|
Name |
Accession |
Description |
Interval |
E-value |
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
23-555 |
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: 980.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:TIGR02188 92 RELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVKHCP-TVQHVLVAHRTDNKV-HMGD-LDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM 179
Cdd:TIGR02188 172 RGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVEgRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLK 259
Cdd:TIGR02188 252 PKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 260 INQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSee 339
Cdd:TIGR02188 332 VTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPG-- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 340 GAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG 419
Cdd:TIGR02188 410 ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKD 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 420 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKI 499
Cdd:TIGR02188 490 GYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEI 569
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 500 AKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 555
Cdd:TIGR02188 570 GPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIE 625
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
23-546 |
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: 976.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:cd05966 88 RELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHM-GDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPK 181
Cdd:cd05966 168 RGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKIN 261
Cdd:cd05966 248 GVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 262 QFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEegA 341
Cdd:cd05966 328 IFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGA--T 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 342 EILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGY 421
Cdd:cd05966 406 PLKPGSATRPFFGIEPAILDEEGNEVEG-EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGY 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 422 YQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAK 501
Cdd:cd05966 485 YWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGP 564
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 358248211 502 YAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLED 546
Cdd:cd05966 565 IATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEE-ELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
23-561 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 896.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK00174 102 RELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGD-LDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK00174 182 RGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEgRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKIN 261
Cdd:PRK00174 262 GVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVT 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 262 QFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPseeGA 341
Cdd:PRK00174 342 IFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLP---GA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 342 -EILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGG 420
Cdd:PRK00174 419 tPLKPGSATRPLPGIQPAVVDEEGNPLEG-GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDG 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 421 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 500
Cdd:PRK00174 498 YYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIG 577
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 501 KYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLEDPSIIAEILSVYQKCK 561
Cdd:PRK00174 578 PIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEARQNRK 637
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
23-553 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 775.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:COG0365 43 AELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDlDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKG 182
Cdd:COG0365 123 RGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEG-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQ 262
Cdd:COG0365 202 VVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAE 342
Cdd:COG0365 282 FFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP---GLP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYY 422
Cdd:COG0365 356 VKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYF 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 423 QITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKY 502
Cdd:COG0365 435 WILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPY 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 358248211 503 AVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTLEDPSIIAEI 553
Cdd:COG0365 515 AYPREIEFVDELPKTRSGKIMRRLLRKIA--EGRPLGDTSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
24-556 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 615.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLR 103
Cdd:PLN02654 125 ELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 GGRVVELKKIVDEA----------VKHCPTVQHVLVAHRTDNKVHMGDlDVPLEQEMAKEDPVCAPESMGSEDMLFMLYT 173
Cdd:PLN02654 205 GPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-DVWWQDVVPNYPTKCEVEWVDAEDPLFLLYT 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 174 SGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWE 253
Cdd:PLN02654 284 SGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 254 TVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIA 333
Cdd:PLN02654 364 IVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMIT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 334 PRPseeGAEIL-PAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGD 412
Cdd:PLN02654 444 PLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGD 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 413 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELK 492
Cdd:PLN02654 520 GCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLI 599
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 493 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILSV 556
Cdd:PLN02654 600 LTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIAL 663
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
23-523 |
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: 589.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:cd17634 88 RELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVK-HCPTVQHVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 180
Cdd:cd17634 168 RAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKI 260
Cdd:cd17634 248 KGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPseeG 340
Cdd:cd17634 328 NILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLP---G 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 341 AEILPA-MAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG 419
Cdd:cd17634 405 AIELKAgSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDED 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 420 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKI 499
Cdd:cd17634 484 GYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEI 563
|
490 500
....*....|....*....|....
gi 358248211 500 AKYAVPDEILVVKRLPKTRSGKVM 523
Cdd:cd17634 564 GPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
23-553 |
5.15e-180 |
|
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: 521.49 E-value: 5.15e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:cd05967 86 AELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVK---HCPtvQHVLVAHRTDNKVHMGD--LDVPLEQEMAKEDPV-CAPesMGSEDMLFMLYTSGS 176
Cdd:cd05967 166 EPGKVVPYKPLLDKALElsgHKP--HHVLVLNRPQVPADLTKpgRDLDWSELLAKAEPVdCVP--VAATDPLYILYTSGT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV-YPNAGRYWETV 255
Cdd:cd05967 242 TGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGG---- 329
Cdd:cd05967 322 EKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTETGWpita 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 330 --ICIAPRPSEEGAEILPAMAMRpffgiVPVLmDEKGSVVeGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAYPG 406
Cdd:cd05967 399 npVGLEPLPIKAGSPGKPVPGYQ-----VQVL-DEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 407 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSD 485
Cdd:cd05967 472 YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKiTAE 551
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248211 486 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTLEDPSIIAEI 553
Cdd:cd05967 552 ELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
23-553 |
1.51e-162 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 477.13 E-value: 1.51e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK10524 88 RQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAV---KHCPtvQHVLVAHR-TDNKVHMGDLDVPLEQEMAK-EDPVCAPESMGSEDMLFMLYTSGST 177
Cdd:PRK10524 168 RGGKVVPYKPLLDEAIalaQHKP--RHVLLVDRgLAPMARVAGRDVDYATLRAQhLGARVPVEWLESNEPSYILYTSGTT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVER 257
Cdd:PRK10524 246 GKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETGGICIAPRPS 337
Cdd:PRK10524 326 YKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP---VIDNYWQTETGWPILAIARG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 338 EEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAY-PGYYFTGDGAY 415
Cdd:PRK10524 403 VEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGI 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 416 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD-----VVVQE 490
Cdd:PRK10524 483 RDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADrearlALEKE 562
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248211 491 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitSEAQELGDTTTLEDPSIIAEI 553
Cdd:PRK10524 563 IMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI--AEGRDPGDLTTIEDPAALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
23-547 |
5.30e-159 |
|
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: 467.35 E-value: 5.30e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:cd05968 95 GELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd05968 175 RRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGR-DLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQ 262
Cdd:cd05968 254 TVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITH 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTE-TGGI--CIAPRPsee 339
Cdd:cd05968 333 LGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiSGGIlgNVLIKP--- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 340 gaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG 419
Cdd:cd05968 410 ---IKPSSFNGPVPGMKADVLDESGKPARPE--VGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 420 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKI 499
Cdd:cd05968 485 GYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADEL 564
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 358248211 500 AKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEaqELGDTTTLEDP 547
Cdd:cd05968 565 GKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
23-546 |
2.25e-144 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 428.54 E-value: 2.25e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK04319 77 KELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RggrvvelKKIVDEavkhCPTVQHVLVahrTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKG 182
Cdd:PRK04319 157 E-------RKPADD----LPSLKHVLL---VGEDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQagyllYAALTH----KLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERL 258
Cdd:PRK04319 223 VLHVH-----NAMLQHyqtgKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 259 KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSE 338
Cdd:PRK04319 295 KVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAM 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 339 EgaeILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRFvDAYFKayPGYYFTGDGAYRTE 418
Cdd:PRK04319 372 D---IKPGSMGKPLPGIEAAIVDDQGNELP-PNRMGNLAIKKGWPSMMRGIWNNPEKY-ESYFA--GDWYVSGDSAYMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 419 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATK 498
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKG 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 358248211 499 IAKYAVPDEILVVKRLPKTRSGKVMRRLLRkiitseAQEL----GDTTTLED 546
Cdd:PRK04319 525 LGAHAAPREIEFKDKLPKTRSGKIMRRVLK------AWELglpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
24-530 |
1.40e-129 |
|
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: 386.09 E-value: 1.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglr 103
Cdd:cd05969 5 QLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvplEQEMAkedpvcapESMGSEDMLFMLYTSGSTGMPKGI 183
Cdd:cd05969 79 -------------------------------------------TEELY--------ERTDPEDPTLLHYTSGTTGTPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQAGYLLYAaLTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKINQF 263
Cdd:cd05969 108 LHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKVTVW 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 264 YGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAEI 343
Cdd:cd05969 184 YTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP---CMPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 344 LPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRFvDAYFKAypGYYFTGDGAYRTEGGYYQ 423
Cdd:cd05969 258 KPGSMGKPLPGVKAAVVDENGNELP-PGTKGILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDGYFW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 424 ITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYA 503
Cdd:cd05969 334 FVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHV 413
|
490 500
....*....|....*....|....*..
gi 358248211 504 VPDEILVVKRLPKTRSGKVMRRLLRKI 530
Cdd:cd05969 414 APREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
23-529 |
3.10e-109 |
|
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: 333.53 E-value: 3.10e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05972 4 RELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd05972 79 ------------------------------------------------------------DAEDPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNagRYWETVERLKINQ 262
Cdd:cd05972 99 VLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgICIAPRPseeGAE 342
Cdd:cd05972 176 FCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP---DMP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYY 422
Cdd:cd05972 246 VKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTGDRAYRDEDGYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 423 QITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKY 502
Cdd:cd05972 322 WFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPY 401
|
490 500
....*....|....*....|....*..
gi 358248211 503 AVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05972 402 KYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
23-435 |
4.54e-99 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 306.93 E-value: 4.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFnqgl 102
Cdd:pfam00501 25 RELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITD---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrVVELKKIVDEAVKHCPTVQHVLVAHRTDnkvhMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKG 182
Cdd:pfam00501 101 ----DALKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQaGYLLYAALTHKLVFDHQ----PGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVyPNAGRYWETVERL 258
Cdd:pfam00501 173 VMLTH-RNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 259 KINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSE 338
Cdd:pfam00501 251 KVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 339 EGAEILPAmAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKayPGYYFTGDGAYRTE 418
Cdd:pfam00501 326 EDLRSLGS-VGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGYLNDPELTAEAFDE--DGWYRTGDLGRRDE 400
|
410
....*....|....*..
gi 358248211 419 GGYYQITGRMDDVINIS 435
Cdd:pfam00501 401 DGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
23-537 |
2.70e-93 |
|
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: 292.87 E-value: 2.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFnqgl 102
Cdd:COG0318 28 AELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVTA---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsedmlFMLYTSGSTGMPKG 182
Cdd:COG0318 104 ------------------------------------------------------------------LILYTSGTTGRPKG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQ 262
Cdd:COG0318 118 VMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR----FDPERVLELIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRpsEEGAE 342
Cdd:COG0318 193 LFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNP--EDPGE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDayfkaypGYYFTGDGAYRTE 418
Cdd:COG0318 266 RRPGSVGRPLPGVEVRIVDEDGREL-PPGEVGEIVVRG--PNVMKGYWNDpeatAEAFRD-------GWLRTGDLGRLDE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 419 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATK 498
Cdd:COG0318 336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRP---GAELDAEELRAFLRER 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 358248211 499 IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 537
Cdd:COG0318 413 LARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
166-523 |
9.58e-81 |
|
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: 256.44 E-value: 9.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 166 DMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHqPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFEStpvy 245
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-EGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT 325
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 326 ETGGICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDayfkaYP 405
Cdd:cd04433 150 ETGGTVATGPPDDD--ARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVD-----ED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 406 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 485
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---D 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 358248211 486 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 523
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
23-531 |
6.23e-72 |
|
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: 242.18 E-value: 6.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:cd05943 102 AELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVP----LEQEMAKE-DPVCAPESMGSEDMLFMLYTSGST 177
Cdd:cd05943 182 YNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPLPFDHPLYILYSSGTT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVvyGPLCNGATSVLFESTPVYPNAGRYWETVER 257
Cdd:cd05943 262 GLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSPFYPDTNALWDLADE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTWWQTETGG--IC---- 331
Cdd:cd05943 340 EGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGGtdIIscfv 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 332 ----IAP-RPSEEGAEILpAMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMARTIYGDH--QRFVDAYFKAY 404
Cdd:cd05943 414 ggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWNDPdgSRYRAAYFAKY 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 405 PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDS 484
Cdd:cd05943 483 PGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELD 562
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 358248211 485 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 531
Cdd:cd05943 563 DELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII 609
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
24-529 |
2.71e-70 |
|
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: 232.79 E-value: 2.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglr 103
Cdd:cd05973 5 ELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvelkkivDEAVKHcptvqhvlvahrtdnkvhmgDLDvpleqemakedpvcapesmgsEDMLFMLYTSGSTGMPKGI 183
Cdd:cd05973 79 -----------DAANRH--------------------KLD---------------------SDPFVMMFTSGTTGLPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQAGYLLYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgryWETVERLKINQF 263
Cdd:cd05973 107 PVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLGVTNL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 264 YGAPTAVRLLLKYGdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgICIA-----PRPSE 338
Cdd:cd05973 183 AGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELG-MVLAnhhalEHPVH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 339 EGAEILPAMAMRpffgiVPVLMDEKGSVVEGsnVSGALCISQA-WPGMArtiYGDHQRFVDAYFKAypGYYFTGDGAYRT 417
Cdd:cd05973 258 AGSAGRAMPGWR-----VAVLDDDGDELGPG--EPGRLAIDIAnSPLMW---FRGYQLPDTPAIDG--GYYLTGDTVEFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 418 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVAT 497
Cdd:cd05973 326 PDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKK 405
|
490 500 510
....*....|....*....|....*....|..
gi 358248211 498 KIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05973 406 RLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
23-527 |
5.06e-67 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 229.68 E-value: 5.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqGL 102
Cdd:PRK03584 118 AELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVD-GY 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 R-GGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLD--VPLEQEMAK-EDPVCAPESMGSEDMLFMLYTSGSTG 178
Cdd:PRK03584 197 RyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEPVPFDHPLWILYSSGTTG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 179 MPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF----GCvadiGWITgHSYVVYGPLCnGATSVLFESTPVYPNAGRYWET 254
Cdd:PRK03584 277 LPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLVLYDGSPFYPDPNVLWDL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 255 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTWWQTETGG--IC- 331
Cdd:PRK03584 351 AAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtdICs 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 332 --IAprpseeGAEILP-----------AMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMArtIY----GDHQ 394
Cdd:PRK03584 425 cfVG------GNPLLPvyrgeiqcrglGMAVEAW--------DEDGRPVVG--EVGELVCTKPFPSMP--LGfwndPDGS 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 395 RFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 474
Cdd:PRK03584 487 RYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLF 566
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 475 IVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM----RRLL 527
Cdd:PRK03584 567 VVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
23-528 |
9.91e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 225.45 E-value: 9.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTV-IFagFSAESLAGRINDAKCKVVItFNQ 100
Cdd:PRK06187 35 AELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 101 glrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKVHmGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 180
Cdd:PRK06187 112 --------EFVPLLAAILPQLPTVRTVIVEGDGPAAPL-APEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTqagyllyaaltHKLVFDHqpgdIFGCVADIGWITGHSYVV-------------YGPLCNGATSVL---FESTPV 244
Cdd:PRK06187 183 KGVVLS-----------HRNLFLH----SLAVCAWLKLSRDDVYLVivpmfhvhawglpYLALMAGAKQVIprrFDPENL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 ypnagryWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPIN---CEAWEWLHRvvgdsrCTLVDT 321
Cdd:PRK06187 248 -------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFSSLRLVIYGGAALPpalLREFKEKFG------IDLVQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTETGGICIAPRPSEEGAEILPAM--AMRPFFGIVPVLMDEKGSVVEGSNVS-GALCISQAWpgMARTIYGDHQRFVD 398
Cdd:PRK06187 313 YGMTETSPVVSVLPPEDQLPGQWTKRrsAGRPLPGVEARIVDDDGDELPPDGGEvGEIIVRGPW--LMQGYWNRPEATAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 399 AYfkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVK 478
Cdd:PRK06187 391 TI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 358248211 479 DsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK06187 468 P---GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
23-529 |
1.53e-65 |
|
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: 222.73 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGavhTVIFAG---FSAESLAGRINDAKCKVVITF 98
Cdd:cd05928 45 RELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTG---LVFIPGtiqLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 99 NqglrggrvvELKKIVDEAVKHCPTVQ-HVLVAHRTDNkvhmGDLDVPLEQEMAKEDPVCApeSMGSEDMLFMLYTSGST 177
Cdd:cd05928 122 D---------ELAPEVDSVASECPSLKtKLLVSEKSRD----GWLNFKELLNEASTEHHCV--ETGSQEPMAIYFTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATsVLFESTPVYpNAGRYWETVER 257
Cdd:cd05928 187 GSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVGDsrctLVDTWWQTETGGICIAPRp 336
Cdd:cd05928 265 YPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLNPEVLEkWKAQTGLD----IYEGYGQTETGLICANFK- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 337 seeGAEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAY 415
Cdd:cd05928 337 ---GMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 416 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD--SAGDSDVVVQELKS 493
Cdd:cd05928 412 MDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQ 491
|
490 500 510
....*....|....*....|....*....|....*.
gi 358248211 494 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05928 492 HVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
20-528 |
4.72e-65 |
|
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: 220.70 E-value: 4.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 20 PHGR----ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 95
Cdd:cd05959 26 DAGSltyaELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 96 itfnqglrggrVVE---LKKIVDEAVKHCPTVQHVLVAhrtdnKVHMGDLDVP-LEQEMAKEDPVCAPESMGSEDMLFML 171
Cdd:cd05959 106 -----------VVSgelAPVLAAALTKSEHTLVVLIVS-----GGAGPEAGALlLAELVAAEAEQLKPAATHADDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 172 YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRY 251
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 252 WETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVgdsrCTLVDTWWQTETGGI 330
Cdd:cd05959 247 FKRIRRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGErWKARFG----LDILDGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 331 CIAPRPSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQawPGMArTIYGdHQRfvDAYFKAYPGYYF- 409
Cdd:cd05959 321 FLSNRPGR----VRYGTTGKPVPGYEVELRDEDGGDVADG-EPGELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTr 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 410 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQ 489
Cdd:cd05959 390 TGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEE 469
|
490 500 510
....*....|....*....|....*....|....*....
gi 358248211 490 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05959 470 ELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
24-559 |
3.15e-64 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 221.92 E-value: 3.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLR 103
Cdd:PTZ00237 97 QLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 GGRVVELKKIVDEAV---KHCPTvqHVLVAHRTD-----NKVHMGD-------LDVPLEQEMAKED---PVCAPESMGSE 165
Cdd:PTZ00237 177 NDEIITFTPNLKEAIelsTFKPS--NVITLFRNDitsesDLKKIETiptipntLSWYDEIKKIKENnqsPFYEYVPVESS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 166 DMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNGATSVLFESTPVY 245
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 PNAGR--YWETVERLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdSRCTLVd 320
Cdd:PTZ00237 334 NKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLK-IKSSRG- 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 321 tWWQTETGG---ICIAPRPSEEGAEILPAmamrPFfgIVPVLMDEKGSVVeGSNVSGALCISQAWP-GMARTIYGDHQRF 396
Cdd:PTZ00237 412 -YGQTEIGItylYCYGHINIPYNATGVPS----IF--IKPSILSEDGKEL-NVNEIGEVAFKLPMPpSFATTFYKNDEKF 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 397 vDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 476
Cdd:PTZ00237 484 -KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 477 VKDSAGDSDVVVQELKS----MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTtlEDPSIIAE 552
Cdd:PTZ00237 563 LKQDQSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNV--NDSEIFYK 640
|
....*..
gi 358248211 553 ILSVYQK 559
Cdd:PTZ00237 641 IKELYMK 647
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
23-528 |
4.40e-64 |
|
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: 216.14 E-value: 4.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05971 10 KELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd05971 85 ---------------------------------------------------D--------GSDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQA---GYLLYAALTHKLVfdHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnaGRYWETVERLK 259
Cdd:cd05971 106 ALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDP--KAALDLMSRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 260 INQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG---GICIAPRP 336
Cdd:cd05971 182 VTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFGVE---VNEFYGQTECNlviGNCSALFP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 337 SEEGAeilpaMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYR 416
Cdd:cd05971 257 IKPGS-----MG-KPIPGHRVAIVDDNGTPLP-PGEVGEIAVELPDPVAFLG-YWNNPSATEKKMAG--DWLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 417 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVA 496
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVK 406
|
490 500 510
....*....|....*....|....*....|..
gi 358248211 497 TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05971 407 TRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
22-523 |
6.25e-63 |
|
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: 214.38 E-value: 6.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 22 GRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQG 101
Cdd:cd05911 13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 LrggrvvelkKIVDEAVKHCPTVQHV-LVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTSGSTGMP 180
Cdd:cd05911 93 L---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGivhtqagyllyAALTHK-LVFDH-----------QPGDIFGCVADIGWITGHSYVVYGPLCnGATSVLFEStpvyPNA 248
Cdd:cd05911 162 KG-----------VCLSHRnLIANLsqvqtflygndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK----FDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 249 GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTWWQTETG 328
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGYGMTETG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 GICIAPRPSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS--QAWPG-------MARTIYGDhqr 395
Cdd:cd05911 302 GILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyynnpeaTKETFDED--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 fvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:cd05911 371 ----------GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYV 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 358248211 476 VVKDSAGDSDvvvQELKSMVATKIAKY-AVPDEILVVKRLPKTRSGKVM 523
Cdd:cd05911 441 VRKPGEKLTE---KEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
24-528 |
7.92e-63 |
|
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: 215.44 E-value: 7.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGlr 103
Cdd:cd05970 52 ELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvELKKIVDEAVKHCPTVQhVLVahrtdnKVHMGDLD--VPLEQEMAKEDPV----CAPESMGSEDMLFMLYTSGST 177
Cdd:cd05970 130 -----NIPEEIEKAAPECPSKP-KLV------WVGDPVPEgwIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgrYWETVER 257
Cdd:cd05970 198 GMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETGgICIAPRPs 337
Cdd:cd05970 275 YGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFP- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 338 eeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNvSGALCI--SQAWP-GMARTIYGDHQRFVDAYFKaypGYYFTGDGA 414
Cdd:cd05970 347 --WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtSKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 415 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 494
Cdd:cd05970 421 WMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDH 500
|
490 500 510
....*....|....*....|....*....|....
gi 358248211 495 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05970 501 VKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
23-528 |
2.92e-58 |
|
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: 200.77 E-value: 2.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05919 14 GQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd05919 89 ------------------------------------------------------------SADDIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADI--GWITGHSyvVYGPLCNGATSVLFestPVYPNAGRYWETVERLKI 260
Cdd:cd05919 109 VMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLARFRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEeg 340
Cdd:cd05919 184 TVLYGVPTFYANLLDSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPGA-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 341 aeILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI--SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTE 418
Cdd:cd05919 257 --WRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVrgPSAAVGYWNNPEKSRATFNG-------GWYRTGDKFCRDA 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 419 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATK 498
Cdd:cd05919 327 DGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLER 406
|
490 500 510
....*....|....*....|....*....|
gi 358248211 499 IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05919 407 LSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
23-527 |
4.52e-57 |
|
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: 197.75 E-value: 4.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05930 16 AELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd05930 91 ------------------------------------------------------------DPDDLAYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFESTPVYpNAGRYWETVERLKINQ 262
Cdd:cd05930 111 VMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPEEVRK-DPEALADLLAEEGITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTWWQTETGGICIAPRPSEEGAE 342
Cdd:cd05930 188 LHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNLYGPTEATVDATYYRVPPDDEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGDH----QRFVDAYFKAYPGYYFTGDGAYRTE 418
Cdd:cd05930 262 DGRVPIGRPIPNTRVYVLDENLRPV-PPGVPGELYIGGA--GLARGYLNRPeltaERFVPNPFGPGERMYRTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 419 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATK 498
Cdd:cd05930 339 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV---PDEGGELDEEELRAHLAER 415
|
490 500
....*....|....*....|....*....
gi 358248211 499 IAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05930 416 LPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
23-524 |
9.74e-57 |
|
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: 196.68 E-value: 9.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqgl 102
Cdd:cd17631 24 AELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGMPKG 182
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQ 262
Cdd:cd17631 116 AMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinceAWEWLHRVVGDSRCTLVDTWWQTETG-GICIAPRpseEGA 341
Cdd:cd17631 191 FFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQARGVKFVQGYGMTETSpGVTFLSP---EDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 342 EILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGY 421
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPDGREVPP-GEVGEIVVRG--PHVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 422 YQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAK 501
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA---ELDEDELIAHCRERLAR 412
|
490 500
....*....|....*....|...
gi 358248211 502 YAVPDEILVVKRLPKTRSGKVMR 524
Cdd:cd17631 413 YKIPKSVEFVDALPRNATGKILK 435
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
24-564 |
1.37e-56 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 201.26 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLR 103
Cdd:TIGR01217 119 ELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 GGRVVELKKIVDEAVKHCPTVQHVLVahrtdnkvhmgdldVPLEQEMAKEDPVcAPESMGSEDM---------------- 167
Cdd:TIGR01217 199 NGKEHDRRDKVAEVRKELPTLRAVVH--------------IPYLGPRETEAPK-IDGALDLEDFtaaaqaaelvfeqlpf 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 168 ---LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITgHSYVVYGpLCNGATSVLFESTPV 244
Cdd:TIGR01217 264 dhpLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM-WNWLVSG-LATGATLVLYDGSPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 YPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgdsRCTLVDTWWQ 324
Cdd:TIGR01217 342 FPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY------DEIKADVWLA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 325 TETGGI----CIAPRPSEEGAEILPAMAmrPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQ--RFVD 398
Cdd:TIGR01217 416 SISGGTdicsCFAGANPTLPVHIGEIQA--PGLGTAVQSWDPEGKPVTGE--VGELVCTNPMPSMPIRFWNDPDgsKYRD 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 399 AYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVK 478
Cdd:TIGR01217 492 AYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLA 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 479 DSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSeaqelgdtTTLEDPSIIA--EILSV 556
Cdd:TIGR01217 572 PGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQG--------TPVDNPGAIDnpELLDL 643
|
....*...
gi 358248211 557 YQKCKDKQ 564
Cdd:TIGR01217 644 YEELAELR 651
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
23-529 |
1.09e-52 |
|
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: 187.84 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTvIFAGFSAESLAGRINDAKCKVVITFNqg 101
Cdd:cd12119 29 AEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT-INPRLFPEQIAYIINHAEDRVVFVDR-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggrvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPL---EQEMAKEDPVCAPESMGSEDMLFMLYTSGSTG 178
Cdd:cd12119 106 -------DFLPLLEAIAPRLPTVEHVVVM--TDDAAMPEPAGVGVlayEELLAAESPEYDWPDFDENTAAAICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 179 MPKGIVHTQAGYLLYA-ALTHKLVFDHQPGDIFGCVADI----GW-------ITGHSYVVYGPLCNGATSVlfestpvyp 246
Cdd:cd12119 177 NPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVGAKLVLPGPYLDPASLA--------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 247 nagrywETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINCEAWEWLHrvvgdsrctlVDT-- 321
Cdd:cd12119 248 ------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG----------VRVih 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 -WWQTETGGICIAPRP-------SEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVS-GALCISQAWpgMARTIYGD 392
Cdd:cd12119 310 aWGMTETSPLGTVARPpsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAvGELQVRGPW--VTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 393 HQR----FVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 468
Cdd:cd12119 388 DEEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWG 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 469 EAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd12119 461 ERPLAVVVLKE---GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-528 |
7.28e-48 |
|
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: 173.52 E-value: 7.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI---TFN 99
Cdd:cd05936 28 RELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIvavSFT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 QGLRGGRVVELKKIVDEavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGM 179
Cdd:cd05936 108 DLLAAGAPLGERVALTP------------------------------------------------EDVAVLQYTSGTTGV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQaGYLLYAALTHK--LVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEStpvyPNAGRYWETVER 257
Cdd:cd05936 140 PKGAMLTH-RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR----FRPIGVLKEIRK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETG-GICIAP-- 334
Cdd:cd05936 215 HRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpVVAVNPld 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 ---RPSEEGaeilpamamRPFFGIVPVLMDEKGSVVEGSNVsGALCIS--QAWPGmartiYGDH-----QRFVDayfkay 404
Cdd:cd05936 290 gprKPGSIG---------IPLPGTEVKIVDDDGEELPPGEV-GELWVRgpQVMKG-----YWNRpeetaEAFVD------ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 405 pGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDS 484
Cdd:cd05936 349 -GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE---GA 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 358248211 485 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05936 425 SLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
23-528 |
2.88e-46 |
|
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: 168.43 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHR-GDRVAIYMPVSPLAVAAMLACARIGAVhtvifagfsaeslagrindakCKVVITFnqg 101
Cdd:cd05958 14 RDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVATMPL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 LRGGrvvELKKIVDEAvkhcpTVQHVLVAHRTdnkvhmgdldvpleqemakedpvcapesMGSEDMLFMLYTSGSTGMPK 181
Cdd:cd05958 70 LRPK---ELAYILDKA-----RITVALCAHAL----------------------------TASDDICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKIN 261
Cdd:cd05958 114 ATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAIARYKPT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 262 QFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEega 341
Cdd:cd05958 190 VLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISARPGD--- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 342 eILPAMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQawPGMARTIYGDHQRfvdAYFKAypGYYFTGDGAYRTEGGY 421
Cdd:cd05958 262 -ARPGATGKPVPGYEAKVVDDEGNPVPDGTI-GRLAVRG--PTGCRYLADKRQR---TYVQG--GWNITGDTYSRDPDGY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 422 YQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAK 501
Cdd:cd05958 333 FRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAP 412
|
490 500
....*....|....*....|....*..
gi 358248211 502 YAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05958 413 YKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
24-529 |
9.00e-45 |
|
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: 165.78 E-value: 9.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglr 103
Cdd:TIGR02262 35 ELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNkvhmGDLDvpLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGI 183
Cdd:TIGR02262 111 -----ALLPVIKAALGKSPHLEHRVVVGRPEA----GEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETVERLKINQF 263
Cdd:TIGR02262 180 VHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 264 YGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVVGDsrctLVDTWWQTETGGICIAPRPSEegae 342
Cdd:TIGR02262 257 YGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTEMLHIFLSNLPGD---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYY 422
Cdd:TIGR02262 327 VRYGTSGKPVPGYRLRLVGDGGQDV-ADGEPGELLISG---PSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRNDDGSY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 423 QITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDIKGEaafAFIVVKDSAGDSDvvvQELKSMVATKI 499
Cdd:TIGR02262 401 TYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVAdedGLIKPK---AFVVLRPGQTALE---TELKEHVKDRL 474
|
490 500 510
....*....|....*....|....*....|
gi 358248211 500 AKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:TIGR02262 475 APYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
23-528 |
1.36e-44 |
|
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: 163.23 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05934 7 AELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPVCapesmgsedmlfMLYTSGSTGMPKG 182
Cdd:cd05934 82 ---------------------------------------------------DPAS------------ILYTSGTTGPPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQ 262
Cdd:cd05934 99 VVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseega 341
Cdd:cd05934 174 TNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRD----- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 342 EILPAMAM-RPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWP-GMARTIYGDHqrfvDAYFKAYP-GYYFTGDGAYRTE 418
Cdd:cd05934 241 EPRRPGSIgRPAPGYEVRIVDDDGQELP-AGEPGELVIRGLRGwGFFKGYYNMP----EATAEAMRnGWFHTGDLGYRDA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 419 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATK 498
Cdd:cd05934 316 DGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD---PEELFAFCEGQ 392
|
490 500 510
....*....|....*....|....*....|
gi 358248211 499 IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05934 393 LAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
23-529 |
1.50e-43 |
|
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: 162.10 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:cd05926 18 ADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 ---------RGGRVVELKkiVDEAVKHCPTVQHVLVAHRTDNKVhmgdldvpleqemAKEDPVCAPEsmgseDMLFMLYT 173
Cdd:cd05926 98 gpasraaskLGLAILELA--LDVGVLIRAPSAESLSNLLADKKN-------------AKSEGVPLPD-----DLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 174 SGSTGMPKGIVHTQAGYLL---YAALTHKLvfdhQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfestPVYPNAGR 250
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAAsatNITNTYKL----TPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL----PPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 251 YWETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGg 329
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFG---APVLEAYGMTEAA- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 330 iciaprpseegaeilPAMAMRPF------FGIVP-------VLMDEKGSVVEgSNVSGALCISQawPGMARTIYGDHQRF 396
Cdd:cd05926 304 ---------------HQMTSNPLppgprkPGSVGkpvgvevRILDEDGEILP-PGVVGEICLRG--PNVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 397 VDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 476
Cdd:cd05926 366 AEAAFKD--GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 358248211 477 VKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05926 444 LR---EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
23-537 |
3.00e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 161.64 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfNQGL 102
Cdd:PRK08316 40 AELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV-DPAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGgrvvelkkIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKEDPVCAPE-SMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK08316 119 AP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVAEPDvELADDDLAQILYTSGTESLPK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTqagyllYAALTHKLVfdhqpgdifGCVADIGWITG----------HS---YVVYGP-LCNGATSVLFEStpvyPN 247
Cdd:PRK08316 188 GAMLT------HRALIAEYV---------SCIVAGDMSADdiplhalplyHCaqlDVFLGPyLYVGATNVILDA----PD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 AGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTlGSVGEPI-NCEAWEWLHRVVGDSRctLVDTWWQTE 326
Cdd:PRK08316 249 PELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRK-GYYGASImPVEVLKELRERLPGLR--FYNCYGQTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 327 tggicIAP-----RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMARTIYGDHQRFVDAYF 401
Cdd:PRK08316 324 -----IAPlatvlGPEE--HLRRPGSAGRPVLNVETRVVDDDGNDVA--------------PGEVGEIVHRSPQLMLGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 402 K-------AYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFA 473
Cdd:PRK08316 383 DdpektaeAFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 474 FIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 537
Cdd:PRK08316 463 VVVPKAGA---TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAFTD 523
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
23-532 |
3.36e-43 |
|
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: 161.85 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtVIFAGFS-----AESLAGRInDAKCKVVIT 97
Cdd:COG1021 54 AELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFALPAhrraeISHFAEQS-EAVAYIIPD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 98 FNQGLRggrvveLKKIVDEAVKHCPTVQHVLVAHRTDNKVhmgDLDVPLEQEMAKEDPVCAPEsmgseDMLFMLYTSGST 177
Cdd:COG1021 131 RHRGFD------YRALARELQAEVPSLRHVLVVGDAGEFT---SLDALLAAPADLSEPRPDPD-----DVAFFQLSGGTT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLlYAALTHKLVFDHQPGDIFGCVADIGwitgHSY-----VVYGPLCNGATSVLFEStpvyPNAGRYW 252
Cdd:COG1021 197 GLPKLIPRTHDDYL-YSVRASAEICGLDADTVYLAALPAA----HNFplsspGVLGVLYAGGTVVLAPD----PSPDTAF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 253 ETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GS---------VGEPINCeaweWLHRVVG-------- 312
Cdd:COG1021 268 PLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLqvgGAklspelarrVRPALGC----TLQQVFGmaeglvny 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 313 ----DSRCTLVDTwwQtetgGiciapRPSEEGAEILpamamrpffgIVpvlmDEKGS-VVEGSnvSGALcisqawpgMAR 387
Cdd:COG1021 342 trldDPEEVILTT--Q----G-----RPISPDDEVR----------IV----DEDGNpVPPGE--VGEL--------LTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 388 ---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 454
Cdd:COG1021 387 gpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 455 PESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 532
Cdd:COG1021 458 HDAAVVAMPDEYLGERSCAFVVPRGEP----LTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
23-529 |
6.68e-43 |
|
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: 159.08 E-value: 6.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05903 5 SELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcPTVqhvlvaHRTDNKVHMGDldvpleqemakedpvcapesmgseDMLFMLYTSGSTGMPKG 182
Cdd:cd05903 80 -------------------PER------FRQFDPAAMPD------------------------AVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTqAGYLLYA--ALTHKLVFDhqPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKI 260
Cdd:cd05903 111 VMHS-HNTLSASirQYAERLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREHGV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPINC----EAWEWLHRVVgdsrctlVDTWWQTETGGICIAP 334
Cdd:cd05903 184 TFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVPRslarRAAELLGAKV-------CSAYGSTECPGAVTSI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 RPSEEGAeilpAMAM--RPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMartIYGDHQRfVDAYFKAYP-GYYFTG 411
Cdd:cd05903 253 TPAPEDR----RLYTdgRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSV---FLGYLDR-PDLTADAAPeGWFRTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 412 DGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQE 490
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALlTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 358248211 491 LKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05903 402 LD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-529 |
8.53e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 160.46 E-value: 8.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFnQGL 102
Cdd:PRK07656 34 AELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVL-GLF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGgrvvelkkiVDEAVKHC-PTVQHVlVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK07656 113 LG---------VDYSATTRlPALEHV-VICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIV--HTQAgYLLYAALTHKLvfDHQPGD----------IFGCVAdiGWITghsyvvygPLCNGATsVLFEstPVYpNAG 249
Cdd:PRK07656 183 GAMltHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA--------PLMRGAT-ILPL--PVF-DPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 250 RYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPInceAWEWLHRVVGDSRCTLVDTWWQ-TETG 328
Cdd:PRK07656 246 EVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM---PVALLERFESELGVDIVLTGYGlSEAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 GI-CIAPRpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCIS-----QAWPGM----ARTIYGDhqrfvd 398
Cdd:PRK07656 321 GVtTFNRL--DDDRKTVAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLVRgpnvmKGYYDDpeatAAAIDAD------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 399 ayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVK 478
Cdd:PRK07656 392 -------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLK 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 358248211 479 DSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK07656 465 PGAE---LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
24-536 |
2.53e-42 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 161.79 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLR 103
Cdd:PLN03052 213 ELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 GGRVVELKKIVDEAvkHCPTVQhVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPES-----MGSEDMLFMLYTSGSTG 178
Cdd:PLN03052 293 GGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEykaveQPVEAFTNILFSSGTTG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 179 MPKGIVHTQAGYLLYAALT--HklvFDHQPGDIFGCVADIGWITGHsYVVYGPLCNGATSVLFESTPVYPNAGRYwetVE 256
Cdd:PLN03052 370 EPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF---VQ 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgdSRCT---LVDTWWQTETG 328
Cdd:PLN03052 443 DAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWLM-----SRAGykpIIEYCGGTELG 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 GICIAP---RPSEEGAEILPAMAMRPFfgivpvLMDEKGSVVEgSNVSG----ALCisqawPGM----ARTIYGDHQrfv 397
Cdd:PLN03052 511 GGFVTGsllQPQAFAAFSTPAMGCKLF------ILDDSGNPYP-DDAPCtgelALF-----PLMfgasSTLLNADHY--- 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 DAYFKAYPGYYFT-----GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI-ADHPAVPESAVIGYPHDIKGEAA 471
Cdd:PLN03052 576 KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEQ 655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 472 FAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVP----DEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 536
Cdd:PLN03052 656 LVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVLRQQLAQELS 724
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
23-528 |
6.37e-41 |
|
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: 154.81 E-value: 6.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd17651 24 AELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGseDMLFMLYTSGSTGMPKG 182
Cdd:cd17651 99 -----------------------HPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDAD--DLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IV--HTQAGYLLYAaltHKLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNGATSVLfESTPVYPNAGRYWETVERLKI 260
Cdd:cd17651 154 VVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAGATLVL-PPEEVRTDPPALAAWLDEQRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAW--EWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSE 338
Cdd:cd17651 229 SRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTEDlrEFCAGLPG---LRLHNHYGPTETHVVTALSLPGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 339 EGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCIsqAWPGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGA 414
Cdd:cd17651 304 PAAWPAPPPIGRPIDNTRVYVLDAALRPVPP-GVPGELYI--GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 415 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSM 494
Cdd:cd17651 381 RWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAA 457
|
490 500 510
....*....|....*....|....*....|....
gi 358248211 495 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd17651 458 LATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
23-527 |
1.78e-40 |
|
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: 153.13 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnQGL 102
Cdd:cd12117 26 AELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT--DRS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDVPLEQEMAKEDPVCApesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd12117 104 LAGRAGGLEVAVV--------------------------IDEALDAGPAGNPAVPV----SPDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLlyaalthKLVFDH-----QPGDIFGCVADIGWiTGHSYVVYGPLCNGATSVLFE-STPVYPNAGRywETVE 256
Cdd:cd12117 154 VAVTHRGVV-------RLVKNTnyvtlGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPkGTLLDPDALG--ALIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFY--------------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGSvGEPINCeawewlhrvVGDSRCTLVDTW 322
Cdd:cd12117 224 EEGVTVLWltaalfnqladedpECFAGLRELLTGGEVVSPPHVRRVLAACPG-LRLVNG---------YGPTENTTFTTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 323 WQTetggiciaPRPSEEGAEILPAmamRPFFGIVPVLMDEKGSVVE-GsnVSGALCISQAwpGMARTIYGD----HQRFV 397
Cdd:cd12117 294 HVV--------TELDEVAGSIPIG---RPIANTRVYVLDEDGRPVPpG--VPGELYVGGD--GLALGYLNRpaltAERFV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 DAYFKayPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:cd12117 359 ADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 358248211 476 VvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd12117 437 V-----AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
23-527 |
2.26e-40 |
|
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: 152.40 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFnqgl 102
Cdd:cd05945 20 RELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIAD---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmGDldvpleqemakedpvcapesmgseDMLFMLYTSGSTGMPKG 182
Cdd:cd05945 96 -------------------------------------GD------------------------DNAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIgwitghS-----YVVYGPLCNGATSVLFESTpVYPNAGRYWETVER 257
Cdd:cd05945 115 VQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALASGATLVPVPRD-ATADPKQLFRFLAE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICIAPRPS 337
Cdd:cd05945 187 HGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFPDAR--IYNTYGPTEATVAVTYIEVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 338 EE---GAEILPAMamRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTiYGDHQRFVDAYFKAYPGY--YFTGD 412
Cdd:cd05945 263 PEvldGYDRLPIG--YAKPGAKLVILDEDGRPVPP-GEKGELVISG--PSVSKG-YLNNPEKTAAAFFPDEGQraYRTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 413 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsaGDSDVVVQELK 492
Cdd:cd05945 337 LVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP--GAEAGLTKAIK 414
|
490 500 510
....*....|....*....|....*....|....*
gi 358248211 493 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05945 415 AELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
9-529 |
9.69e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 153.57 E-value: 9.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 9 PWDRFHFLHFAphgrELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgFSAESLAGRIN 88
Cdd:PRK07529 52 PLDRPETWTYA----ELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPL-LEPEQIAELLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 89 DAKCKVVITfnqgLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTD--------------NKVHMGDLDvpLEQEMAKE- 153
Cdd:PRK07529 127 AAGAKVLVT----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARylpgpkrlavplirRKAHARILD--FDAELARQp 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 154 -DPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGD----------IFGCVAdigwitgh 222
Cdd:PRK07529 201 gDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV-------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 223 syVVYGPLCNGATSVLfeSTPV-YPNAG---RYWETVERLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRTLGSVGEP 298
Cdd:PRK07529 272 --TGLAPLARGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 299 INCEAWEWLHRVVGdsrCTLVDTWWQTE-TGGICIAPR--PSEEGA--EILPAMAMRpffgIVPVlmDEKGSVVEGSNVS 373
Cdd:PRK07529 345 LPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPdgERRIGSvgLRLPYQRVR----VVIL--DDAGRYLRDCAVD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 374 --GALCISQA--WPGMARtiyGDHQRfvDAYFkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 449
Cdd:PRK07529 416 evGVLCIAGPnvFSGYLE---AAHNK--GLWL--EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 450 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK07529 489 RHPAVALAAAVGRPDAHAGELPVAYVQLKP---GASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
.
gi 358248211 529 K 529
Cdd:PRK07529 566 R 566
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
23-459 |
1.52e-39 |
|
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: 148.95 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQg 101
Cdd:TIGR01733 3 RELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggrvvelkkivdeavkHCPTVQHVLVAHrtdnkVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTSGSTGMPK 181
Cdd:TIGR01733 82 ------------------LASRLAGLVLPV-----ILLDPLELAALDDAPAPPPPDAPS--GPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGyLLYAALTHKLVFDHQPGDIfgcvadigWITGHSYV-------VYGPLCNGATSVLFESTPVYPNAGRYWET 254
Cdd:TIGR01733 137 GVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 255 VERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICIA- 333
Cdd:TIGR01733 208 IAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTVWSTAt 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 334 --PRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDAYFKAYPGY 407
Cdd:TIGR01733 281 lvDPDDAPRESPVPIG--RPLANTRLYVLDDDLRPV-PVGVVGELYIGG--PGVARGYLNRpeltAERFVPDPFAGGDGA 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 358248211 408 --YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 459
Cdd:TIGR01733 356 rlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
23-527 |
6.01e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 150.11 E-value: 6.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqg 101
Cdd:PRK08314 39 RELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggrVVELKKIVDEAVKHCPtVQHVLVAHRTDN-KVHMGD-----LDVPLEQEMAKEDPVCA------------PESMG 163
Cdd:PRK08314 115 -----GSELAPKVAPAVGNLR-LRHVIVAQYSDYlPAEPEIavpawLRAEPPLQALAPGGVVAwkealaaglappPHTAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 164 SEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF---- 239
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMprwd 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 240 -EStpvypnAGRyweTVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTL 318
Cdd:PRK08314 268 rEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTG---LDY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 319 VDTWWQTETggicIAP-------RPSEEGAEIlpamamrPFFGIVPVLMD----------EKGSVVegsnVSGALCISQA 381
Cdd:PRK08314 334 VEGYGLTET----MAQthsnppdRPKLQCLGI-------PTFGVDARVIDpetleelppgEVGEIV----VHGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 382 WPGMART----IYGDHQRFvdayFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 457
Cdd:PRK08314 399 WNRPEATaeafIEIDGKRF----FR-------TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 458 AVIGYPHDIKGEAAFAFIVVKDSAGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK08314 468 CVIATPDPRRGETVKAVVVLRPEARGK-TTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
51-536 |
1.19e-38 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 148.43 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 51 MPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTV-----Q 125
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVlpaagE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 126 HVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQ 205
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 206 PGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYwetVERLKINQFYGAPTAVRLLLKYGDAWVKKYD 285
Cdd:PLN03051 159 PGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 286 RSSLRTLGSVGEPINCEAWEWLHRVVGDSRcTLVDTWWQTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLMDEKG- 364
Cdd:PLN03051 235 WSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQA---PGAFSTASLGTRFVLLNDNGv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 365 SVVEGSNVSGALCISQAWPGMA-RTIYGDHQRfvdAYFKAYPGYYFT-------GDGAYRTEGGYYQITGRMDDVINISG 436
Cdd:PLN03051 311 PYPDDQPCVGEVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 437 HRLGTAEIEDAI-ADHPAVPESAVIGYPhDIKGEAAFAFIVVKDS-------AGDSDVVVQELKSMVATKIAKYAVPDEI 508
Cdd:PLN03051 388 IKTSSVEIERACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGeekkgfdQARPEALQKKFQEAIQTNLNPLFKVSRV 466
|
490 500
....*....|....*....|....*...
gi 358248211 509 LVVKRLPKTRSGKVMRRLLRKIITSEAQ 536
Cdd:PLN03051 467 KIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
23-528 |
5.86e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 146.76 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK13391 28 RELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLD--VPLEQEMAK--EDPVcAPESMGSEdmlfMLYTSGSTG 178
Cdd:PRK13391 108 ---------DVARALLKQCPGVRHRLVLDGD------GELEgfVGYAEAVAGlpATPI-ADESLGTD----MLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 179 MPKGIvhtqagyllYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPL--------CN-----GATSVLFESTpvy 245
Cdd:PRK13391 168 RPKGI---------KRPLPEQPP-DTPLPLTAFLQRLWGFRSDMVYLSPAPLyhsapqraVMlvirlGGTVIVMEHF--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 pNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAwewlhrvvgDSRCTLVDtWW-- 323
Cdd:PRK13391 235 -DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAP--CPP---------QVKEQMID-WWgp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 324 -------QTETGGICiAPRPSEEGAEilPAMAMRPFFGIVPVLMDekgsvvegsnvSGALCIsqawPGMARTIYGDHQR- 395
Cdd:PRK13391 302 iiheyyaATEGLGFT-ACDSEEWLAH--PGTVGRAMFGDLHILDD-----------DGAELP----PGEPGTIWFEGGRp 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 FVdaYFK----------AYPGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIG 461
Cdd:PRK13391 364 FE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISG---GVniypQEAENLLITHPKVADAAVFG 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 462 YPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK13391 438 VPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
24-529 |
2.32e-37 |
|
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: 143.48 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINdakckvvitfnqglR 103
Cdd:cd05974 5 EMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD--------------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 GGRVVelkKIVDEAVKhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgSEDMLFMLYTSGSTGMPKGI 183
Cdd:cd05974 71 GGAVY---AAVDENTH--------------------------------------------ADDPMLLYFTSGTTSKPKLV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQAGYLLyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVypNAGRYWETVERLKINQF 263
Cdd:cd05974 104 EHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYGVTTL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 264 YGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGIcIAPRPseeGAEI 343
Cdd:cd05974 181 CAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP---GQPV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 344 LPAMAMRPFFGIVPVLMDEKGSVVEGSNVsgALCISQAWP-GMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGGYY 422
Cdd:cd05974 250 KAGSMGRPLPGYRVALLDPDGAPATEGEV--ALDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDEDGYL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 423 QITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKY 502
Cdd:cd05974 325 TYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPY 404
|
490 500
....*....|....*....|....*..
gi 358248211 503 AVPDEiLVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05974 405 KRIRR-LEFAELPKTISGKIRRVELRR 430
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
24-527 |
2.60e-37 |
|
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: 143.39 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglr 103
Cdd:cd05935 6 ELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvELkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGMPKGI 183
Cdd:cd05935 82 -----EL------------------------------------------------------DDLALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF-----ESTPvypnagrywETVERL 258
Cdd:cd05935 103 MHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL---------ELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 259 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETggiCIAPRPSE 338
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTET---MSQTHTNP 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 339 EGAEILPAMAMrPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAYPGYYF-TGDGAYRT 417
Cdd:cd05935 245 PLRPKLQCLGI-P*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIKGRRFFrTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 418 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsAGDSDVVVQELKSMVAT 497
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYRGKVTEEDIIEWARE 400
|
490 500 510
....*....|....*....|....*....|
gi 358248211 498 KIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05935 401 QMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
23-527 |
5.76e-37 |
|
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: 143.20 E-value: 5.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd12116 16 AELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivDEAvkhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd12116 91 ------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYL-LYAALTHKLVFdhQPGDIFGCVADIGW-ITGHSyvVYGPLCNGATSVLFESTPVYpNAGRYWETVERLKI 260
Cdd:cd12116 144 VVVSHRNLVnFLHSMRERLGL--GPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIAPRETQR-DPEALARLIEAHSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFYGAPTAVRLLLKYGdaWvkkYDRSSLRTL-GsvGEPinceawewLHRVVGDSRCTLVDTWWQ----TETGGICIAPR 335
Cdd:cd12116 219 TVMQATPATWRMLLDAG--W---QGRAGLTALcG--GEA--------LPPDLAARLLSRVGSLWNlygpTETTIWSTAAR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 336 PSEEGAeilPAMAMRPFFGIVPVLMDEKG-SVVEGsnVSGALCIsqAWPGMARTIYGD----HQRFVDAYFkAYPG--YY 408
Cdd:cd12116 284 VTAAAG---PIPIGRPLANTQVYVLDAALrPVPPG--VPGELYI--GGDGVAQGYLGRpaltAERFVPDPF-AGPGsrLY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 409 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAfAFIVVKD-SAGDSDvv 487
Cdd:cd12116 356 RTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAgAAPDAA-- 432
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 358248211 488 vqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd12116 433 --ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
24-522 |
1.00e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 144.03 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQglr 103
Cdd:PRK06178 63 ELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQ--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvveLKKIVdEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED--------------PVCAPESMGSEDMLF 169
Cdd:PRK06178 140 ------LAPVV-EQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAaagaidllpalracTAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 170 ML-YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNA 248
Cdd:PRK06178 213 ALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARW----DA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 249 GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVG-----EPINCEAWewlHRVVGdsrCTLVDT-W 322
Cdd:PRK06178 289 VAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVVSfvkklNPDYRQRW---RALTG---SVLAEAaW 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 323 WQTETGGICIAPRPSEEGAEILPAmamRPFFGIVPV------LMDEKGSVVEGSNVSGALCISQawPGMARTIYG----D 392
Cdd:PRK06178 361 GMTETHTCDTFTAGFQDDDFDLLS---QPVFVGLPVpgtefkICDFETGELLPLGAEGEIVVRT--PSLLKGYWNkpeaT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 393 HQRFVDayfkaypGYYFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 471
Cdd:PRK06178 436 AEALRD-------GWLHTGDiGKI-DEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVP 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 358248211 472 FAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPdEILVVKRLPKTRSGKV 522
Cdd:PRK06178 508 VAFVQLKP---GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV 554
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-535 |
1.73e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 142.88 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI---TFn 99
Cdd:PRK13295 59 RELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVvpkTF- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 qglrggRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM 179
Cdd:PRK13295 138 ------RGFDHAAMARRLRPELPALRHVVVVGGDGADSFEALLITPAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQ----AGYLLYAALthklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEStpvypnagryWETV 255
Cdd:PRK13295 212 PKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDI----------WDPA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETG 328
Cdd:PRK13295 277 RAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAPIPGALVERARAALG---AKIVSAWGMTENG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 GIC-IAPRPSEEGAEI-----LPAMAMRpffgIV-----PVLMDEKGS-VVEG-SNVSGALcisqAWPGMARTiygdhqr 395
Cdd:PRK13295 351 AVTlTKLDDPDERASTtdgcpLPGVEVR----VVdadgaPLPAGQIGRlQVRGcSNFGGYL----KRPQLNGT------- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 fvDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:PRK13295 416 --DA-----DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 476 VVKDSAG-DSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEA 535
Cdd:PRK13295 489 VPRPGQSlDFEEMVEFLKA---QKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
23-527 |
2.31e-36 |
|
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: 141.88 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI-NDAKCKVVITFNQG 101
Cdd:cd05923 32 SELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMTAAVIAVDAQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 ------LRGGRVVELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDVPLEQEMAKEDPVCAPESMGsedmlFMLYTSG 175
Cdd:cd05923 112 vmdaifQSGVRVLALSDLVG--------------------------LGEPESAGPLIEDPPREPEQPA-----FVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 176 STGMPKGIVHTQAgyllyAALTHKLVFDHQPGDIFGC------VADIGWITGHSYVVYGPLCNGATSVLfestPVYPNAG 249
Cdd:cd05923 161 TTGLPKGAVIPQR-----AAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 250 RYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctlVDTWWQTETGG 329
Cdd:cd05923 232 DALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK---VNIYGTTEAMN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 330 ICIAPRPSEEGAeilpamaMRPFFG----IVPVL--MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDayfka 403
Cdd:cd05923 307 SLYMRDARTGTE-------MRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQD----- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 404 ypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGD 483
Cdd:cd05923 375 --GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLS 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 358248211 484 SDvvvqELKSM-VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05923 453 AD----ELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
22-528 |
1.35e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 139.65 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 22 GRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqg 101
Cdd:PRK08276 14 YGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrGGRVVELkkiVDEAVKHCPT-VQHVLVAHrtdnkvhmGDLD--VPLEQEMAKEDPV-CAPESMGSEdmlfMLYTSGST 177
Cdd:PRK08276 90 --SAALADT---AAELAAELPAgVPLLLVVA--------GPVPgfRSYEEALAAQPDTpIADETAGAD----MLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVhtqagyllyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGA-------------TSVLFESTpv 244
Cdd:PRK08276 153 GRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVVVMEKF-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 ypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP----INCEAWEWLHRVVgdsrctlVD 320
Cdd:PRK08276 222 --DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPcpveVKRAMIDWWGPII-------HE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 321 TWWQTETGGICIAprPSEEGAEiLPAMAMRPFFGIVPVLmDEKGSVVEgsnvsgalcisqawPGMARTIY---------- 390
Cdd:PRK08276 293 YYASSEGGGVTVI--TSEDWLA-HPGSVGKAVLGEVRIL-DEDGNELP--------------PGEIGTVYfemdgypfey 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 391 -GDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIGYPHD 465
Cdd:PRK08276 355 hNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVAVFGVPDE 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248211 466 IKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK08276 429 EMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
24-527 |
1.71e-35 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 139.68 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQG-- 101
Cdd:cd05904 37 ELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 -LRGG--RVVelkkIVDEAVKHCptvqhvlvAHRTDNKVHMGDLDVPleQEMAKEDPVCApesmgsedmlfMLYTSGSTG 178
Cdd:cd05904 117 kLASLalPVV----LLDSAEFDS--------LSFSDLLFEADEAEPP--VVVIKQDDVAA-----------LLYSSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 179 MPKGIVHTQAGYLLYAALTHKLV-FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVlfestpVYP--NAGRYWETV 255
Cdd:cd05904 172 RSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVV------VMPrfDLEELLAAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICIAPR 335
Cdd:cd05904 246 ERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVD--LGQGYGMTESTGVVAMCF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 336 PSEEGAE-------ILPAMAMRpffgIVpvlmDEKGSVVEGSNVSGALCISQawPGM-----------ARTIYGDhqrfv 397
Cdd:cd05904 322 APEKDRAkygsvgrLVPNVEAK----IV----DPETGESLPPNQTGELWIRG--PSImkgylnnpeatAATIDKE----- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 dayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 477
Cdd:cd05904 387 --------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVR 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 358248211 478 KdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05904 459 K---PGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
23-527 |
1.89e-35 |
|
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: 138.59 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd17643 16 GELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapesmgsEDMLFMLYTSGSTGMPKG 182
Cdd:cd17643 91 ---------------------------------------------------DP---------DDLAYVIYTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYL-LYAALTHKLVFDHQpgdifgcvaDIgWITGHSYV-------VYGPLCNGATSVLFES----TPVypnagR 250
Cdd:cd17643 111 VVVSHANVLaLFAATQRWFGFNED---------DV-WTLFHSYAfdfsvweIWGALLHGGRLVVVPYevarSPE-----D 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 251 YWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINCEAWE-WLHRVvGDSRCTLVDTWWQTET 327
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRpWAGRF-GLDRPQLVNMYGITET 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 328 ggiCIAPRPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEGSnVSGALCISQawPGMARTIYG----DHQRFVDA 399
Cdd:cd17643 251 ---TVHVTFRPLDAADLPAAAAspigRPLPGLRVYVLDADGRPVPPG-VVGELYVSG--AGVARGYLGrpelTAERFVAN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 400 YFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYpHDIKGEAAFAFIVV 477
Cdd:cd17643 325 PFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVR-EDEPGDTRLVAYVV 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 358248211 478 KDSAgdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17643 403 ADDG--AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-556 |
2.49e-34 |
|
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: 139.22 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:COG1020 505 AELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLT----- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:COG1020 580 ------------QSA----------LAARLPELGVPVLALDALALAAEPATNPPVPV---TPDDLAYVIYTSGSTGRPKG 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVADIG-----WitghsyVVYGPLCNGATSVLFESTPVyPNAGRYWETVE 256
Cdd:COG1020 635 VMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSfdasvW------EIFGALLSGATLVLAPPEAR-RDPAALAELLA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrCTLVDTWWQTETGGICIA--P 334
Cdd:COG1020 706 RHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLPG--ARLVNLYGPTETTVDSTYyeV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 RPSEEGAEILP---AMA----------MRPffgiVPVlmdekgsvvegsNVSGALCIsqAWPGMARTIYGDH----QRFV 397
Cdd:COG1020 779 TPPDADGGSVPigrPIAntrvyvldahLQP----VPV------------GVPGELYI--GGAGLARGYLNRPeltaERFV 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 DAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIKGEAAFAFI 475
Cdd:COG1020 841 ADPF-GFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARE-DAPGDKRLVAY 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 476 VVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 555
Cdd:COG1020 919 VV--PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALL 996
|
.
gi 358248211 556 V 556
Cdd:COG1020 997 L 997
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
23-528 |
6.99e-34 |
|
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: 134.03 E-value: 6.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd17649 16 AELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvQHvlvahrtdnkvhmgdldvpleqemakedpvcaPESMGsedmlFMLYTSGSTGMPKG 182
Cdd:cd17649 91 ----------------------HH--------------------------------PRQLA-----YVIYTSGSTGTPKG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAgyllyaALTH-----KLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNGAtSVLFESTPVYPNAGRYWETVER 257
Cdd:cd17649 112 VAVSHG------PLAAhcqatAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCE-AWEWLhrvvgDSRCTLVDTWWQTETGGICIAPRP 336
Cdd:cd17649 184 LGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRWL-----KAPVRLFNAYGPTEATVTPLVWKC 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 337 SEEGAEILPAMAM-RPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG----DHQRFV-DAYFKAYPGYYFT 410
Cdd:cd17649 258 EAGAARAGASMPIgRPLGGRSAYILDADLNPVP-VGVTGELYI--GGEGLARGYLGrpelTAERFVpDPFGAPGSRLYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 411 GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIkGEAAFAFIVVKDSAGDSDvVVQE 490
Cdd:cd17649 335 GDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQPE-LRAQ 412
|
490 500 510
....*....|....*....|....*....|....*...
gi 358248211 491 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd17649 413 LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
24-546 |
1.64e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.49 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT---FNQ 100
Cdd:PRK06087 54 ALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlFKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 101 glrggrvVELKKIVDEAVKHCPTVQHVLVAhrtdNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 180
Cdd:PRK06087 134 -------TRPVDLILPLQNQLPQLQQIVGV----DKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAGYLL----YAALTHkLVFDhqpgDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVE 256
Cdd:PRK06087 203 KGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF----TPDACLALLE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINC----EAWEwlHRVVgdsrctLVDTWWQTETggici 332
Cdd:PRK06087 274 QQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIPKkvarECQQ--RGIK------LLSVYGSTES----- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 333 APR---PSEEGAEILPAMAMRPFFGI-VPVLMDEKGSV---VEGSNVSGAlcisqawPGMARTIYGDHQ---RFVDAyfk 402
Cdd:PRK06087 339 SPHavvNLDDPLSRFMHTDGYAAAGVeIKVVDEARKTLppgCEGEEASRG-------PNVFMGYLDEPEltaRALDE--- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 403 ayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSag 482
Cdd:PRK06087 409 --EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP-- 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 483 DSDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQELGDTTTLED 546
Cdd:PRK06087 485 HHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI---MRRLTQDVCEEI 546
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
23-527 |
3.23e-33 |
|
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: 132.78 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfNQGL 102
Cdd:cd17646 27 RELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT-TADL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKivdeavkhcPTVQHVLVAHRTDnkvhmGDLDVPLeqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd17646 106 AARLPAGGDV---------ALLGDEALAAPPA-----TPPLVPP----------------RPDNLAYVIYTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAG---YLLYaaLTHKlvFDHQPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFEstpvyPNAGR---YW-ETV 255
Cdd:cd17646 156 VMVTHAGivnRLLW--MQDE--YPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVAR-----PGGHRdpaYLaALI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERLKINQFYGAPTAVRLLLkygdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETgGICIAPR 335
Cdd:cd17646 226 REHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAARFLALPG---AELHNLYGPTEA-AIDVTHW 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 336 PSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG----DHQRFVDAYFKAYPGYYFTG 411
Cdd:cd17646 298 PVRGPAETPSVPIGRPVPNTRLYVLDDALRPVP-VGVPGELYL--GGVQLARGYLGrpalTAERFVPDPFGPGSRMYRTG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 412 DGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdSAGDSDVVVQEL 491
Cdd:cd17646 375 DLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVP--AAGAAGPDTAAL 452
|
490 500 510
....*....|....*....|....*....|....*.
gi 358248211 492 KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17646 453 RAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
25-529 |
2.73e-32 |
|
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: 130.29 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 25 LLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRg 104
Cdd:TIGR03098 31 LSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERLD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 105 grvvelkkIVDEAVKHCPTVQHVLvahRTDNKVHMGDLDVPLE----QEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 180
Cdd:TIGR03098 110 --------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEEpaswPKLLALGDADPPHPVIDSDMAAILYTSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAGYLLYA-ALTHKLvfDHQPGDIFGCVADIGWITGHSYVVYGpLCNGATSVLFEstpvYPNAGRYWETVERLK 259
Cdd:TIGR03098 179 KGVVLSHRNLVAGAqSVATYL--ENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHD----YLLPRDVLKALEKHG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 260 INQFYGAPTAVRLLLKygDAWvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVdtWWQTETGGICIAP----- 334
Cdd:TIGR03098 252 ITGLAAVPPLWAQLAQ--LDW-PESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLM--YGLTEAFRSTYLPpeevd 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 -RPSEEGAEIlpamamrPFFGIvpVLMDEKGSVVEgSNVSGALCisQAWPGMARTIYGDHQRfVDAYFKAYPGYY----- 408
Cdd:TIGR03098 327 rRPDSIGKAI-------PNAEV--LVLREDGSECA-PGEEGELV--HRGALVAMGYWNDPEK-TAERFRPLPPFPgelhl 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 409 -----FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEaafAFIVVKDSAGD 483
Cdd:TIGR03098 394 pelavWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQ---AIVLVVTPPGG 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 358248211 484 SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:TIGR03098 471 EELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
23-527 |
3.14e-32 |
|
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: 129.12 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd17650 16 RELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapesmgsEDMLFMLYTSGSTGMPKG 182
Cdd:cd17650 91 ---------------------------------------------------QP---------EDLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYL-LYAALTHKLVFDHQPGDIFGcvadigwITGHSYVVYG-----PLCNGATSVLFESTPVYpNAGRYWETVE 256
Cdd:cd17650 111 VMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFDVFAgdfarSLLNGGTLVICPDEVKL-DPAALYDLIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPIncEAWEWLHRVVGdSRCTLVDTWWQTETggiCIAP 334
Cdd:cd17650 183 KSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QDFKTLAARFG-QGMRIINSYGVTEA---TIDS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 RPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYGD----HQRFVDAYFKAYPG 406
Cdd:cd17650 255 TYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQP-VGVAGELYIGGA--GVARGYLNRpeltAERFVENPFAPGER 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 407 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgYPHDIKGEAAFAFIVVKDSAGDSdv 486
Cdd:cd17650 332 MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEARLCAYVVAAATLNT-- 408
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248211 487 vvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17650 409 --AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
23-529 |
6.69e-32 |
|
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: 128.18 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqg 101
Cdd:cd05941 15 ADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSGSTGMPK 181
Cdd:cd05941 90 ----------------------------------------------------------------DPALILYTSGTTGRPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGylLYA---ALTHKLVFdhQPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlFESTPvYPNAGRYWETVERL 258
Cdd:cd05941 106 GVVLTHAN--LAAnvrALVDAWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGAS---VEFLP-KFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 259 KINQFYGAPTAVRLLLKYGDAWVKKYD---RSSLRTL-----GSVGEPINC-EAWEWL--HRvvgdsrctLVDTWWQTET 327
Cdd:cd05941 178 SITVFMGVPTIYTRLLQYYEAHFTDPQfarAAAAERLrlmvsGSAALPVPTlEEWEAItgHT--------LLERYGMTEI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 328 GGICIAP-----RPSEEGAEiLPAMAMRpffgivpVLMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQRFVDAyFK 402
Cdd:cd05941 250 GMALSNPldgerRPGTVGMP-LPGVQAR-------IVDEETGEPLPRGEV-GEIQV--RGPSVFKEYWNKPEATKEE-FT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 403 AyPGYYFTGDGAYRTEGGYYQITGRM-DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSA 481
Cdd:cd05941 318 D-DGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA--VVVLRA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 358248211 482 GDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05941 395 GAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
13-543 |
1.33e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 129.00 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 13 FHFLHFAPHGRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 92
Cdd:PRK06710 43 LHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 93 KVVITFNqgLRGGRVVELKK-------IVDEAVKHCPTVQHVL---VAHRTDNKV------HMGDLDVPLEQEM-AKEDP 155
Cdd:PRK06710 123 KVILCLD--LVFPRVTNVQSatkiehvIVTRIADFLPFPKNLLypfVQKKQSNLVvkvsesETIHLWNSVEKEVnTGVEV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 156 VCAPESmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGD--IFGcVADIGWITGHSYVVYGPLCNG 233
Cdd:PRK06710 201 PCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEevVLG-VLPFFHVYGMTAVMNLSIMQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 234 ATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVG- 312
Cdd:PRK06710 276 YKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGg 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 313 ----------DSRCTLVDTWWQTETGGICIAPRPSEEG--AEILPAMAMRPffgivpvlmDEKGSVVegsnVSGALCISQ 380
Cdd:PRK06710 350 klvegyglteSSPVTHSNFLWEKRVPGSIGVPWPDTEAmiMSLETGEALPP---------GEIGEIV----VKGPQIMKG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 381 AW--PGMARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 458
Cdd:PRK06710 417 YWnkPEETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 459 VIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLrkiITSEAQEL 538
Cdd:PRK06710 484 TIGVPDPYRGETVKAFVVLKE---GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL---IEEEKRKN 557
|
....*
gi 358248211 539 GDTTT 543
Cdd:PRK06710 558 EDEQT 562
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-530 |
1.95e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 128.12 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 96
Cdd:PRK07788 78 AELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 97 TFNqglrggrvvELKKIVDEAVKHCPTVqHVLVAHrTDNKVHMGDLDVPLEQEMAKED--PVCAPESMGSedmlFMLYTS 174
Cdd:PRK07788 152 YDD---------EFTDLLSALPPDLGRL-RAWGGN-PDDDEPSGSTDETLDDLIAGSStaPLPKPPKPGG----IVILTS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 175 GSTGMPKGIVHTQAGYLLYAALthklVFDHQP---GDIFGCVADIGWITGHSYVVYGpLCNGATSVL---FestpvypNA 248
Cdd:PRK07788 217 GTTGTPKGAPRPEPSPLAPLAG----LLSRVPfraGETTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrF-------DP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 249 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLvdtWWQTETG 328
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNL---YGSTEVA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 GICIApRPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPgMARTIYGDHQRFVDayfkaypGYY 408
Cdd:PRK07788 362 FATIA-TPED--LAEAPGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNGFP-FEGYTDGRDKQIID-------GLL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 409 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVV 488
Cdd:PRK07788 430 SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP---GAALDE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 358248211 489 QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 530
Cdd:PRK07788 507 DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
23-521 |
3.15e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 127.31 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItFNQGL 102
Cdd:PRK07798 32 AELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALV-YEREF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rGGRVVELKkivDEavkhCPTVQHVL-VAHRTDNKVHMGDldVPLEQEMAKEDPVCAPESmGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK07798 111 -APRVAEVL---PR----LPKLRTLVvVEDGSGNDLLPGA--VDYEDALAAGSPERDFGE-RSPDDLYLLYTGGTTGMPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGylLYAALTHKLVFDH--QPGDIFGCVADIGWITGHSYVVYGPLCNGAT------------SVLFESTPVYpN 247
Cdd:PRK07798 180 GVMWRQED--IFRVLLGGRDFATgePIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafaalfsgqTVVLLPDVRF-D 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 AGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrcT 317
Cdd:PRK07798 257 ADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIASGGALFSPSVKEALLELLPNV--V 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 318 LVDTWWQTETG--GICIAPRPSEEGAeilpamamRPFFGIVP--VLMDEKGSVVE-GSNVSGALcisqawpgmART---- 388
Cdd:PRK07798 325 LTDSIGSSETGfgGSGTVAKGAVHTG--------GPRFTIGPrtVVLDEDGNPVEpGSGEIGWI---------ARRghip 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 389 --IYGDHQRfVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPH 464
Cdd:PRK07798 388 lgYYKDPEK-TAETFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPD 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 465 DIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 521
Cdd:PRK07798 467 ERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
23-527 |
1.40e-29 |
|
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: 121.66 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd12115 28 AELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd12115 103 ------------------------------------------------------------DPDDLAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 --IVHTQAGYLLYAALTH-------------KLVFDHQPGDIFGcvadigwitghsyvvygPLCNGATSVLFESTPVYPN 247
Cdd:cd12115 123 vaIEHRNAAAFLQWAAAAfsaeelagvlastSICFDLSVFELFG-----------------PLATGGKVVLADNVLALPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 AGRYWETVerlKINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTET 327
Cdd:cd12115 186 LPAAAEVT---LINT---VPSAAAELLRHDAL------PASVRVVNLAGEPLPRDLVQRLYARLQVER--VVNLYGPSED 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 328 ---GGICIAPRPSEEGAEIlpamaMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGD----HQRFVDAY 400
Cdd:cd12115 252 ttySTVAPVPPGASGEVSI-----GRPLANTQAYVLDRALQPV-PLGVPGELYIGGA--GVARGYLGRpgltAERFLPDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 401 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPEsAVIGYPHDIKGEAAF-AFIVVKD 479
Cdd:cd12115 324 FGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVVAIGDAAGERRLvAYIVAEP 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 358248211 480 SAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd12115 403 GAA---GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
23-529 |
1.42e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 122.58 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:PRK07786 46 RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT----- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rGGRVVELKKIVDEAVkhcPTVQHVLVA-HRTDNKVhmgdldVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK07786 121 -EAALAPVATAVRDIV---PLLSTVVVAgGSSDDSV------LGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGyLLYAALTHKLVFDHQPGDifgcvaDIGWITGHSYVVYGpLCNGATSVLFESTPV-YP----NAGRYWETVE 256
Cdd:PRK07786 191 GAVLTHAN-LTGQAMTCLRTNGADINS------DVGFVGVPLFHIAG-IGSMLPGLLLGAPTViYPlgafDPGQLLDVLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRLLLkyGDAWVKKYDRSsLRTLGSVGEPinceAWEWLHRVVGDS--RCTLVDTWWQTETGGI-CI- 332
Cdd:PRK07786 263 AEKVTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAP----ASDTLLRQMAATfpEAQILAAFGQTEMSPVtCMl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 333 ----APRPSEEGAEILPAMAMRpffgIVPVLMDE--KGSVVEgsnvsgalcISQAWPGMARTIYGDHQRFVDAYfkaYPG 406
Cdd:PRK07786 336 lgedAIRKLGSVGKVIPTVAAR----VVDENMNDvpVGEVGE---------IVYRAPTLMSGYWNNPEATAEAF---AGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 407 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsaGDSDV 486
Cdd:PRK07786 400 WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN--DDAAL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 358248211 487 VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK07786 478 TLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
23-530 |
1.75e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 122.57 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqGL 102
Cdd:PRK12583 49 RQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAD-AF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVElkkIVDEAVKHCPTVQHVLVAH----RTDNKVHMGDLDVP---LEQEMAKEDPVCAPE-------SMGSEDML 168
Cdd:PRK12583 128 KTSDYHA---MLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflAWHELQARGETVSREalaerqaSLDRDDPI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 169 FMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDHqpgdifgcvadiGWITGHSY--------VVYGPL--CNGAT--- 235
Cdd:PRK12583 205 NIQYTSGTTGFPKG-----------ATLSHHNILNN------------GYFVAESLgltehdrlCVPVPLyhCFGMVlan 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 236 --SVLFESTPVYPN----AGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPinCEAwEWLHR 309
Cdd:PRK12583 262 lgCMTVGACLVYPNeafdPLATLQAVEEERCTALYGVPTMFIAELDHPQ--RGNFDLSSLRTGIMAGAP--CPI-EVMRR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 310 VVGDSRCTLVD-TWWQTETGGICIA-------PRPSEEGAEILPAMAMRpffgivpvLMDEKGSVVEGSNVsGALC---- 377
Cdd:PRK12583 337 VMDEMHMAEVQiAYGMTETSPVSLQttaaddlERRVETVGRTQPHLEVK--------VVDPDGATVPRGEI-GELCtrgy 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 378 -ISQAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 452
Cdd:PRK12583 408 sVMKGYWNNpeatAESIDED-------------GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHP 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248211 453 AVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 530
Cdd:PRK12583 475 AVADVQVFGVPDEKYGEEIVAWVRLHP---GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
23-528 |
3.85e-29 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.94 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK08008 41 LELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKivdeavKHCPtvQHVLVAhRTDNKVHMGDLDvpLEQEMAKEDP-VCAPESMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK08008 121 PMYRQIQQED------ATPL--RHICLT-RVALPADDGVSS--FTQLKAQQPAtLCYAPPLSTDDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQ-----AGYllYAALTHKLVFDhqpgDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEStpvYpNAGRYWETVE 256
Cdd:PRK08008 190 GVVITHynlrfAGY--YSAWQCALRDD----DVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEK---Y-SARAFWGQVC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVR-LLLKYGDAWvkkyDRS-SLRTLG-----SVGEPincEAWEWLHRVvgdsrcTLVDTWWQTETGG 329
Cdd:PRK08008 260 KYRATITECIPMMIRtLMVQPPSAN----DRQhCLREVMfylnlSDQEK---DAFEERFGV------RLLTSYGMTETIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 330 ICIAPRPSEEgaEILPAMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCIsQAWPGmaRTIYGDHQRFVDAYFKAYP--GY 407
Cdd:PRK08008 327 GIIGDRPGDK--RRWPSIG-RPGFCYEAEIRDDHNRPLP-AGEIGEICI-KGVPG--KTIFKEYYLDPKATAKVLEadGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 408 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVV 487
Cdd:PRK08008 400 LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE---TLS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248211 488 VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK08008 477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-537 |
6.05e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.14 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:PRK12316 540 AELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS----- 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPvcAPE-SMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK12316 615 ---------------------QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEE--NPGtELNPENLAYVIYTSGSTGKPK 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTqagyllYAALTHKLVFDHQP-----GDIFGCVADIGWITGHsYVVYGPLCNGATSVLfESTPVYPNAGRYWETVE 256
Cdd:PRK12316 672 GAGNR------HRALSNRLCWMQQAyglgvGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV-AAPGDHRDPAKLVELIN 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLHRVVGD-SRCTLVDTWWQTE-TGGICIAP 334
Cdd:PRK12316 744 REGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEAL---PADAQEQVFAKlPQAGLYNLYGPTEaAIDVTHWT 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 RPSEEGAEILPAmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYG----DHQRFVDAYFKAYPGYYFT 410
Cdd:PRK12316 817 CVEEGGDSVPIG---RPIANLACYILDANLEPVP-VGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAGERMYRT 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 411 GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGyphdIKGEAAFAFIVVKDSAGDsdvVVQE 490
Cdd:PRK12316 891 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGD---WREA 963
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 358248211 491 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 537
Cdd:PRK12316 964 LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-528 |
1.05e-28 |
|
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: 116.99 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 165 EDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFD--HQPGD------------------IFGCVADIGWITGHsy 224
Cdd:cd05917 2 DDVINIQFTSGTTGSPKG-----------ATLTHHNIVNngYFIGErlglteqdrlcipvplfhCFGSVLGVLACLTH-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 225 vvygplcnGATSVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAW 304
Cdd:cd05917 69 --------GATMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 305 EWLHRVVGDSRCTLVdtWWQTETGGICIAPR---PSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALC 377
Cdd:cd05917 136 KRVIEVMNMKDVTIA--YGMTETSPVSTQTRtddSIEKRVNtvgrIMPHTEAK--------IVDPEGGIVPPVGVPGELC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 378 ISQAwpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 457
Cdd:cd05917 206 IRGY--SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDV 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 458 AVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05917 282 QVVGVPDERYGEEVCAWIRLKEGA---ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-528 |
1.43e-28 |
|
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: 118.70 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 29 TCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgfsaeslagRINDAKCKVVITFNQGLRGGRVV 108
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV---------PLNPTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 109 elkkIVDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQE--MAKEDPVCAPESMGsEDMLFMLYTSGSTGMPKGIV-- 184
Cdd:cd05922 74 ----LADAG----------AADRLRDALPASPDPGTVLDADgiRAARASAPAHEVSH-EDLALLLYTSGSTGSPKLVRls 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 185 HTQagyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfESTPVYPNAgrYWETVERLKINQFY 264
Cdd:cd05922 139 HQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 265 GAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTE-TGGICIAPrPSEEGAEi 343
Cdd:cd05922 212 GVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEaTRRMTYLP-PERILEK- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 344 lPAMAMRPFFGIVPVLMDEKGS----------VVEGSNVSGALCISQAWPGMARtiygdhqRFVDAYFkaypgyyfTGDG 413
Cdd:cd05922 285 -PGSIGLAIPGGEFEILDDDGTptppgepgeiVHRGPNVMKGYWNDPPYRRKEG-------RGGGVLH--------TGDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 414 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIKGEAAFAFIVVKDSAGDSDVVVqelks 493
Cdd:cd05922 349 ARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLR----- 422
|
490 500 510
....*....|....*....|....*....|....*
gi 358248211 494 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05922 423 SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
23-525 |
2.28e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 118.84 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK05852 47 RDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRvvelkkivDEAVKHCPtvqhVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMlYTSGSTGMPKG 182
Cdd:PRK05852 127 HDRA--------EPTTRWWP----LTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAMIM-FTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGyllYAALTHKLVFDHQPGDIFGCVADIGWITGHSYV--VYGPLCNGATSVLfestpvyPNAGR-----YWETV 255
Cdd:PRK05852 194 VPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLATLASGGAVLL-------PARGRfsahtFWDDI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVG--------------DSRCTLVDT 321
Cdd:PRK05852 264 KAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAapvvcafgmteathQVTTTQIEG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTETGGICIAPRPSEEGAEIlpaMAMRPFFGIVPVlmDEKGSV-VEGSNVsgalcisqawpgmARTIYGD----HQRF 396
Cdd:PRK05852 344 IGQTENPVVSTGLVGRSTGAQI---RIVGSDGLPLPA--GAVGEVwLRGTTV-------------VRGYLGDptitAANF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 397 VDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 476
Cdd:PRK05852 406 TDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 358248211 477 VKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 525
Cdd:PRK05852 479 PRESAP---PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
23-528 |
2.43e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 119.09 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItFNQgl 102
Cdd:PRK13382 72 RELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVI-YDE-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKV-HMGDLDVPLEQEmakedpvcaPESMGSEDMLFMLyTSGSTGMPK 181
Cdd:PRK13382 149 ------EFSATVDRALADCPQATRIVAWTDEDHDLtVEVLIAAHAGQR---------PEPTGRKGRVILL-TSGTTGTPK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGyllyAALTHKLVFDHQPgdifgcvadigWITGHSYVVYGPL------CNGATSVLFESTPVYPNAGRYWETV 255
Cdd:PRK13382 213 GARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMfhawgfSQLVLAASLACTIVTRRRFDPEATL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERLKINQFYG---APTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrcTLVDTWWQTETGGICI 332
Cdd:PRK13382 278 DLIDRHRATGlavVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYNATEAGMIAT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 333 ApRPSEEGAEilPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMARTIYGDHQRFVDAYFKA-----YPGY 407
Cdd:PRK13382 355 A-TPADLRAA--PDTAGRPAEGTEIRILDQDFREVP--------------TGEVGTIFVRNDTQFDGYTSGstkdfHDGF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 408 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVV 487
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK---PGASAT 494
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248211 488 VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK13382 495 PETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
23-527 |
4.82e-28 |
|
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: 117.37 E-value: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd12114 16 GELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkiVDEAVKHCPTVQHVLVahrtdnkvhmgDLDVPLEQEMAKEDPVCAPEsmgseDMLFMLYTSGSTGMPKG 182
Cdd:cd12114 91 -----------DGPDAQLDVAVFDVLI-----------LDLDALAAPAPPPPVDVAPD-----DLAYVIFTSGSTGTPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVA----DIGwitghSYVVYGPLCNGATSVLfestpvyPNAGR-----YW 252
Cdd:cd12114 144 VMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATLVL-------PDEARrrdpaHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 253 -ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGDsrCTLVDTWWQTEtGGIC 331
Cdd:cd12114 210 aELIERHGVTLWNSVPALLEMLLDVLEAAQALL--PSLRLVLLSGDWIPLDLPARLRALAPD--ARLISLGGATE-ASIW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 332 -----IAPRPsEEGAEI-----LPAMAMRpffgivpvLMDEKGS-VVEGsnVSGALCISQAwpGMARTIYGDHQRFVDAY 400
Cdd:cd12114 285 siyhpIDEVP-PDWRSIpygrpLANQRYR--------VLDPRGRdCPDW--VPGELWIGGR--GVALGYLGDPELTAARF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 401 FKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDikGEAAFAFIVVK 478
Cdd:cd12114 352 VTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--GGKRLAAFVVP 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 358248211 479 DSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd12114 430 DNDGTPI-APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-528 |
5.11e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.78 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 22 GRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItFNQG 101
Cdd:PRK06188 40 YGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLI-VDPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 LRGGRVVELkkivdeaVKHCPTVQHVLVahrtdnkvhMGDLD--VPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM 179
Cdd:PRK06188 119 PFVERALAL-------LARVPSLKHVLT---------LGPVPdgVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQAGYLLYAALthklvfdhqpgdifgCVADIGWITGHSYVVYGPLCNGAtsvlfeSTPVYP------------- 246
Cdd:PRK06188 183 PKGVMGTHRSIATMAQI---------------QLAEWEWPADPRFLMCTPLSHAG------GAFFLPtllrggtvivlak 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 247 -NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN----CEAwewlHRVVGDsrcTLVDT 321
Cdd:PRK06188 242 fDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSpvrlAEA----IERFGP---IFAQY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTETGgICIAPRPSEEGAEILPAM---AMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQawPGMArtiygdhqrfvD 398
Cdd:PRK06188 313 YGQTEAP-MVITYLRKRDHDPDDPKRltsCGRPTPGLRVALLDEDGREVAQGEV-GEICVRG--PLVM-----------D 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 399 AYFKAyP---------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 469
Cdd:PRK06188 378 GYWNR-PeetaeafrdGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGE 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 470 AAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK06188 457 AVTAVVVLRP---GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
21-529 |
5.56e-28 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 117.93 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 21 HGRELlettcRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTVIFAGFsAESLAGRINDAKCKVVI--- 96
Cdd:PRK06018 46 HDRAL-----KVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINHAEDRVVItdl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 97 TFnqglrggrVVELKKIVDeavkHCPTVQHVLVAhrTDnKVHMGDLDVP----LEQEMAKEDPVCAPESMGSEDMLFMLY 172
Cdd:PRK06018 120 TF--------VPILEKIAD----KLPSVERYVVL--TD-AAHMPQTTLKnavaYEEWIAEADGDFAWKTFDENTAAGMCY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 173 TSGSTGMPKGIVHTQAGYLLYAALTHKlvfdhqpGDIFGCVA-DI-----------GW-------ITGHSYVVYGPLCNG 233
Cdd:PRK06018 185 TSGTTGDPKGVLYSHRSNVLHALMANN-------GDALGTSAaDTmlpvvplfhanSWgiafsapSMGTKLVMPGAKLDG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 234 ATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinceawEWLHRVVGD 313
Cdd:PRK06018 258 AS--------VY-------ELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP------RSMIKAFED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 314 SRCTLVDTWWQTET---GGICIAPRPSEE--GAEILPAMAM--RPFFGIVPVLMDEKG-SVVEGSNVSGALCISQawPGM 385
Cdd:PRK06018 317 MGVEVRHAWGMTEMsplGTLAALKPPFSKlpGDARLDVLQKqgYPPFGVEMKITDDAGkELPWDGKTFGRLKVRG--PAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 386 ARTIYGDHQRFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 465
Cdd:PRK06018 395 AAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 466 IKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK06018 470 KWDERPLLIVQLKP---GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
23-529 |
7.22e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 117.01 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqgl 102
Cdd:cd12118 33 RQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkiVDEAvkhcptvqhvlvaHRTDNKVHMGDLDVPLEQemakedpvcaPESmgSEDMLFMLYTSGSTGMPKG 182
Cdd:cd12118 107 -----------VDRE-------------FEYEDLLAEGDPDFEWIP----------PAD--EWDPIALNYTSGTTGRPKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAG-YL--LYAALTHKLvfDHQPG-----DIFGCVadiGWItghsyVVYGPLCNGATSVLFESTpvypNAGRYWET 254
Cdd:cd12118 151 VVYHHRGaYLnaLANILEWEM--KQHPVylwtlPMFHCN---GWC-----FPWTVAAVGGTNVCLRKV----DAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 255 VERLKINQFYGAPTAVRLLLKYGDAWVKKYD-RSSLRTLGSVGEPINCEAWEWLHRVVgdsrctlVDTWWQTETGG---I 330
Cdd:cd12118 217 IEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDV-------THVYGLTETYGpatV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 331 CI---------------------APRPSEEGAEILPAMAMRPffgiVPVLMDEKGSVV-EGSNV-SGALCISQAwpgmar 387
Cdd:cd12118 290 CAwkpewdelpteerarlkarqgVRYVGLEEVDVLDPETMKP----VPRDGKTIGEIVfRGNIVmKGYLKNPEA------ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 388 tiygdhqrfVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 467
Cdd:cd12118 360 ---------TAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKW 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248211 468 GEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd12118 429 GEVPCAFVELKEGA---KVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
24-536 |
8.32e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 116.83 E-value: 8.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglr 103
Cdd:PRK09088 27 ELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvelkkivDEAVKhcptvqhvlvAHRTDnkvhMGDLDVpLEQEMAKEDPVCAPeSMGSEDMLFMLYTSGSTGMPKGI 183
Cdd:PRK09088 101 -----------DDAVA----------AGRTD----VEDLAA-FIASADALEPADTP-SIPPERVSLILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHT----QAGYLLYAALTHklvFDHQpgDIFGCVADIGWITGHSYVVYGPLCNGAT---SVLFEstpvyPNAGRYWETVE 256
Cdd:PRK09088 154 MLSernlQQTAHNFGVLGR---VDAH--SSFLCDAPMFHIIGLITSVRPVLAVGGSilvSNGFE-----PKRTLGRLGDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQFYGAPTAVRLLLKYGDawvkkYDRSSLRTLGSV---GEPINCEAWE-WLhrvvgDSRCTLVDTWWQTETGGICI 332
Cdd:PRK09088 224 ALGITHYFCVPQMAQAFRAQPG-----FDAAALRHLTALftgGAPHAAEDILgWL-----DDGIPMVDGFGMSEAGTVFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 333 APRPSEEGAEILPAMAMrPFFGIVPVLMDEKGSVVEgSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAypGYYFTGD 412
Cdd:PRK09088 294 MSVDCDVIRAKAGAAGI-PTPTVQTRVVDDQGNDCP-AGVPGELLLRG--PNLSPGYWRRPQATARAFTGD--GWFRTGD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 413 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELK 492
Cdd:PRK09088 368 IARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA---PLDLERIR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 358248211 493 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 536
Cdd:PRK09088 445 SHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
169-529 |
1.31e-27 |
|
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: 113.58 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 169 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVfdhqpgdifGCVADIGW--------ITGHSYVVYGPLCNGATSVLFE 240
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---------GFGGGDSWllslplyhVGGLAILVRSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 241 STPVYPNAGRYWETVERLkinqfygAPTAVRLLLKYG--DAWVKkydrsSLRTLGSVGEPINCEawewLHRVVGDSRCTL 318
Cdd:cd17630 75 NQALAEDLAPPGVTHVSL-------VPTQLQRLLDSGqgPAALK-----SLRAVLLGGAPIPPE----LLERAADRGIPL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 319 VDTWWQTETGGICIAPRPSEEGA----EILPAMAMRpffgivpvlmdekgsVVEGsnvsGALCISQAWPGMARTIYGDHQ 394
Cdd:cd17630 139 YTTYGMTETASQVATKRPDGFGRggvgVLLPGRELR---------------IVED----GEIWVGGASLAMGYLRGQLVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 395 RFVDayfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 474
Cdd:cd17630 200 EFNE------DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 475 IVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd17630 274 IV-----GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
24-530 |
2.32e-27 |
|
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: 116.09 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLR 103
Cdd:cd17642 49 EYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggRVVELKKIVdeavkhcPTVQHVLVahrTDNKVHMGDLDVpLEQEMAKEDPVC-------APESMGSEDMLFMLYTSGS 176
Cdd:cd17642 129 --KVLNVQKKL-------KIIKTIII---LDSKEDYKGYQC-LYTFITQNLPPGfneydfkPPSFDRDEQVALIMNSSGS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIvhtqagyllyaALTHKLV---FDHQPGDIFGC-----VADIGWITGHS----YVVYGPLCNGATSVL---FES 241
Cdd:cd17642 196 TGLPKGV-----------QLTHKNIvarFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRVVLmykFEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 242 TpvypnagRYWETVERLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrcTLVDT 321
Cdd:cd17642 265 E-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLP--GIRQG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTE-TGGICIAP----RPSEEGAeilpamaMRPFFGIVPVLMDEKGSVveGSNVSGALCISQawPGMARTIYGDHQRF 396
Cdd:cd17642 334 YGLTEtTSAILITPegddKPGAVGK-------VVPFFYAKVVDLDTGKTL--GPNERGELCVKG--PMIMKGYVNNPEAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 397 VDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFiv 476
Cdd:cd17642 403 KALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAV-- 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 477 vkdsagdsdVVVQELKSMVATKIAKYaVPDEILVVKRL----------PKTRSGKVMRRLLRKI 530
Cdd:cd17642 479 ---------VVLEAGKTMTEKEVMDY-VASQVSTAKRLrggvkfvdevPKGLTGKIDRRKIREI 532
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1-530 |
2.44e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 116.01 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 1 MRRRKERQPwDRfHFLHFAPHGR---ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 77
Cdd:PRK06155 27 LARQAERYP-DR-PLLVFGGTRWtyaEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 78 FSAESLAGRINDAKCKVVITFNQGLrggrvvELKKIVDEAVKHCPTVqhVLVAHRTDNKVHMGDLDVPLEQEMAkedPVC 157
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVEAALL------AALEAADPGDLPLPAV--WLLDAPASVSVPAGWSTAPLPPLDA---PAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 158 APESMGSeDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALThklvfdhqpgdifgcVADIGWITGHSYVVYGPL------- 230
Cdd:PRK06155 174 AAAVQPG-DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLPLfhtnaln 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 231 ------CNGATSVLfesTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvKKYDR-SSLRTLGSVGEPINcea 303
Cdd:PRK06155 238 affqalLAGATYVL---EPRF-SASGFWPAVRRHGATVTYLLGAMVSILLSQPA---RESDRaHRVRVALGPGVPAA--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 304 wewLHRVVGDsRC--TLVDTWWQTETGGICIAPRPSEEgaeilPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQA 381
Cdd:PRK06155 308 ---LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGSQR-----PGSMGRLAPGFEARVVDEHDQELP-DGEPGELLLRAD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 382 WPG-MARTIYGDHQRFVDAYFKAYpgyYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 460
Cdd:PRK06155 378 EPFaFATGYFGMPEKTVEAWRNLW---FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVF 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 461 GYPHDIKGEAAFAFIVVKD-SAGDSDVVVQELKSMvatkIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 530
Cdd:PRK06155 455 PVPSELGEDEVMAAVVLRDgTALEPVALVRHCEPR----LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-527 |
6.61e-27 |
|
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: 113.96 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtVIFAgfsaeslagrindakckvvitfnqgL 102
Cdd:cd05920 44 RELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLA-------------------------L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVD--EAVkhcptvqhVLVAHRTdnkvHMGDLDVPLEQEMAKEDPvcapesmgseDMLFMLYTSGSTGMP 180
Cdd:cd05920 97 PSHRRSELSAFCAhaEAV--------AYIVPDR----HAGFDHRALARELAESIP----------EVALFLLSGGTTGTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAGYLLYAALTHKLV-FDHQpgDIFGCVADIGwitgHSYV-----VYGPLCNGATSVLFEStpvyPNAGRYWET 254
Cdd:cd05920 155 KLIPRTHNDYAYNVRASAEVCgLDQD--TVYLAVLPAA----HNFPlacpgVLGTLLAGGRVVLAPD----PSPDAAFPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 255 VERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTEtGGICIAp 334
Cdd:cd05920 225 IEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALARRVPPVLG---CTLQQVFGMAE-GLLNYT- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 RPsEEGAEILPAMAMRPffgIVP----VLMDEKGSVVeGSNVSGALcisqawpgMAR---TIYGdhqrfvdaYFKAyP-- 405
Cdd:cd05920 298 RL-DDPDEVIIHTQGRP---MSPddeiRVVDEEGNPV-PPGEEGEL--------LTRgpyTIRG--------YYRA-Peh 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 406 --------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 477
Cdd:cd05920 356 naraftpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 358248211 478 KDSAGDSDVVVQELKSMvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05920 436 RDPPPSAAQLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
23-532 |
6.63e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 113.90 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:PRK03640 31 MELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivDEAVKHcptvqhvlvAHRTDNKVHMGDLdvpleQEMAKEDPVcaPESMGSEDMLF-MLYTSGSTGMPK 181
Cdd:PRK03640 106 ------------DDDFEA---------KLIPGISVKFAEL-----MNGPKEEAE--IQEEFDLDEVAtIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGYLlYAALTHKLVFDHQPGDIFGCVADIGWITGHSY----VVYGplcngATSVLFESTpvypNAGRYWETVER 257
Cdd:PRK03640 158 GVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSIlmrsVIYG-----MRVVLVEKF----DAEKINKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAV-RLLLKYGDAwvkKYDrSSLRT--LGsvGEPIN------CEAWewlhrvvgdsRCTLVDTWWQTETg 328
Cdd:PRK03640 228 GGVTIISVVSTMLqRLLERLGEG---TYP-SSFRCmlLG--GGPAPkplleqCKEK----------GIPVYQSYGMTET- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 giC--IAPRPSEEGAEILPAmAMRPFFGI--------VPVLMDEKGS-VVEGSNV-SGALCISQAwpgmartiygDHQRF 396
Cdd:PRK03640 291 --AsqIVTLSPEDALTKLGS-AGKPLFPCelkiekdgVVVPPFEEGEiVVKGPNVtKGYLNREDA----------TRETF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 397 VDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 476
Cdd:PRK03640 358 QDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 477 VkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 532
Cdd:PRK03640 431 K-----SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-529 |
7.44e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 111.80 E-value: 7.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 164 SEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAtSVLFESTP 243
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 244 VYPNAGRY---WETVERLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLV 319
Cdd:cd05944 79 GYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVELRARFEDATG---LPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 320 DTWWQTETggICIAPRPSEEGAEILPAMAMR-PFFGIVPVLMDEKGSVVE--GSNVSGALCIsqAWPGMAR-TIYGDHQR 395
Cdd:cd05944 151 EGYGLTEA--TCLVAVNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRdcAPDEVGEICV--AGPGVFGgYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 FVDAYfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:cd05944 227 NAFVA----DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 476 VVKDSAgdsDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05944 303 QLKPGA---VVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
30-528 |
9.09e-27 |
|
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: 113.63 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 30 CRLANTLKRHGVHRG----DRVAIYMPVSPLAvaamlacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrgg 105
Cdd:cd05929 12 FHQRRLLLLDVYSIAlnrnARAAAAEGVWIAD--------GVYIYLINSILTVFAAAAAWKCGACPAYKSSR-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 106 rvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvh 185
Cdd:cd05929 76 ---APRAEACAIIEIKAAALVCGLF--TGGGALDGLEDYEAAEGGSPETPI-EDEAAGWK----MLYSGGTTGRPKGI-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 186 tqagyllyaalthKLVFDHQPGD---IFGCVADIGWITGHSYVVYGPL-------------CNGATSVLFESTpvypNAG 249
Cdd:cd05929 144 -------------KRGLPGGPPDndtLMAAALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTLVLMEKF----DPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 250 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAW---EWLHrvvgdsrctlvdtWW--- 323
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAP--CPPWvkeQWID-------------WGgpi 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 324 ------QTETGGICIAprpseEGAEILpamamrpffgivpvlmDEKGSVveGSNVSGALCI-----SQAWPGMARTIYgd 392
Cdd:cd05929 272 iweyygGTEGQGLTII-----NGEEWL----------------THPGSV--GRAVLGKVHIldedgNEVPPGEIGEVY-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 393 hqrFVDAYFKAYPGYYF-------------TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 459
Cdd:cd05929 327 ---FANGPGFEYTNDPEktaaarneggwstLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 460 IGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:cd05929 404 VGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
23-529 |
2.24e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 112.83 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI---TFN 99
Cdd:PRK07470 36 REIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIchaDFP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 QGLRGGRVVELK---KIVDEAVKHCPTVQHVLVAHRtDNKVHMGDLDvpleqemaKEDPvcapesmgsedmLFMLYTSGS 176
Cdd:PRK07470 116 EHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD--------HDDP------------CWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIV--HTQAGYLLyaalTHKLVfDHQPGdifgcvadigwITGH--SYVVyGPL---------CN---GATSVLFE 240
Cdd:PRK07470 175 TGRPKAAVltHGQMAFVI----TNHLA-DLMPG-----------TTEQdaSLVV-APLshgagihqlCQvarGAATVLLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 241 STPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrcTLVD 320
Cdd:PRK07470 238 SERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGK---VLVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 321 TWWQTE-TGGICIAPrPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVeGSNVSGALCISqawpGMArtIYGDHQR 395
Cdd:PRK07470 311 YFGLGEvTGNITVLP-PALHDAEDGPDARIgtcgFERTGMEVQIQDDEGREL-PPGETGEICVI----GPA--VFAGYYN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 FVDAYFKAYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 474
Cdd:PRK07470 383 NPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAV 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 475 IVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK07470 463 CVARDGA---PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
23-528 |
3.11e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 112.53 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItFNQGL 102
Cdd:PRK06164 39 AELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV-VWPGF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGgrvVELKKIVDEAVKHC-PTVQHVLVAHRTDNKVH---MGDLDVPLEQEMAKEDPVCAPESmGSEDMLFMLY-TSGST 177
Cdd:PRK06164 118 KG---IDFAAILAAVPPDAlPPLRAIAVVDDAADATPapaPGARVQLFALPDPAPPAAAGERA-ADPDAGALLFtTSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLLYAALTHKlVFDHQPGDIFGCVADIGWITGHSYVVyGPLCNGATSVLFestPVYpNAGRYWETVER 257
Cdd:PRK06164 194 SGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-GALAGGAPLVCE---PVF-DAARTARALRR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVG-EPINCEAWEW-------LHRVVGDSR------CTLVDTWW 323
Cdd:PRK06164 268 HRVTHTFGNDEMLRRILDTAGE---RADFPSARLFGFASfAPALGELAALarargvpLTGLYGSSEvqalvaLQPATDPV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 324 QT--ETGGiciapRPSEEGAEilpamamrpffgiVPVLMDEKGSVVEgSNVSGALCISQawPGMARTiYGDHQrfvDAYF 401
Cdd:PRK06164 345 SVriEGGG-----RPASPEAR-------------VRARDPQDGALLP-DGESGEIEIRA--PSLMRG-YLDNP---DATA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 402 KAYP--GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAfAFIVVKD 479
Cdd:PRK06164 400 RALTddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTD 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 358248211 480 SAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSG---KVMRRLLR 528
Cdd:PRK06164 479 GASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-558 |
4.47e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.90 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVvel 110
Cdd:PRK12316 4588 RLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPI--- 4664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 111 kkivdeavkhcPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAkedpvcapesmgsEDMLFMLYTSGSTGMPKGivhtqagy 190
Cdd:PRK12316 4665 -----------PDGLASLALDRDEDWEGFPAHD-PAVRLHP-------------DNLAYVIYTSGSTGRPKG-------- 4711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 191 llyAALTHK--LVFDHQPGDIFGCVADIGWITGHSYV-------VYGPLCNGAtSVLFESTPVYPNAGRYWETVE-RLKI 260
Cdd:PRK12316 4712 ---VAVSHGslVNHLHATGERYELTPDDRVLQFMSFSfdgshegLYHPLINGA-SVVIRDDSLWDPERLYAEIHEhRVTV 4787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFygAPTAVRLLLKyGDAwvKKYDRSSLRTLGSVGEPIN----CEAWE-----WLHRVVGDSRCTLVDTWWQTETGGIC 331
Cdd:PRK12316 4788 LVF--PPVYLQQLAE-HAE--RDGEPPSLRVYCFGGEAVAqasyDLAWRalkpvYLFNGYGPTETTVTVLLWKARDGDAC 4862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 332 iaprpseeGAEILPAMamRPFFGIVPVLMDEKGSV----VEGSNVSGALCISQAW---PGMARtiygdhQRFVDAYFKAY 404
Cdd:PRK12316 4863 --------GAAYMPIG--TPLGNRSGYVLDGQLNPlpvgVAGELYLGGEGVARGYlerPALTA------ERFVPDPFGAP 4926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 405 PG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIkGEAAFAFIVVKDSA-G 482
Cdd:PRK12316 4927 GGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPAlA 5005
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 483 DSDVV----VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDTTTLED--PSIIAEIL 554
Cdd:PRK12316 5006 DADEAqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQayVAPRSELEQqvAAIWAEVL 5085
|
....
gi 358248211 555 SVYQ 558
Cdd:PRK12316 5086 QLER 5089
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
19-529 |
7.55e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 111.61 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 19 APHGREL----LETTCR-LANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 93
Cdd:PLN02246 45 GATGRVYtyadVELLSRrVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 94 VVITfnqglrGGRVVElkKIVDEAvkHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAK-----EDPVCAPesmgsedml 168
Cdd:PLN02246 125 LIIT------QSCYVD--KLKGLA--EDDGVTVVTIDDPPEGCLHFSELTQADENELPEveispDDVVALP--------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 169 fmlYTSGSTGMPKGIVhtqagyllyaaLTHK-LV-------------FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGA 234
Cdd:PLN02246 186 ---YSSGTTGLPKGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 235 TSVL---FEstpvypnAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLHRVV 311
Cdd:PLN02246 252 AILImpkFE-------IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKE----LEDAF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 312 GDS--RCTLVDTWWQTETG---GICiaprpseegaeilPAMAMRPFfgivPVLMDEKGSVVE---------------GSN 371
Cdd:PLN02246 319 RAKlpNAVLGQGYGMTEAGpvlAMC-------------LAFAKEPF----PVKSGSCGTVVRnaelkivdpetgaslPRN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 372 VSGALCI--SQAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTA 442
Cdd:PLN02246 382 QPGEICIrgPQIMKGylndpeaTANTIDKD-------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 443 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 522
Cdd:PLN02246 449 ELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV---RSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKI 525
|
....*..
gi 358248211 523 MRRLLRK 529
Cdd:PLN02246 526 LRKDLRA 532
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
23-533 |
1.27e-25 |
|
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: 110.32 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05918 28 AELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLT----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakEDPvcapesmgsEDMLFMLYTSGSTGMPKG 182
Cdd:cd05918 103 --------------------------------------------------SSP---------SDAAYVIFTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLyAALTHKLVFDHQPGD--------IFG-CVADIgwitghsyvvYGPLCNGAT------SVLFESTPvypn 247
Cdd:cd05918 124 VVIEHRALST-SALAHGRALGLTSESrvlqfasyTFDvSILEI----------FTTLAAGGClcipseEDRLNDLA---- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 agrywETVERLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVGEPIN---CEAWEwlhrvvgdSRCTLVDT 321
Cdd:cd05918 189 -----GFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGGEALTqsdVDTWA--------DRVRLINA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTET--GGICIAPRPSEEGAEILPAMAMRPFfgIV-PVLMDE---KGSVvegsnvsGALCISQawPGMARTIYGDHQR 395
Cdd:cd05918 245 YGPAECtiAATVSPVVPSTDPRNIGRPLGATCW--VVdPDNHDRlvpIGAV-------GELLIEG--PILARGYLNDPEK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 ----FV-DAYFKAYPGY------YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY-- 462
Cdd:cd05918 314 taaaFIeDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvk 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 463 PHDIKGEAAF-AFIVVKDSAGDSD--------------VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05918 394 PKDGSSSPQLvAFVVLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
....*.
gi 358248211 528 RKIITS 533
Cdd:cd05918 474 RELAES 479
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
23-528 |
1.35e-25 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 110.88 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVItfn 99
Cdd:PRK07059 52 GELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 qglrggrVVE-LKKIVDEAVKHCPtVQHVLVAHrtdnkvhMGDL-----------------DVP---LEQEMAKEDPVCA 158
Cdd:PRK07059 126 -------VLEnFATTVQQVLAKTA-VKHVVVAS-------MGDLlgfkghivnfvvrrvkkMVPawsLPGHVRFNDALAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 159 -------PESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYL---LYAALTHKLVFDHQPGD---IFGCVADIgwitghsYV 225
Cdd:PRK07059 191 garqtfkPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPL-------YH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 226 VYGPLCN-------GATSVLFestpvyPN----AGRYWEtVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR-TLG 293
Cdd:PRK07059 264 IFALTVCgllgmrtGGRNILI------PNprdiPGFIKE-LKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIvANG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 294 ---SVGEPInceAWEWLHRvvgdSRCTLVDTWWQTETGGICIA--------------PRPSEEgaeilpaMAMRpffgiv 356
Cdd:PRK07059 335 ggmAVQRPV---AERWLEM----TGCPITEGYGLSETSPVATCnpvdatefsgtiglPLPSTE-------VSIR------ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 357 pvlmDEKGSVVEGSNVsGALCIS--QAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGR 427
Cdd:PRK07059 395 ----DDDGNDLPLGEP-GEICIRgpQVMAGywnrpdeTAKVMTAD-------------GFFRTGDVGVMDERGYTKIVDR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 428 MDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDE 507
Cdd:PRK07059 457 KKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA----LTEEDVKAFCKERLTNYKRPKF 532
|
570 580
....*....|....*....|.
gi 358248211 508 ILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK07059 533 VEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
23-529 |
1.38e-25 |
|
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: 109.32 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqgl 102
Cdd:cd17653 26 GELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKEDPVCApesmgsedmlfmLYTSGSTGMPKG 182
Cdd:cd17653 103 ------------------------------------------------SPDDLAYI------------IFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGW--ITGhsyVVYGPLCNGATSVLfeSTPVYPnagryWETVERlKI 260
Cdd:cd17653 123 VMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCNGGTLVL--ADPSDP-----FAHVAR-TV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 NQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPINCE-AWEWLHRVV-----GDSRCTLVDTWWQTETGgiciap 334
Cdd:cd17653 191 DALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEAVPPSlLDRWSPGRRlynayGPTECTISSTMTELLPG------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 335 RPSEEGAEIlPAMAMRpffgivpvLMDE-KGSVVEGsnVSGALCISQawPGMARTIYGDHQRFVDAY--FKAYPG--YYF 409
Cdd:cd17653 257 QPVTIGKPI-PNSTCY--------ILDAdLQPVPEG--VVGEICISG--VQVARGYLGNPALTASKFvpDPFWPGsrMYR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 410 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVIgyphdIKGEAAFAFIVvkdsagDSDVVV 488
Cdd:cd17653 324 TGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI-----VVNGRLVAFVT------PETVDV 392
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248211 489 QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd17653 393 DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
443-521 |
4.83e-25 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 98.39 E-value: 4.83e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 443 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 521
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-558 |
8.53e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.05 E-value: 8.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglr 103
Cdd:PRK12316 3087 ELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS------ 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDldvPLEQEMAKEDPvcaPESMGSEDMLFMLYTSGSTGMPKGI 183
Cdd:PRK12316 3161 --------------------QSHLRLPLAQGVQVLDLD---RGDENYAEANP---AIRTMPENLAYVIYTSGSTGKPKGV 3214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNGATSVLfESTPVYPNAGRYWETVERLKINQF 263
Cdd:PRK12316 3215 GIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSEGVDVL 3291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 264 YGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEpinceAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEI 343
Cdd:PRK12316 3292 HAYPSMLQAFLEEEDA----HRCTSLKRIVCGGE-----ALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDA 3362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 344 LPAMamRPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMARtiyGDHQR-------FVDAYFKAYPGYYFTGDGAYR 416
Cdd:PRK12316 3363 VPIG--RPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR---GYHNRpgltaerFVPDPFVPGERLYRTGDLARY 3434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 417 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyphDIKGEAAFAFIVVKDSAGDsdvVVQELKSMVA 496
Cdd:PRK12316 3435 RADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGD---LREALKAHLK 3507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 497 TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDTTTLED--PSIIAEILSVYQ 558
Cdd:PRK12316 3508 ASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdyVAPVNELERrlAAIWADVLKLEQ 3573
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
31-528 |
9.65e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 108.26 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGAV-HTV---IFAgfsaESLAGRINDAKCKVV---IT 97
Cdd:PRK07008 51 QLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTInprLFP----EQIAYIVNHAEDRYVlfdLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 98 FnqglrggrvvelKKIVDEAVKHCPTVQHVLVAhrTDnKVHMGDLDVPL---EQEMAKEDPVCAPESMGSEDMLFMLYTS 174
Cdd:PRK07008 121 F------------LPLVDALAPQCPNVKGWVAM--TD-AAHLPAGSTPLlcyETLVGAQDGDYDWPRFDENQASSLCYTS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 175 GSTGMPKGIVHTQAGYLLYA---ALThklvfdhqpgDIFGCVA-DI-----------GW-------ITGHSYVVYGPLCN 232
Cdd:PRK07008 186 GTTGNPKGALYSHRSTVLHAygaALP----------DAMGLSArDAvlpvvpmfhvnAWglpysapLTGAKLVLPGPDLD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 233 GATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSL-RTL--GSVGEPINCEAWEwlhr 309
Cdd:PRK07008 256 GKS--------LY-------ELIEAERVTFSAGVPTVWLGLLNHMREAGLRF--STLrRTVigGSACPPAMIRTFE---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 310 vvGDSRCTLVDTWWQTET---GGICI-----APRPSEEGAEILPAMAmRPFFGIVPVLMDEKGSvvegsnvsgalciSQA 381
Cdd:PRK07008 315 --DEYGVEVIHAWGMTEMsplGTLCKlkwkhSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGR-------------ELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 382 WPGMArtiYGD-HQR---FVDAYFK--AYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 452
Cdd:PRK07008 379 WDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHP 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 453 AVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK07008 456 AVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
3-529 |
1.02e-24 |
|
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: 108.09 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 3 RRKERQPwDR--FHFLHFAPHG------RELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 74
Cdd:cd05931 1 RRAAARP-DRpaYTFLDDEGGReetltyAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 75 FA---GFSAESLAGRINDAKCKVVITfnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHrTDNKvhmgDLDVPleqema 151
Cdd:cd05931 79 PPptpGRHAERLAAILADAGPRVVLT---------TAAALAAVRAFAASRPAAGTPRLLV-VDLL----PDTSA------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 152 keDPVCAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFG----CVADIGWITGhsyvVY 227
Cdd:cd05931 139 --ADWPPP-SPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 228 GPLCNGATSVLFEstpvyPNA-----GRYWETVERLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPIN 300
Cdd:cd05931 211 TPLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 301 CEAwewLHRVV-----------------GDSRCTL------------VDTWWQTETGGICIAPRPSEEGAEILPAMAmRP 351
Cdd:cd05931 285 PAT---LRRFAeafapfgfrpeafrpsyGLAEATLfvsggppgtgpvVLRVDRDALAGRAVAVAADDPAARELVSCG-RP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 352 FFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARtiyGDHQR--FVDAYFKAYP-----GYYFTGDGAYRTEGGYYqI 424
Cdd:cd05931 361 LPDQEVRIVDPETGRELPDGEVGEIWVRG--PSVAS---GYWGRpeATAETFGALAatdegGWLRTGDLGFLHDGELY-I 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 425 TGRMDDVINISGHRLGTAEIEDAIAD-HPAVPESAVigyphdikgeAAFA---------FIVVKDSAGDSDVVVQELKSM 494
Cdd:cd05931 435 TGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPGCV----------AAFSvpddgeerlVVVAEVERGADPADLAAIAAA 504
|
570 580 590
....*....|....*....|....*....|....*....
gi 358248211 495 VATKIAK-YAV-PDEILVVKR--LPKTRSGKVMRRLLRK 529
Cdd:cd05931 505 IRAAVAReHGVaPADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
17-528 |
1.09e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 108.58 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 17 HFAP----HGrELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 92
Cdd:PRK06060 25 FYAAdvvtHG-QIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 93 KVVITfNQGLR----GGRVVELKKIVDEAVKHCPTvqhvlvahrtdnkvhmgDLdvpleqemakedpvcapESMGSEDML 168
Cdd:PRK06060 104 ALVVT-SDALRdrfqPSRVAEAAELMSEAARVAPG-----------------GY-----------------EPMGGDALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 169 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfESTPVYPNA 248
Cdd:PRK06060 149 YATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 249 GRYWETveRLKINQFYGAPTavrLLLKYGDAWVKKYDRSsLRTLGSVGEPINCEAWEWLHRVVGDsrCTLVDTWWQTETG 328
Cdd:PRK06060 228 AAILSA--RFGPSVLYGVPN---FFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 GICIAP-----RPSEEGaEILPAMAMRPffgIVPvlmdekGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAyfka 403
Cdd:PRK06060 300 QTFVSNrvdewRLGTLG-RVLPPYEIRV---VAP------DGTTAGPGVEGDLWVRG--PAIAKGYWNRPDSPVAN---- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 404 yPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGD 483
Cdd:PRK06060 364 -EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATI 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 358248211 484 SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK06060 443 DGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
23-528 |
1.12e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 107.65 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqgL 102
Cdd:PRK07514 32 GDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVV-----C 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIvdeAVKHcpTVQHV--LVAHRTDnkvhmgdldvPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 180
Cdd:PRK07514 107 DPANFAWLSKI---AAAA--GAPHVetLDADGTG----------SLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQaGYLLYAALTHKLVFDHQPGD-------IFgcvadigwitgHSYVVY----GPLCNGATSVL---FESTPV-- 244
Cdd:PRK07514 172 KGAMLSH-GNLLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvatnVALLAGASMIFlpkFDPDAVla 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 -YPNAgryweTVerlkinqFYGAPT-AVRLLlkyGDAWVKKYDRSSLRTLGSVGEPINCEAW-EWLHRVvGDsrcTLVDT 321
Cdd:PRK07514 240 lMPRA-----TV-------MMGVPTfYTRLL---QEPRLTREAAAHMRLFISGSAPLLAETHrEFQERT-GH---AILER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTETGGICIAPRpseEGAEI-------LPAMAMR---PFFGiVPVLMDEKGSV-VEGSNVsgalcisqawpgmartiy 390
Cdd:PRK07514 301 YGMTETNMNTSNPY---DGERRagtvgfpLPGVSLRvtdPETG-AELPPGEIGMIeVKGPNV------------------ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 391 gdhqrfvdayFKAY---P----------GYYFTGDGAYRTEGGYYQITGRMDDVInISG-HRLGTAEIEDAIADHPAVPE 456
Cdd:PRK07514 359 ----------FKGYwrmPektaeefradGFFITGDLGKIDERGYVHIVGRGKDLI-ISGgYNVYPKEVEGEIDELPGVVE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248211 457 SAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKPGAAlDEAAILAALKG----RLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
33-528 |
1.57e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 107.28 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 33 ANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqglrggrvvelkk 112
Cdd:PRK06145 41 AGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL---------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 113 iVDEAVKHCPTVQH---VLVAHRTDNKVHMGDLDVPleqemakedpvCAPESMGSEDMLF-MLYTSGSTGMPKGIVHTqa 188
Cdd:PRK06145 105 -VDEEFDAIVALETpkiVIDAAAQADSRRLAQGGLE-----------IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHS-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 189 gyllYAALTHKlVFDHqpgdifgcVADIGWITGHSYVVYGPLCN-GA-----TSVL-----------FESTPVYpnagry 251
Cdd:PRK06145 171 ----YGNLHWK-SIDH--------VIALGLTASERLLVVGPLYHvGAfdlpgIAVLwvggtlrihreFDPEAVL------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 252 wETVERLKINQFYGAPTAVRLLLKYGDAWvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETggiC 331
Cdd:PRK06145 232 -AAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEKTPESRIRDFTRVFTRAR--YIDAYGLTET---C 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 332 IAPRPSEEGAEI---------LPAMAMRpffgivpvLMDEKGSVVEgSNVSGALCISQawPGMARTIYGDHQRFVDAYFK 402
Cdd:PRK06145 304 SGDTLMEAGREIekigstgraLAHVEIR--------IADGAGRWLP-PNMKGEICMRG--PKVTKGYWKDPEKTAEAFYG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 403 aypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAg 482
Cdd:PRK06145 373 ---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA- 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 358248211 483 dsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK06145 449 --TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
24-529 |
2.91e-24 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 105.12 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVvitfnqglr 103
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGMPKGI 183
Cdd:cd05912 77 -------------------------------------------------------------DDIATIMYTSGTTGKPKGV 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGpLCNGATSVLFESTpvypNAGRYWETVERLKINQF 263
Cdd:cd05912 96 QQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 264 YGAPTAV-RLLLKYGDAWvkkydRSSLRT--LGsvGEPINCEAWEwlhrvvgdsRCT-----LVDTWWQTETGGICIAPR 335
Cdd:cd05912 170 SVVPTMLqRLLEILGEGY-----PNNLRCilLG--GGPAPKPLLE---------QCKekgipVYQSYGMTETCSQIVTLS 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 336 PseEGAEILPAMAMRPFFG----IVPVLMDEKGS---VVEGSNVSGALcisqawpgMARTIYGDhQRFVDAYFKaypgyy 408
Cdd:cd05912 234 P--EDALNKIGSAGKPLFPvelkIEDDGQPPYEVgeiLLKGPNVTKGY--------LNRPDATE-ESFENGWFK------ 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 409 fTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVV 488
Cdd:cd05912 297 -TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-----SERPISE 370
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248211 489 QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05912 371 EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
23-533 |
3.48e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 106.10 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVitFNQG 101
Cdd:PRK06839 31 KQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL--FVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 LRGGRVVELKKIVdeavkhcpTVQHVlvahrtdnkVHMGDLDVPLEQEMAKEDPvcapesmGSEDMLFML-YTSGSTGMP 180
Cdd:PRK06839 109 TFQNMALSMQKVS--------YVQRV---------ISITSLKEIEDRKIDNFVE-------KNESASFIIcYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL---FESTpvypnagRYWETVER 257
Cdd:PRK06839 165 KGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVprkFEPT-------KALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLHRVVGDSRCTLVDTWWQTETggiciAPRP- 336
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEE----LMREFIDRGFLFGQGFGMTET-----SPTVf 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 337 --SEEGAEILPAMAMRP-FFGIVPVLMDEKGSVVEGS----NVSGALCISQAW---PGMARTIYGdhqrfvdayfkaypG 406
Cdd:PRK06839 306 mlSEEDARRKVGSIGKPvLFCDYELIDENKNKVEVGEvgelLIRGPNVMKEYWnrpDATEETIQD--------------G 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 407 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDV 486
Cdd:PRK06839 372 WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS---VL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 358248211 487 VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 533
Cdd:PRK06839 449 IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
23-528 |
3.72e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 105.86 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:PRK13390 28 RQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrVVELKKIVDEAVKHCPTvqHVLVAHRTDNkvhMGDLdvplEQEMAKEDPVCAPESMGSedmlFMLYTSGSTGMPKG 182
Cdd:PRK13390 103 ----SAALDGLAAKVGADLPL--RLSFGGEIDG---FGSF----EAALAGAGPRLTEQPCGA----VMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IvhtqagyllYAALTHKLVfdHQPGDifGCVADIGWITGHSyvvygplcngATSVLFESTPVYPNAGRYW---------- 252
Cdd:PRK13390 166 I---------QPDLPGRDV--DAPGD--PIVAIARAFYDIS----------ESDIYYSSAPIYHAAPLRWcsmvhalggt 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 253 -------------ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP----INCEAWEWLHRVVgdsr 315
Cdd:PRK13390 223 vvlakrfdaqatlGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdVKHAMIDWLGPIV---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 316 ctlVDTWWQTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLmDEKGSVVEGSNVSGALCISQAWPgmaRTIYGDHQR 395
Cdd:PRK13390 299 ---YEYYSSTEAHGMTFIDSPDWLAH---PGSVGRSVLGDLHIC-DDDGNELPAGRIGTVYFERDRLP---FRYLNDPEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:PRK13390 369 TAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVI 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 358248211 476 VVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK13390 449 QLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
24-524 |
5.31e-24 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 104.84 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglr 103
Cdd:TIGR01923 4 DLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 gGRVVELKKIVdeavkhcptvqhVLVAHRTdnkvhmgdldvpleqEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGI 183
Cdd:TIGR01923 78 -DSLLEEKDFQ------------ADSLDRI---------------EAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 VHTQAGYLLYA-ALTHKLVFDhqPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfestpVYPNAgRYWETVERLKINQ 262
Cdd:TIGR01923 130 PHTFRNHYASAvGSKENLGFT--EDDNWLLSLPLYHISGLS-ILFRWLIEGATLRI-----VDKFN-QLLEMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPTAVRLLLKygdawvKKYDRSSLRTLGSVGEPINCEawewLHRVVGDSRCTLVDTWWQTETGGICIAPRPseegaE 342
Cdd:TIGR01923 201 ISLVPTQLNRLLD------EGGHNENLRKILLGGSAIPAP----LIEEAQQYGLPIYLSYGMTETCSQVTTATP-----E 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ILPAM--AMRPFFGI-VPVLMDEKGSVVEgsnvsgalcISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYRTEG 419
Cdd:TIGR01923 266 MLHARpdVGRPLAGReIKIKVDNKEGHGE---------IMVKGANLMKG-YLYQGELTPAFEQQ--GWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 420 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKI 499
Cdd:TIGR01923 334 GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-----SESDISQAKLIAYLTEKL 408
|
490 500
....*....|....*....|....*
gi 358248211 500 AKYAVPDEILVVKRLPKTRSGKVMR 524
Cdd:TIGR01923 409 AKYKVPIAFEKLDELPYNASGKILR 433
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
23-527 |
5.45e-24 |
|
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: 104.64 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFnqgl 102
Cdd:cd17652 16 AELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgSEDMLFMLYTSGSTGMPKG 182
Cdd:cd17652 92 -------------------------------------------------------------PDNLAYVIYTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGY--LLYAALTHklvFDHQPGDifgCVADIGWITGHSYV--VYGPLCNGATSVLFESTPVYPNAGrYWETVERL 258
Cdd:cd17652 111 VVVTHRGLanLAAAQIAA---FDVGPGS---RVLQFASPSFDASVweLLMALLAGATLVLAPAEELLPGEP-LADLLREH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 259 KINQFYGAPTAVrlllkygdAWVKKYDRSSLRTLGSVGEPINCE---AWEWLHRVV---GDSRCTLVDTWWQTETGG--I 330
Cdd:cd17652 184 RITHVTLPPAAL--------AALPPDDLPDLRTLVVAGEACPAElvdRWAPGRRMInayGPTETTVCATMAGPLPGGgvP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 331 CIAPRPSEEGAEILPAmAMRPffgiVPVlmdekgsvvegsNVSGALCIsqAWPGMARTiYGDH-----QRFVDAYFKAyP 405
Cdd:cd17652 256 PIGRPVPGTRVYVLDA-RLRP----VPP------------GVPGELYI--AGAGLARG-YLNRpgltaERFVADPFGA-P 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 406 G--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGD 483
Cdd:cd17652 315 GsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAP 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 358248211 484 SdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17652 395 T---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-210 |
8.41e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 105.57 E-value: 8.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 3 RRKERQPWDRFHFlhfaphgRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAES 82
Cdd:COG1022 31 REKEDGIWQSLTW-------AEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 83 LAGRINDAKCKVVITFNQGLrggrvveLKKiVDEAVKHCPTVQHVLVAhrtDNKVHMGDLDV-PLEQEMAKEDPVCAPE- 160
Cdd:COG1022 104 VAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVL---DPRGLRDDPRLlSLDELLALGREVADPAe 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 161 ------SMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIF 210
Cdd:COG1022 173 learraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRT 227
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
24-553 |
1.45e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.01 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLR 103
Cdd:PRK12467 542 ELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLA 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ------GGRVVELKKIVDEaVKHCPtvqhvlvAHRTDnkvhmgdldVPLEqemakedpvcaPESMGsedmlFMLYTSGST 177
Cdd:PRK12467 622 qlpvpaGLRSLCLDEPADL-LCGYS-------GHNPE---------VALD-----------PDNLA-----YVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWITGHsYVVYGPLCNGATSVLFESTPVYpNAGRYWETVER 257
Cdd:PRK12467 669 GQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALASGATLHLLPPDCAR-DAEAFAALMAD 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLHRVVGDS-RCTLVDTWWQTETGGICIAPRP 336
Cdd:PRK12467 746 QGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEAL---QVDLLARVRALGpGARLINHYGPTETTVGVSTYEL 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 337 SEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARtiyGDHQR-------FVDAYFKAYPG-YY 408
Cdd:PRK12467 819 SDEERDFGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGA--GLAR---GYHRRpaltaerFVPDPFGADGGrLY 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 409 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAGDSD--V 486
Cdd:PRK12467 893 RTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPAAVADGAEhqA 971
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 487 VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEI 553
Cdd:PRK12467 972 TRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAI 1038
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-528 |
1.67e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 104.01 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYM----PVSPLAVAAMlacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 99
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMrndfAFFEAAYAAM----RLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 QGLRGgrvveLKKIVDEAVK--HCPTVQHVLVAHRTDN---KVHMGDLDvpLEQEMAKEDPVCAPESMGSEDMLfmlYTS 174
Cdd:PRK12406 92 DLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISPallTPPAGAID--WEGWLAQQEPYDGPPVPQPQSMI---YTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 175 GSTGMPKGiVHTQAGYLLYAALTHKLVfdhqpGDIFGcvadigWITGHSYVVYGPLcngatsvlFESTP-VYP-NAGRYW 252
Cdd:PRK12406 162 GTTGHPKG-VRRAAPTPEQAAAAEQMR-----ALIYG------LKPGIRALLTGPL--------YHSAPnAYGlRAGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 253 ET---------------VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAwewlhrvvgDSRCT 317
Cdd:PRK12406 222 GVlvlqprfdpeellqlIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAP--CPA---------DVKRA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 318 LVDtWW---------QTETGGICIAprpSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISqawPGMART 388
Cdd:PRK12406 291 MIE-WWgpviyeyygSTESGAVTFA---TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI---AGNPDF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 389 IYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIGYPH 464
Cdd:PRK12406 364 TYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMV-ISG---GVniypAEIEAVLHAVPGVHDCAVFGIPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 465 DIKGEAAFAFIVVKDSAG-DSDVVVQELKSMVAtkiaKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK12406 438 AEFGEALMAVVEPQPGATlDEADIRAQLKARLA----GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
23-527 |
2.88e-23 |
|
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: 102.94 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqgl 102
Cdd:cd17656 17 RELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkHCPTVQhvlvahrTDNKVHMgdldVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd17656 94 -----------------HLKSKL-------SFNKSTI----LLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IV--HTQAGYLLyaalthKLVFDHQPGDIFGCVADIgwiTGHSYVV-----YGPLCNGAT------------SVLFE--- 240
Cdd:cd17656 146 VQleHKNMVNLL------HFEREKTNINFSDKVLQF---ATCSFDVcyqeiFSTLLSGGTlyiireetkrdvEQLFDlvk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 241 ----STPVYPNAgrYWETV--ERLKINQFygaPTAVRLLLKYGDAWVkkydrsslrtlgsvgepINCEAWEWLHRvvgdS 314
Cdd:cd17656 217 rhniEVVFLPVA--FLKFIfsEREFINRF---PTCVKHIITAGEQLV-----------------ITNEFKEMLHE----H 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 315 RCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYGD-- 392
Cdd:cd17656 271 NVHLHNHYGPSETHVVTTYTINPEAEIPELPPIG-KPISNTWIYILDQEQQLQP-QGIVGELYISGA--SVARGYLNRqe 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 393 --HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEA 470
Cdd:cd17656 347 ltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKY 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 471 AFAFIVVKDSAGDSDvvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17656 427 LCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
23-535 |
3.58e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 103.49 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqgl 102
Cdd:PRK08162 47 AETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvELKKIVDEAVKHCPtVQHVLVAHRTDNK----VHMGDLDvpLEQEMAKEDPVCAPESMGSE-DMLFMLYTSGST 177
Cdd:PRK08162 124 ------EFAEVAREALALLP-GPKPLVIDVDDPEypggRFIGALD--YEAFLASGDPDFAWTLPADEwDAIALNYTSGTT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIV-HTQAGYLlyAALTHKLVFDHQPGDI-------FGCVadiGWitGHSYVVygpLCNGATSVLFESTpvypNAG 249
Cdd:PRK08162 195 GNPKGVVyHHRGAYL--NALSNILAWGMPKHPVylwtlpmFHCN---GW--CFPWTV---AARAGTNVCLRKV----DPK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 250 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRS-SLRTLG-----SVGEPINCEAWEWLHrVVGdsrctLVDTW- 322
Cdd:PRK08162 261 LIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPvHAMVAGaappaAVIAKMEEIGFDLTH-VYG-----LTETYg 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 323 ------WQTETGGICIAPR-----------PSEEGAEILPAMAMRPffgiVPVLMDEKGSVVegsnVSGALCISQawpgm 385
Cdd:PRK08162 335 patvcaWQPEWDALPLDERaqlkarqgvryPLQEGVTVLDPDTMQP----VPADGETIGEIM----FRGNIVMKG----- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 386 artiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISG-HRLGTAEIEDAIADHPAVPESAVIGYPH 464
Cdd:PRK08162 402 ----YLKNPKATEEAFAG--GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENISSIEVEDVLYRHPAVLVAAVVAKPD 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 465 DIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRKIITSEA 535
Cdd:PRK08162 475 PKWGEVPCAFVELKDGAS---ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLREQAKSLK 541
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
23-527 |
7.00e-23 |
|
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: 102.02 E-value: 7.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd17655 26 RELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivDEAVKHcptvqhvlvahrtdNKVHMGDLDVpLEQEMAKEDPV--CAPESmGSEDMLFMLYTSGSTGMP 180
Cdd:cd17655 101 ------------QSHLQP--------------PIAFIGLIDL-LDEDTIYHEESenLEPVS-KSDDLAYVIYTSGSTGKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAG-------------------YLLYAALThklvFDHQPGDIFGCVadigwITGHSYVVYG--PLCNGATSVlf 239
Cdd:cd17655 153 KGVMIEHRGvvnlvewankviyqgehlrVALFASIS----FDASVTEIFASL-----LSGNTLYIVRkeTVLDGQALT-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 240 estpvypnagrywETVERLKINQFYGAPTAVRLLlkygdAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVvgDSRCTL 318
Cdd:cd17655 222 -------------QYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGEALSTElAKKIIELF--GTNPTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 319 VDTWWQTETggiCIaprpseeGAEILPAMAMRPFFGIVPV----------LMDEKGSVV-EGsnVSGALCISQAwpGMAR 387
Cdd:cd17655 282 TNAYGPTET---TV-------DASIYQYEPETDQQVSVPIgkplgntriyILDQYGRPQpVG--VAGELYIGGE--GVAR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 388 TiYGDH-----QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 462
Cdd:cd17655 348 G-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIAR 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 463 PHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17655 427 KDEQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-558 |
7.64e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrggrvvel 110
Cdd:PRK12316 2040 RLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT------------- 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 111 kkivDEAVKH---CPTVQHVLvahrtdnkvhmgDLDVPLEQEmakEDPVCAPE-SMGSEDMLFMLYTSGSTGMPKGIVHT 186
Cdd:PRK12316 2107 ----QRHLLErlpLPAGVARL------------PLDRDAEWA---DYPDTAPAvQLAGENLAYVIYTSGSTGLPKGVAVS 2167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 187 QAGYLLYAALTHKlVFDHQPGDifgCVADIGWIT--GHSYVVYGPLCNGAtSVLFESTPVYpNAGRYWETVERLKINQFY 264
Cdd:PRK12316 2168 HGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNGA-RVLIRDDELW-DPEQLYDEMERHGVTILD 2241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 265 GAPTAVRLLLKYGDawvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETggiCIAP-----RPSE- 338
Cdd:PRK12316 2242 FPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPllwkcRPQDp 2313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 339 EGAEILPamamrpffgIVPVLMDEKGSVVEGS------NVSGALCISQAwpGMARTIYG----DHQRFVDAYFKAYPG-Y 407
Cdd:PRK12316 2314 CGAAYVP---------IGRALGNRRAYILDADlnllapGMAGELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErL 2382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 408 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGypHDIKGEAAFAFIVVKDSAGDSDvv 487
Cdd:PRK12316 2383 YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA--QDGASGKQLVAYVVPDDAAEDL-- 2458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 488 VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDTTTLED--PSIIAEILSVYQ 558
Cdd:PRK12316 2459 LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQayVAPQEGLEQrlAAIWQAVLKVEQ 2533
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
170-524 |
1.20e-22 |
|
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: 99.11 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 170 MLYTSGSTGMPKGIV--HTQAgYLLYAALthklvfdhqpgdifgcvADIGWIT-GHSYVVYGPLCN------GATSVLFE 240
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAAW-----------------ADCADLTeDDRYLIINPFFHtfgykaGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 241 STPVYPNA----GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrc 316
Cdd:cd17638 67 GATVVPVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 317 TLVDTWWQTETGGICIApRPSEEgAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNV-SGALCISQAwpgMARTIYGDhqr 395
Cdd:cd17638 143 TVLTAYGLTEAGVATMC-RPGDD-AETVATTCGRACPGFEVRIADDGEVLVRGYNVmQGYLDDPEA---TAEAIDAD--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 fvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:cd17638 215 ----------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFV 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 358248211 476 VVKDSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMR 524
Cdd:cd17638 285 VARPGVTlTEEDVIAWCRE----RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
166-524 |
3.46e-22 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 97.48 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 166 DMLFMLYTSGSTGMPKGIVHTQAGYLLYaalthklvFDHQPGDIFGCVADIGWITG---HSYVVYGplcngATSVLFEST 242
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYG-----AISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 243 PVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctL 318
Cdd:cd17633 68 TFIgqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKNIFPKAN--L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 319 VDTWWQTETGgiCIAPRPSEEGAEilPAMAMRPFFGIVPVLMDEKGSVVegsnvsGALCISQAwpgMARTIYgdhqrfVD 398
Cdd:cd17633 140 IEFYGTSELS--FITYNFNQESRP--PNSVGRPFPNVEIEIRNADGGEI------GKIFVKSE---MVFSGY------VR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 399 AYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvk 478
Cdd:cd17633 201 GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS-- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 358248211 479 dsaGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 524
Cdd:cd17633 279 ---GDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
23-541 |
4.94e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 99.89 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqGL 102
Cdd:PRK08315 47 REFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD-GF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVE-LKKIVDEaVKHC----------PTVQHVLvahRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSE----DM 167
Cdd:PRK08315 126 KDSDYVAmLYELAPE-LATCepgqlqsarlPELRRVI---FLGDEKHPGMLNFDELLALGRAVDDAELAARQATldpdDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 168 LFMLYTSGSTGMPKGivhtqagyllyAALTHK-------LVFDHQ---PGD----------IFGCVadIGwitghsyvVY 227
Cdd:PRK08315 202 INIQYTSGTTGFPKG-----------ATLTHRnilnngyFIGEAMkltEEDrlcipvplyhCFGMV--LG--------NL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 228 GPLCNGATSVlfestpvYPNAG----RYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRT---LGSVGePIn 300
Cdd:PRK08315 261 ACVTHGATMV-------YPGEGfdplATLAAVEEERCTALYGVPTMFIAELDHPD--FARFDLSSLRTgimAGSPC-PI- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 301 ceawEWLHRVVGDSRCTLVdT--WWQTETG-GIC-------IAPRPSEEGaEILPAMAMR---PFFG-IVPVlmdekgsv 366
Cdd:PRK08315 330 ----EVMKRVIDKMHMSEV-TiaYGMTETSpVSTqtrtddpLEKRVTTVG-RALPHLEVKivdPETGeTVPR-------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 367 vegsNVSGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVI----- 432
Cdd:PRK08315 396 ----GEQGELCtrgysVMKGYWNDpektAEAIDAD-------------GWMHTGDLAVMDEEGYVNIVGRIKDMIirgge 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 433 NISghrlgTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVK 512
Cdd:PRK08315 459 NIY-----PREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP---GATLTEEDVRDFCRGKIAHYKIPRYIRFVD 530
|
570 580
....*....|....*....|....*....
gi 358248211 513 RLPKTRSGKVMRRLLRKIItseAQELGDT 541
Cdd:PRK08315 531 EFPMTVTGKIQKFKMREMM---IEELGLQ 556
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-536 |
5.34e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrggrvvel 110
Cdd:PRK12467 1611 RLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT------------- 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 111 kkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVplEQEMAKEDPVCAPES-MGSEDMLFMLYTSGSTGMPKGivhtqag 189
Cdd:PRK12467 1678 -------------QSHLQARLPLPDGLRSLVLDQ--EDDWLEGYSDSNPAVnLAPQNLAYVIYTSGSTGRPKG------- 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 190 yllyAALTHKLVFDH--QPGDIFGCVADIGWITGHSYV-------VYGPLCNGAtSVLFESTPVYPNAGRYWETVERLKI 260
Cdd:PRK12467 1736 ----AGNRHGALVNRlcATQEAYQLSAADVVLQFTSFAfdvsvweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQV 1810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 261 ----------NQF------YGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGepinceawewLHRVVGDSRCTLVDTWWQ 324
Cdd:PRK12467 1811 ttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG----------LFNLYGPTETAVDVTHWT 1880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 325 tetggiciAPRPSEEGAEILPamamrpffgIVPVLMDEKGSVVEGS------NVSGALCISQAwpGMARtiyGDH----- 393
Cdd:PRK12467 1881 --------CRRKDLEGRDSVP---------IGQPIANLSTYILDASlnpvpiGVAGELYLGGV--GLAR---GYLnrpal 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 394 --QRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyPHD-IKG 468
Cdd:PRK12467 1939 taERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI--AQDgANG 2015
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248211 469 EAAFAFIVVKDSAGDSDVVVQ-----ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 536
Cdd:PRK12467 2016 KQLVAYVVPTDPGLVDDDEAQvalraILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQ 2088
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
23-536 |
6.97e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 99.29 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAaMLACARIGAVhtVIFAGFSAESL-----AGRINDAkckVVI 96
Cdd:PRK10946 52 RELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYIT-FFALLKLGVA--PVNALFSHQRSelnayASQIEPA---LLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 97 tfnqGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLDvpLEQEMAKEDPVCAPESMGSEDMLFMLYTSGS 176
Cdd:PRK10946 126 ----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDD------GEHS--LDDAINHPAEDFTATPSPADEVAFFQLSGGS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIVHTQAGYLlYAAlthklvfdHQPGDIFGCVADIGWI----TGHSYVVYGPlcnGATSVLFESTPVY----PNA 248
Cdd:PRK10946 194 TGTPKLIPRTHNDYY-YSV--------RRSVEICGFTPQTRYLcalpAAHNYPMSSP---GALGVFLAGGTVVlapdPSA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 249 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLgSVG-------------EPINCEawewLHRVVGDSR 315
Cdd:PRK10946 262 TLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL-QVGgarlsetlarripAELGCQ----LQQVFGMAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 316 cTLV------DTWWQT-ETGGiciapRPSEEGAEILPAmamrpffgivpvlmDEKGS-VVEGSnvSGALcisqawpgMAR 387
Cdd:PRK10946 337 -GLVnytrldDSDERIfTTQG-----RPMSPDDEVWVA--------------DADGNpLPQGE--VGRL--------MTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 388 ---TIYG-----DHQRFVdayFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 459
Cdd:PRK10946 387 gpyTFRGyykspQHNASA---FDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 460 IGYPHDIKGEAAFAFIVVKDsagdsdvvvqELKSMVATK------IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 533
Cdd:PRK10946 463 VSMEDELMGEKSCAFLVVKE----------PLKAVQLRRflreqgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
...
gi 358248211 534 EAQ 536
Cdd:PRK10946 533 RAS 535
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-521 |
1.88e-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.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 96.30 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 164 SEDMLFMLYTSGSTGMPKGIVHTQA---GYLLYAALTHKLVFdhQPGDIFGCVADIGwiTGHSYVVYGPLCNGA------ 234
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEF--TPSEDAHKAAAAA--AGTVMFPAPPLMHGTgswtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 235 TSVLFESTPVYP----NAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPIN 300
Cdd:cd05924 78 GGLLGGQTVVLPddrfDPEEVWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 301 CEAWEWLHRVVGDSrcTLVDTWWQTETGGICIApRPSEEGAEilpamaMRPFFGIVP--VLMDEKGSVVE-GSNVSGALc 377
Cdd:cd05924 148 PEVKQGLLELVPNI--TLVDAFGSSETGFTGSG-HSAGSGPE------TGPFTRANPdtVVLDDDGRVVPpGSGGVGWI- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 378 isqAWPG-MARTIYGDHQRfVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 454
Cdd:cd05924 218 ---ARRGhIPLGYYGDEAK-TAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 455 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 521
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-537 |
1.99e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.47 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVEl 110
Cdd:PRK12467 3132 RLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT------QAHLLE- 3204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 111 kkivdeavkHCPTVQHVLVAhrtdnkvhmgDLDVPLEQEMAKEDPvcAPESMGsEDMLFMLYTSGSTGMPKGI------- 183
Cdd:PRK12467 3205 ---------QLPAPAGDTAL----------TLDRLDLNGYSENNP--STRVMG-ENLAYVIYTSGSTGKPKGVgvrhgal 3262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 184 -VHTQAGYLLYAALTHKLVFDHQPGDIFGCVADigwitghsyvVYGPLCNGATSVLfestpvypNAGRYW---ETV---- 255
Cdd:PRK12467 3263 aNHLCWIAEAYELDANDRVLLFMSFSFDGAQER----------FLWTLICGGCLVV--------RDNDLWdpeELWqaih 3324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 -ERLKINQFygAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWEWLHRVV---------GDSRCTLVDTWWQT 325
Cdd:PRK12467 3325 aHRISIACF--PPAYLQQFAEDAGG----ADCASLDIYVFGGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKC 3398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 326 ETGGICIAPrpseegaeILPamAMRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARtiyGDHQ-------RFVD 398
Cdd:PRK12467 3399 GGDAVCEAP--------YAP--IGRPVAGRSIYVLDGQLNPVP-VGVAGELYI--GGVGLAR---GYHQrpsltaeRFVA 3462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 399 AYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVV 477
Cdd:PRK12467 3463 DPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVP 3541
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 478 KDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 537
Cdd:PRK12467 3542 ADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSRE 3598
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
23-525 |
2.42e-21 |
|
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: 96.90 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05907 9 AEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakEDPvcapesmgsEDMLFMLYTSGSTGMPKG 182
Cdd:cd05907 84 --------------------------------------------------EDP---------DDLATIIYTSGTTGRPKG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnagrywETVERLKINQ 262
Cdd:cd05907 105 VMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL------DDLSEVRPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 263 FYGAPtavRLLLK-YGDAWVKK--------YDR---SSLRTLGSVGEPINCEAWEWLHRvVGdsrCTLVDTWWQTETGGI 330
Cdd:cd05907 178 FLAVP---RVWEKvYAAIKVKAvpglkrklFDLavgGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTETSAV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 331 CIAPRPSeegaeilpamamRPFFGIVpvlmdekGSVVEGSNV----SGALCISQawPGMARTIYGDHQRFVDAYFKayPG 406
Cdd:cd05907 251 VTLNPPG------------DNRIGTV-------GKPLPGVEVriadDGEILVRG--PNVMLGYYKNPEATAEALDA--DG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 407 YYFTGDGAYRTEGGYYQITGRMDDVI-NISGHRLGTAEIEDAIADHPAVPESAVIG--YPH-----DIKGEAAFAFIVVK 478
Cdd:cd05907 308 WLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgRPFlvaliVPDPEALEAWAEEH 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248211 479 DSAGDSDV-------VVQELKSMV---------ATKIAKYAVPDEILVVKRLPKTRSGKVMRR 525
Cdd:cd05907 388 GIAYTDVAelaanpaVRAEIEAAVeaanarlsrYEQIKKFLLLPEPFTIENGELTPTLKLKRP 450
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
44-530 |
2.60e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.59 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 44 GDRVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqgLRGGRVVELkkIVDEAVKH 120
Cdd:PRK12492 75 GDRIAVQMPnvlQYPIAVFGAL---RAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN--MFGKLVQEV--LPDTGIEY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 121 C---------PTVQHVLVAHRTDNKVHMgdldVP---LEQEMA-------KEDPVCAPESMGSEDMLFMLYTSGSTGMPK 181
Cdd:PRK12492 148 LieakmgdllPAAKGWLVNTVVDKVKKM----VPayhLPQAVPfkqalrqGRGLSLKPVPVGLDDIAVLQYTGGTTGLAK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GivhtqagyllyAALTH-KLVFDHQpgDIFGCVADIGwITGHsyvvygPLCNGATSVLFESTPVY--------------- 245
Cdd:PRK12492 224 G-----------AMLTHgNLVANML--QVRACLSQLG-PDGQ------PLMKEGQEVMIAPLPLYhiyaftancmcmmvs 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 ---------P-NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPI---NCEAWEWLhrvvg 312
Cdd:PRK12492 284 gnhnvlitnPrDIPGFIKELGKWRFSALLGLNTLFVALMDHPG--FKDLDFSALKLTNSGGTALvkaTAERWEQL----- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 313 dSRCTLVDTWWQTETGGICIApRPSEEGAEI------LPAMAMRpffgivpVLMDEKGSVVEGSNvsGALCIS--QAWPG 384
Cdd:PRK12492 357 -TGCTIVEGYGLTETSPVAST-NPYGELARLgtvgipVPGTALK-------VIDDDGNELPLGER--GELCIKgpQVMKG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 385 MARTIYGDHQrFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPH 464
Cdd:PRK12492 426 YWQQPEATAE-ALDA-----EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPD 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 465 DIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 530
Cdd:PRK12492 500 ERSGEAVKLFVVARDPG----LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
32-529 |
5.08e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.78 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 32 LANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQglrggrvveL 110
Cdd:PRK05620 51 LAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR---------L 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 111 KKIVDEAVKHCPTVQHVLVAHRTD---------NKVHMGDLDVPLEQEMAKEDPVCAPESMGSEdmlfMLYTSGSTGMPK 181
Cdd:PRK05620 122 AEQLGEILKECPCVRAVVFIGPSDadsaaahmpEGIKVYSYEALLDGRSTVYDWPELDETTAAA----ICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHT-QAGYLLYAALTHKLVFDHQPGDIFGCVADI-----------GWITGHSYVVYGPLCNGAT--SVLFESTPvypn 247
Cdd:PRK05620 198 GVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPIyhvlswgvplaAFMSGTPLVFPGPDLSAPTlaKIIATAMP---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 agrywetverlkiNQFYGAPTA-VRLLLKYGDawvKKYDRSSLRTL---GSVGEPINCEAWEWLHRVvgdsrcTLVDTWW 323
Cdd:PRK05620 274 -------------RVAHGVPTLwIQLMVHYLK---NPPERMSLQEIyvgGSAVPPILIKAWEERYGV------DVVHVWG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 324 QTETGGICIAPRPSEeGAEILPAMAMRPFFGIVPVLMDEK----GSVVEGSN-------VSGALCI-------SQAWPGM 385
Cdd:PRK05620 332 MTETSPVGTVARPPS-GVSGEARWAYRVSQGRFPASLEYRivndGQVMESTDrnegeiqVRGNWVTasyyhspTEEGGGA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 386 ARTIYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 465
Cdd:PRK05620 411 ASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDD 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 466 IKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK05620 490 KWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
23-537 |
5.36e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 96.61 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV---HTVIFagfSAESLAGRINDAKCKVVITFN 99
Cdd:PRK05605 61 AELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 ------QGLRGGrvVELKKIVD-EAVKHCPTVQHVLV------AHRTDNKVHMGDLD-VPLEQ----EMAKEDPVCAPES 161
Cdd:PRK05605 138 kvaptvERLRRT--TPLETIVSvNMIAAMPLLQRLALrlpipaLRKARAALTGPAPGtVPWETlvdaAIGGDGSDVSHPR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 162 MGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHklvfdhqpGDIFGCVAD-IGWITG---------------HSY- 224
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKG-----------AQLTH--------RNLFANAAQgKAWVPGlgdgpervlaalpmfHAYg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 225 ----VVYGPLCnGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTL--GSVGEP 298
Cdd:PRK05605 277 ltlcLTLAVSI-GGELVLLPA----PDIDLILDAMKKHPPTWLPGVPPLYEKIAE--AAEERGVDLSGVRNAfsGAMALP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 299 IN-CEAWEwlhRVVGDSrctLVDTWWQTETGGIcIAPRPSEEGAeilpamamRPFFGIVPvLMDEKGSVVEGSNVSGALC 377
Cdd:PRK05605 350 VStVELWE---KLTGGL---LVEGYGLTETSPI-IVGNPMSDDR--------RPGYVGVP-FPDTEVRIVDPEDPDETMP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 378 ISQAWPGMARtiygDHQRFvDAYFKA--------YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 449
Cdd:PRK05605 414 DGEEGELLVR----GPQVF-KGYWNRpeetaksfLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 450 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdvVVQE--LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK05605 489 EHPGVEDAAVVGLPREDGSEEVVAAVVLEPGA-----ALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
570
....*....|
gi 358248211 528 RKIITSEAQE 537
Cdd:PRK05605 564 REELLEKLGA 573
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
406-528 |
1.05e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 95.06 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 406 GYYFTGDGAYRTEGGYYQITGRMD-DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 484
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-----GAD 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 358248211 485 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
32-528 |
7.81e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.19 E-value: 7.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 32 LANTLKrhgVHRGDRVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAESLAGRINDAKCK---VVITFNQglrgg 105
Cdd:PRK08974 65 LQNGLG---LKKGDRVALMMPnllQYPIALFGIL---RAGMIVVNVNPLYTPRELEHQLNDSGAKaivIVSNFAH----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 106 rvvELKKIVDE-AVKHC---------PTVQHVLV------AHRTDNKVHMGD-------LDVPLEQEMAKEDpvcapesM 162
Cdd:PRK08974 134 ---TLEKVVFKtPVKHViltrmgdqlSTAKGTLVnfvvkyIKRLVPKYHLPDaisfrsaLHKGRRMQYVKPE-------L 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 163 GSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHklvfdhqpGDIFGCVADIGWItghsyvvYGPLCNGATSVLFEST 242
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKG-----------AMLTH--------RNMLANLEQAKAA-------YGPLLHPGKELVVTAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 243 PVYP------NAGRYWE----------------TVERLKINQFYgAPTAVRLLLkygDAWV-----KKYDRSSLRTLGSV 295
Cdd:PRK08974 258 PLYHifaltvNCLLFIElggqnllitnprdipgFVKELKKYPFT-AITGVNTLF---NALLnneefQELDFSSLKLSVGG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 296 GEPInceawewlHRVVGDSrctlvdtwWQTETGGICIaprpseEG---AEILPAMAMRPF--------FGiVPV------ 358
Cdd:PRK08974 334 GMAV--------QQAVAER--------WVKLTGQYLL------EGyglTECSPLVSVNPYdldyysgsIG-LPVpsteik 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 359 LMDEKGSVVEGSNvSGALCIS--QAWPGmartiYGDHQRFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISG 436
Cdd:PRK08974 391 LVDDDGNEVPPGE-PGELWVKgpQVMLG-----YWQRPEATDEVIK--DGWLATGDIAVMDEEGFLRIVDRKKDMILVSG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 437 HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPK 516
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE----ELITHCRRHLTGYKVPKLVEFRDELPK 538
|
570
....*....|..
gi 358248211 517 TRSGKVMRRLLR 528
Cdd:PRK08974 539 SNVGKILRRELR 550
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
22-522 |
9.86e-20 |
|
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: 92.39 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 22 GRELLETTCRLANTLKRhGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQG 101
Cdd:cd05909 10 YRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 LRGGRVVELKKIVDEAvkhcptvqHVLVAHRTDNKVHMGD-LDVPLEQEMAKEDPV----CAPESmgSEDMLFMLYTSGS 176
Cdd:cd05909 89 IEKLKLHHLFDVEYDA--------RIVYLEDLRAKISKADkCKAFLAGKFPPKWLLrifgVAPVQ--PDDPAVILFTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIVHTQAGYL--LYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfestpvYPNAGRYW-- 252
Cdd:cd05909 159 EGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF------HPNPLDYKki 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 253 -ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVGEPINC---EAWEWLHRVVgdsrctLVDTWWQTETG 328
Cdd:cd05909 230 pELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGIR------ILEGYGTTECS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 ---GICIAPRPSEEGA--EILPAMAMR--PFFGIVPVLMDEKGSV-VEGSNV-SGALcisqAWPGMARTIYGDhqrfvda 399
Cdd:cd05909 300 pviSVNTPQSPNKEGTvgRPLPGMEVKivSVETHEEVPIGEGGLLlVRGPNVmLGYL----NEPELTSFAFGD------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 400 yfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH-PAVPESAVIGYPHDIKGEAAFAFIVvk 478
Cdd:cd05909 369 ------GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT-- 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 358248211 479 DSAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKV 522
Cdd:cd05909 441 TTDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
43-528 |
9.90e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.63 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 43 RGDRVAIYMPVS---PLAVAAMLaCARIGAV------------HTVIFAGFSA--------ESLAGRINDAKCKVVITfn 99
Cdd:PRK08751 75 KGDRVALMMPNClqyPIATFGVL-RAGLTVVnvnplytprelkHQLIDSGASVlvvidnfgTTVQQVIADTPVKQVIT-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 QGLrgGRVVELKK--IVDEAVKHcptVQHVLVAHRTDNKVHMGD-LDVPLEQEMAKEDpvcapesMGSEDMLFMLYTSGS 176
Cdd:PRK08751 152 TGL--GDMLGFPKaaLVNFVVKY---VKKLVPEYRINGAIRFREaLALGRKHSMPTLQ-------IEPDDIAFLQYTGGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGivhtqagyllyAALTHK-LVFDHQPGDifgcvadiGWITGHS---------------YVVYGPLCNGATSVLFE 240
Cdd:PRK08751 220 TGVAKG-----------AMLTHRnLVANMQQAH--------QWLAGTGkleegcevvitalplYHIFALTANGLVFMKIG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 241 ------STPvyPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLR-TLGSvGEPINCEAWEWLHRVVGd 313
Cdd:PRK08751 281 gcnhliSNP--RDMPGFVKELKKTRFTAFTGVNTLFNGLLN--TPGFDQIDFSSLKmTLGG-GMAVQRSVAERWKQVTG- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 314 srCTLVDTWWQTETG-GICIAPRPSEE--GAEILPamamrpffgiVP----VLMDEKGSVVEGSNVsGALCISQAwpgma 386
Cdd:PRK08751 355 --LTLVEAYGLTETSpAACINPLTLKEynGSIGLP----------IPstdaCIKDDAGTVLAIGEI-GELCIKGP----- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 387 RTIYGDHQR------FVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 460
Cdd:PRK08751 417 QVMKGYWKRpeetakVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248211 461 GYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK08751 492 GVPDEKSGEIVKVVIVKKDPA----LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
165-524 |
1.27e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.40 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 165 EDMLFMLYTSGSTGMPKGIVhtQAGYLLYAALTH--KLVFDHQPGDIFGCVADIGWITGHSYVvygplcngATSVLFEST 242
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVL--LANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWI--------LTCLIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 243 PVYPNAGRYWETVerLKINQFYGA------PTA---VRLLLKYGDAWVKKydrssLRTLGSVGE-PINCEA--WEWLHRV 310
Cdd:cd17635 71 CVTGGENTTYKSL--FKILTTNAVtttclvPTLlskLVSELKSANATVPS-----LRLIGYGGSrAIAADVrfIEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 311 vgdsrcTLVDTWWQTETGGICIAPrpSEEGAEILPAMAmRPFFGIVPVLMDEKG-SVVEGSNvsGALCISQAWpgMARTI 389
Cdd:cd17635 144 ------NTAQVYGLSETGTALCLP--TDDDSIEINAVG-RPYPGVDVYLAATDGiAGPSASF--GTIWIKSPA--NMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 390 YGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 469
Cdd:cd17635 211 WNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 470 AAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 524
Cdd:cd17635 288 LVGLAVVA--SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
23-529 |
1.72e-19 |
|
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: 91.33 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05939 7 RELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKEDPVCAPesMGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd05939 82 --------------------------------------NLLDPLLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTGLPKA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGYLLYAALTHKlVFDHQPGDIFgcvadigWITGHSYVVYGPLCNGATSVLFESTPVYP---NAGRYWETVERLK 259
Cdd:cd05939 122 AVIVHSRYYRIAAGAYY-AFGMRPEDVV-------YDCLPLYHSAGGIMGVGQALLHGSTVVIRkkfSASNFWDDCVKYN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 260 --INQFYGapTAVRLLLkygDAWVKKYD-RSSLRTLgsVGEPINCEAWEWLHRVVG-----------DSRCTLVDTwwQT 325
Cdd:cd05939 194 ctIVQYIG--EICRYLL---AQPPSEEEqKHNVRLA--VGNGLRPQIWEQFVRRFGipqigefygatEGNSSLVNI--DN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 326 ETGGICIAPRpseegaeILPAMamrpfFGIVPVLMDE-KGSVVEGSNvsgALCISQAwPG-----MARTIYGDHQRFVDA 399
Cdd:cd05939 265 HVGACGFNSR-------ILPSV-----YPIRLIKVDEdTGELIRDSD---GLCIPCQ-PGepgllVGKIIQNDPLRRFDG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 400 Y--------------FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY--P 463
Cdd:cd05939 329 YvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 464 HdIKGEAAFAFIVVKDSAGDSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05939 409 G-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
31-529 |
4.29e-19 |
|
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: 90.57 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvEL 110
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP---------NL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 111 KKIVDEAVKhcptvqhvLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSE-DMLFMLYTSGSTGMPKGIVHTQAG 189
Cdd:cd05915 107 LPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 190 -YLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEstpvYPNAGRYWETVERLKINQFYGAPT 268
Cdd:cd05915 178 lVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVELFDGEGVTFTAGVPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 269 AVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinceawEWLHRVVGDSRCTLVDTWWQTETGGICIA----PR----PSEEG 340
Cdd:cd05915 254 VWLALADYLESTGHRLKTLRRLVVGGSAAP------RSLIARFERMGVEVRQGYGLTETSPVVVQnfvkSHleslSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 341 AEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNVSgalCISQAWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEG 419
Cdd:cd05915 328 LTLKAKTGLPIPLVRLRVADEEGRPVPkDGKALG---EVQLKGPWITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 420 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATki 499
Cdd:cd05915 403 GYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFA-- 480
|
490 500 510
....*....|....*....|....*....|
gi 358248211 500 aKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05915 481 -KWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
23-536 |
2.34e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 87.91 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLkRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT---FN 99
Cdd:PRK07638 30 KDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTeryKL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 QGLRG--GRVVELKKIvdeavkhcptvqhvlvahrtdnkvhMGDLDVPLEQEMAKEDPVCAPESMGsedmlfmlYTSGST 177
Cdd:PRK07638 109 NDLPDeeGRVIEIDEW-------------------------KRMIEKYLPTYAPIENVQNAPFYMG--------FTSGST 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLL-YAALTHKLVFDHQ-----PGDIFgcvadigwitgHSYVVYGplcngATSVLFESTPVY------ 245
Cdd:PRK07638 156 GKPKAFLRAQQSWLHsFDCNVHDFHMKREdsvliAGTLV-----------HSLFLYG-----AISTLYVGQTVHlmrkfi 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 PNAGRywETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSvGEPINCEAWE-----WLHrvvgdsrCTLVD 320
Cdd:PRK07638 220 PNQVL--DKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISS-GAKWEAEAKEkikniFPY-------AKLYE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 321 TWWQTETGGICIAprpSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMARTIY-GDHQRFV-- 397
Cdd:PRK07638 285 FYGASELSFVTAL---VDEESERRPNSVGRPFHNVQVRICNEAGEEVQ--------------KGEIGTVYvKSPQFFMgy 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 --DAYFKAYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 472
Cdd:PRK07638 348 iiGGVLARELnadGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPV 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 473 AfiVVKDSAGdsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 536
Cdd:PRK07638 428 A--IIKGSAT-----KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
165-527 |
3.55e-18 |
|
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: 87.49 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 165 EDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPgDIFGCVADIGWITGhSYVVYGPLCNGATSVLfESTPV 244
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGATLVL-RPEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 YPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINCEAWEWLHRVVGDsRCTLVDTWWQ 324
Cdd:cd17644 183 RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN-FIQLINVYGP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 325 TE---TGGICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYG----DHQRFV 397
Cdd:cd17644 261 TEatiAATVCRLTQLTER--NITSVPIGRPIANTQVYILDENLQPVP-VGVPGELHIGGV--GLARGYLNrpelTAEKFI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 DAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:cd17644 336 SHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYI 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 358248211 476 VVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17644 416 VPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
47-529 |
5.23e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 87.04 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 47 VAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavKHCPTVQH 126
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTES-------------------AHAELLDG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 127 VlvahrtDNKVHMGDLDVPL-EQEMAKEDPVCAPESMGSEDMLFMLY-TSGSTGMPKGIVHTQaGYLLYAALTHKLVFDH 204
Cdd:PRK07867 118 L------DPGVRVINVDSPAwADELAAHRDAEPPFRVADPDDLFMLIfTSGTSGDPKAVRCTH-RKVASAGVMLAQRFGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 205 QPGDIfgCVADIGWItgHSYVV---YGP-LCNGATSVL---FestpvypNAGRYWETVERlkinqfYGAPTA--VRLLLK 275
Cdd:PRK07867 191 GPDDV--CYVSMPLF--HSNAVmagWAVaLAAGASIALrrkF-------SASGFLPDVRR------YGATYAnyVGKPLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 276 Y--------GDAwvkkydRSSLRTL-GSVGEPINCEAWEwlhRVVGdsrCTLVDTWWQTEtGGICIAPRPSEegaeilPA 346
Cdd:PRK07867 254 YvlatperpDDA------DNPLRIVyGNEGAPGDIARFA---RRFG---CVVVDGFGSTE-GGVAITRTPDT------PP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 347 MAMRPFFGIVPVLMDEKGS-----------VVEGSNVSGALcISQAWPGMARTIY----GDHQRFVDayfkaypGYYFTG 411
Cdd:PRK07867 315 GALGPLPPGVAIVDPDTGTecppaedadgrLLNADEAIGEL-VNTAGPGGFEGYYndpeADAERMRG-------GVYWSG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 412 DGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQE 490
Cdd:PRK07867 387 DLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEF 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 358248211 491 LKSmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK07867 467 LAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
23-528 |
1.08e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 86.36 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAV-AAMlacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 97
Cdd:PRK05677 53 GELYKLSGAFAAWLQQHtDLKPGDRIAVQLPnvlQYPVAVfGAM----RAGLIVVNTNPLYTAREMEHQFNDSGAKALVC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 98 F------------NQGLRGGRVVEL--------KKIVDEAVKHcptVQHVLVAHRTDNKVHMGDLdvpleQEMAKEDPVc 157
Cdd:PRK05677 129 LanmahlaekvlpKTGVKHVIVTEVadmlpplkRLLINAVVKH---VKKMVPAYHLPQAVKFNDA-----LAKGAGQPV- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 158 APESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-LVfdhqpGDIFGCVADIGWITGH-SYVVYGPL----- 230
Cdd:PRK05677 200 TEANPQADDVAVLQYTGGTTGVAKG-----------AMLTHRnLV-----ANMLQCRALMGSNLNEgCEILIAPLplyhi 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 231 ------CnGATSVLFESTPVYPNAGRYWETVERL---KINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINC 301
Cdd:PRK05677 264 yaftfhC-MAMMLIGNHNILISNPRDLPAMVKELgkwKFSGFVGLNTLFVALCNNEA--FRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 302 EAWEWLHRVVGdsrCTLVDTWWQTETGGI-CIAPRPSEEGAEI-LPAMAMrpffgIVPVLMDEKGSVVEGSnvSGALCIS 379
Cdd:PRK05677 341 ATAERWKEVTG---CAICEGYGMTETSPVvSVNPSQAIQVGTIgIPVPST-----LCKVIDDDGNELPLGE--VGELCVK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 380 --QAWPGmartiYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 457
Cdd:PRK05677 411 gpQVMKG-----YWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQC 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 458 AVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 528
Cdd:PRK05677 485 AAIGVPDEKSGEAIKVFVVVKPGET---LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
20-527 |
1.60e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 85.83 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 20 PHGrELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAgRINDAKCKVVITFN 99
Cdd:PRK05857 43 RYR-ELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIE-RFCQITDPAAALVA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 100 qglRGGRVvelkkivdeAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPvcapeSMGSEDMLFMLYTSGSTGM 179
Cdd:PRK05857 121 ---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA-----DQGSEDPLAMIFTSGTTGE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIvhtqagyLLyaalthklvfdhqPGDIFGCVADI---------GWITGHSyvVYGPLcnGATSVlfestpvypnAGR 250
Cdd:PRK05857 184 PKAV-------LL-------------ANRTFFAVPDIlqkeglnwvTWVVGET--TYSPL--PATHI----------GGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 251 YW----------------------ETVERLKINQFYGAPTAVRLL---LKYGDAwvkkyDRSSLRTLGSVGEPInceawe 305
Cdd:PRK05857 230 WWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLvseLKSANA-----TVPSLRLVGYGGSRA------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 306 wlhrVVGDSR---CTLVDT---WWQTETG--GICIaPRPSEEGAEILPAMAMRPFFGIVPVLMDEKG----SVVEGSNVS 373
Cdd:PRK05857 299 ----IAADVRfieATGVRTaqvYGLSETGctALCL-PTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptAPGAGPSAS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 374 -GALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 452
Cdd:PRK05857 374 fGTLWIKS--PANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVS 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 453 AVPESAVIGYPhDIKGEAAFAFIVVKDSAGDSDVVVqELKSMVATKIAK----YAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK05857 449 GVREAACYEIP-DEEFGALVGLAVVASAELDESAAR-ALKHTIAARFRResepMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
141-528 |
1.64e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 85.85 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 141 DLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKlvFDHQPGDIFGCVADIGw 218
Cdd:PRK13388 125 DVDTPAYAELVAAAGALTPHReVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPLF- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 219 itgHSYVVY---GP-LCNGATSVLfestPVYPNAGRYWETVerlkinQFYGAP--TAVRLLLKYGDAWVKKYDRS--SLR 290
Cdd:PRK13388 202 ---HSNAVMagwAPaVASGAAVAL----PAKFSASGFLDDV------RRYGATyfNYVGKPLAYILATPERPDDAdnPLR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 291 T-LGSVGEPINCEAWEwlhRVVGdsrCTLVDTWWQTETGGICIAPRPSEEGAeilpamAMRPFFGIV-----------PV 358
Cdd:PRK13388 269 VaFGNEASPRDIAEFS---RRFG---CQVEDGYGSSEGAVIVVREPGTPPGS------IGRGAPGVAiynpetltecaVA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 359 LMDEKGSVVEGSNVSGALcISQAWPGMARTIYGDH----QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINI 434
Cdd:PRK13388 337 RFDAHGALLNADEAIGEL-VNTAGAGFFEGYYNNPeataERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 435 SGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATK--IAKYAVPDEILVVK 512
Cdd:PRK13388 409 DGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD---GATFDPDAFAAFLAAQpdLGTKAWPRYVRIAA 485
|
410
....*....|....*.
gi 358248211 513 RLPKTRSGKVMRRLLR 528
Cdd:PRK13388 486 DLPSTATNKVLKRELI 501
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
23-529 |
2.03e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.70 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:PRK08279 66 AELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIV----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rGGRVVELkkiVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKEDPVCAPESMGS---EDMLFMLYTSGSTGM 179
Cdd:PRK08279 141 -GEELVEA---FEEARADLARPPRLWVAGGDTLDDPEGYEDL---AAAAAGAPTTNPASRSGvtaKDTAFYIYTSGTTGL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQAGYLLY----AALThklvfDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 255
Cdd:PRK08279 214 PKAAVMSHMRWLKAmggfGGLL-----RLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKF----SASRFWDDV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 256 ERlkinqfYGApTAV-------RLLLkygDAWVKKYDRS-SLRTLgsVGEPINCEAW-EWLHRvVGDSRctLVDTWWQTE 326
Cdd:PRK08279 285 RR------YRA-TAFqyigelcRYLL---NQPPKPTDRDhRLRLM--IGNGLRPDIWdEFQQR-FGIPR--ILEFYAASE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 327 --TGGICIAPRPSEEGaeILPAMAMRPfFGIVPVlmD-EKGSVVEGSNvsgALCI--SQAWPGMARTIYGDHQRFvDAY- 400
Cdd:PRK08279 350 gnVGFINVFNFDGTVG--RVPLWLAHP-YAIVKY--DvDTGEPVRDAD---GRCIkvKPGEVGLLIGRITDRGPF-DGYt 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 401 -------------FKayPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP-- 463
Cdd:PRK08279 421 dpeasekkilrdvFK--KGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvp 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 464 -HDikGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:PRK08279 499 gTD--GRAGMAAIVLADGA---EFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
23-527 |
5.44e-17 |
|
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: 83.37 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd17645 27 KQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd17645 102 ------------------------------------------------------------NPDDLAYVIYTSGSTGLPKG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 I-VHTQAgyLLYAALTHKLVFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNGATsvlfesTPVYPNAGRYweTVERLkiN 261
Cdd:cd17645 122 VmIEHHN--LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAA------LHVVPSERRL--DLDAL--N 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 262 QFYGAPTAVRLLLKYGDA-WVKKYDRSSLRTLGSVGEPINcEAWEWLHRVV---GDSRCTLVDTWWQTEtggiciaprPS 337
Cdd:cd17645 189 DYFNQEGITISFLPTGAAeQFMQLDNQSLRVLLTGGDKLK-KIERKGYKLVnnyGPTENTVVATSFEID---------KP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 338 EEGAEILPAMAMrpffgiVPVLMDEKGSVVEGSNVSGALCIsqAWPGMARTIYG----DHQRFVDAYFKAYPGYYFTGDG 413
Cdd:cd17645 259 YANIPIGKPIDN------TRVYILDEALQLQPIGVAGELCI--AGEGLARGYLNrpelTAEKFIVHPFVPGERMYRTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 414 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKdsagdSDVVVQELKS 493
Cdd:cd17645 331 AKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP-----EEIPHEELRE 405
|
490 500 510
....*....|....*....|....*....|....
gi 358248211 494 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd17645 406 WLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
30-530 |
1.29e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.14 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 30 CRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvE 109
Cdd:PLN03102 50 CRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR---------S 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 110 LKKIVDEAVKHCPTVQH-----VLVAHRTDNKVHMGDLDVPLEQEMAKEDPvcAPESMGS-------EDMLFMLYTSGST 177
Cdd:PLN03102 121 FEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqdeHDPISLNYTSGTT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 178 GMPKGIVHTQAGYLLyAALThkLVFDHQPG---------DIFGCVadiGWItghsyVVYGPLCNGATSVLFEstpvYPNA 248
Cdd:PLN03102 199 ADPKGVVISHRGAYL-STLS--AIIGWEMGtcpvylwtlPMFHCN---GWT-----FTWGTAARGGTSVCMR----HVTA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 249 GRYWETVERLKINQFYGAPTAVRLLLKyGDAWVKKYDRSSLRTLGSVGEP-------INCEAWEWLHrVVGDSRCT--LV 319
Cdd:PLN03102 264 PEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPPpaalvkkVQRLGFQVMH-AYGLTEATgpVL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 320 DTWWQTETGGIciaprPSEEGAEILPAMAMRpFFGIVPVLMDEKG---SVVEGSNVSGALCISqawpgmARTIYGDHQRF 396
Cdd:PLN03102 342 FCEWQDEWNRL-----PENQQMELKARQGVS-ILGLADVDVKNKEtqeSVPRDGKTMGEIVIK------GSSIMKGYLKN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 397 VDAYFKAYP-GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:PLN03102 410 PKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248211 476 VVKDS----AGDSDVVVQELKSMVA---TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 530
Cdd:PLN03102 490 VLEKGettkEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
30-539 |
1.48e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.97 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 30 CRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfNQglrggrvvE 109
Cdd:PLN02479 56 RRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV-DQ--------E 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 110 LKKIVDEAVK---------HCPTVQHVLVAHRTDNKV---HMGDLDVPLEQEMAKEDPVCAPESMGSE-DMLFMLYTSGS 176
Cdd:PLN02479 127 FFTLAEEALKilaekkkssFKPPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADEwQSIALGYTSGT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIV-HTQAGYLLyaALTHKLVFDHQPGDI-------FGCVadiGWITGHSYVVygpLCngATSVLF---ESTPVY 245
Cdd:PLN02479 207 TASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVylwtlpmFHCN---GWCFTWTLAA---LC--GTNICLrqvTAKAIY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 pnagrywETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWL-HRVVgdsrctlvDTW 322
Cdd:PLN02479 277 -------SAIANYGVTHFCAAPVVLNTIVNApkSETILPLPRVVHVMTAGAAPPPSVLFAMSEKgFRVT--------HTY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 323 WQTETGG---ICI-APR----PSEEGAEILPAMAMRpFFGI-----------VPVLMDEK--GSVVEGSNVsgalcisqA 381
Cdd:PLN02479 342 GLSETYGpstVCAwKPEwdslPPEEQARLNARQGVR-YIGLegldvvdtktmKPVPADGKtmGEIVMRGNM--------V 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 382 WPGMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 461
Cdd:PLN02479 413 MKGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 462 YPHDIKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRkiitSEAQELG 539
Cdd:PLN02479 486 RPDERWGESPCAFVTLKPGVDKSDeaALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR----AKAKEMG 560
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-527 |
3.27e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.91 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDakCKVVITFNQGLR 103
Cdd:PRK05691 1161 ELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLAD--SGVELLLTQSHL 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 GGRVvelkkivdeavkhcPTVQHVLVahrtdnkvhmgdldVPLEQEMAKEDPVCAPE-SMGSEDMLFMLYTSGSTGMPKG 182
Cdd:PRK05691 1239 LERL--------------PQAEGVSA--------------IALDSLHLDSWPSQAPGlHLHGDNLAYVIYTSGSTGQPKG 1290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTqagyllYAALTHKL-----VFDHQPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLfESTPVYPNAGRYWETVER 257
Cdd:PRK05691 1291 VGNT------HAALAERLqwmqaTYALDDSDVLMQKAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQ 1362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE---------WLHRVVGDSRCTLVDTWWQtetg 328
Cdd:PRK05691 1363 YGVTTLHFVPPLLQLFIDEPLA----AACTSLRRLFSGGEALPAELRNrvlqrlpqvQLHNRYGPTETAINVTHWQ---- 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 giCIAprpsEEGaEILPAMamRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARTIYG----DHQRFV-DAYFKA 403
Cdd:PRK05691 1435 --CQA----EDG-ERSPIG--RPLGNVLCRVLDAELNLLPPG-VAGELCIGGA--GLARGYLGrpalTAERFVpDPLGED 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 404 YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyphdIKGEAAFAFIVVKDSAGD 483
Cdd:PRK05691 1503 GARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLVGYYTGEA 1577
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 358248211 484 S-DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK05691 1578 GqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
401-532 |
4.03e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.81 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 401 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDS 480
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 358248211 481 AGDsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 532
Cdd:PRK07445 399 SIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
24-533 |
4.10e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 81.18 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAAMLACARIGavhtvIFAGFSAESLAGRIND----AKCKVVITf 98
Cdd:PLN02330 60 EVVRDTRRFAKALRSLGLRKGQVVVVVLPnVAEYGIVALGIMAAGG-----VFSGANPTALESEIKKqaeaAGAKLIVT- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 99 nQGLRGGRVVELKkivdeavkhCPTVqhVLVAHRTDNKVHMGDLdvpLEQEMAKEDPVcAPESMGSEDMLFMLYTSGSTG 178
Cdd:PLN02330 134 -NDTNYGKVKGLG---------LPVI--VLGEEKIEGAVNWKEL---LEAADRAGDTS-DNEEILQTDLCALPFSSGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 179 MPKGIVHTQAGylLYAALTHKLvFDHQPgDIFGCVADIGWITG-HSYVVYGPLCngATsvlfestpvYPNAGRYwETVER 257
Cdd:PLN02330 198 ISKGVMLTHRN--LVANLCSSL-FSVGP-EMIGQVVTLGLIPFfHIYGITGICC--AT---------LRNKGKV-VVMSR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGA------------PTAVRLLLKygDAWVKKYDRSSL--RTLGSVGEPINCE---AWEWLHRVVgdsrcTLVD 320
Cdd:PLN02330 262 FELRTFLNAlitqevsfapivPPIILNLVK--NPIVEEFDLSKLklQAIMTAAAPLAPElltAFEAKFPGV-----QVQE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 321 TWWQTETGGICIAPRPSEEGAEIlpamAMRPFFG-IVPVL----MDEKGSVVEGSNVSGALCI-SQAwpgMARTIYGDHQ 394
Cdd:PLN02330 335 AYGLTEHSCITLTHGDPEKGHGI----AKKNSVGfILPNLevkfIDPDTGRSLPKNTPGELCVrSQC---VMQGYYNNKE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 395 ---RFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 471
Cdd:PLN02330 408 etdRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIP 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248211 472 FAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 533
Cdd:PLN02330 483 AACVVINPKAKESE---EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
409-527 |
1.54e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.92 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 409 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfIVVKDSAGDSDvvv 488
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA-KVISHEEIDPV--- 369
|
90 100 110
....*....|....*....|....*....|....*....
gi 358248211 489 qELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK08308 370 -QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
23-527 |
1.68e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 79.27 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQgl 102
Cdd:PRK13383 64 RELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkIVDEAVKhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPESMgsedmlfMLYTSGSTGMPKG 182
Cdd:PRK13383 142 ----------FAERIAG-------------ADDAVAVIDPATAGAEESGGRPAVAAPGRI-------VLLTSGTTGKPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHT---QAGYLLYAALTHKLVFDhqpgdifgcvadigwiTGHSYVVYGPLCNG---ATSVLFESTPVYPNAGRYWETVE 256
Cdd:PRK13383 192 VPRApqlRSAVGVWVTILDRTRLR----------------TGSRISVAMPMFHGlglGMLMLTIALGGTVLTHRHFDAEA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RL------KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrcTLVDTWWQTETGgI 330
Cdd:PRK13383 256 ALaqaslhRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVG-I 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 331 CIAPRPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGmartiygdhQRFVDAYFKAY-PGYYF 409
Cdd:PRK13383 332 GALATPAD--LRDAPETVGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAG---------TRYTDGGGKAVvDGMTS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 410 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSagdSDVVVQ 489
Cdd:PRK13383 400 TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SGVDAA 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 358248211 490 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK13383 477 QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
403-534 |
2.86e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 77.39 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 403 AYPGYYFTGD-GAYrtEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsA 481
Cdd:PRK07824 231 AEPGWFRTDDlGAL--DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG---D 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 358248211 482 GDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSE 534
Cdd:PRK07824 306 GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
37-532 |
2.17e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 76.03 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 37 KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDakCKVVITFnqglrggrvvelkkIVDE 116
Cdd:PLN02574 85 HVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVD--CSVGLAF--------------TSPE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 117 AVKHCPTVQhVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGSTGMPKGIVHTQAGYL--- 191
Cdd:PLN02574 149 NVEKLSPLG-VPVIGVPENYDFdSKRIEFPKFYELIKEDFDFVPKPvIKQDDVAAIMYSSGTTGASKGVVLTHRNLIamv 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 192 -LYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAV 270
Cdd:PLN02574 228 eLFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 271 RLLLKYgdawVKKYDRSSLRTLGSVgepiNCEAWEWLHRVVGD-----SRCTLVDTWWQTETGGICIAPRPSEEGAE--- 342
Cdd:PLN02574 304 MALTKK----AKGVCGEVLKSLKQV----SCGAAPLSGKFIQDfvqtlPHVDFIQGYGMTESTAVGTRGFNTEKLSKyss 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 343 ---ILPAMAMRpffgivpVLMDEKGSVVEGSNvSGALCISQawPGMARTIYGDHQRFVDAYFKayPGYYFTGDGAYRTEG 419
Cdd:PLN02574 376 vglLAPNMQAK-------VVDWSTGCLLPPGN-CGELWIQG--PGVMKGYLNNPKATQSTIDK--DGWLRTGDIAYFDED 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 420 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKI 499
Cdd:PLN02574 444 GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQ---EAVINYVAKQV 520
|
490 500 510
....*....|....*....|....*....|...
gi 358248211 500 AKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 532
Cdd:PLN02574 521 APYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
8-343 |
2.17e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.09 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 8 QPWDRFHFLHFAPHG-RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGR 86
Cdd:PRK09274 29 GGRGADGKLAYDELSfAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 87 INDAKCKVVITFNQGLRGGRVVELKKivdEAVKHCPTVqhvlvahrtDNKVHMG--DLDvPLEQEMAKEDPVCAPesMGS 164
Cdd:PRK09274 109 LAEAQPDAFIGIPKAHLARRLFGWGK---PSVRRLVTV---------GGRLLWGgtTLA-TLLRDGAAAPFPMAD--LAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 165 EDMLFMLYTSGSTGMPKGIVHTQAGYLlyAALTH-KLVFDHQPGDIfgcvaDIgwitgHSY---VVYGPLCnGATSVLFE 240
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEAlREDYGIEPGEI-----DL-----PTFplfALFGPAL-GMTSVIPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 241 STPVYP---NAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD---- 313
Cdd:PRK09274 241 MDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIERFRAMLPPdaei 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 358248211 314 ----------------SRCTLVDTWWQTETG-GICIApRPSeEGAEI 343
Cdd:PRK09274 319 ltpygatealpissieSREILFATRAATDNGaGICVG-RPV-DGVEV 363
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
169-527 |
4.65e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 169 FMLYTSGSTGMPKGIVHTQAGYLLY-AALTHKlvFDHQPGDifgCVADIGWIT--GHSYVVYGPLCNGATSVLfestpvy 245
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHcQAVIER--FGMRADD---CELHFYSINfdAASERLLVPLLCGARVVL------- 2404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 pNAGRYWETVE--------RLKINQF---YGAPTAVRLllkygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDS 314
Cdd:PRK05691 2405 -RAQGQWGAEEicqlireqQVSILGFtpsYGSQLAQWL--------AGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ 2475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 315 rcTLVDTWWQTETGGI---CIAPRPSEEGAEILP---AMAMRpffgiVPVLMDEKGSVV-EGSnvSGALCISQAwpGMAR 387
Cdd:PRK05691 2476 --LFFNAYGPTETVVMplaCLAPEQLEEGAASVPigrVVGAR-----VAYILDADLALVpQGA--TGELYVGGA--GLAQ 2544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 388 tiyGDHQR-------FVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 459
Cdd:PRK05691 2545 ---GYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVV 2621
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248211 460 IGypHDIKGEAAFAFIVVKDSAGDSDVVVQEL----KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK05691 2622 LA--LDTPSGKQLAGYLVSAVAGQDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
163-556 |
7.59e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 163 GSEDMLFMLYTSGSTGMPKGIVHTQAGYL-------LYAALTHKLVFDHQPGDIFgcvaDIG-WitghsYVVYGPLCNGA 234
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLnnqlskvPYLALSEADVIAQTASQSF----DISvW-----QFLAAPLFGAR 3937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 235 TSVLfestpvyPNA-----GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVkkydrSSLRTLGSVGEPINCE-AWEWLH 308
Cdd:PRK05691 3938 VEIV-------PNAiahdpQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL-----DGLRWMLPTGEAMPPElARQWLQ 4005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 309 RVvgdSRCTLVDTWWQTETGGICIAPRPSEEGAE--ILPAMAmrPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMA 386
Cdd:PRK05691 4006 RY---PQIGLVNAYGPAECSDDVAFFRVDLASTRgsYLPIGS--PTDNNRLYLLDEALELVPLGAV-GELCV--AGTGVG 4077
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 387 RTIYGDHQR----FVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVi 460
Cdd:PRK05691 4078 RGYVGDPLRtalaFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV- 4155
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 461 GYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--- 537
Cdd:PRK05691 4156 AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSqay 4235
|
410 420
....*....|....*....|.
gi 358248211 538 LGDTTTLED--PSIIAEILSV 556
Cdd:PRK05691 4236 LAPRNELEQtlATIWADVLKV 4256
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
23-527 |
2.44e-13 |
|
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: 72.47 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:cd05914 11 KDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrTDNkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGMPKG 182
Cdd:cd05914 86 ------------------------------SDE-----------------------------DDVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAG----------YLLYAALTHKLVFdhQP-GDIFGCVADIgwitghsyvVYgPLCNGATSVLFESTP-------- 243
Cdd:cd05914 107 VMLTYRNivsnvdgvkeVVLLGKGDKILSI--LPlHHIYPLTFTL---------LL-PLLNGAHVVFLDKIPsakiiala 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 244 ---VYPNAG--RYWETVERLK---INQFYGAPTAVRLLLKYGDAWVKKYDRSSL--------RTLGSVGEPINCEAWEWL 307
Cdd:cd05914 175 faqVTPTLGvpVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINPDVEEFL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 308 HRVvgdsRCTLVDTWWQTETGGICIAPRPSEE----GAEILPAMAMRPFfgiVPVLMDEKGS-VVEGSNVsgalcisqaw 382
Cdd:cd05914 255 RTI----GFPYTIGYGMTETAPIISYSPPNRIrlgsAGKVIDGVEVRID---SPDPATGEGEiIVRGPNV---------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 383 pgMaRTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINI-SGHRLGTAEIEDAIADHPAVPESAVIG 461
Cdd:cd05914 318 --M-KGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVV 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 462 YPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYA-VPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:cd05914 393 QEKKLVAlayiDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-527 |
7.10e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 71.61 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqgl 102
Cdd:PRK10252 487 REMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT----- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkiVDEavkhcptvqhvlVAHRTDNkvhmGDLDVPLEQEMAKEDPVCAPESMGS-EDMLFMLYTSGSTGMPK 181
Cdd:PRK10252 562 -----------TAD------------QLPRFAD----VPDLTSLCYNAPLAPQGAAPLQLSQpHHTAYIIFTSGSTGRPK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAgyllyaALTHKLVFDHqpgDIFGCVAD--IGWITGHSYVV-----YGPLCNGATSVLFEstpvyPNAGRYWET 254
Cdd:PRK10252 615 GVMVGQT------AIVNRLLWMQ---NHYPLTADdvVLQKTPCSFDVsvwefFWPFIAGAKLVMAE-----PEAHRDPLA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 255 VERL----KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGE--PIN-CEAWEW-----LHRVVGDSRCTlVD-T 321
Cdd:PRK10252 681 MQQFfaeyGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEalPADlCREWQQltgapLHNLYGPTEAA-VDvS 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WW--------QTETGGICIAPRPSEEGAEILPAMaMRPffgiVPVlmdekgsvvegsNVSGALCIS--QawpgMARTIYG 391
Cdd:PRK10252 760 WYpafgeelaAVRGSSVPIGYPVWNTGLRILDAR-MRP----VPP------------GVAGDLYLTgiQ----LAQGYLG 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 392 ----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP----AVPESAVIGYP 463
Cdd:PRK10252 819 rpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQA 898
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 464 HDIKGEAA--FAFIVVKDSAG-DSDVvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK10252 899 AATGGDARqlVGYLVSQSGLPlDTSA----LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
164-530 |
4.87e-12 |
|
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: 68.46 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 164 SEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFgcvadIGW-----ITGHSYVVYGPLCNGATSVL 238
Cdd:cd05906 166 PDDLALLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVH 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 239 FESTPVYPNAGRYWETVERLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdS 314
Cdd:cd05906 240 VPTEEILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLL--E 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 315 RCTLVDT-----WWQTETGGICI------APRPSEE------GAEIlPAMAMRpffgivpvLMDEKGSVVEGSNVsGALC 377
Cdd:cd05906 315 PYGLPPDairpaFGMTETCSGVIysrsfpTYDHSQAlefvslGRPI-PGVSMR--------IVDDEGQLLPEGEV-GRLQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 378 ISqawpGMARTiygdhqrfvdayfkayPGYY---------FTGDGAYRT------EGGYYQITGRMDDVINISGHRLGTA 442
Cdd:cd05906 385 VR----GPVVT----------------KGYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIVNGVNYYSH 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 443 EIEDAIADHPAVPESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAkyAVPDEILVVKR--LPK 516
Cdd:cd05906 445 EIEAAVEEVPGVEPSFTAAFAVRDPGaeteELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLPKeeIPK 522
|
410
....*....|....
gi 358248211 517 TRSGKVMRRLLRKI 530
Cdd:cd05906 523 TSLGKIQRSKLKAA 536
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-524 |
1.07e-11 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 66.14 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 166 DMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLFESTpvy 245
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 pNAGRYWETVERLKINqFYG--APTAVRLLlkygDAWVKK-YDRSSLRTLGSVGEPINCEAWEwlhrVVGDSrctlvdTW 322
Cdd:cd17637 76 -DPAEALELIEEEKVT-LMGsfPPILSNLL----DAAEKSgVDLSSLRHVLGLDAPETIQRFE----ETTGA------TF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 323 W----QTETGG-ICIAP---RPSEEGAEIlPAMAMRpffgIV-----PVLMDEKGSVVegsnVSGALCISQAWPGMARTI 389
Cdd:cd17637 140 WslygQTETSGlVTLSPyreRPGSAGRPG-PLVRVR----IVddndrPVPAGETGEIV----VRGPLVFQGYWNLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 390 YGdhqrfvdayFKAypGYYFTGDGAYRTEGGYYQITGRM--DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIK 467
Cdd:cd17637 211 YT---------FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPK 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 358248211 468 -GEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 524
Cdd:cd17637 279 wGEGIKAVCVLKPGAT---LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
165-533 |
2.09e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 66.36 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 165 EDMLFMLYTSGSTGMPKGIVHTQagyllyaaltHKLVFDhqpgdIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV 244
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVHN-----MFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 YPNAGRY-------------W-ETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPIN---CEAWEW 306
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDyelCHEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 307 LHRVVGDSRCTLVDTWWQTE-TGGICIAPrpseegaeilpamAMRPFFGIV----PVLMDEKGSVVEGSNVSGALCISQA 381
Cdd:cd05908 251 HMSKYGLKRNAILPVYGLAEaSVGASLPK-------------AQSPFKTITlgrrHVTHGEPEPEVDKKDSECLTFVEVG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 382 WP---GMARTIYGDHQRFVDAYF--------KAYPGYY---------FTGDGAYRT------EGGYYQITGRMDDVINIS 435
Cdd:cd05908 318 KPideTDIRICDEDNKILPDGYIghiqirgkNVTPGYYnnpeatakvFTDDGWLKTgdlgfiRNGRLVITGREKDIIFVN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 436 GHRLGTAEIEDAIADHPAVP--ESAVIG-YPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVaTKIAKYAVpDEILVVK 512
Cdd:cd05908 398 GQNVYPHDIERIAEELEGVElgRVVACGvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHL-NKRGGWQI-NEVLPIR 475
|
410 420
....*....|....*....|.
gi 358248211 513 RLPKTRSGKVMRRLLRKIITS 533
Cdd:cd05908 476 RIPKTTSGKVKRYELAQRYQS 496
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
23-526 |
2.03e-10 |
|
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: 63.19 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGD-RVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqg 101
Cdd:cd17648 16 RELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVIT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPK 181
Cdd:cd17648 92 -------------------------------------------------------------NSTDLAYAIYTSGTTGKPK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAG-----------YLLYAALTHKL------VFDHqpgdiFGCVADIGWITGHSYVVYGPlcngatSVLFEStpv 244
Cdd:cd17648 111 GVLVEHGSvvnlrtslserYFGRDNGDEAVlffsnyVFDF-----FVEQMTLALLNGQKLVVPPD------EMRFDP--- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 245 ypnaGRYWETVERLKINQFYGAPTAVRLllkygdawvkkYD---RSSLRTLGSVGEPINCEAWEWLHrvvGDSRCTLVDT 321
Cdd:cd17648 177 ----DRFYAYINREKVTYLSGTPSVLQQ-----------YDlarLPHLKRVDAAGEEFTAPVFEKLR---SRFAGLIINA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 322 WWQTETGGICI-APRPSEEGAE-------------ILPAmAMRPffgiVPVlmdekGSVveGSNVSGALCISQAW---PG 384
Cdd:cd17648 239 YGPTETTVTNHkRFFPGDQRFDkslgrpvrntkcyVLND-AMKR----VPV-----GAV--GELYLGGDGVARGYlnrPE 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 385 MARtiygdhQRFVDAYFKA--------YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 456
Cdd:cd17648 307 LTA------ERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRE 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 457 SAVI-GYPHDIKGEAAFAFIV---VKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV-MRRL 526
Cdd:cd17648 381 CAVVaKEDASQAQSRIQKYLVgyyLPEPGHVPE---SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRAL 452
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
23-529 |
2.23e-10 |
|
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: 62.83 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqg 101
Cdd:cd05937 9 SETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKEDPVCApesmgsedmlfMLYTSGSTGMPK 181
Cdd:cd05937 84 -------------------------------------------------VDPDDPAI-----------LIYTSGTTGLPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 GIVHTQAGYLLYAALTHKlVFDHQPGD-IFGCVA---DIGWITGHSYVVYGPLC------------------NGATSVLF 239
Cdd:cd05937 104 AAAISWRRTLVTSNLLSH-DLNLKNGDrTYTCMPlyhGTAAFLGACNCLMSGGTlalsrkfsasqfwkdvrdSGATIIQY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 240 E--------STP------------VYPNAGR--YWETV-ERL---KINQFYGAPTAVRLLLKYG-DAWvkkydrsslrTL 292
Cdd:cd05937 183 VgelcryllSTPpspydrdhkvrvAWGNGLRpdIWERFrERFnvpEIGEFYAATEGVFALTNHNvGDF----------GA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 293 GSVGE--PInceaWEWLHRvvGDSRCTLVDT-----WWQTETGGICIAPRpsEEGAEILpamaMRPFFgivpvlmdekgs 365
Cdd:cd05937 253 GAIGHhgLI----RRWKFE--NQVVLVKMDPetddpIRDPKTGFCVRAPV--GEPGEML----GRVPF------------ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 366 vvegSNVSgalcisqAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 445
Cdd:cd05937 309 ----KNRE-------AFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVA 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 446 DAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAGD-SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 521
Cdd:cd05937 378 DVLGAHPDIAEANVYGVKvpgHD--GRAGCAAITLEESSAVpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHK 455
|
....*...
gi 358248211 522 VMRRLLRK 529
Cdd:cd05937 456 QQKGVLRD 463
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
23-561 |
3.42e-10 |
|
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: 62.38 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqgl 102
Cdd:cd17640 9 KDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMPKG 182
Cdd:cd17640 86 ------------------------------------------------------------DSDDLATIIYTSGTTGNPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIgWitgHSY---VVYGPLCNGAtSVLFESTPVYPN------------ 247
Cdd:cd17640 106 VMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAYTSIRTLKDdlkrvkphyivs 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 AGRYWETVERLKINQFYGAPTAVRLLLKYgdawvkkydrssLRTLGSVGEPINCeawewlhrvvGDSRCTLVDTWWQ--- 324
Cdd:cd17640 180 VPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGISG----------GGALPPHVDTFFEaig 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 325 ---------TETGGICIAPRPSeegaEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALcisqawpgMARtiyGDHqr 395
Cdd:cd17640 238 ievlngyglTETSPVVSARRLK----CNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIV--------WVR---GPQ-- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 396 FVDAYFK---------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAVIGypHD 465
Cdd:cd17640 301 VMKGYYKnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG--QD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 466 IKgeAAFAFIVvkdsaGDSDVVVQELKSmVATKIAKyaVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLE 545
Cdd:cd17640 379 QK--RLGALIV-----PNFEELEKWAKE-SGVKLAN--DRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLE 448
|
570
....*....|....*.
gi 358248211 546 DPSIIAEILSVYQKCK 561
Cdd:cd17640 449 EPFIENGEMTQTMKIK 464
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
31-461 |
4.07e-10 |
|
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: 62.10 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 31 RLANTLKRHGVHRGDRVAIYMP------VSPLAVaaMLAcariGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrg 104
Cdd:cd05932 18 RLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLEHSESKALFV------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 105 GRV---VELKKIVDEAVKHCPTVQH-VLVAHRT-DNKVHMGDldvPLEqemakEDPVCAPESMGSedmlfMLYTSGSTGM 179
Cdd:cd05932 85 GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLAT-----LIYTSGTTGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQA--GYLLYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnagrywETVER 257
Cdd:cd05932 152 PKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFV------EDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGAPtavRLLLK-----YGDAWVKKYDR-------SSL--------------RTLGSVGEPINCEAWEWLHRVV 311
Cdd:cd05932 223 ARPTLFFSVP---RLWTKfqqgvQDKIPQQKLNLllkipvvNSLvkrkvlkglgldqcRLAGCGSAPVPPALLEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 312 GDsrctLVDTWWQTETGGICIAPRP--SEEG--AEILPAMAMRpffgivpvlMDEKGSVVEGSnvsgalcisqawPGMAR 387
Cdd:cd05932 300 LN----ILEAYGMTENFAYSHLNYPgrDKIGtvGNAGPGVEVR---------ISEDGEILVRS------------PALMM 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 388 TIYGDHQRFVDAyFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAVIG 461
Cdd:cd05932 355 GYYKDPEATAEA-FTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
24-210 |
4.59e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.44 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQglr 103
Cdd:PLN02387 111 QVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvELKKIVDEAvKHCPTVQHVLVAHRTDNKVHMGDLDV--------PLEQEMAKEDPVcAPESMGSEDMLFMLYTSG 175
Cdd:PLN02387 188 -----QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGSsnwtvssfSEVEKLGKENPV-DPDLPSPNDIAVIMYTSG 260
|
170 180 190
....*....|....*....|....*....|....*
gi 358248211 176 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF 210
Cdd:PLN02387 261 STGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
408-522 |
7.85e-10 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 61.38 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 408 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDIKGEAAFA 473
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSYivPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 474 FIVVKDSAGDSDVVV----------QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 522
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
23-529 |
9.41e-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: 60.83 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIfagfsaeslagrindakckvvitfNQGL 102
Cdd:cd05940 7 AELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------------------------NYNL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGgrvvelkkivdEAVKHCPTV---QHVLVahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSGSTGM 179
Cdd:cd05940 63 RG-----------ESLAHCLNVssaKHLVV------------------------------------DAALYIYTSGTTGL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 180 PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVAdIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV--ER 257
Cdd:cd05940 96 PKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLP-LYHSTALIVGWSACLASGATLVIRKKF----SASNFWDDIrkYQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 258 LKINQFYGapTAVRLLLKygdAWVKKYDRS-SLRTLgsVGEPINCEAWEWLHRVVGDSRCTlvDTWWQTEtGGICIAPRP 336
Cdd:cd05940 171 ATIFQYIG--ELCRYLLN---QPPKPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPRIA--EFYAATE-GNSGFINFF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 337 SEEGAEILPAMAMRPFFGIVPVLMD-EKGSVVEGSNvsgALCI--SQAWPGMARTIYGDHQRFvDAYF-------KAYPG 406
Cdd:cd05940 241 GKPGAIGRNPSLLRKVAPLALVKYDlESGEPIRDAE---GRCIkvPRGEPGLLISRINPLEPF-DGYTdpaatekKILRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 407 YYFTGDGAYRT-------EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAFIV 476
Cdd:cd05940 317 VFKKGDAWFNTgdlmrldGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAGMAAIV 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 358248211 477 VKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 529
Cdd:cd05940 395 LQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
23-510 |
2.42e-09 |
|
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: 59.78 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQG 101
Cdd:cd17632 71 AELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEH 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 LRGGRvvelkkivdEAVKHCPTVQHVLV-AHRTDNKVHMGDLD------------VPLEQEMAKED------PVCAPESm 162
Cdd:cd17632 151 LDLAV---------EAVLEGGTPPRLVVfDHRPEVDAHRAALEsarerlaavgipVTTLTLIAVRGrdlppaPLFRPEP- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 163 gSEDMLFML-YTSGSTGMPKGIVHT--------------QAGYLLYAALTHKLVFDHQPGDIfgcvadigwitghsyVVY 227
Cdd:cd17632 221 -DDDPLALLiYTSGSTGTPKGAMYTerlvatfwlkvssiQDIRPPASITLNFMPMSHIAGRI---------------SLY 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 228 GPLCNGAT---------SVLFES-TPVYPNA----GRYWETVerlkiNQFYGAPTAVRLLLKYGDAWVKKYDRSSLR--T 291
Cdd:cd17632 285 GTLARGGTayfaaasdmSTLFDDlALVRPTElflvPRVCDML-----FQRYQAELDRRSVAGADAETLAERVKAELRerV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 292 LG-------SVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETGGIciaprpseegaeILPAMAMRPffgivPV----LM 360
Cdd:cd17632 360 LGgrllaavCGSAPLSAEMKAFMESLLDLD---LHDGYGSTEAGAV------------ILDGVIVRP-----PVldykLV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 361 D--EKGSVVEGS-NVSGALCI--SQAWPGMARTIYGDHQRFvDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINIS 435
Cdd:cd17632 420 DvpELGYFRTDRpHPRGELLVktDTLFPGYYKRPEVTAEVF-DE-----DGFYRTGDVMAELGPDRLVYVDRRNNVLKLS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 436 -GHRLGTAEIEDAIADHPAVPESAVIGyphdiKGEAAF--AFIVVKDSAGDsDVVVQELKSMVAT---KIAK------YA 503
Cdd:cd17632 494 qGEFVTVARLEAVFAASPLVRQIFVYG-----NSERAYllAVVVPTQDALA-GEDTARLRAALAEslqRIAReaglqsYE 567
|
....*..
gi 358248211 504 VPDEILV 510
Cdd:cd17632 568 IPRDFLI 574
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
3-461 |
4.98e-09 |
|
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: 58.97 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 3 RRKERQPWDRFHFlhfaphgRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAES 82
Cdd:cd17641 2 REKDFGIWQEFTW-------ADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 83 LAGRINDAKCKVVITFNQglrgGRVVELKKIVDEAvkhcPTVQHVLVA-------HRTDNKVHMGDLdVPLEQEMAKEDP 155
Cdd:cd17641 75 VAYLLNYTGARVVIAEDE----EQVDKLLEIADRI----PSVRYVIYCdprgmrkYDDPRLISFEDV-VALGRALDRRDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 156 VCAPESMGS---EDMLFMLYTSGSTGMPKGIVhTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCN 232
Cdd:cd17641 146 GLYEREVAAgkgEDVAVLCTTSGTTGKPKLAM-LSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 233 G--------ATSVLFESTPVYPN----AGRYWETV---------ERLKINQFY-----------------GAPTAVRLLL 274
Cdd:cd17641 225 GfivnfpeePETMMEDLREIGPTfvllPPRVWEGIaadvrarmmDATPFKRFMfelgmklglraldrgkrGRPVSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 275 KYG--DAWVKK--YDR---SSLRTLGSVGEPINCEAWEWLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPAM 347
Cdd:cd17641 305 ASWlaDALLFRplRDRlgfSRLRSAATGGAALGPDTFRFFHAIGVP----LKQLYGQTELAGAYTVHR----DGDVDPDT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 348 AMRPFFGiVPVLMDEKGSVVEGSnvsgalcisqawPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGR 427
Cdd:cd17641 377 VGVPFPG-TEVRIDEVGEILVRS------------PGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDR 441
|
490 500 510
....*....|....*....|....*....|....*
gi 358248211 428 MDDVINIS-GHRLGTAEIEDAIADHPAVPESAVIG 461
Cdd:cd17641 442 AKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
408-522 |
1.58e-08 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 57.77 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 408 YFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDiKGEAAF 472
Cdd:TIGR03443 680 YRTGDlGRY-LPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENvtlvrrdkdeepTLVSYivPQD-KSDELE 757
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 473 AFIVVKDSAGDSDVVVQ----------ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 522
Cdd:TIGR03443 758 EFKSEVDDEESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
7-533 |
2.64e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 56.54 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 7 RQPWDRFHflhfaphgrellETTCRLANTLKRHGVHRGDRVAIY--MPV--SPLAVAAMLACARIGAVHT----VIFAGF 78
Cdd:PRK07768 29 RHTWGEVH------------ERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 79 SAESLAgrindakckvVItfnqGLRGGRVVELKKIVDEAVkhcPTVQHVLVAHRTdnkvhMGDLDvpleqemaKEDPVcA 158
Cdd:PRK07768 97 AEDTLR----------VI----GMIGAKAVVVGEPFLAAA---PVLEEKGIRVLT-----VADLL--------AADPI-D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 159 PESMGSEDMLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVFDHQPGDIFG---CVADIGWItGHSYVvygPLCN 232
Cdd:PRK07768 146 PVETGEDDLALMQLTSGSTGSPKAVQITHGN--LYAnaeAMFVAAEFDVETDVMVSwlpLFHDMGMV-GFLTV---PMYF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 233 GATSVLfeSTPV-YPNAGRYWETVerlkINQFYGAPTA---------VRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCE 302
Cdd:PRK07768 220 GAELVK--VTPMdFLRDPLLWAEL----ISKYRGTMTAapnfayallARRLRRQAKP--GAFDLSSLRFALNGAEPIDPA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 303 AWEWLHRV---VGDSRCTLVDTWWQTETG-GICIAPR---------------------PSEEGAEILPAMAMRPFFGIVP 357
Cdd:PRK07768 292 DVEDLLDAgarFGLRPEAILPAYGMAEATlAVSFSPCgaglvvdevdadllaalrravPATKGNTRRLATLGPPLPGLEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 358 VLMDEKGSV----------VEGSNVSgalcisqawPGMaRTIYGdHQRFVDAYfkaypGYYFTGDGAYRTEGGYYQITGR 427
Cdd:PRK07768 372 RVVDEDGQVlpprgvgvieLRGESVT---------PGY-LTMDG-FIPAQDAD-----GWLDTGDLGYLTEEGEVVVCGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 428 MDDVINISGHRLGTAEIEDAIADHPAV-PESAV-IGYPHDIKGEaAFAfIVVKDSAGDSDVVVQELKSMVATKIAKyAV- 504
Cdd:PRK07768 436 VKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE-GFA-VAVESNAFEDPAEVRRIRHQVAHEVVA-EVg 512
|
570 580 590
....*....|....*....|....*....|...
gi 358248211 505 --PDEILVVK--RLPKTRSGKVMRRLLRKIITS 533
Cdd:PRK07768 513 vrPRNVVVLGpgSIPKTPSGKLRRANAAELVTP 545
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
24-522 |
4.50e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 55.56 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtviFAGFSAESLAGRIndakckvvitfnqglr 103
Cdd:cd17654 21 DLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQRS---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvveLKKIVDEAVKHCPTVQHVLVA--HRTDNKVHMgdlDVPLEQEMAkedpvcapesmgsedmlFMLYTSGSTGMPK 181
Cdd:cd17654 81 ------LTVMKKCHVSYLLQNKELDNAplSFTPEHRHF---NIRTDECLA-----------------YVIHTSGTTGTPK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 182 G-----------IVHTQAGYLLYAA----LTHKLVFDHQPGDIFGCVADIG-WITGHSYVVYGPLCngATSVLFESTPVy 245
Cdd:cd17654 135 IvavphkcilpnIQHFRSLFNITSEdilfLTSPLTFDPSVVEIFLSLSSGAtLLIVPTSVKVLPSK--LADILFKRHRI- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 246 pnagryweTVERLkinqfygAPTavrLLLKYGDAWVKKYDRS---SLRTLGSVGE--PINCEAWEWLHRVVGDSRCTLVD 320
Cdd:cd17654 212 --------TVLQA-------TPT---LFRRFGSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWRGKGNRTRIFNIYG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 321 TwwqTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGAL---CISQAWPGMARTIYgdhqrfv 397
Cdd:cd17654 274 I---TEVSCWALAYKVPEEDS---PVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLnrvCILDDEVTVPKGTM------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 dayfkaypgyYFTGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYphdiKGEAAFAFIVV 477
Cdd:cd17654 341 ----------RATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS----DQQRLIAFIVG 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 358248211 478 KDSagdSDVVVQELksmVATKIAKYAVPDEILVVKRLPKTRSGKV 522
Cdd:cd17654 406 ESS---SSRIHKEL---QLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
22-538 |
1.11e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 54.80 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 22 GRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAEslagrinDAKCKVVITfnqg 101
Cdd:PLN02860 35 GHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFE-------EAKSAMLLV---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 102 lrggRVVELkkIVDEAVKH---------CPTVQ-HVLVAHRTDNKVHmGDLDVpLEQEMAKE--------DPVCAPEsmg 163
Cdd:PLN02860 104 ----RPVML--VTDETCSSwyeelqndrLPSLMwQVFLESPSSSVFI-FLNSF-LTTEMLKQralgttelDYAWAPD--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 164 seDMLFMLYTSGSTGMPKG--IVHTqagyllyAALTHKLvfdhqpgdifGCVADIGWITGHSYVVYGPLCN--------- 232
Cdd:PLN02860 173 --DAVLICFTSGTTGRPKGvtISHS-------ALIVQSL----------AKIAIVGYGEDDVYLHTAPLCHigglssala 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 233 ----GATSVL---FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWE 305
Cdd:PLN02860 234 mlmvGACHVLlpkFDAKAAL-------QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 306 wlhrvvgdsrctlvdtwwqtetGGICIAPRpseegAEILPAMAM-------------RPFFGIVPVLMDEKGSVVEGSN- 371
Cdd:PLN02860 307 ----------------------DAKKLFPN-----AKLFSAYGMteacssltfmtlhDPTLESPKQTLQTVNQTKSSSVh 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 372 VSGALCISQAWPGMARTIY-------------GDH-------QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDV 431
Cdd:PLN02860 360 QPQGVCVGKPAPHVELKIGldessrvgriltrGPHvmlgywgQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDR 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 432 INISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD----------SAGDSDVVVQE-LKSMVATK-I 499
Cdd:PLN02860 440 IKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiwsdnekeNAKKNLTLSSEtLRHHCREKnL 519
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 358248211 500 AKYAVPDEILV-VKRLPKTRSGKVMRRLLRKIITSEAQEL 538
Cdd:PLN02860 520 SRFKIPKLFVQwRKPFPLTTTGKIRRDEVRREVLSHLQSL 559
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
23-536 |
1.26e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 54.72 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGL 102
Cdd:PRK08043 235 RKLLKKTLFVGRILEKYSV-EGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELKKIVDEAvkhcptvqhvlvahrtdNKVHMGDL--DVPLEQEMAKEDPVCAPE----SMGSEDMLFMLYTSGS 176
Cdd:PRK08043 314 DKGKLWHLPEQLTQV-----------------RWVYLEDLkdDVTTADKLWIFAHLLMPRlaqvKQQPEDAALILFTSGS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 177 TGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfestpvYPNAGRYwETVE 256
Cdd:PRK08043 377 EGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL------YPSPLHY-RIVP 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 257 RLKINQ----FYGAPTavrLLLKYGdAWVKKYDRSSLRTLGSVGEPINceawewlhrvvgDSRCTLvdtwWQTETG---- 328
Cdd:PRK08043 449 ELVYDRnctvLFGTST---FLGNYA-RFANPYDFARLRYVVAGAEKLQ------------ESTKQL----WQDKFGlril 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 329 ---GI--C---------IAPRPSEEGaEILPAMAMRpffgIVPVLMDEKGSVVE--GSNV-SGALCISQawPGMARTIYG 391
Cdd:PRK08043 509 egyGVteCapvvsinvpMAAKPGTVG-RILPGMDAR----LLSVPGIEQGGRLQlkGPNImNGYLRVEK--PGVLEVPTA 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 392 DhqrfvDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVIgYPHDIKGEA 470
Cdd:PRK08043 582 E-----NARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGEA 655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248211 471 AFAFivVKDSAGDSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 536
Cdd:PRK08043 656 LVLF--TTDSELTREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
40-239 |
3.79e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 53.06 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 40 GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglRGGRVVELKKIVDEAVK 119
Cdd:PTZ00216 142 GLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC-----NGKNVPNLLRLMKSGGM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 120 HCPTVqhvlvahrtdnkVHMGDLDVPLEQE----MAKEDPVCAPESMGS----------EDMLFMLYTSGSTGMPKGIVH 185
Cdd:PTZ00216 217 PNTTI------------IYLDSLPASVDTEgcrlVAWTDVVAKGHSAGShhplnipennDDLALIMYTSGTTGDPKGVMH 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 186 TQAGylLYA---ALTHKLVfdhqpgDIFGCVADigwitGHSYVVYGPLCN----GATSVLF 239
Cdd:PTZ00216 285 THGS--LTAgilALEDRLN------DLIGPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
168-522 |
3.99e-07 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 52.30 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 168 LFMLYTSGSTGMPKGIVHTQAGyLLYAALTHklvfdhqpgdifgcvADIGWITGHS-YVVYGPLCNGATsvLFESTPVYP 246
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQA-LLAQALVL---------------AVLQAIDEGTvFLNSGPLFHIGT--LMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 247 NAGR-----------YWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSvgepinceAWEWLHRVVGDsr 315
Cdd:cd17636 65 AGGTnvfvrrvdaeeVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSSPA--------APEWNDMATVD-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 316 ctlvDTWW--------QTETGG-----------ICIAPRPSeegaeilPAMAMRpffgivpvLMDEKGSVVEGSNVsGAL 376
Cdd:cd17636 133 ----TSPWgrkpggygQTEVMGlatfaalgggaIGGAGRPS-------PLVQVR--------ILDEDGREVPDGEV-GEI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 377 CIsQAWPGMARtiYGDH-----QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 451
Cdd:cd17636 193 VA-RGPTVMAG--YWNRpevnaRRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQH 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248211 452 PAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 522
Cdd:cd17636 263 PAVADAAVIGVPDPRWAQSVKAIVVLKPGAS---VTEAELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
30-253 |
8.56e-07 |
|
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: 51.91 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 30 CRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrggrVV 108
Cdd:cd05938 16 NQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV---------AP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 109 ELKKIVDEAvkhCPTVQ----HVLVAHRTDNKVHMGDLDVPLEQemAKEDPVcaPESMGSE----DMLFMLYTSGSTGMP 180
Cdd:cd05938 87 ELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVISLLDKVDA--ASDEPV--PASLRAHvtikSPALYIYTSGTTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 181 KGIVHTQAGYLLYAALTHklvfdhqpgdIFGCVA-DIGWITGHSYVVYGPL-----C--NGATSVL---FestpvypNAG 249
Cdd:cd05938 160 KAARISHLRVLQCSGFLS----------LCGVTAdDVIYITLPLYHSSGFLlgiggCieLGATCVLkpkF-------SAS 222
|
....
gi 358248211 250 RYWE 253
Cdd:cd05938 223 QFWD 226
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
398-527 |
9.71e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 51.43 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 398 DAYFKAYPGY--YFTGDGAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 475
Cdd:PRK04813 366 AEAFFTFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYV 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 358248211 476 VVKDSAGDSDV-VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 527
Cdd:PRK04813 445 VPKEEDFEREFeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
406-538 |
5.46e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 49.54 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 406 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIadHPAVPES----AVIGYPHDIKGEAafafIVV--KD 479
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEK----LVVlhTC 1092
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 358248211 480 SAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitseAQEL 538
Cdd:PRK08633 1093 GAEDVEELKRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL----ALAL 1144
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
23-461 |
1.22e-05 |
|
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: 47.84 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfnqgl 102
Cdd:cd05910 6 RELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdlDVPLEQEMAKedpvcapesmgsedmlfMLYTSGSTGMPKG 182
Cdd:cd05910 80 ----------------------------------------GIPKADEPAA-----------------ILFTSGSTGTPKG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 183 IVHTQAgylLYAALTHKL--VFDHQPGDI----FGCVAdigwitghsyvVYGPLCnGATSVLFESTPVYP---NAGRYWE 253
Cdd:cd05910 103 VVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQKLVG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 254 TVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD-------------------- 313
Cdd:cd05910 168 AIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSDeaeiltpygatealpvssig 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 314 SRCTLVDTWWQTETG-GICIAPRPSEEGAEILPAMA--MRPFFGIVPVLMDEKGSVVegsnVSGalcisqawPGMARTIY 390
Cdd:cd05910 246 SRELLATTTAATSGGaGTCVGRPIPGVRVRIIEIDDepIAEWDDTLELPRGEIGEIT----VTG--------PTVTPTYV 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248211 391 GDHQrfVDAYFKAYPG----YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 461
Cdd:cd05910 314 NRPV--ATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
405-526 |
1.43e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.84 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 405 PGYYF-TGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAG- 482
Cdd:PRK05851 394 PDDWFpTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG-EGSARPGLVIAAEFRGp 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 358248211 483 DSDVVVQELKSMVATKIAkyAVPDEILVVK--RLPKTRSGKvMRRL 526
Cdd:PRK05851 472 DEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
23-187 |
1.94e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 47.31 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT-----VIFAGFSA--ESLAGRINDAKCKVV 95
Cdd:PRK09192 53 QTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 96 ITfnqglrggrVVELKKIVDEAVKHCPTVqhvlvahrtdnkvhmgdLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSG 175
Cdd:PRK09192 133 IT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSSG 186
|
170
....*....|..
gi 358248211 176 STGMPKGIVHTQ 187
Cdd:PRK09192 187 STRFPRGVIITH 198
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
444-554 |
2.05e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 47.07 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 444 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIvvkdsAGDSDVVVQELKSMVATKIAKYAvPDEILVVKRLPKTRSGKVM 523
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|..
gi 358248211 524 RRLLRKIITSEAQELGD-TTTLEDPSIIAEIL 554
Cdd:PRK09188 319 DDILRLIAMNQIDELDDlLREPEIRGLVEAIA 350
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
24-186 |
2.44e-05 |
|
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: 47.21 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 24 ELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglr 103
Cdd:cd17639 10 EVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 104 ggrvvelkkivdeavkhcptvqhvlvahrtDNKvhmgdldvpleqemaKEDPVCapesmgsedmlfMLYTSGSTGMPKGI 183
Cdd:cd17639 84 ------------------------------DGK---------------PDDLAC------------IMYTSGSTGNPKGV 106
|
...
gi 358248211 184 VHT 186
Cdd:cd17639 107 MLT 109
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
23-191 |
1.63e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 44.48 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtVIFagfsaeslagrINDAkckvvitFNQGL 102
Cdd:PRK09029 32 QQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR--VLP-----------LNPQ-------LPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 RGGRVVELkkivdeavkhcpTVQHVLVAHRTDNkvhMGDLDVPLEQEMAKEDPVC-APESMGSedmlfMLYTSGSTGMPK 181
Cdd:PRK09029 92 LEELLPSL------------TLDFALVLEGENT---FSALTSLHLQLVEGAHAVAwQPQRLAT-----MTLTSGSTGLPK 151
|
170
....*....|
gi 358248211 182 GIVHTQAGYL 191
Cdd:PRK09029 152 AAVHTAQAHL 161
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
23-184 |
5.92e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 42.70 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 23 RELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQgl 102
Cdd:PLN02614 83 QEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 103 rggRVVELKKIVDEAVKHCPTVQHV---------------LVAHRTDNKVHMGD---LDVPLEQEmakedpvcapesmgs 164
Cdd:PLN02614 161 ---KISELFKTCPNSTEYMKTVVSFggvsreqkeeaetfgLVIYAWDEFLKLGEgkqYDLPIKKK--------------- 222
|
170 180
....*....|....*....|
gi 358248211 165 EDMLFMLYTSGSTGMPKGIV 184
Cdd:PLN02614 223 SDICTIMYTSGTTGDPKGVM 242
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
406-537 |
7.76e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.65 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 406 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAafaFIVVKDSAgdsD 485
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER---IILLTTAS---D 1083
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248211 486 VVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKV----MRRLLRKIITSEAQE 537
Cdd:PRK06814 1084 ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEAA 1140
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
6-187 |
6.90e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 39.09 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 6 ERQPWDRFHFLHFAphgrELLETTCRLANTLKRHGVHRGDRVAIYMPVSP----LAVAAMLACARIGAVHtvifagfSAE 81
Cdd:PRK08180 60 ERGADGGWRRLTYA----EALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYAGVPYAPVS-------PAY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 82 SLAGRiNDAKCKVVItfnQGLRGGRVvelkkIVDEAVKHCPTVQHVLVAHR---TDNKVHMGDLDVPLEQEMAKEDPVCA 158
Cdd:PRK08180 129 SLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAATPFAALLATPPTAAV 199
|
170 180 190
....*....|....*....|....*....|..
gi 358248211 159 PESM---GSEDMLFMLYTSGSTGMPKGIVHTQ 187
Cdd:PRK08180 200 DAAHaavGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
43-189 |
6.96e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 39.34 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 43 RGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA----GfSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAV 118
Cdd:PRK12476 91 PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApelpG-HAERLDTALRDAEPTVVLT-----------------TTAA 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248211 119 KhcPTVQHVLVAHRTDNKVHMGDLD-VPleqEMAKEDPVCAPesMGSEDMLFMLYTSGSTGMPKG--IVHTQAG 189
Cdd:PRK12476 153 A--EAVEGFLRNLPRLRRPRVIAIDaIP---DSAGESFVPVE--LDTDDVSHLQYTSGSTRPPVGveITHRAVG 219
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
171-414 |
7.93e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 39.26 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 171 LYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVAD-IGW--ITGHSYVVYGPLCNGATSVLFESTPVypn 247
Cdd:PRK12582 226 LFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPDPPPPVSLDwMPWnhTMGGNANFNGLLWGGGTLYIDDGKPL--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 248 AGRYWETVERLK-INQ--FYGAPTAVRLL---LKYGDAWVKKYdRSSLRTLGSVGEPINCEAWEWLH----RVVGdSRCT 317
Cdd:PRK12582 302 PGMFEETIRNLReISPtvYGNVPAGYAMLaeaMEKDDALRRSF-FKNLRLMAYGGATLSDDLYERMQalavRTTG-HRIP 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248211 318 LVDTWWQTETGGI-CIAPRPSEEGAEI---LPAMAMRpffgIVPVlmDEKGSV-VEGSNVSgalcisqawPGMartiYGD 392
Cdd:PRK12582 380 FYTGYGATETAPTtTGTHWDTERVGLIglpLPGVELK----LAPV--GDKYEVrVKGPNVT---------PGY----HKD 440
|
250 260
....*....|....*....|..
gi 358248211 393 HQRFVDAYFKAypGYYFTGDGA 414
Cdd:PRK12582 441 PELTAAAFDEE--GFYRLGDAA 460
|
|
| |
