAGESFVPVE--LDTDDVSHLQYTSGSTRPPVGveITHRAVG 219
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
278-534 |
1.81e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 41.18 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 278 APESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVAD-IGW--ITGHSYVVYGPLCNGA 354
Cdd:PRK12582 213 AIAAITPDTVAKYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPDPPPPVSLDwMPWnhTMGGNANFNGLLWGGG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 355 TSVLFESTPVypnAGRYWETVERLK-INQ--FYGAPTAVRLL---LKYGDAWVKKYdRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:PRK12582 292 TLYIDDGKPL---PGMFEETIRNLReISPtvYGNVPAGYAMLaeaMEKDDALRRSF-FKNLRLMAYGGATLSDDLYERMQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 429 ----RVVGdSRCTLVDTWWQTETGGI-CIAPRPSEEGAEI---LPGMAMRpffgIVPVlmDEKGSV-VEGSNVSgalcis 499
Cdd:PRK12582 368 alavRTTG-HRIPFYTGYGATETAPTtTGTHWDTERVGLIglpLPGVELK----LAPV--GDKYEVrVKGPNVT------ 434
|
250 260 270
....*....|....*....|....*....|....*
gi 1622839332 500 qawPGMartiYGDHQRFVDAYFKAypGYYFTGDGA 534
Cdd:PRK12582 435 ---PGY----HKDPELTAAAFDEE--GFYRLGDAA 460
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
285-422 |
4.80e-03 |
|
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: 39.78 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839332 285 EDVLFMLYTSGSTGMPKGIVHTQagyllyaaltHKLVFdhrpgDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV 364
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVH-----NMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839332 365 YPNAGRY-------------W-ETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPINCE 422
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
23-83 |
6.22e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.47 E-value: 6.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839332 23 QPARPLSRVSAPRRAASGPSGSAPAVAAASQPGSYPALSAQAAREPAAFWGPLARDTLLWD 83
Cdd:PRK12323 440 SARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWE 500
|
|
| |
