|
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 ... |
54-676 |
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: 1108.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 54 QPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTgKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERD 133
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWEGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 213
Cdd:TIGR02188 82 EPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 214 KVVITFNQGLRGGRVVELKKIVDEAVKHCP-TVQHVLVAHRTDNKV-HMGD-LDVPLEQEMAKEDPVCAPESMGSEDMLF 290
Cdd:TIGR02188 162 KLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVEgRDVWWHDLMAKASAYCEPEPMDSEDPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 291 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAG 370
Cdd:TIGR02188 242 ILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 371 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGG 450
Cdd:TIGR02188 322 RFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 451 ICIAPRPSeeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYF 530
Cdd:TIGR02188 402 IMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 531 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQ 610
Cdd:TIGR02188 480 TGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 611 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 676
Cdd:TIGR02188 560 ELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIE 625
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
57-667 |
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: 1096.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 57 SYPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPG 136
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 217 ITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHM-GDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTS 295
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 296 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWET 375
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 376 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAP 455
Cdd:cd05966 321 VEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 456 RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 535
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNEVEG-EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 536 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 615
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 28416953 616 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLED 667
Cdd:cd05966 558 VRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEE-ELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
58-682 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 983.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 58 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDfsTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPGT 137
Cdd:PRK00174 19 YKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIWEGDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 TFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGD-LDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSG 296
Cdd:PRK00174 176 TADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEgRDLWWHELVAGASDECEPEPMDAEDPLFILYTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETV 376
Cdd:PRK00174 256 STGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 377 ERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPR 456
Cdd:PRK00174 336 DKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 457 PseeGA-EILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 535
Cdd:PRK00174 416 P---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEG-GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGA 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 536 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 615
Cdd:PRK00174 492 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNW 571
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 616 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLEDPSIIAEILSVYQKCK 682
Cdd:PRK00174 572 VRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEARQNRK 637
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
102-674 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 830.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 102 WFLGGQLNVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAA 181
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 182 MLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMG 261
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 262 DlDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWIT 341
Cdd:COG0365 161 G-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 342 GHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN 421
Cdd:COG0365 240 GHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 CEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQ 501
Cdd:COG0365 320 PEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 502 AWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 581
Cdd:COG0365 393 PWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 582 GYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGD 661
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA--EGRPLGD 550
|
570
....*....|...
gi 28416953 662 TTTLEDPSIIAEI 674
Cdd:COG0365 551 TSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
55-677 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 667.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 55 PGSYPALSAQAAREPAAFWGPLArDTLVWDTPYHTVWDC----DFSTG--KIGWFLGGQLNVSVNCLDQHVRK-SPESVA 127
Cdd:PLN02654 29 PQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCLDRNVEAgNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 128 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGR 207
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 208 INDAKCKVVITFNQGLRGGRVVELKKIVDEA----------VKHCPTVQHVLVAHRTDNKVHMGDlDVPLEQEMAKEDPV 277
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-DVWWQDVVPNYPTK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 278 CAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATS 357
Cdd:PLN02654 267 CEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 358 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRC 437
Cdd:PLN02654 347 LVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRC 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 438 TLVDTWWQTETGGICIAPRPseeGAEIL-PAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAWPGMARTIYGDHQR 516
Cdd:PLN02654 427 PISDTWWQTETGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSWPGAFRTLYGDHER 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 517 FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 596
Cdd:PLN02654 503 YETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFV 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 597 VVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 676
Cdd:PLN02654 583 TLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIA 662
|
.
gi 28416953 677 V 677
Cdd:PLN02654 663 L 663
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
64-644 |
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: 645.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 64 QAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEpGTEVR- 140
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 QGLRGGRVVELKKIVDEAVK-HCPTVQHVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGST 298
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 299 GMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVER 378
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 379 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPs 458
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLP- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 459 eeGAEILPA-MAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYR 537
Cdd:cd17634 404 --GAIELKAgSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 538 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVA 617
Cdd:cd17634 481 DEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
570 580
....*....|....*....|....*..
gi 28416953 618 TKIAKYAVPDEILVVKRLPKTRSGKVM 644
Cdd:cd17634 561 KEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
58-674 |
0e+00 |
|
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: 578.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 58 YPALSAQAAREPAAFWGPLARdTLVWDTPYHTVWDCDfSTGKIGWFLGGQLNVSVNCLDQHVRKS-PESVALIWERDEPG 136
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 217 ITFNQGLRGGRVVELKKIVDEAVK---HCPtvQHVLVAHRTDNKVHMGD--LDVPLEQEMAKEDPV-CAPesMGSEDMLF 290
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALElsgHKP--HHVLVLNRPQVPADLTKpgRDLDWSELLAKAEPVdCVP--VAATDPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 291 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV-YPNA 369
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 370 GRYWETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTE 447
Cdd:cd05967 315 GAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 448 TGG------ICIAPRPSEEGAEILPAMAMRpffgiVPVLmDEKGSVVeGSNVSGALCISQAW-PGMARTIYGDHQRFVDA 520
Cdd:cd05967 392 TGWpitanpVGLEPLPIKAGSPGKPVPGYQ-----VQVL-DEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 521 YFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD 600
Cdd:cd05967 465 YLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKE 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 601 SAG-DSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTLEDPSIIAEI 674
Cdd:cd05967 545 GVKiTAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
57-674 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 532.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 57 SYPALSAQAAREPAAFWGPLARdtLV-WDTPYHTVwdCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVALIWERDE 134
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR--RIdWQTPFTQV--LDYSNPPFArWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 135 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 214
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 215 VVITFNQGLRGGRVVELKKIVDEAV---KHCPtvQHVLVAHR-TDNKVHMGDLDVPLEQEMAK-EDPVCAPESMGSEDML 289
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVDRgLAPMARVAGRDVDYATLRAQhLGARVPVEWLESNEPS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 290 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNA 369
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 370 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG 449
Cdd:PRK10524 317 GIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP---VIDNYWQTETG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 450 GICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAY-PG 527
Cdd:PRK10524 394 WPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 528 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD- 606
Cdd:PRK10524 474 VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADr 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 607 ----VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitSEAQELGDTTTLEDPSIIAEI 674
Cdd:PRK10524 554 earlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI--AEGRDPGDLTTIEDPAALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
56-668 |
3.13e-177 |
|
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: 518.58 E-value: 3.13e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 56 GSYPALSAQAAREPAAFWGPLARDTLVW--DTPYHTVwdcDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWE 131
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIEwyEPPYQTL---DLSGGKpwAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 132 rDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDA 211
Cdd:cd05968 84 -GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 212 KCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSEDMLFM 291
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGR-DLSYDEEKETAGDGAERTESEDPLMI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 292 LYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGR 371
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 372 YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTE-TGG 450
Cdd:cd05968 321 LWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 451 I--CIAPRPseegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGY 528
Cdd:cd05968 401 IlgNVLIKP------IKPSSFNGPVPGMKADVLDESGKPARPE--VGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 529 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVV 608
Cdd:cd05968 473 WVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEAL 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 609 VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEaqELGDTTTLEDP 668
Cdd:cd05968 553 AEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
102-667 |
1.56e-150 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 448.58 E-value: 1.56e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 102 WFLGGQLNVSVNCLDQHVrKSP--ESVALIWERdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAV 179
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 180 AAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRggrvvelKKIVDEavkhCPTVQHVLVahrTDNKVH 259
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD----LPSLKHVLL---VGEDVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 260 MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQagyllYAALTH----KLVFDHQPGDIFGCVA 335
Cdd:PRK04319 179 EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NAMLQHyqtgKYVLDLHEDDVYWCTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 336 DIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 415
Cdd:PRK04319 254 DPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 416 VGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEEgaeILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSG 495
Cdd:PRK04319 331 VGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAMD---IKPGSMGKPLPGIEAAIVDDQGNELP-PNRMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 ALCISQAWPGMARTIYGDHQRFvDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 575
Cdd:PRK04319 404 NLAIKKGWPSMMRGIWNNPEKY-ESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 576 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRkiitse 655
Cdd:PRK04319 481 AEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK------ 554
|
570
....*....|....*.
gi 28416953 656 AQEL----GDTTTLED 667
Cdd:PRK04319 555 AWELglpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
142-651 |
5.49e-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: 388.78 E-value: 5.49e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 222 glrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvplEQEMAkedpvcapESMGSEDMLFMLYTSGSTGMP 301
Cdd:cd05969 79 ----------------------------------------------TEELY--------ERTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 302 KGIVHTQAGYLLYAaLTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKI 381
Cdd:cd05969 105 KGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 382 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeG 461
Cdd:cd05969 181 TVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP---C 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 462 AEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRFvDAYFKAypGYYFTGDGAYRTEGG 541
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELP-PGTKGILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 542 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 621
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLG 410
|
490 500 510
....*....|....*....|....*....|
gi 28416953 622 KYAVPDEILVVKRLPKTRSGKVMRRLLRKI 651
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
142-650 |
6.40e-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: 336.62 E-value: 6.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 222 glrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMP 301
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 302 KGIVHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNagRYWETVERLKI 381
Cdd:cd05972 97 KGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 382 NQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgICIAPRPseeG 461
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP---D 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 462 AEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGG 541
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 542 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 621
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
gi 28416953 622 KYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
115-556 |
6.05e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 323.11 E-value: 6.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHRTDnkvhMGDLDVPLEQEMAKE 274
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITD--------DALKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQ----PGDIFGCVADIGWITGHSYVVYGP 350
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHR 430
Cdd:pfam00501 223 LLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 431 VVGdsrCTLVDTWWQTETGGICIAPRPSEEGAEILPAmAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTI 510
Cdd:pfam00501 300 LFG---GALVNGYGLTETTGVVTTPLPLDEDLRSLGS-VGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 28416953 511 YGDHQRFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINIS 556
Cdd:pfam00501 374 LNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
115-658 |
8.16e-99 |
|
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: 310.97 E-value: 8.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemake 274
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 dpvcapesmgsedmlFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG 354
Cdd:COG0318 104 ---------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 355 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGd 434
Cdd:COG0318 168 ATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 srCTLVDTWWQTETGGICIAPRpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD- 513
Cdd:COG0318 241 --VRIVEGYGLTETSPVVTVNP--EDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPGEVGEIVVRG--PNVMKGYWNDp 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 514 ---HQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 590
Cdd:COG0318 314 eatAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 591 AAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 658
Cdd:COG0318 387 RVVAFVVLRP---GAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
56-652 |
1.97e-82 |
|
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: 273.38 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 56 GSYPALSAQAAREPAAFWgplardTLVWD---TPYHTVWDCDFSTGKI----GWFLGGQLNVSVNCLdQHvRKSPESVAL 128
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLL-RH-ADADDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 129 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 209 NDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVP----LEQEMAKE-DPVCAPESM 283
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVvyGPLCNGATSVLFEST 363
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 364 PVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTW 443
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 444 WQTETGG--IC--------IAP-RPSEEGAEILpAMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMARTIYG 512
Cdd:cd05943 399 LASISGGtdIIscfvggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 513 DH--QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 590
Cdd:cd05943 468 DPdgSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDE 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 591 AAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 652
Cdd:cd05943 548 RVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII 609
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
287-644 |
3.38e-79 |
|
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: 255.67 E-value: 3.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 287 DMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHqPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFEStpvy 366
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-EGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 367 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT 446
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 447 ETGGICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDayfkaYP 526
Cdd:cd04433 150 ETGGTVATGPPDDD--ARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVD-----ED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 527 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 606
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---D 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 28416953 607 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 644
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
54-680 |
5.21e-79 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 264.68 E-value: 5.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 54 QPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVwdcdFSTGKI--GWFLGGQLNVSVNCLDQHVrKSP---ESVAL 128
Cdd:PTZ00237 6 DPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKV----YSGDEIypDWFKGGELNTCYNVLDIHV-KNPlkrDQDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 129 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:PTZ00237 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 209 NDAKCKVVITFNQGLRGGRVVELKKIVDEAV---KHCPTvqHVLVAHRTD-----NKVHMGD-------LDVPLEQEMAK 273
Cdd:PTZ00237 161 ETITPKLIITTNYGILNDEIITFTPNLKEAIelsTFKPS--NVITLFRNDitsesDLKKIETiptipntLSWYDEIKKIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 ED---PVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVvYGP 350
Cdd:PTZ00237 239 ENnqsPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCNGATSVLFESTPVYPNAGR--YWETVERLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPINCEAW 425
Cdd:PTZ00237 318 LSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 426 EWLHRVVGdSRCTLVdtWWQTETGG---ICIAPRPSEEGAEILPAmamrPFfgIVPVLMDEKGSVVeGSNVSGALCISQA 502
Cdd:PTZ00237 398 EYIENKLK-IKSSRG--YGQTEIGItylYCYGHINIPYNATGVPS----IF--IKPSILSEDGKEL-NVNEIGEVAFKLP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 WP-GMARTIYGDHQRFvDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 581
Cdd:PTZ00237 468 MPpSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 582 GYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS----MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 657
Cdd:PTZ00237 547 GIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNY 626
|
650 660
....*....|....*....|...
gi 28416953 658 ELGDTTtlEDPSIIAEILSVYQK 680
Cdd:PTZ00237 627 QLPDNV--NDSEIFYKIKELYMK 647
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
56-648 |
1.26e-77 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 261.27 E-value: 1.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 56 GSYPALSAQAAREPAAFWgplardTLVWD-------TPYHTVWDcdfSTGKIG--WFLGGQLNVSVNCLDQHvrkSPESV 126
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 127 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAG 206
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 207 RINDAKCKVVITFNqGLR-GGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLD--VPLEQEMAK-EDPVCAPES 282
Cdd:PRK03584 181 RFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF----GCvadiGWITgHSYVVYGPLCnGATSV 358
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 359 LFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrct 438
Cdd:PRK03584 334 LYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA---- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 439 lvDTWWQTETGG--IC---IAprpseeGAEILP-----------AMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQA 502
Cdd:PRK03584 410 --DVWLASISGGtdICscfVG------GNPLLPvyrgeiqcrglGMAVEAW--------DEDGRPVVG--EVGELVCTKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 WPGMArtIY----GDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 578
Cdd:PRK03584 472 FPSMP--LGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDS 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28416953 579 AVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM----RRLL 648
Cdd:PRK03584 550 LVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
107-649 |
1.03e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 244.33 E-value: 1.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 107 QLNVSvNCLDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACA 186
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 187 RIGAV-HTV-IFagFSAESLAGRINDAKCKVVItFNQglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKVHmGDLD 264
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS--------EFVPLLAAILPQLPTVRTVIVEGDGPAAPL-APEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 265 VPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTqagyllyaaltHKLVFDHqpgdIFGCVADIGWITGHS 344
Cdd:PRK06187 146 GEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS-----------HRNLFLH----SLAVCAWLKLSRDDV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 345 YVV-------------YGPLCNGATSVL---FESTPVypnagryWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRS 408
Cdd:PRK06187 211 YLVivpmfhvhawglpYLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 409 SLRTLGSVGEPIN---CEAWEWLHRvvgdsrCTLVDTWWQTETGGICIAPRPSEEGAEILPAM--AMRPFFGIVPVLMDE 483
Cdd:PRK06187 282 SLRLVIYGGAALPpalLREFKEKFG------IDLVQGYGMTETSPVVSVLPPEDQLPGQWTKRrsAGRPLPGVEARIVDD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 484 KGSVVEGSNVS-GALCISQAWpgMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGT 562
Cdd:PRK06187 356 DGDELPPDGGEvGEIIVRGPW--LMQGYWNRPEATAETI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 563 AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 642
Cdd:PRK06187 431 RELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP---GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGK 507
|
....*..
gi 28416953 643 VMRRLLR 649
Cdd:PRK06187 508 ILKRVLR 514
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
109-649 |
1.16e-70 |
|
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: 239.32 E-value: 1.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 109 NVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 188
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWC-DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 189 GAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGlrggrvvELKKIVDEAVKHCPTVQhVLVahrtdnKVHMGDLD--VP 266
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECPSKP-KLV------WVGDPVPEgwID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 267 LEQEMAKEDPV----CAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITG 342
Cdd:cd05970 162 FRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 343 HSYVVYGPLCNGATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINC 422
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAWEWLHRVVGDSrctLVDTWWQTETGgICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNvSGALCI--S 500
Cdd:cd05970 316 EVFNTFKEKTGIK---LMEGFGQTETT-LTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 501 QAWP-GMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 579
Cdd:cd05970 388 KGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 580 VIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05970 465 VTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
141-650 |
1.99e-69 |
|
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: 233.18 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 220
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglrggrvvelkkivDEAVKHcptvqhvlvahrtdnkvhmgDLDvpleqemakedpvcapesmgsEDMLFMLYTSGSTGM 300
Cdd:cd05973 79 ---------------DAANRH--------------------KLD---------------------SDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTQAGYLLYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgryWETVERLK 380
Cdd:cd05973 103 PKGVPVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 381 INQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgICIA-----P 455
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELG-MVLAnhhalE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 456 RPSEEGAEILPAMAMRpffgiVPVLMDEKGSVVEGsnVSGALCISQA-WPGMArtiYGDHQRFVDAYFKAypGYYFTGDG 534
Cdd:cd05973 254 HPVHAGSAGRAMPGWR-----VAVLDDDGDELGPG--EPGRLAIDIAnSPLMW---FRGYQLPDTPAIDG--GYYLTGDT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 535 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS 614
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQL 401
|
490 500 510
....*....|....*....|....*....|....*.
gi 28416953 615 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
109-650 |
2.33e-68 |
|
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: 233.13 E-value: 2.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 109 NVSVNCLDQHVRKS-----PESVALIWERDEpGTEVRITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAM 182
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGK-GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 183 LACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVQ-HVLVAHRTDNkvhmG 261
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKtKLLVSEKSRD----G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 262 DLDVPLEQEMAKEDPVCApeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWIT 341
Cdd:cd05928 152 WLNFKELLNEASTEHHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 342 GHSYVVYGPLCNGATsVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPIN 421
Cdd:cd05928 230 SAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 CEAWE-WLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNVSGALCI 499
Cdd:cd05928 305 PEVLEkWKAQTGLD----IYEGYGQTETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEGDIGIRV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 500 SQAWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 579
Cdd:cd05928 377 KPIRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28416953 580 VIGYPHDIKGEAAFAFIVVKD--SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05928 455 VVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
140-649 |
3.84e-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: 223.78 E-value: 3.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVitf 219
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 nqglrggrVVE---LKKIVDEAVKHCPTVQHVLVAhrtdnKVHMGDLDVP-LEQEMAKEDPVCAPESMGSEDMLFMLYTS 295
Cdd:cd05959 106 --------VVSgelAPVLAAALTKSEHTLVVLIVS-----GGAGPEAGALlLAELVAAEAEQLKPAATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 296 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWET 375
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 376 VERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVgdsrCTLVDTWWQTETGGICIA 454
Cdd:cd05959 250 IRRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGErWKARFG----LDILDGIGSTEMLHIFLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 455 PRPSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQawPGMArTIYGdHQRfvDAYFKAYPGYYF-TGD 533
Cdd:cd05959 324 NRPGR----VRYGTTGKPVPGYEVELRDEDGGDVADG-EPGELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTrTGD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 534 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELK 613
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELK 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 28416953 614 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05959 473 EFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
137-644 |
4.34e-65 |
|
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: 222.86 E-value: 4.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 217 ITFNQGLrggrvvelkKIVDEAVKHCPTVQHV-LVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTS 295
Cdd:cd05911 87 FTDPDGL---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 296 GSTGMPKGivhtqagyllyAALTHK-LVFDH-----------QPGDIFGCVADIGWITGHSYVVYGPLCnGATSVLFESt 363
Cdd:cd05911 156 GTTGLPKG-----------VCLSHRnLIANLsqvqtflygndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 364 pvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTW 443
Cdd:cd05911 223 ---FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 444 WQTETGGICIAPRPSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS--QAWPG-------MARTI 510
Cdd:cd05911 296 GMTETGGILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyynnpeaTKETF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 590
Cdd:cd05911 368 DED-------------GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 591 AAFAFIVVKDSAGDSDvvvQELKSMVATKIAKY-AVPDEILVVKRLPKTRSGKVM 644
Cdd:cd05911 435 LPRAYVVRKPGEKLTE---KEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-649 |
2.37e-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: 219.61 E-value: 2.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 215
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 216 VITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDpvcapesmGSEDMLFMLYTS 295
Cdd:cd05971 82 LVT--------------------------------------------------------D--------GSDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 296 GSTGMPKGIVHTQA---GYLLYAALTHKLVfdHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnaGRY 372
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDP--KAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 373 WETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG--- 449
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFGVE---VNEFYGQTECNlvi 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 450 GICIAPRPSEEGAeilpaMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYY 529
Cdd:cd05971 249 GNCSALFPIKPGS-----MG-KPIPGHRVAIVDDNGTPLP-PGEVGEIAVELPDPVAFLG-YWNNPSATEKKMAG--DWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 530 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVV 609
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 28416953 610 QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05971 399 REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
115-645 |
7.76e-64 |
|
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: 218.25 E-value: 7.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVItfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemake 274
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 dpvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG 354
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 355 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinceAWEWLHRVVGD 434
Cdd:cd17631 166 GTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 SRCTLVDTWWQTETG-GICIAPRpseEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTIYGD 513
Cdd:cd17631 236 RGVKFVQGYGMTETSpGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVPP-GEVGEIVVRG--PHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 514 HQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 593
Cdd:cd17631 310 PEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 28416953 594 AFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 645
Cdd:cd17631 387 AVVVPRPGA---ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
56-685 |
3.88e-63 |
|
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: 222.06 E-value: 3.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 56 GSYPALSAQAAREPAAFWGPLARDT-LVWDTPYHTVWDCDFSTGKIgWFLGGQLNVSVNCLdqhvRKSPESVALIWeRDE 134
Cdd:TIGR01217 35 GGYDALHRWSVDELDTFWKAVWEWFdVRFSTPCARVVDDRTMPGAQ-WFPGARLNYAENLL----RAAGTEPALLY-VDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 135 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 214
Cdd:TIGR01217 109 THEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 215 VVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVahrtdnkvhmgdldVPLEQEMAKEDPVcAPESMGSEDM------ 288
Cdd:TIGR01217 189 LLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVH--------------IPYLGPRETEAPK-IDGALDLEDFtaaaqa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 289 -------------LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITgHSYVVYGpLCNGA 355
Cdd:TIGR01217 254 aelvfeqlpfdhpLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM-WNWLVSG-LATGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 356 TSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgds 435
Cdd:TIGR01217 332 TLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY------ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 436 RCTLVDTWWQTETGGI----CIAPRPSEEGAEILPAMAmrPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIY 511
Cdd:TIGR01217 406 DEIKADVWLASISGGTdicsCFAGANPTLPVHIGEIQA--PGLGTAVQSWDPEGKPVTGE--VGELVCTNPMPSMPIRFW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 512 GDHQ--RFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 589
Cdd:TIGR01217 482 NDPDgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 590 EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSeaqelgdtTTLEDPS 669
Cdd:TIGR01217 562 YRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQG--------TPVDNPG 633
|
650
....*....|....*...
gi 28416953 670 IIA--EILSVYQKCKDKQ 685
Cdd:TIGR01217 634 AIDnpELLDLYEELAELR 651
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
123-648 |
3.89e-61 |
|
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: 211.23 E-value: 3.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapes 282
Cdd:cd05930 75 RLAYILEDSGAKLVLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 mGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFES 362
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 363 TPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDT 442
Cdd:cd05930 168 EVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 443 WWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGDH----QRFV 518
Cdd:cd05930 241 YGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPV-PPGVPGELYIGGA--GLARGYLNRPeltaERFV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 519 DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVv 598
Cdd:cd05930 318 PNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV- 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 28416953 599 kdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05930 397 --PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
141-649 |
2.25e-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: 203.46 E-value: 2.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 220
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGM 300
Cdd:cd05919 89 ---------------------------------------------------------------SADDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADI--GWITGHSyvVYGPLCNGATSVLFestPVYPNAGRYWETVER 378
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 379 LKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPS 458
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 459 EegaeILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI--SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAY 536
Cdd:cd05919 256 A----WRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVrgPSAAVGYWNNPEKSRATFNG-------GWYRTGDKFC 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 537 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMV 616
Cdd:cd05919 324 RDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHL 403
|
490 500 510
....*....|....*....|....*....|...
gi 28416953 617 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05919 404 LERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
129-650 |
1.17e-56 |
|
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: 200.93 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 129 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTvIFAGFSAESLAGR 207
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT-INPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 208 INDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPL---EQEMAKEDPVCAPESMG 284
Cdd:cd12119 93 INHAEDRVVFVDR---------DFLPLLEAIAPRLPTVEHVVVM--TDDAAMPEPAGVGVlayEELLAAESPEYDWPDFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 285 SEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLVFDHQPGDIFGCVADI----GW-------ITGHSYVVYGPLC 352
Cdd:cd12119 162 ENTAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVGAKLVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 353 NGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINCEAWEWLH 429
Cdd:cd12119 242 DPASLA---------------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 rvvgdsrctlVDT---WWQTETGGICIAPRP-------SEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVS-GALC 498
Cdd:cd12119 305 ----------VRVihaWGMTETSPLGTVARPpsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAvGELQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 499 ISQAWpgMARTIYGDHQR----FVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPA 574
Cdd:cd12119 375 VRGPW--VTKSYYKNDEEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 575 VPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd12119 446 VAEAAVIGVPHPKWGERPLAVVVLKE---GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
115-649 |
1.79e-52 |
|
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: 188.16 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVI---TFNQGLRGGRVVELKKIVDEavkhcptvqhvlvahrtdnkvhmgdldvpleqem 271
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIvavSFTDLLAAGAPLGERVALTP---------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 272 akedpvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHK--LVFDHQPGDIFGCVADIGWITGHSYVVYG 349
Cdd:cd05936 125 --------------EDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:cd05936 190 PLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVVGdsrCTLVDTWWQTETG-GICIAP-----RPSEEGaeilpamamRPFFGIVPVLMDEKGSVVEGSNVsGALCIS--Q 501
Cdd:cd05936 264 ELTG---VPIVEGYGLTETSpVVAVNPldgprKPGSIG---------IPLPGTEVKIVDDDGEELPPGEV-GELWVRgpQ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 502 AWPGmartiYGDH-----QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 576
Cdd:cd05936 331 VMKG-----YWNRpeetaEAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVA 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28416953 577 ESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05936 399 EAAVVGVPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
115-653 |
2.66e-49 |
|
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: 180.73 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtV 194
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFS-----AESLAGRInDAKCKVVITFNQGLRggrvveLKKIVDEAVKHCPTVQHVLVAHRTDNKVhmgDLDVPLEQ 269
Cdd:COG1021 103 VFALPAhrraeISHFAEQS-EAVAYIIPDRHRGFD------YRALARELQAEVPSLRHVLVVGDAGEFT---SLDALLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 270 EMAKEDPVCAPEsmgseDMLFMLYTSGSTGMPKGIVHTQAGYLlYAALTHKLVFDHQPGDIFGCVADIGwitgHSY---- 345
Cdd:COG1021 173 PADLSEPRPDPD-----DVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAEICGLDADTVYLAALPAA----HNFplss 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 346 -VVYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GS------ 415
Cdd:COG1021 243 pGVLGVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLqvgGAklspel 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 416 ---VGEPINCeaweWLHRVVG------------DSRCTLVDTwwQtetgGiciapRPSEEGAEILpamamrpffgIVpvl 480
Cdd:COG1021 317 arrVRPALGC----TLQQVFGmaeglvnytrldDPEEVILTT--Q----G-----RPISPDDEVR----------IV--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 481 mDEKGS-VVEGSnvSGALcisqawpgMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAYRTEGGYYQIT 546
Cdd:COG1021 369 -DEDGNpVPPGE--VGEL--------LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 547 GRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATK-IAKYAV 625
Cdd:COG1021 429 GRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEP----LTLAELRRFLRERgLAAFKL 504
|
570 580
....*....|....*....|....*...
gi 28416953 626 PDEILVVKRLPKTRSGKVMRRLLRKIIT 653
Cdd:COG1021 505 PDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
57-657 |
3.38e-49 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 184.13 E-value: 3.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 57 SYPALSAQAAREPAAFWgplardTLVWDT---PYHT----VWDCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVAL 128
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW------SIVLDElslVFSVpprcILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 129 IWeRDEPGTEV---RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLA 205
Cdd:PLN03052 195 IW-RDEGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 206 GRINDAKCKVVITFNQGLRGGRVVELKKIVDEAvkHCPTVQhVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPES--- 282
Cdd:PLN03052 274 TRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEyka 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 --MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALT--HklvFDHQPGDIFGCVADIGWITGHsYVVYGPLCNGATSV 358
Cdd:PLN03052 351 veQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLA 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 359 LFESTPVYPNAGRYwetVERLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINCEAWEWLHrvvg 433
Cdd:PLN03052 427 LYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWLM---- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 434 dSRCT---LVDTWWQTETGGICIAP---RPSEEGAEILPAMAMRPFfgivpvLMDEKGSVVEgSNVSG----ALCisqaw 503
Cdd:PLN03052 493 -SRAGykpIIEYCGGTELGGGFVTGsllQPQAFAAFSTPAMGCKLF------ILDDSGNPYP-DDAPCtgelALF----- 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 504 PGM----ARTIYGDHQrfvDAYFKAYPGYYFT-----GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI-ADHP 573
Cdd:PLN03052 560 PLMfgasSTLLNADHY---KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADE 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 574 AVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVP----DEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PLN03052 637 SVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVLR 716
|
....*...
gi 28416953 650 KIITSEAQ 657
Cdd:PLN03052 717 QQLAQELS 724
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-658 |
1.10e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 176.28 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK08316 21 ARRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITfNQGLRGgrvvelkkIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKEDPVC 278
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLV-DPALAP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 APE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVfdhqpgdifGCVADIGWITG----------HS--- 344
Cdd:PRK08316 163 EPDvELADDDLAQILYTSGTESLPKGAMLT------HRALIAEYV---------SCIVAGDMSADdiplhalplyHCaql 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 345 YVVYGP-LCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTlGSVGEPI-NC 422
Cdd:PRK08316 228 DVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRK-GYYGASImPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAWEWLHRVVGDSRctLVDTWWQTEtggicIAP-----RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgal 497
Cdd:PRK08316 301 EVLKELRERLPGLR--FYNCYGQTE-----IAPlatvlGPEE--HLRRPGSAGRPVLNVETRVVDDDGNDVA-------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 498 cisqawPGMARTIYGDHQRFVDAYFK-------AYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 569
Cdd:PRK08316 364 ------PGEVGEIVHRSPQLMLGYWDdpektaeAFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEAL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 570 ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK08316 438 YTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA---TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
....*....
gi 28416953 650 KIITSEAQE 658
Cdd:PRK08316 515 ERYAGAFTD 523
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
138-649 |
2.42e-47 |
|
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: 173.43 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHR-GDRVAIYMPVSPLAVAAMLACARIGAVhtvifagfsaeslagrindakCKVV 216
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 217 ITFnqgLRGGrvvELKKIVDEAvkhcpTVQHVLVAHRTdnkvhmgdldvpleqemakedpvcapesMGSEDMLFMLYTSG 296
Cdd:cd05958 67 MPL---LRPK---ELAYILDKA-----RITVALCAHAL----------------------------TASDDICILAFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 376
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 377 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPR 456
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 457 PSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQawPGMARTIYGDHQRfvdAYFKAypGYYFTGDGAY 536
Cdd:cd05958 259 PGD----ARPGATGKPVPGYEAKVVDDEGNPVPDGTI-GRLAVRG--PTGCRYLADKRQR---TYVQG--GWNITGDTYS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 537 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMV 616
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHA 406
|
490 500 510
....*....|....*....|....*....|...
gi 28416953 617 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05958 407 KAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-650 |
1.21e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 173.17 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK07656 11 LARAARRFGDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFnQGLRGgrvvelkkiVDEAVKHC-PTVQHVlVAHRTDNKVHMGDLDVPLEQEMAK 273
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVL-GLFLG---------VDYSATTRlPALEHV-VICETEEDDPHTEKMKTFTDFLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 EDPVCAPESMGSEDMLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHKLvfDHQPGD----------IFGCVAdiGWIT 341
Cdd:PRK07656 154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMltHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 342 ghsyvvygPLCNGATsVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPIn 421
Cdd:PRK07656 229 --------PLMRGAT-ILPL--PVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 ceAWEWLHRVVGDSRCTLVDTWWQ-TETGGI-CIAPRpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI 499
Cdd:PRK07656 294 --PVALLERFESELGVDIVLTGYGlSEASGVtTFNRL--DDDRKTVAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 500 S-----QAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 570
Cdd:PRK07656 369 RgpnvmKGYYDDpeatAAAIDAD-------------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 571 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:PRK07656 436 EHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE---LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
123-650 |
1.97e-46 |
|
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: 172.11 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05926 1 PDAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITFNQGL---------RGGRVVELKkiVDEAVKHCPTVQHVLVAHRTDNKVhmgdldvpleqemAK 273
Cdd:cd05926 77 EFEFYLADLGSKLVLTPKGELgpasraaskLGLAILELA--LDVGVLIRAPSAESLSNLLADKKN-------------AK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 EDPVCAPEsmgseDMLFMLYTSGSTGMPKGIVHTQAGYLL---YAALTHKLvfdhQPGDIFGCVADIGWITGHSYVVYGP 350
Cdd:cd05926 142 SEGVPLPD-----DLALILHTSGTTGRPKGVPLTHRNLAAsatNITNTYKL----TPDDRTLVVMPLFHVHGLVASLLST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLH 429
Cdd:cd05926 213 LAAGGSVVL----PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPP--PKLRFIRSCSASLPPAVLEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVVGdsrCTLVDTWWQTETGgiciaprpseegaeilPAMAMRPF------FGIVP-------VLMDEKGSVVEgSNVSGA 496
Cdd:cd05926 287 ATFG---APVLEAYGMTEAA----------------HQMTSNPLppgprkPGSVGkpvgvevRILDEDGEILP-PGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 497 LCISQawPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 576
Cdd:cd05926 347 ICLRG--PNVTRGYLNNPEANAEAAFKD--GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVL 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28416953 577 ESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05926 423 EAVAFGVPDEKYGEEVAAAVVLR---EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
117-649 |
3.36e-46 |
|
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: 171.37 E-value: 3.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 197 AGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqHVLVAHRTDNKVHMGDLDVPLEQEMAKEDP 276
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLT----------------------------HPALAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 277 VCAPESMGseDMLFMLYTSGSTGMPKGIV--HTQAGYLLYAaltHKLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNG 354
Cdd:cd17651 129 PDPALDAD--DLAYVIYTSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 355 ATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAW--EWLHRVV 432
Cdd:cd17651 203 ATLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTEDlrEFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 433 GdsrCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCIsqAWPGMARTIYG 512
Cdd:cd17651 280 G---LRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPP-GVPGELYI--GGAGLARGYLN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 513 D----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 588
Cdd:cd17651 354 RpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28416953 589 GEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd17651 434 EKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
140-649 |
3.87e-46 |
|
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: 169.39 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 219
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPVCapesmgsedmlfMLYTSGSTG 299
Cdd:cd05934 82 -------------------------------------------------------DPAS------------ILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 300 MPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 379
Cdd:cd05934 95 PPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 380 KINQFYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPs 458
Cdd:cd05934 170 GATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRD- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 459 eegaEILPAMAM-RPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWP-GMARTIYGDHqrfvDAYFKAYP-GYYFTGDGA 535
Cdd:cd05934 241 ----EPRRPGSIgRPAPGYEVRIVDDDGQELP-AGEPGELVIRGLRGwGFFKGYYNMP----EATAEAMRnGWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 536 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSM 615
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD---PEELFAF 388
|
490 500 510
....*....|....*....|....*....|....
gi 28416953 616 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05934 389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
140-650 |
3.01e-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: 168.86 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 219
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 NqglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNkvhmGDLDvpLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTG 299
Cdd:TIGR02262 110 G---------ALLPVIKAALGKSPHLEHRVVVGRPEA----GEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 300 MPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETVERL 379
Cdd:TIGR02262 175 MPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 380 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVVGDsrctLVDTWWQTETGGICIAPRPS 458
Cdd:TIGR02262 252 QPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTEMLHIFLSNLPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 459 EegaeILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRT 538
Cdd:TIGR02262 326 D----VRYGTSGKPVPGYRLRLVGDGGQDV-ADGEPGELLISG---PSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 539 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDIKGEaafAFIVVKDSAGDSDvvvQELKSM 615
Cdd:TIGR02262 396 DDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVAdedGLIKPK---AFVVLRPGQTALE---TELKEH 469
|
490 500 510
....*....|....*....|....*....|....*
gi 28416953 616 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:TIGR02262 470 VKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
116-648 |
1.93e-44 |
|
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: 166.22 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITfnQGLRGGRVVELKKIVdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKED 275
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAV--------------------------VIDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 PVCApesmGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlyaalthKLVFDH-----QPGDIFGCVADIGWiTGHSYVVYGP 350
Cdd:cd12117 130 AVPV----SPDDLAYVMYTSGSTGRPKGVAVTHRGVV-------RLVKNTnyvtlGPDDRVLQTSPLAF-DASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCNGATSVLFE-STPVYPNAGRywETVERLKINQFY--------------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 415
Cdd:cd12117 198 LLNGARLVLAPkGTLLDPDALG--ALIAEEGVTVLWltaalfnqladedpECFAGLRELLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 416 vGEPINCeawewlhrvVGDSRCTLVDTWWQTetggiciaPRPSEEGAEILPAmamRPFFGIVPVLMDEKGSVVEgSNVSG 495
Cdd:cd12117 276 -LRLVNG---------YGPTENTTFTTSHVV--------TELDEVAGSIPIG---RPIANTRVYVLDEDGRPVP-PGVPG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 ALCISQAwpGMARTIYGD----HQRFVDAYFKayPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 569
Cdd:cd12117 334 ELYVGGD--GLALGYLNRpaltAERFVADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAAL 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 570 ADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd12117 410 RAHPGVREAVVVVREDAGGDKRLVAYVV-----AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-648 |
6.19e-44 |
|
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: 163.96 E-value: 6.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmGDldvpleqemakedpvc 278
Cdd:cd05945 75 SPAERIREILDAAKPALLIAD-----------------------------------------GD---------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 apesmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIgwitghS-----YVVYGPLCN 353
Cdd:cd05945 98 --------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 354 GATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINCEAWEWLHRVVG 433
Cdd:cd05945 163 GATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 434 DSRctLVDTWWQTETGGICIAPRPSEE---GAEILPAMamRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTi 510
Cdd:cd05945 240 DAR--IYNTYGPTEATVAVTYIEVTPEvldGYDRLPIG--YAKPGAKLVILDEDGRPVPP-GEKGELVISG--PSVSKG- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGDHQRFVDAYFKAYPGY--YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 588
Cdd:cd05945 312 YLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEK 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 589 GEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05945 392 VTELIAFVVPKP--GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
140-650 |
6.94e-44 |
|
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: 163.71 E-value: 6.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 219
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 nqglrggrvvelkkivdeavkhcPTVqhvlvaHRTDNKVHMGDldvpleqemakedpvcapesmgseDMLFMLYTSGSTG 299
Cdd:cd05903 80 -----------------------PER------FRQFDPAAMPD------------------------AVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 300 MPKGIVHTqAGYLLYA--ALTHKLVFDhqPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVE 377
Cdd:cd05903 107 EPKGVMHS-HNTLSASirQYAERLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 378 RLKINQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPINC----EAWEWLHRVVgdsrctlVDTWWQTETGGI 451
Cdd:cd05903 180 EHGVTFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVPRslarRAAELLGAKV-------CSAYGSTECPGA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 452 CIAPRPSEEGAeilpAMAM--RPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMartIYGDHQRfVDAYFKAYP-GY 528
Cdd:cd05903 249 VTSITPAPEDR----RLYTdgRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSV---FLGYLDR-PDLTADAAPeGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 529 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDV 607
Cdd:cd05903 318 FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALlTFDE 397
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 28416953 608 VVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05903 398 LVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
115-656 |
1.72e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 164.84 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVI---TFnqglrggRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEM 271
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVvpkTF-------RGFDHAAMARRLRPELPALRHVVVVGGDGADSFEALLITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 272 AKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQ----AGYLLYAALthklvFDHQPGDIFGCVADIGWITGHSYVV 347
Cdd:PRK13295 183 PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 348 YGPLCNGATSVLFEStpvypnagryWETVERLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEPI 420
Cdd:PRK13295 258 MMPVMLGATAVLQDI----------WDPARAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 421 NCEAWEWLHRVVGdsrCTLVDTWWQTETGGIC-IAPRPSEEGAEI-----LPAMAMRpffgIV-----PVLMDEKGS-VV 488
Cdd:PRK13295 325 PGALVERARAALG---AKIVSAWGMTENGAVTlTKLDDPDERASTtdgcpLPGVEVR----VVdadgaPLPAGQIGRlQV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 489 EG-SNVSGALcisqAWPGMARTiygdhqrfvDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 567
Cdd:PRK13295 398 RGcSNFGGYL----KRPQLNGT---------DA-----DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 568 AIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRR 646
Cdd:PRK13295 460 LLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSlDFEEMVEFLKA---QKVAKQYIPERLVVRDALPRTPSGKIQKF 536
|
570
....*....|
gi 28416953 647 LLRKIITSEA 656
Cdd:PRK13295 537 RLREMLRGED 546
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
116-649 |
1.63e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 161.40 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITFNQGLrggrvvelkKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLD--VPLEQEMAK 273
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPGVRHRLVLDGD------GELEgfVGYAEAVAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 --EDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvhtqagyllYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPL 351
Cdd:PRK13391 145 lpATPI-ADESLGTD----MLYSSGTTGRPKGI---------KRPLPEQPP-DTPLPLTAFLQRLWGFRSDMVYLSPAPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 352 --------CN-----GATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGE 418
Cdd:PRK13391 210 yhsapqraVMlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 419 PinCEAwewlhrvvgDSRCTLVDtWW---------QTETGGICiAPRPSEEGAEilPAMAMRPFFGIVPVLMDekgsvve 489
Cdd:PRK13391 286 P--CPP---------QVKEQMID-WWgpiiheyyaATEGLGFT-ACDSEEWLAH--PGTVGRAMFGDLHILDD------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 490 gsnvSGALCIsqawPGMARTIYGDHQR-FVdaYFK----------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGH 558
Cdd:PRK13391 344 ----DGAELP----PGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 559 RLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKT 638
Cdd:PRK13391 414 NIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRL 493
|
570
....*....|.
gi 28416953 639 RSGKVMRRLLR 649
Cdd:PRK13391 494 PTGKLYKRLLR 504
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
139-650 |
3.33e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 159.35 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 139 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgFSAESLAGRINDAKCKVVIT 218
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPL-LEPEQIAELLRAAGAKVLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 219 fnqgLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTD--------------NKVHMGDLDvpLEQEMAKE--DPVCAPES 282
Cdd:PRK07529 136 ----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARylpgpkrlavplirRKAHARILD--FDAELARQpgDRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 MGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGD----------IFGCVAdigwitghsyVVYGPLC 352
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV----------TGLAPLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 353 NGATSVLfeSTPV-YPNAG---RYWETVERLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRTLGSVGEPINCEAWEWL 428
Cdd:PRK07529 279 RGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 429 HRVVGdsrCTLVDTWWQTE-TGGICIAPR--PSEEGA--EILPAMAMRpffgIVPVlmDEKGSVVEGSNVS--GALCISQ 501
Cdd:PRK07529 354 EAATG---VRIVEGYGLTEaTCVSSVNPPdgERRIGSvgLRLPYQRVR----VVIL--DDAGRYLRDCAVDevGVLCIAG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 502 A--WPGMARtiyGDHQRfvDAYFkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 579
Cdd:PRK07529 425 PnvFSGYLE---AAHNK--GLWL--EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAA 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 580 VIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:PRK07529 498 AVGRPDAHAGELPVAYVQLKP---GASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
140-648 |
9.70e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 156.66 E-value: 9.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 219 fnqglrggrVVELKKIVDEAVKHCPtVQHVLVAHRTDN-KVHMGD-----LDVPLEQEMAKEDPVCA------------P 280
Cdd:PRK08314 115 ---------GSELAPKVAPAVGNLR-LRHVIVAQYSDYlPAEPEIavpawLRAEPPLQALAPGGVVAwkealaaglappP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 281 ESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF 360
Cdd:PRK08314 185 HTAGPDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 361 -----EStpvypnAGRyweTVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGds 435
Cdd:PRK08314 264 prwdrEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTG-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 436 rCTLVDTWWQTETggicIAP-------RPSEEGAEIlpamamrPFFGIVPVLMD----------EKGSVVegsnVSGALC 498
Cdd:PRK08314 331 -LDYVEGYGLTET----MAQthsnppdRPKLQCLGI-------PTFGVDARVIDpetleelppgEVGEIV----VHGPQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 499 ISQAWPGMART----IYGDHQRFvdayFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPA 574
Cdd:PRK08314 395 FKGYWNRPEATaeafIEIDGKRF----FR-------TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28416953 575 VPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:PRK08314 464 IQEACVIATPDPRRGETVKAVVVLRPEARGK-TTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
142-580 |
1.39e-40 |
|
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: 153.58 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 QglrggrvvelkkivdeavkHCPTVQHVLVAHrtdnkVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTSGSTGM 300
Cdd:TIGR01733 81 A-------------------LASRLAGLVLPV-----ILLDPLELAALDDAPAPPPPDAPS--GPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTQAGyLLYAALTHKLVFDHQPGDIfgcvadigWITGHSYV-------VYGPLCNGATSVLFESTPVYPNAGRYW 373
Cdd:TIGR01733 135 PKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 374 ETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICI 453
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTVWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 454 A---PRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDAYFKAYP 526
Cdd:TIGR01733 279 AtlvDPDDAPRESPVPIG--RPLANTRLYVLDDDLRPV-PVGVVGELYIGG--PGVARGYLNRpeltAERFVPDPFAGGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 527 GY--YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 580
Cdd:TIGR01733 354 GArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
115-677 |
8.98e-40 |
|
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: 157.71 E-value: 8.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQEMAKE 274
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLT-----------------QSA----------LAARLPELGVPVLALDALALAAEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPesmGSEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVADIG-----WitghsyVVY 348
Cdd:COG1020 609 NPPVPV---TPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSfdasvW------EIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 349 GPLCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINCEAWEWL 428
Cdd:COG1020 678 GALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 429 HRVVGDsrCTLVDTWWQTETGGICIA--PRPSEEGAEILP---AMA----------MRPffgiVPVlmdekgsvvegsNV 493
Cdd:COG1020 752 RARLPG--ARLVNLYGPTETTVDSTYyeVTPPDADGGSVPigrPIAntrvyvldahLQP----VPV------------GV 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 494 SGALCIsqAWPGMARTIYGDH----QRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 567
Cdd:COG1020 814 PGELYI--GGAGLARGYLNRPeltaERFVADPF-GFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 568 AIADHPAVPESAVIGYPhDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 647
Cdd:COG1020 891 ALLQHPGVREAVVVARE-DAPGDKRLVAYVV--PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
|
570 580 590
....*....|....*....|....*....|
gi 28416953 648 LRKIITSEAQELGDTTTLEDPSIIAEILSV 677
Cdd:COG1020 968 LPAPAAAAAAAAAAPPAEEEEEEAALALLL 997
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
120-643 |
1.09e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 154.04 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 120 RKSPESVALIWErdepGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 199
Cdd:PRK06178 44 RERPQRPAIIFY----GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 200 SAESLAGRINDAKCKVVITFNQglrggrvveLKKIVdEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED---- 275
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQ---------LAPVV-EQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAaaga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 ----------PVCAPESMGSEDMLFML-YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHS 344
Cdd:PRK06178 188 idllpalracTAPVPLPPPALDALAALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGEN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 345 YVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVG-----EP 419
Cdd:PRK06178 268 FGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVVSfvkklNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 420 INCEAWewlHRVVGdsrCTLVDT-WWQTETGGICIAPRPSEEGAEILPAmamRPFFGIVPV------LMDEKGSVVEGSN 492
Cdd:PRK06178 342 DYRQRW---RALTG---SVLAEAaWGMTETHTCDTFTAGFQDDDFDLLS---QPVFVGLPVpgtefkICDFETGELLPLG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 493 VSGALCISQawPGMARTIYG----DHQRFVDayfkaypGYYFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIED 567
Cdd:PRK06178 413 AEGEIVVRT--PSLLKGYWNkpeaTAEALRD-------GWLHTGDiGKI-DEQGFLHYLGRRKEMLKVNGMSVFPSEVEA 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 568 AIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPdEILVVKRLPKTRSGKV 643
Cdd:PRK06178 483 LLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP---GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV 554
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
119-648 |
3.85e-39 |
|
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: 151.12 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd05923 11 ASRAPDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRI-NDAKCKVVITFNQG------LRGGRVVELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDVPLEQEM 271
Cdd:cd05923 87 LKAAELAELIeRGEMTAAVIAVDAQvmdaifQSGVRVLALSDLVG--------------------------LGEPESAGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 272 AKEDPVCAPESMGsedmlFMLYTSGSTGMPKGIVHTQAgyllyAALTHKLVFDHQPGDIFGC------VADIGWITGHSY 345
Cdd:cd05923 141 LIEDPPREPEQPA-----FVFYTSGTTGLPKGAVIPQR-----AAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 346 VVYGPLCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAW 425
Cdd:cd05923 211 VLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 426 EWLHRVVGDSRctlVDTWWQTETGGICIAPRPSEEGAeilpamaMRPFFG----IVPVL--MDEKGSVVEGSNVSGALCI 499
Cdd:cd05923 285 ERVNQHLPGEK---VNIYGTTEAMNSLYMRDARTGTE-------MRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 500 SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 579
Cdd:cd05923 355 DAAFTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 580 VIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqELKSM-VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05923 428 VIGVADERWGQSVTACVVPREGTLSAD----ELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
123-648 |
6.75e-39 |
|
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: 149.77 E-value: 6.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapes 282
Cdd:cd17643 75 RIAFILADSGPSLLLT--------------------------------------------------------DP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHQpgdifgcvaDIgWITGHSYV-------VYGPLCNG 354
Cdd:cd17643 93 ---DDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFNED---------DV-WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 355 ATSVLFES----TPVypnagRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINCEAWE-W 427
Cdd:cd17643 160 GRLVVVPYevarSPE-----DFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRpW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 428 LHRVvGDSRCTLVDTWWQTETggiCIAPRPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEGSnVSGALCISQaw 503
Cdd:cd17643 231 AGRF-GLDRPQLVNMYGITET---TVHVTFRPLDAADLPAAAAspigRPLPGLRVYVLDADGRPVPPG-VVGELYVSG-- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 504 PGMARTIYG----DHQRFVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 577
Cdd:cd17643 304 AGVARGYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRD 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28416953 578 SAVIGYpHDIKGEAAFAFIVVKDSAgdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17643 383 AAVIVR-EDEPGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
140-648 |
1.35e-38 |
|
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: 148.40 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 219
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 NqglrggrvvELkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTG 299
Cdd:cd05935 81 S---------EL------------------------------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 300 MPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF-----ESTPvypnagrywE 374
Cdd:cd05935 98 LPKGCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL---------E 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 375 TVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETggiCIA 454
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTET---MSQ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 455 PRPSEEGAEILPAMAMrPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAYPGYYF-TGD 533
Cdd:cd05935 240 THTNPPLRPKLQCLGI-P*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIKGRRFFrTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 534 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsAGDSDVVVQELK 613
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYRGKVTEEDII 395
|
490 500 510
....*....|....*....|....*....|....*
gi 28416953 614 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05935 396 EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
123-648 |
1.03e-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: 146.67 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALiweRDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd12116 1 PDATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivDEAvkhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPES 282
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 MGSEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFdhQPGDIFGCVADIGW-ITGHSyvVYGPLCNGATSVLF 360
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGL--GPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 361 ESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdaWvkkYDRSSLRTL-GsvGEPinceawewLHRVVGDSRCTL 439
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAG--W---QGRAGLTALcG--GEA--------LPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 440 VDTWWQ----TETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLMDEKG-SVVEGsnVSGALCIsqAWPGMARTIYGD- 513
Cdd:cd12116 263 VGSLWNlygpTETTIWSTAARVTAAAG---PIPIGRPLANTQVYVLDAALrPVPPG--VPGELYI--GGDGVAQGYLGRp 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 514 ---HQRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 588
Cdd:cd12116 336 altAERFVPDPF-AGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGD 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28416953 589 GEAAfAFIVVKD-SAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd12116 415 RRLV-AYVVLKAgAAPDAA----ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
123-648 |
2.17e-37 |
|
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: 146.23 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITFNQG---LRGG--RVVelkkIVDEAVKHCptvqhvlvAHRTDNKVHMGDLDVPleQEMAKEDPV 277
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaekLASLalPVV----LLDSAEFDS--------LSFSDLLFEADEAEPP--VVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 278 CApesmgsedmlfMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT 356
Cdd:cd05904 161 AA-----------LLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGAT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 SVlfestpVYP--NAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGD 434
Cdd:cd05904 230 VV------VMPrfDLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 SRctLVDTWWQTETGGICIAPRPSEEGAE-------ILPAMAMRpffgIVpvlmDEKGSVVEGSNVSGALCISQawPGM- 506
Cdd:cd05904 302 VD--LGQGYGMTESTGVVAMCFAPEKDRAkygsvgrLVPNVEAK----IV----DPETGESLPPNQTGELWIRG--PSIm 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 507 ----------ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 576
Cdd:cd05904 370 kgylnnpeatAATIDKE-------------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEIL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 577 ESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05904 437 DAAVIPYPDEEAGEVPMAFVVRK---PGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
115-648 |
2.24e-37 |
|
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: 145.88 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERdepgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITfNQGLRGGRVVELKKivdeavkhcPTVQHVLVAHRTDnkvhmgdldvpleqemAKE 274
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLT-TADLAARLPAGGDV---------ALLGDEALAAPPA----------------TPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPesmgsEDMLFMLYTSGSTGMPKGIVHTQAG---YLLYaaLTHKlvFDHQPGDIFGCVADIGWITGhSYVVYGPL 351
Cdd:cd17646 132 LVPPRP-----DNLAYVIYTSGSTGRPKGVMVTHAGivnRLLW--MQDE--YPLGPGDRVLQKTPLSFDVS-VWELFWPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 352 CNGATSVLFEstpvyPNAGR---YW-ETVERLKINQFYGAPTAVRLLLkygdAWVKKYDRSSLRTLGSVGEPINCEAWEW 427
Cdd:cd17646 202 VAGARLVVAR-----PGGHRdpaYLaALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 428 LHRVVGdsrCTLVDTWWQTETgGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMA 507
Cdd:cd17646 273 FLALPG---AELHNLYGPTEA-AIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVP-VGVPGELYL--GGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 508 RTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 583
Cdd:cd17646 346 RGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 584 PHDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17646 426 AAPAGAARLVGYVVP--AAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
117-667 |
2.80e-37 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 146.82 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALIwerDEPGTevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 197 AGFSAESLAGRINDAKCKVVIT---FNQGLRGGRVVELKKIVdeavkhcPTVQHVLVAhrtdNKVHMGDLDVPLEQEMAK 273
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlFKQTRPVDLILPLQNQL-------PQLQQIVGV----DKLAPATSSLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 EDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLL----YAALTHkLVFDhqpgDIFGCVADIGWITGHSYVVYG 349
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINC----EAW 425
Cdd:PRK06087 250 PFLIGARSVLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIPKkvarECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 426 EwlHRVVgdsrctLVDTWWQTETggiciAPR---PSEEGAEILPAMAMRPFFGI-VPVLMDEKGSV---VEGSNVSGAlc 498
Cdd:PRK06087 324 Q--RGIK------LLSVYGSTES-----SPHavvNLDDPLSRFMHTDGYAAAGVeIKVVDEARKTLppgCEGEEASRG-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 499 isqawPGMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 575
Cdd:PRK06087 389 -----PNVFMGYLDEPEltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 576 PESAVIGYPHDIKGEAAFAFIVVKDSagDSDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIts 654
Cdd:PRK06087 459 HDACVVAMPDERLGERSCAYVVLKAP--HHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI-- 534
|
570
....*....|...
gi 28416953 655 eAQELGDTTTLED 667
Cdd:PRK06087 535 -MRRLTQDVCEEI 546
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
172-657 |
3.77e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 145.73 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 172 MPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTV-----Q 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVlpaagE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 247 HVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQ 326
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 327 PGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYwetVERLKINQFYGAPTAVRLLLKYGDAWVKKYD 406
Cdd:PLN03051 159 PGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 407 RSSLRTLGSVGEPINCEAWEWLHRVVGDSRcTLVDTWWQTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLMDEKG- 485
Cdd:PLN03051 235 WSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQA---PGAFSTASLGTRFVLLNDNGv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 486 SVVEGSNVSGALCISQAWPGMA-RTIYGDHQRfvdAYFKAYPGYYFT-------GDGAYRTEGGYYQITGRMDDVINISG 557
Cdd:PLN03051 311 PYPDDQPCVGEVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 558 HRLGTAEIEDAI-ADHPAVPESAVIGYPhDIKGEAAFAFIVVKDS-------AGDSDVVVQELKSMVATKIAKYAVPDEI 629
Cdd:PLN03051 388 IKTSSVEIERACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGeekkgfdQARPEALQKKFQEAIQTNLNPLFKVSRV 466
|
490 500
....*....|....*....|....*...
gi 28416953 630 LVVKRLPKTRSGKVMRRLLRKIITSEAQ 657
Cdd:PLN03051 467 KIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
136-649 |
6.08e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 145.05 E-value: 6.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 215
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 216 VITfnqglrGGRVVELkkiVDEAVKHCPT-VQHVLVAHrtdnkvhmGDLD--VPLEQEMAKEDPV-CAPESMGSEdmlfM 291
Cdd:PRK08276 87 LIV------SAALADT---AAELAAELPAgVPLLLVVA--------GPVPgfRSYEEALAAQPDTpIADETAGAD----M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 292 LYTSGSTGMPKGIVhtqagyllyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGA-------------TSV 358
Cdd:PRK08276 146 LYSSGTTGRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 359 LFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP----INCEAWEWLHRVVgd 434
Cdd:PRK08276 217 VMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPcpveVKRAMIDWWGPII-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 srctlVDTWWQTETGGICIAprPSEEGAEiLPAMAMRPFFGIVPVLmDEKGSVVEgsnvsgalcisqawPGMARTIY--- 511
Cdd:PRK08276 291 -----HEYYASSEGGGVTVI--TSEDWLA-HPGSVGKAVLGEVRIL-DEDGNELP--------------PGEIGTVYfem 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 512 --------GDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESA 579
Cdd:PRK08276 348 dgypfeyhNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVA 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 580 VIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK08276 422 VFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
141-650 |
1.17e-36 |
|
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: 142.71 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINdakckvvitfn 220
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglRGGRVVelkKIVDEAVKhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgSEDMLFMLYTSGSTGM 300
Cdd:cd05974 70 ---RGGAVY---AAVDENTH--------------------------------------------ADDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTQAGYLLyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVypNAGRYWETVERLK 380
Cdd:cd05974 100 PKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 381 INQFYGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGIcIAPRPsee 460
Cdd:cd05974 177 VTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP--- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 461 GAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVsgALCISQAWP-GMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTE 539
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGAPATEGEV--ALDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 540 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATK 619
Cdd:cd05974 321 DGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRER 400
|
490 500 510
....*....|....*....|....*....|.
gi 28416953 620 IAKYAVPDEiLVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05974 401 LAPYKRIRR-LEFAELPKTISGKIRRVELRR 430
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
117-651 |
3.57e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 143.53 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGA 190
Cdd:PRK07788 57 HAARRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 191 VHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVqHVLVAHrTDNKVHMGDLDVPLEQE 270
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAAREGVKALVYDD---------EFTDLLSALPPDLGRL-RAWGGN-PDDDEPSGSTDETLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 271 MAKED--PVCAPESMGSedmlFMLYTSGSTGMPKGIVHTQAGYLLYAALthklVFDHQP---GDIFGCVADIGWITGHSY 345
Cdd:PRK07788 194 IAGSStaPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLAG----LLSRVPfraGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 346 VVYGpLCNGATSVL---FestpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINC 422
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAWEWLHRVVGDSRCTLvdtWWQTETGGICIApRPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQA 502
Cdd:PRK07788 338 ELATRALEAFGPVLYNL---YGSTEVAFATIA-TPED--LAEAPGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 WPgMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 582
Cdd:PRK07788 411 FP-FEGYTDGRDKQIID-------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 583 YPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 651
Cdd:PRK07788 483 VDDEEFGQRLRAFVVKAP---GAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
123-649 |
8.38e-36 |
|
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: 140.58 E-value: 8.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17649 1 PDAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvQHvlvahrtdnkvhmgdldvpleqemakedpvcaPES 282
Cdd:cd17649 75 RLRYMLEDSGAGLLLT---------------------------HH--------------------------------PRQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 MGsedmlFMLYTSGSTGMPKGIVHTQAgyllyaALTH-----KLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNGAtS 357
Cdd:cd17649 96 LA-----YVIYTSGSTGTPKGVAVSHG------PLAAhcqatAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-C 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 358 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKyDRSSLRTLGSVGEPINCE-AWEWLhrvvgDSR 436
Cdd:cd17649 163 VVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPElLRRWL-----KAP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 437 CTLVDTWWQTETGGICIAPRPSEEGAEILPAMAM-RPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG--- 512
Cdd:cd17649 237 VRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIgRPLGGRSAYILDADLNPVP-VGVTGELYI--GGEGLARGYLGrpe 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 513 -DHQRFV-DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIkGE 590
Cdd:cd17649 314 lTAERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GK 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 591 AAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd17649 393 QLVAYVVLRAAAAQPE-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
123-642 |
7.39e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 139.25 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVItFNQGLrGGRVVELKkivDEavkhCPTVQHVL-VAHRTDNKVHMGdlDVPLEQEMAKEDPVCAPE 281
Cdd:PRK07798 91 ELRYLLDDSDAVALV-YEREF-APRVAEVL---PR----LPKLRTLVvVEDGSGNDLLPG--AVDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 282 SmGSEDMLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLVFDH--QPGDIFGCVADIGWITGHSYVVYGPLCNGAT--- 356
Cdd:PRK07798 160 E-RSPDDLYLLYTGGTTGMPKGVMWRQED--IFRVLLGGRDFATgePIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 ---------SVLFESTPVYpNAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVG 417
Cdd:PRK07798 237 afaalfsgqTVVLLPDVRF-DADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIASGG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 418 EPINCEAWEWLHRVVGDSrcTLVDTWWQTETG--GICIAPRPSEEGAeilpamamRPFFGIVP--VLMDEKGSVVE-GSN 492
Cdd:PRK07798 306 ALFSPSVKEALLELLPNV--VLTDSIGSSETGfgGSGTVAKGAVHTG--------GPRFTIGPrtVVLDEDGNPVEpGSG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 493 VSGALcisqawpgmART------IYGDHQRfVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 564
Cdd:PRK07798 376 EIGWI---------ARRghiplgYYKDPEK-TAETFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEE 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 565 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 642
Cdd:PRK07798 446 VEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
123-648 |
4.32e-34 |
|
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: 135.67 E-value: 4.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17650 1 PDAIAVSDA------TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapes 282
Cdd:cd17650 75 RLQYMLEDSGAKLLLT--------------------------------------------------------QP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHQPGDIFGcvadigwITGHSYVVYG-----PLCNGAT 356
Cdd:cd17650 93 ---EDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFDVFAgdfarSLLNGGT 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 SVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPIncEAWEWLHRVVGd 434
Cdd:cd17650 163 LVICPDEVKL-DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QDFKTLAARFG- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 SRCTLVDTWWQTETggiCIAPRPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTI 510
Cdd:cd17650 237 QGMRIINSYGVTEA---TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQP-VGVAGELYIGGA--GVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgYPHD 586
Cdd:cd17650 311 LNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VRED 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 587 IKGEAAFAFIVVKDSAGDSdvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17650 390 KGGEARLCAYVVAAATLNT----AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
115-650 |
8.40e-34 |
|
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: 136.07 E-value: 8.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:TIGR03098 6 LEDAAARLPDATALVH------HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFNQGLRggrvvelkkIVDEAVKHCPTVQHVLvahRTDNKVHMGDLDVPLE----QE 270
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLLVTSSERLD---------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEEpaswPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 271 MAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLvfDHQPGDIFGCVADIGWITGHSYVVYG 349
Cdd:TIGR03098 148 LLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAqSVATYL--ENRPDDRLLAVLPLSFDYGFNQLTTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCnGATSVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWvKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:TIGR03098 226 FYV-GATVVLHD----YLLPRDVLKALEKHGITGLAAVPPLWAQLAQ--LDW-PESAAPSLRYLTNSGGAMPRATLSRLR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVVGDSRCTLVdtWWQTETGGICIAP------RPSEEGAEIlpamamrPFFGIvpVLMDEKGSVVEgSNVSGALCisQAW 503
Cdd:TIGR03098 298 SFLPNARLFLM--YGLTEAFRSTYLPpeevdrRPDSIGKAI-------PNAEV--LVLREDGSECA-PGEEGELV--HRG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 504 PGMARTIYGDHQRfVDAYFKAYPGYY----------FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 573
Cdd:TIGR03098 364 ALVAMGYWNDPEK-TAERFRPLPPFPgelhlpelavWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATG 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 574 AVPESAVIGYPHDIKGEaafAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:TIGR03098 443 LVAEAVAFGVPDPTLGQ---AIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
140-650 |
9.83e-34 |
|
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: 134.34 E-value: 9.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIt 218
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 219 fnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSGST 298
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 299 GMPKGIVHTQAGylLYA---ALTHKLVFdhQPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlFESTPvYPNAGRYWET 375
Cdd:cd05941 102 GRPKGVVLTHAN--LAAnvrALVDAWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGAS---VEFLP-KFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 376 VERLKINQFYGAPTAVRLLLKYGDAWVKKYD---RSSLRTL-----GSVGEPINC-EAWEWL--HRvvgdsrctLVDTWW 444
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQYYEAHFTDPQfarAAAAERLrlmvsGSAALPVPTlEEWEAItgHT--------LLERYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 445 QTETGGICIAP-----RPSEEGAEiLPAMAMRpffgivpVLMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQRFVD 519
Cdd:cd05941 246 MTEIGMALSNPldgerRPGTVGMP-LPGVQAR-------IVDEETGEPLPRGEV-GEIQV--RGPSVFKEYWNKPEATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 520 AyFKAyPGYYFTGDGAYRTEGGYYQITGRM-DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfiVV 598
Cdd:cd05941 315 E-FTD-DGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA--VV 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 28416953 599 KDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05941 391 VLRAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-649 |
7.53e-33 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 133.27 E-value: 7.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK08008 14 DDLADVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKivdeavKHCPtvQHVLVAhRTDNKVHMGDLDvpLEQEMAKED 275
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQED------ATPL--RHICLT-RVALPADDGVSS--FTQLKAQQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 P-VCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQ-----AGYllYAALTHKLVFDhqpgDIFGCVADIGWITGHSYVVYG 349
Cdd:PRK08008 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLTVMPAFHIDCQCTAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCNGATSVLFEStpvYpNAGRYWETVERLKINQFYGAPTAVR-LLLKYGDAWvkkyDRS-SLRTLG-----SVGEPinc 422
Cdd:PRK08008 236 AFSAGATFVLLEK---Y-SARAFWGQVCKYRATITECIPMMIRtLMVQPPSAN----DRQhCLREVMfylnlSDQEK--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRPSEEgaEILPAMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCIsQA 502
Cdd:PRK08008 305 DAFEERFGV------RLLTSYGMTETIVGIIGDRPGDK--RRWPSIG-RPGFCYEAEIRDDHNRPLP-AGEIGEICI-KG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 WPGmaRTIYGDHQRFVDAYFKAYP--GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 580
Cdd:PRK08008 374 VPG--KTIFKEYYLDPKATAKVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 581 IGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK08008 452 VGIKDSIRDEAIKAFVVLNEGE---TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
115-664 |
1.08e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 133.23 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFNqgLRGGRVVELKK-------IVDEAVKHCPTVQHVL---VAHRTDNKV------ 258
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLD--LVFPRVTNVQSatkiehvIVTRIADFLPFPKNLLypfVQKKQSNLVvkvses 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 259 HMGDLDVPLEQEM-AKEDPVCAPESmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGD--IFGcVA 335
Cdd:PRK06710 182 ETIHLWNSVEKEVnTGVEVPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEevVLG-VL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 336 DIGWITGHSYVVYGPLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGS 415
Cdd:PRK06710 257 PFFHVYGMTAVMNLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 416 VGEPINCEAWEWLHRVVG-----------DSRCTLVDTWWQTETGGICIAPRPSEEG--AEILPAMAMRPffgivpvlmD 482
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGgklvegyglteSSPVTHSNFLWEKRVPGSIGVPWPDTEAmiMSLETGEALPP---------G 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 483 EKGSVVegsnVSGALCISQAW--PGMARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRL 560
Cdd:PRK06710 402 EIGEIV----VKGPQIMKGYWnkPEETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 561 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 640
Cdd:PRK06710 465 YPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE---GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTV 541
|
570 580
....*....|....*....|....
gi 28416953 641 GKVMRRLLrkiITSEAQELGDTTT 664
Cdd:PRK06710 542 GKILRRVL---IEEEKRKNEDEQT 562
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
119-648 |
1.39e-32 |
|
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: 131.29 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd12115 9 AARTPDAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvc 278
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 apesmGSEDMLFMLYTSGSTGMPKG--IVHTQAGYLLYAALTH-------------KLVFDHQPGDIFGcvadigwitgh 343
Cdd:cd12115 103 -----DPDDLAYVIYTSGSTGRPKGvaIEHRNAAAFLQWAAAAfsaeelagvlastSICFDLSVFELFG----------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 344 syvvygPLCNGATSVLFESTPVYPNAGRYWETVerlKINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCE 423
Cdd:cd12115 167 ------PLATGGKVVLADNVLALPDLPAAAEVT---LINT---VPSAAAELLRHDAL------PASVRVVNLAGEPLPRD 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 424 AWEWLHRVVGDSRctLVDTWWQTET---GGICIAPRPSEEGAEIlpamaMRPFFGIVPVLMDEKGSVVeGSNVSGALCIS 500
Cdd:cd12115 229 LVQRLYARLQVER--VVNLYGPSEDttySTVAPVPPGASGEVSI-----GRPLANTQAYVLDRALQPV-PLGVPGELYIG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 501 QAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 576
Cdd:cd12115 301 GA--GVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVR 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28416953 577 EsAVIGYPHDIKGEAAF-AFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd12115 379 E-AVVVAIGDAAGERRLvAYIVAEPGAA---GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
113-653 |
1.56e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 131.62 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 113 NCLDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFEEKK------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 193 TVIFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKHcptvqhvlvAHRTDNKVHMGDLdvpleQEMA 272
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLIT-----------------DDDFEA---------KLIPGISVKFAEL-----MNGP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 273 KEDPVcaPESMGSEDMLF-MLYTSGSTGMPKGIVHTQAGYLlYAALTHKLVFDHQPGDIFGCVADIGWITGHSY----VV 347
Cdd:PRK03640 129 KEEAE--IQEEFDLDEVAtIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSIlmrsVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 348 YGplcngATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAV-RLLLKYGDAwvkKYDrSSLRT--LGsvGEPIN--- 421
Cdd:PRK03640 206 YG-----MRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLqRLLERLGEG---TYP-SSFRCmlLG--GGPAPkpl 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 ---CEAWewlhrvvgdsRCTLVDTWWQTETggiC--IAPRPSEEGAEILPAmAMRPFFGI--------VPVLMDEKGS-V 487
Cdd:PRK03640 271 leqCKEK----------GIPVYQSYGMTET---AsqIVTLSPEDALTKLGS-AGKPLFPCelkiekdgVVVPPFEEGEiV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 488 VEGSNV-SGALCISQAwpgmartiygDHQRFVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 566
Cdd:PRK03640 337 VKGPNVtKGYLNREDA----------TRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 567 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 646
Cdd:PRK03640 400 EVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-----SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
....*..
gi 28416953 647 LLRKIIT 653
Cdd:PRK03640 475 ELKQLVE 481
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-651 |
1.84e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 132.59 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFNqGLRGGRVVElkkIVDEAVKHCPTVQHVLVAH----RTDNKVHMGDLDVP---L 267
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTSDYHA---MLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 268 EQEMAKEDPVCAPE-------SMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDHqpgdifgcvadiGWI 340
Cdd:PRK12583 176 WHELQARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKG-----------ATLSHHNILNN------------GYF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 341 TGHS---------------YVVYGPLCNGATSVLFESTPVYPN----AGRYWETVERLKINQFYGAPTAVRLLLKYGDaw 401
Cdd:PRK12583 233 VAESlgltehdrlcvpvplYHCFGMVLANLGCMTVGACLVYPNeafdPLATLQAVEEERCTALYGVPTMFIAELDHPQ-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 402 VKKYDRSSLRTLGSVGEPinCEAwEWLHRVVGDSRCTLVD-TWWQTETGGICIA-------PRPSEEGAEILPAMAMRpf 473
Cdd:PRK12583 311 RGNFDLSSLRTGIMAGAP--CPI-EVMRRVMDEMHMAEVQiAYGMTETSPVSLQttaaddlERRVETVGRTQPHLEVK-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 474 fgivpvLMDEKGSVVEGSNVsGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQ 544
Cdd:PRK12583 386 ------VVDPDGATVPRGEI-GELCtrgysVMKGYWNNpeatAESIDED-------------GWMHTGDLATMDEQGYVR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 545 ITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYA 624
Cdd:PRK12583 446 IVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP---GHAASEEELREFCKARIAHFK 522
|
570 580
....*....|....*....|....*..
gi 28416953 625 VPDEILVVKRLPKTRSGKVMRRLLRKI 651
Cdd:PRK12583 523 VPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
115-648 |
5.17e-32 |
|
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: 130.14 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtV 194
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAgfsaeslagrindakckvvitfnqgLRGGRVVELKKIVD--EAVkhcptvqhVLVAHRTdnkvHMGDLDVPLEQEMA 272
Cdd:cd05920 93 VLA-------------------------LPSHRRSELSAFCAhaEAV--------AYIVPDR----HAGFDHRALARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 273 KEDPvcapesmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHQpgDIFGCVADIGwitgHSYV----- 346
Cdd:cd05920 136 ESIP----------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLDQD--TVYLAVLPAA----HNFPlacpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 347 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE 426
Cdd:cd05920 200 VLGTLLAGGRVVLAPD----PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 427 WLHRVVGdsrCTLVDTWWQTEtGGICIApRPsEEGAEILPAMAMRPffgIVP----VLMDEKGSVVeGSNVSGALcisqa 502
Cdd:cd05920 274 RVPPVLG---CTLQQVFGMAE-GLLNYT-RL-DDPDEVIIHTQGRP---MSPddeiRVVDEEGNPV-PPGEEGEL----- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 wpgMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 569
Cdd:cd05920 339 ---LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLL 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 570 ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05920 407 LRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
115-646 |
1.28e-31 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 129.62 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFNQGLRGGRvvelkkivDEAVKHCPtvqhVLVAHRTDNKVHMGDLDVPLEQEMAKE 274
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRA--------EPTTRWWP----LTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPESMGSEDMLFMlYTSGSTGMPKGIVHTQAGyllYAALTHKLVFDHQPGDIFGCVADIGWITGHSYV--VYGPLC 352
Cdd:PRK05852 166 PATSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 353 NGATSVLfestpvyPNAGR-----YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEW 427
Cdd:PRK05852 242 SGGAVLL-------PARGRfsahtFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 428 LHRVVG--------------DSRCTLVDTWWQTETGGICIAPRPSEEGAEIlpaMAMRPFFGIVPVlmDEKGSV-VEGSN 492
Cdd:PRK05852 315 LQTEFAapvvcafgmteathQVTTTQIEGIGQTENPVVSTGLVGRSTGAQI---RIVGSDGLPLPA--GAVGEVwLRGTT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 493 VsgalcisqawpgmARTIYGD----HQRFVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 568
Cdd:PRK05852 390 V-------------VRGYLGDptitAANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 569 IADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 646
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP---PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-658 |
2.81e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.62 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK12316 518 EEQVERTPEAPALAF------GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED 275
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLS--------------------------QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 PvcAPE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVFDHQP-----GDIFGCVADIGWITGHsYVVYG 349
Cdd:PRK12316 646 E--NPGtELNPENLAYVIYTSGSTGKPKGAGNR------HRALSNRLCWMQQAyglgvGDTVLQKTPFSFDVSV-WEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLH 429
Cdd:PRK12316 717 PLMSGARLVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEAL---PADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVVGD-SRCTLVDTWWQTE-TGGICIAPRPSEEGAEILPAmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMA 507
Cdd:PRK12316 789 QVFAKlPQAGLYNLYGPTEaAIDVTHWTCVEEGGDSVPIG---RPIANLACYILDANLEPVP-VGVLGELYLAGR--GLA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 508 RTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGy 583
Cdd:PRK12316 863 RGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA- 941
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 584 phdIKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 658
Cdd:PRK12316 942 ---VDGKQLVGYVVLESEGGD---WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
112-650 |
1.38e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 126.82 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 112 VNCLDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 192 HTVIFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVELKKIVDEAVkhcPTVQHVLVA-HRTDNKVhmgdldVPLEQE 270
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT------EAALAPVATAVRDIV---PLLSTVVVAgGSSDDSV------LGYEDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 271 MAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDifgcvaDIGWITGHSYVVYGp 350
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGADINS------DVGFVGVPLFHIAG- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCNGATSVLFESTPV-YP----NAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSsLRTLGSVGEPinceAW 425
Cdd:PRK07786 231 IGSMLPGLLLGAPTViYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAP----AS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 426 EWLHRVVGDS--RCTLVDTWWQTETGGI-CI-----APRPSEEGAEILPAMAMRpffgIVPVLMDE--KGSVVEgsnvsg 495
Cdd:PRK07786 304 DTLLRQMAATfpEAQILAAFGQTEMSPVtCMllgedAIRKLGSVGKVIPTVAAR----VVDENMNDvpVGEVGE------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 alcISQAWPGMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 575
Cdd:PRK07786 374 ---IVYRAPTLMSGYWNNPEATAEAF---AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDI 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 576 PESAVIGYPHDIKGEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:PRK07786 448 VEVAVIGRADEKWGEVPVAVAAVRN--DDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
120-649 |
1.50e-30 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 126.41 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 120 RKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 199
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 200 SAESLAGRINDAKCKVVItFNQglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKV-HMGDLDVPLEQEmakedpvc 278
Cdd:PRK13382 128 AGPALAEVVTREGVDTVI-YDE--------EFSATVDRALADCPQATRIVAWTDEDHDLtVEVLIAAHAGQR-------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 aPESMGSEDMLFMLyTSGSTGMPKGIVHTQAGyllyAALTHKLVFDHQPgdifgcvadigWITGHSYVVYGPL------C 352
Cdd:PRK13382 191 -PEPTGRKGRVILL-TSGTTGTPKGARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMfhawgfS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 353 NGATSVLFESTPVYPNAGRYWETVERLKINQFYG---APTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:PRK13382 254 QLVLAASLACTIVTRRRFDPEATLDLIDRHRATGlavVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVVGDsrcTLVDTWWQTETGGICIApRPSEEGAEilPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMART 509
Cdd:PRK13382 334 DQFGD---VIYNNYNATEAGMIATA-TPADLRAA--PDTAGRPAEGTEIRILDQDFREVP--------------TGEVGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 510 IYGDHQRFVDAYFKA-----YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP 584
Cdd:PRK13382 394 IFVRNDTQFDGYTSGstkdfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 585 HDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK13382 474 DEQYGQRLAAFVVLK---PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-649 |
1.64e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 126.25 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK06188 22 LKRYPDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVItFNQGLRGGRVVELkkivdeaVKHCPTVQHVLVahrtdnkvhMGDLD--VPLEQEMAKEDP 276
Cdd:PRK06188 96 GSLDDHAYVLEDAGISTLI-VDPAPFVERALAL-------LARVPSLKHVLT---------LGPVPdgVDLLAAAAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 277 VCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALthklvfdhqpgdifgCVADIGWITGHSYVVYGPLCNGAt 356
Cdd:PRK06188 159 APLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI---------------QLAEWEWPADPRFLMCTPLSHAG- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 svlfeSTPVYP--------------NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN- 421
Cdd:PRK06188 223 -----GAFFLPtllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 ---CEAwewlHRVVGDsrcTLVDTWWQTETGgICIAPRPSEEGAEILPAM---AMRPFFGIVPVLMDEKGSVVEGSNVsG 495
Cdd:PRK06188 296 vrlAEA----IERFGP---IFAQYYGQTEAP-MVITYLRKRDHDPDDPKRltsCGRPTPGLRVALLDEDGREVAQGEV-G 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 ALCISQawPGMArtiygdhqrfvDAYFKAyP---------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 566
Cdd:PRK06188 367 EICVRG--PLVM-----------DGYWNR-PeetaeafrdGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 567 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 646
Cdd:PRK06188 433 DVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP---GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKK 509
|
...
gi 28416953 647 LLR 649
Cdd:PRK06188 510 ALR 512
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
132-650 |
2.40e-30 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 126.02 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 132 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTVIFAGFsAESLAGRIND 210
Cdd:PRK06018 31 RSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 211 AKCKVVI---TFnqglrggrVVELKKIVDeavkHCPTVQHVLVAhrTDnKVHMGDLDVP----LEQEMAKEDPVCAPESM 283
Cdd:PRK06018 110 AEDRVVItdlTF--------VPILEKIAD----KLPSVERYVVL--TD-AAHMPQTTLKnavaYEEWIAEADGDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlvfdhqpGDIFGCVA-DI-----------GW-------ITGHS 344
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANN-------GDALGTSAaDTmlpvvplfhanSWgiafsapSMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 345 YVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPincea 424
Cdd:PRK06018 248 LVMPGAKLDGAS--------VY-------ELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 425 wEWLHRVVGDSRCTLVDTWWQTET---GGICIAPRPSEE--GAEILPAMAM--RPFFGIVPVLMDEKG-SVVEGSNVSGA 496
Cdd:PRK06018 308 -RSMIKAFEDMGVEVRHAWGMTEMsplGTLAALKPPFSKlpGDARLDVLQKqgYPPFGVEMKITDDAGkELPWDGKTFGR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 497 LCISQawPGMARTIYGDHQRFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 576
Cdd:PRK06018 387 LKVRG--PAVAAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28416953 577 ESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:PRK06018 460 EAAVIGVYHPKWDERPLLIVQLKP---GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-650 |
2.52e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 125.92 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 113 NCLDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 193 TVIFAGFSAESLAGRINDAKCKVVI---TFNQGLRGGRVVELK---KIVDEAVKHCPTVQHVLVAHRtDNKVHMGDLDvp 266
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchaDFPEHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 267 leqemaKEDPvcapesmgsedmLFMLYTSGSTGMPKGIV--HTQAGYLLyaalTHKLVfDHQPGdifgcvadigwITGH- 343
Cdd:PRK07470 162 ------HDDP------------CWFFFTSGTTGRPKAAVltHGQMAFVI----TNHLA-DLMPG-----------TTEQd 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 344 -SYVVyGPL---------CN---GATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSL 410
Cdd:PRK07470 208 aSLVV-APLshgagihqlCQvarGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 411 RTLGSVGEPINCEAWEWLHRVVGDsrcTLVDTWWQTE-TGGICIAPrPSEEGAEILPAMAM----RPFFGIVPVLMDEKG 485
Cdd:PRK07470 283 RYVIYAGAPMYRADQKRALAKLGK---VLVQYFGLGEvTGNITVLP-PALHDAEDGPDARIgtcgFERTGMEVQIQDDEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 486 SVVeGSNVSGALCISqawpGMArtIYGDHQRFVDAYFKAYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 564
Cdd:PRK07470 359 REL-PPGETGEICVI----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPRE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 565 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 644
Cdd:PRK07470 432 IEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA---PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKIT 508
|
....*.
gi 28416953 645 RRLLRK 650
Cdd:PRK07470 509 KKMVRE 514
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
115-649 |
4.15e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 125.24 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVItFNQGLRGGRVVELKKIVDEAVKhcPTVQHVLVAHRTDNKV---HMGDLDVPLEQEM 271
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLV-VWPGFKGIDFAAILAAVPPDAL--PPLRAIAVVDDAADATpapAPGARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 272 AKEDPVCAPESmGSEDMLFMLY-TSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHQPGDIFGCVADIGWITGHSYVVyGP 350
Cdd:PRK06164 167 PAPPAAAGERA-ADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-GA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVG-EPINCEAWEW-- 427
Cdd:PRK06164 244 LAGGAPLVCE---PVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFGFASfAPALGELAALar 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 428 -----LHRVVGDSR------CTLVDTWWQT--ETGGiciapRPSEEGAEilpamamrpffgiVPVLMDEKGSVVEgSNVS 494
Cdd:PRK06164 317 argvpLTGLYGSSEvqalvaLQPATDPVSVriEGGG-----RPASPEAR-------------VRARDPQDGALLP-DGES 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 495 GALCISQawPGMARTiYGDHQrfvDAYFKAYP--GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 572
Cdd:PRK06164 378 GEIEIRA--PSLMRG-YLDNP---DATARALTddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 573 PAVPESAVIGYPHDIKGEAAfAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSG---KVMRRLLR 649
Cdd:PRK06164 452 PGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
138-650 |
4.44e-30 |
|
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: 124.33 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 tfnqglrggrvvelkkiVDEAvkhcptvqhvlvaHRTDNKVHMGDLDVPLEQemakedpvcaPESmgSEDMLFMLYTSGS 297
Cdd:cd12118 107 -----------------VDRE-------------FEYEDLLAEGDPDFEWIP----------PAD--EWDPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 298 TGMPKGIVHTQAG-YL--LYAALTHKLvfDHQPG-----DIFGCVadiGWItghsyVVYGPLCNGATSVLFESTpvypNA 369
Cdd:cd12118 145 TGRPKGVVYHHRGaYLnaLANILEWEM--KQHPVylwtlPMFHCN---GWC-----FPWTVAAVGGTNVCLRKV----DA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 370 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYD-RSSLRTLGSVGEPINCEAWEWLHRVVgdsrctlVDTWWQTET 448
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDV-------THVYGLTET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 449 GG---ICI---------------------APRPSEEGAEILPAMAMRPffgiVPVLMDEKGSVV-EGSNV-SGALCISQA 502
Cdd:cd12118 284 YGpatVCAwkpewdelpteerarlkarqgVRYVGLEEVDVLDPETMKP----VPRDGKTIGEIVfRGNIVmKGYLKNPEA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 wpgmartiygdhqrfVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 582
Cdd:cd12118 360 ---------------TAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 583 YPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd12118 423 RPDEKWGEVPCAFVELKEGA---KVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
137-651 |
4.60e-30 |
|
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: 124.95 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 217 ITFNQGLRggRVVELKKIVdeavkhcPTVQHVLVahrTDNKVHMGDLDVpLEQEMAKEDPVC-------APESMGSEDML 289
Cdd:cd17642 121 FCSKKGLQ--KVLNVQKKL-------KIIKTIII---LDSKEDYKGYQC-LYTFITQNLPPGfneydfkPPSFDRDEQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 290 FMLYTSGSTGMPKGIvhtqagyllyaALTHKLV---FDHQPGDIFGC-----VADIGWITGHS----YVVYGPLCNGATS 357
Cdd:cd17642 188 LIMNSSGSTGLPKGV-----------QLTHKNIvarFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 358 VL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGD 434
Cdd:cd17642 257 VLmykFEEE-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 SrcTLVDTWWQTE-TGGICIAP----RPSEEGAeilpamaMRPFFGIVPVLMDEKGSVveGSNVSGALCISQawPGMART 509
Cdd:cd17642 328 P--GIRQGYGLTEtTSAILITPegddKPGAVGK-------VVPFFYAKVVDLDTGKTL--GPNERGELCVKG--PMIMKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 510 IYGDHQRFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 589
Cdd:cd17642 395 YVNNPEATKALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAG 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 590 EAAFAFivvkdsagdsdVVVQELKSMVATKIAKYaVPDEILVVKRL----------PKTRSGKVMRRLLRKI 651
Cdd:cd17642 473 ELPAAV-----------VVLEAGKTMTEKEVMDY-VASQVSTAKRLrggvkfvdevPKGLTGKIDRRKIREI 532
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
123-648 |
5.59e-30 |
|
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: 123.92 E-value: 5.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd12114 1 PDATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITfnqglrggrvvelkkiVDEAVKHCPTVQHVLVahrtdnkvhmgDLDVPLEQEMAKEDPVCAPEs 282
Cdd:cd12114 75 RREAILADAGARLVLT----------------DGPDAQLDVAVFDVLI-----------LDLDALAAPAPPPPVDVAPD- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 mgseDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVA----DIGwitghSYVVYGPLCNGATS 357
Cdd:cd12114 127 ----DLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 358 VLfestpvyPNAGR-----YW-ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRV 431
Cdd:cd12114 196 VL-------PDEARrrdpaHWaELIERHGVTLWNSVPALLEMLLDVLEAAQALL--PSLRLVLLSGDWIPLDLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 432 VGDsrCTLVDTWWQTETGGICIA---PRPSEEGAEI-----LPAMAMRpffgivpvLMDEKGS-VVEGsnVSGALCISQA 502
Cdd:cd12114 267 APD--ARLISLGGATEASIWSIYhpiDEVPPDWRSIpygrpLANQRYR--------VLDPRGRdCPDW--VPGELWIGGR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 wpGMARTIYGDHQRFVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 580
Cdd:cd12114 335 --GVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVV 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 581 IGYPHDikGEAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd12114 413 VVLGDP--GGKRLAAFVVPDNDGTPI-APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
117-654 |
7.35e-30 |
|
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: 123.81 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakED 275
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLT-------------------------------------------------------SS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 PvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLLyAALTHKLVFDHQPGD--------IFG-CVADIgwitghsyv 346
Cdd:cd05918 105 P---------SDAAYVIFTSGSTGKPKGVVIEHRALST-SALAHGRALGLTSESrvlqfasyTFDvSILEI--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 347 vYGPLCNGAT------SVLFESTPvypnagrywETVERLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVG 417
Cdd:cd05918 166 -FTTLAAGGClcipseEDRLNDLA---------GFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 418 EPIN---CEAWEwlhrvvgdSRCTLVDTWWQTET--GGICIAPRPSEEGAEILPAMAMRPFfgIV-PVLMDE---KGSVv 488
Cdd:cd05918 225 EALTqsdVDTWA--------DRVRLINAYGPAECtiAATVSPVVPSTDPRNIGRPLGATCW--VVdPDNHDRlvpIGAV- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 489 egsnvsGALCISQawPGMARTIYGDHQR----FV-DAYFKAYPGY------YFTGDGAYRTEGGYYQITGRMDDVINISG 557
Cdd:cd05918 294 ------GELLIEG--PILARGYLNDPEKtaaaFIeDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRG 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 558 HRLGTAEIEDAIADHPAVPESAVIGY--PHDIKGEAAF-AFIVVKDSAGDSD--------------VVVQELKSMVATKI 620
Cdd:cd05918 366 QRVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLvAFVVLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRL 445
|
570 580 590
....*....|....*....|....*....|....
gi 28416953 621 AKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 654
Cdd:cd05918 446 PSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
115-331 |
1.84e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.06 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFNQGLrggrvveLKKiVDEAVKHCPTVQHVLVAhrtDNKVHMGDLDV-PLEQEMAK 273
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVL---DPRGLRDDPRLlSLDELLAL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 274 EDPVCAPE-------SMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIF 331
Cdd:COG1022 164 GREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRT 227
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-679 |
1.87e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.84 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK12316 4561 ARMTPDAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITFNQGLRGGRVvelkkivdeavkhcPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAkedpvc 278
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRLPI--------------PDGLASLALDRDEDWEGFPAHD-PAVRLHP------ 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 apesmgsEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK--LVFDHQPGDIFGCVADIGWITGHSYV-------VYG 349
Cdd:PRK12316 4694 -------DNLAYVIYTSGSTGRPKG-----------VAVSHGslVNHLHATGERYELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCNGAtSVLFESTPVYPNAGRYWETVE-RLKINQFygAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPIN----CEA 424
Cdd:PRK12316 4756 PLINGA-SVVIRDDSLWDPERLYAEIHEhRVTVLVF--PPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAqasyDLA 4829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 425 WE-----WLHRVVGDSRCTLVDTWWQTETGGICiaprpseeGAEILPAMamRPFFGIVPVLMDEKGSV----VEGSNVSG 495
Cdd:PRK12316 4830 WRalkpvYLFNGYGPTETTVTVLLWKARDGDAC--------GAAYMPIG--TPLGNRSGYVLDGQLNPlpvgVAGELYLG 4899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 ALCISQAW---PGMARtiygdhQRFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 571
Cdd:PRK12316 4900 GEGVARGYlerPALTA------ERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE 4973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 572 HPAVPESAVIGYPHDIkGEAAFAFIVVKDSA-GDSDVV----VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 646
Cdd:PRK12316 4974 HPAVREAVVIAQEGAV-GKQLVGYVVPQDPAlADADEAqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
570 580 590
....*....|....*....|....*....|....*..
gi 28416953 647 LLRKIITSEAQE--LGDTTTLED--PSIIAEILSVYQ 679
Cdd:PRK12316 5053 ALPQPDASLLQQayVAPRSELEQqvAAIWAEVLQLER 5089
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
116-650 |
2.50e-29 |
|
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: 121.26 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALiwerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKED 275
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLLTTD---------------------------------------------------SPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 PVCApesmgsedmlfmLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGW--ITGhsyVVYGPLCN 353
Cdd:cd17653 107 LAYI------------IFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 354 GATSVLfeSTPVYPnagryWETVERlKINQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPINCE-AWEWLHRVV 432
Cdd:cd17653 171 GGTLVL--ADPSDP-----FAHVAR-TVDALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEAVPPSlLDRWSPGRR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 433 -----GDSRCTLVDTWWQTETGgiciapRPSEEGAEIlPAMAMRpffgivpvLMDE-KGSVVEGsnVSGALCISQawPGM 506
Cdd:cd17653 235 lynayGPTECTISSTMTELLPG------QPVTIGKPI-PNSTCY--------ILDAdLQPVPEG--VVGEICISG--VQV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 507 ARTIYGDHQRFVDAY--FKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVI 581
Cdd:cd17653 296 ARGYLGNPALTASKFvpDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 582 gyphdIKGEAAFAFIVvkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd17653 376 -----VVNGRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
286-649 |
4.99e-29 |
|
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: 118.92 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 286 EDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFD--HQPGD------------------IFGCVADIGWITGHsy 345
Cdd:cd05917 2 DDVINIQFTSGTTGSPKG-----------ATLTHHNIVNngYFIGErlglteqdrlcipvplfhCFGSVLGVLACLTH-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 346 vvygplcnGATSVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAW 425
Cdd:cd05917 69 --------GATMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 426 EWLHRVVGDSRCTLVdtWWQTETGGICIAPR---PSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALC 498
Cdd:cd05917 136 KRVIEVMNMKDVTIA--YGMTETSPVSTQTRtddSIEKRVNtvgrIMPHTEAK--------IVDPEGGIVPPVGVPGELC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 499 ISQAwpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 578
Cdd:cd05917 206 IRGY--SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDV 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28416953 579 AVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05917 282 QVVGVPDERYGEEVCAWIRLKEGA---ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
118-657 |
5.04e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.45 E-value: 5.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 118 HVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK09088 4 HARLQPQRLAAV----DLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 198 GFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKhcptvqhvlvAHRTDnkvhMGDLDVpLEQEMAKEDPV 277
Cdd:PRK09088 80 RLSASELDALLQDAEPRLLLG-----------------DDAVA----------AGRTD----VEDLAA-FIASADALEPA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 278 CAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT- 356
Cdd:PRK09088 128 DTP-SIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSi 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 --SVLFEstpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvkkYDRSSLRTLGSV---GEPINCEAWE-WLhr 430
Cdd:PRK09088 206 lvSNGFE-----PKRTLGRLGDPALGITHYFCVPQMAQAFRAQPG-----FDAAALRHLTALftgGAPHAAEDILgWL-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 431 vvgDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMrPFFGIVPVLMDEKGSVVEgSNVSGALCISQawPGMARTI 510
Cdd:PRK09088 274 ---DDGIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGAAGI-PTPTVQTRVVDDQGNDCP-AGVPGELLLRG--PNLSPGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 590
Cdd:PRK09088 347 WRRPQATARAFTGD--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 591 AAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 657
Cdd:PRK09088 425 VGYLAIVPADGA---PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
117-650 |
9.09e-29 |
|
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: 121.19 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 197 A---GFSAESLAGRINDAKCKVVITfnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHrTDNKvhmgDLDVPleqemak 273
Cdd:cd05931 80 PptpGRHAERLAAILADAGPRVVLT---------TAAALAAVRAFAASRPAAGTPRLLV-VDLL----PDTSA------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 eDPVCAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFG----CVADIGWITGhsyvVYG 349
Cdd:cd05931 139 -ADWPPP-SPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCNGATSVLFEstpvyPNA-----GRYWETVERLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPINC 422
Cdd:cd05931 212 PLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAwewLHRVV-----------------GDSRCTL------------VDTWWQTETGGICIAPRPSEEGAEILPAMAmRPF 473
Cdd:cd05931 286 AT---LRRFAeafapfgfrpeafrpsyGLAEATLfvsggppgtgpvVLRVDRDALAGRAVAVAADDPAARELVSCG-RPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 474 FGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDhQRFVDAYFKAYP-----GYYFTGDGAYRTEGGYYqITGR 548
Cdd:cd05931 362 PDQEVRIVDPETGRELPDGEVGEIWVRG--PSVASGYWGR-PEATAETFGALAatdegGWLRTGDLGFLHDGELY-ITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 549 MDDVINISGHRLGTAEIEDAIAD-HPAVPESAVigyphdikgeAAFA---------FIVVKDSAGDSDVVVQELKSMVAT 618
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEaHPALRPGCV----------AAFSvpddgeerlVVVAEVERGADPADLAAIAAAIRA 507
|
570 580 590
....*....|....*....|....*....|....*.
gi 28416953 619 KIAK-YAV-PDEILVVKR--LPKTRSGKVMRRLLRK 650
Cdd:cd05931 508 AVAReHGVaPADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
138-651 |
9.49e-28 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 117.94 E-value: 9.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 TFNQGLRGGRVVELKKIVDEAVkhcptvqhVLVAHRTDNKVHMGDLDVPLEQEMAkedPVCAPESMGSeDMLFMLYTSGS 297
Cdd:PRK06155 124 VEAALLAALEAADPGDLPLPAV--------WLLDAPASVSVPAGWSTAPLPPLDA---PAPAAAVQPG-DTAAILYTSGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 298 TGMPKGIVHTQAGYLLYAALThklvfdhqpgdifgcVADIGWITGHSYVVYGPL-------------CNGATSVLfesTP 364
Cdd:PRK06155 192 TGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVL---EP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 365 VYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvKKYDR-SSLRTLGSVGEPINceawewLHRVVGDsRC--TLVD 441
Cdd:PRK06155 254 RF-SASGFWPAVRRHGATVTYLLGAMVSILLSQPA---RESDRaHRVRVALGPGVPAA------LHAAFRE-RFgvDLLD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 442 TWWQTETGGICIAPRPSEEgaeilPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPG-MARTIYGDHQRFVDA 520
Cdd:PRK06155 323 GYGSTETNFVIAVTHGSQR-----PGSMGRLAPGFEARVVDEHDQELP-DGEPGELLLRADEPFaFATGYFGMPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 521 YFKAYpgyYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD 600
Cdd:PRK06155 397 WRNLW---FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRD 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 28416953 601 -SAGDSDVVVQELKSMvatkIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 651
Cdd:PRK06155 474 gTALEPVALVRHCEPR----LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
115-654 |
1.11e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 117.27 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT 193
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEE------MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 194 VIFAGFSAESLAGRINDAKCKVVitFNQGLRGGRVVELKKIVdeavkhcpTVQHVlvahrtdnkVHMGDLDVPLEQEMAK 273
Cdd:PRK06839 82 PLNIRLTENELIFQLKDSGTTVL--FVEKTFQNMALSMQKVS--------YVQRV---------ISITSLKEIEDRKIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 EDPvcapesmGSEDMLFML-YTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLC 352
Cdd:PRK06839 143 FVE-------KNESASFIIcYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 353 NGATSVL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLH 429
Cdd:PRK06839 215 AGGVIIVprkFEPT-------KALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEE----LM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVVGDSRCTLVDTWWQTETggiciAPRP---SEEGAEILPAMAMRP-FFGIVPVLMDEKGSVVEGS----NVSGALCISQ 501
Cdd:PRK06839 282 REFIDRGFLFGQGFGMTET-----SPTVfmlSEEDARRKVGSIGKPvLFCDYELIDENKNKVEVGEvgelLIRGPNVMKE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 502 AW---PGMARTIYGdhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 578
Cdd:PRK06839 357 YWnrpDATEETIQD--------------GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEV 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 579 AVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 654
Cdd:PRK06839 423 AVVGRQHVKWGEIPIAFIVKKSSS---VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
141-649 |
1.15e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 117.81 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 tfnqglrggrVVE-LKKIVDEAVKHCPtVQHVLVAHrtdnkvhMGDL-----------------DVP---LEQEMAKEDP 276
Cdd:PRK07059 126 ----------VLEnFATTVQQVLAKTA-VKHVVVAS-------MGDLlgfkghivnfvvrrvkkMVPawsLPGHVRFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 277 VCA-------PESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYL---LYAALTHKLVFDHQPGD---IFGCVADIgwitgh 343
Cdd:PRK07059 188 LAEgarqtfkPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPL------ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 344 sYVVYGPLCN-------GATSVLFestpvyPN----AGRYWEtVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR- 411
Cdd:PRK07059 262 -YHIFALTVCgllgmrtGGRNILI------PNprdiPGFIKE-LKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 412 TLG---SVGEPInceAWEWLHRvvgdSRCTLVDTWWQTETGGICIA--------------PRPSEEgaeilpaMAMRpff 474
Cdd:PRK07059 332 ANGggmAVQRPV---AERWLEM----TGCPITEGYGLSETSPVATCnpvdatefsgtiglPLPSTE-------VSIR--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 475 givpvlmDEKGSVVEGSNVsGALCIS--QAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQI 545
Cdd:PRK07059 395 -------DDDGNDLPLGEP-GEICIRgpQVMAGywnrpdeTAKVMTAD-------------GFFRTGDVGVMDERGYTKI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 546 TGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAV 625
Cdd:PRK07059 454 VDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA----LTEEDVKAFCKERLTNYKR 529
|
570 580
....*....|....*....|....
gi 28416953 626 PDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK07059 530 PKFVEFRTELPKTNVGKILRRELR 553
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
150-649 |
1.39e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 116.39 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 150 TCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgfsaeslagRINDAKCKVVITFNQGLRGGRVV 229
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV---------PLNPTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 230 elkkIVDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQE--MAKEDPVCAPESMGsEDMLFMLYTSGSTGMPKGIV-- 305
Cdd:cd05922 74 ----LADAG----------AADRLRDALPASPDPGTVLDADgiRAARASAPAHEVSH-EDLALLLYTSGSTGSPKLVRls 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 306 HTQagyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfESTPVYPNAgrYWETVERLKINQFY 385
Cdd:cd05922 139 HQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 386 GAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTE-TGGICIAPrPSEEGAEi 464
Cdd:cd05922 212 GVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEaTRRMTYLP-PERILEK- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 465 lPAMAMRPFFGIVPVLMDEKGS----------VVEGSNVSGALCISQAWPGMARtiygdhqRFVDAYFkaypgyyfTGDG 534
Cdd:cd05922 285 -PGSIGLAIPGGEFEILDDDGTptppgepgeiVHRGPNVMKGYWNDPPYRRKEG-------RGGGVLH--------TGDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 535 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIKGEAAFAFIVVKDSAGDSDVVVqelks 614
Cdd:cd05922 349 ARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLR----- 422
|
490 500 510
....*....|....*....|....*....|....*
gi 28416953 615 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05922 423 SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
118-649 |
2.55e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 116.14 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 118 HVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 198 GFSAESLAGRINDAKCKVVItfnqglrggrvvelkkiVDEAVKHCPTVQH---VLVAHRTDNKVHMGDLDVPleqemake 274
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETpkiVIDAAAQADSRRLAQGGLE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 dpvCAPESMGSEDMLF-MLYTSGSTGMPKGIVHTqagyllYAALTHKlVFDHqpgdifgcVADIGWITGHSYVVYGPLCN 353
Cdd:PRK06145 140 ---IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHS------YGNLHWK-SIDH--------VIALGLTASERLLVVGPLYH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 354 -GA-----TSVL-----------FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWvkKYDRSSLRTLGSV 416
Cdd:PRK06145 202 vGAfdlpgIAVLwvggtlrihreFDPEAVL-------AAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 417 GEPINCEAWEWLHRVVGDSRctLVDTWWQTETggiCIAPRPSEEGAEI---------LPAMAMRpffgivpvLMDEKGSV 487
Cdd:PRK06145 273 GEKTPESRIRDFTRVFTRAR--YIDAYGLTET---CSGDTLMEAGREIekigstgraLAHVEIR--------IADGAGRW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 488 VEgSNVSGALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 567
Cdd:PRK06145 340 LP-PNMKGEICMRG--PKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 568 AIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 647
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA---TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRV 490
|
..
gi 28416953 648 LR 649
Cdd:PRK06145 491 LR 492
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
118-649 |
3.86e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 115.88 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 118 HVRKSPESVALIWErdEPGTEVriTYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK13390 6 HAQIAPDRPAVIVA--ETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 198 GFSAESLAGRINDAKCKVVITfnqglrggrVVELKKIVDEAVKHCPTvqHVLVAHRTDNkvhMGDLdvplEQEMAKEDPV 277
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVA---------SAALDGLAAKVGADLPL--RLSFGGEIDG---FGSF----EAALAGAGPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 278 CAPESMGSedmlFMLYTSGSTGMPKGIvhtqagyllYAALTHKLVfdHQPGDifGCVADIGWITGHSyvvygplcngATS 357
Cdd:PRK13390 144 LTEQPCGA----VMLYSSGTTGFPKGI---------QPDLPGRDV--DAPGD--PIVAIARAFYDIS----------ESD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 358 VLFESTPVYPNAGRYW-----------------------ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLG 414
Cdd:PRK13390 197 IYYSSAPIYHAAPLRWcsmvhalggtvvlakrfdaqatlGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 415 SVGEP----INCEAWEWLHRVVgdsrctlVDTWWQTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLmDEKGSVVEG 490
Cdd:PRK13390 277 HAAAPcpvdVKHAMIDWLGPIV-------YEYYSSTEAHGMTFIDSPDWLAH---PGSVGRSVLGDLHIC-DDDGNELPA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 491 SNVSGALCISQAWPgmaRTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 570
Cdd:PRK13390 346 GRIGTVYFERDRLP---FRYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 571 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK13390 423 MHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
119-648 |
5.94e-27 |
|
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: 115.12 E-value: 5.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd17655 7 AEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKHcptvqhvlvahrtdNKVHMGDLDVpLEQEMAKEDPV- 277
Cdd:cd17655 81 YPEERIQYILEDSGADILLT-----------------QSHLQP--------------PIAFIGLIDL-LDEDTIYHEESe 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 278 -CAPESmGSEDMLFMLYTSGSTGMPKGIVHTQAG-------------------YLLYAALThklvFDHQPGDIFGCVadi 337
Cdd:cd17655 129 nLEPVS-KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankviyqgehlrVALFASIS----FDASVTEIFASL--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 338 gwITGHSYVVYG--PLCNGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLlkygdAWVKKYDRSSLRTLGS 415
Cdd:cd17655 201 --LSGNTLYIVRkeTVLDGQALT---------------QYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 416 VGEPINCE-AWEWLHRVvgDSRCTLVDTWWQTETggiCIaprpseeGAEILPAMAMRPFFGIVPV----------LMDEK 484
Cdd:cd17655 259 GGEALSTElAKKIIELF--GTNPTITNAYGPTET---TV-------DASIYQYEPETDQQVSVPIgkplgntriyILDQY 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 485 GSVV-EGsnVSGALCISQAwpGMARTiYGDH-----QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGH 558
Cdd:cd17655 327 GRPQpVG--VAGELYIGGE--GVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 559 RLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKT 638
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
570
....*....|
gi 28416953 639 RSGKVMRRLL 648
Cdd:cd17655 477 PNGKVDRKAL 486
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-649 |
6.70e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 114.97 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 121 KSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 200
Cdd:PRK07514 14 ADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 201 AESLAGRINDAKCKVVItfnqgLRGGRVVELKKIvdeAVKHcpTVQHV--LVAHRTDnkvhmgdldvPLEQEMAKEDPVC 278
Cdd:PRK07514 89 LAELDYFIGDAEPALVV-----CDPANFAWLSKI---AAAA--GAPHVetLDADGTG----------SLLEAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 APESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGD-------IFgcvadigwitgHSYVVY--- 348
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSH-GNLLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvat 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 349 -GPLCNGATSVL---FESTPV---YPNAgryweTVerlkinqFYGAPT-AVRLLlkyGDAWVKKYDRSSLRTLGSVGEPI 420
Cdd:PRK07514 217 nVALLAGASMIFlpkFDPDAVlalMPRA-----TV-------MMGVPTfYTRLL---QEPRLTREAAAHMRLFISGSAPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 421 NCEAW-EWLHRVvGDsrcTLVDTWWQTETGGICIAPRpseEGAEI-------LPAMAMR---PFFGiVPVLMDEKGSV-V 488
Cdd:PRK07514 282 LAETHrEFQERT-GH---AILERYGMTETNMNTSNPY---DGERRagtvgfpLPGVSLRvtdPETG-AELPPGEIGMIeV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 489 EGSNVsgalcisqawpgmartiygdhqrfvdayFKAY---P----------GYYFTGDGAYRTEGGYYQITGRMDDVInI 555
Cdd:PRK07514 354 KGPNV----------------------------FKGYwrmPektaeefradGFFITGDLGKIDERGYVHIVGRGKDLI-I 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 556 SG-HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVK 633
Cdd:PRK07514 405 SGgYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAlDEAAILAALKG----RLARFKQPKRVFFVD 480
|
570
....*....|....*.
gi 28416953 634 RLPKTRSGKVMRRLLR 649
Cdd:PRK07514 481 ELPRNTMGKVQKNLLR 496
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-679 |
8.82e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.37 E-value: 8.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK12316 3064 EEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDldvPLEQEMAKED 275
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLS--------------------------QSHLRLPLAQGVQVLDLD---RGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 PvcaPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNGA 355
Cdd:PRK12316 3189 P---AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 356 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEpinceAWEWLHRVVGDS 435
Cdd:PRK12316 3264 RVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA----HRCTSLKRIVCGGE-----ALPADLQQQVFA 3333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 436 RCTLVDTWWQTETGGICIAPRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMARtiyGDHQ 515
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIG--RPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR---GYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 516 R-------FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyphDIK 588
Cdd:PRK12316 3406 RpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVD 3481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 589 GEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDTTTLE 666
Cdd:PRK12316 3482 GRQLVAYVVPEDEAGD---LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdyVAPVNELE 3558
|
570
....*....|....*
gi 28416953 667 D--PSIIAEILSVYQ 679
Cdd:PRK12316 3559 RrlAAIWADVLKLEQ 3573
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
142-650 |
1.06e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 114.69 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 222 glrGGRVVElkKIVDEAvkHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAK-----EDPVCAPesmgsedmlfmlYTSG 296
Cdd:PLN02246 129 ---QSCYVD--KLKGLA--EDDGVTVVTIDDPPEGCLHFSELTQADENELPEveispDDVVALP------------YSSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVhtqagyllyaaLTHK-LV-------------FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL--- 359
Cdd:PLN02246 190 TTGLPKGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpk 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 360 FEstpvypnAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLHRVVGDS--RC 437
Cdd:PLN02246 259 FE-------IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKE----LEDAFRAKlpNA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 438 TLVDTWWQTETG---GICiaprpseegaeilPAMAMRPFfgivPVLMDEKGSVVE---------------GSNVSGALCI 499
Cdd:PLN02246 326 VLGQGYGMTEAGpvlAMC-------------LAFAKEPF----PVKSGSCGTVVRnaelkivdpetgaslPRNQPGEICI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 500 --SQAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 570
Cdd:PLN02246 389 rgPQIMKGylndpeaTANTIDKD-------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 571 DHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:PLN02246 456 SHPSIADAAVVPMKDEVAGEVPVAFVV---RSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
122-648 |
1.19e-26 |
|
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: 114.11 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 122 SPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 201
Cdd:cd17656 1 TPDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 202 ESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavkHCPTVQhvlvahrTDNKVHMgdldVPLEQEMAKEDPVCAPE 281
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQR--------------------HLKSKL-------SFNKSTI----LLEDPSISQEDTSNIDY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 282 SMGSEDMLFMLYTSGSTGMPKGIV--HTQAGYLLyaalthKLVFDHQPGDIFGCVADIgwiTGHSYVV-----YGPLCNG 354
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL------HFEREKTNINFSDKVLQF---ATCSFDVcyqeiFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 355 AT------------SVLFE-------STPVYPNAgrYWETV--ERLKINQFygaPTAVRLLLKYGDAWVkkydrsslrtl 413
Cdd:cd17656 195 GTlyiireetkrdvEQLFDlvkrhniEVVFLPVA--FLKFIfsEREFINRF---PTCVKHIITAGEQLV----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 414 gsvgepINCEAWEWLHRvvgdSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAmRPFFGIVPVLMDEKGSVVEgSNV 493
Cdd:cd17656 259 ------ITNEFKEMLHE----HNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIG-KPISNTWIYILDQEQQLQP-QGI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 494 SGALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 569
Cdd:cd17656 327 VGELYISGA--SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQL 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 570 ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17656 405 LNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
290-650 |
2.08e-26 |
|
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: 110.50 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 290 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVfdhqpgdifGCVADIGW--------ITGHSYVVYGPLCNGATSVLFE 361
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---------GFGGGDSWllslplyhVGGLAILVRSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 362 STPVYPNAGRYWETVERLkinqfygAPTAVRLLLKYG--DAWVKkydrsSLRTLGSVGEPINCEawewLHRVVGDSRCTL 439
Cdd:cd17630 75 NQALAEDLAPPGVTHVSL-------VPTQLQRLLDSGqgPAALK-----SLRAVLLGGAPIPPE----LLERAADRGIPL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 440 VDTWWQTETGGICIAPRPSEEGA----EILPAMAMRpffgivpvlmdekgsVVEGsnvsGALCISQAWPGMARTIYGDHQ 515
Cdd:cd17630 139 YTTYGMTETASQVATKRPDGFGRggvgVLLPGRELR---------------IVED----GEIWVGGASLAMGYLRGQLVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 516 RFVDayfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 595
Cdd:cd17630 200 EFNE------DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 596 IVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd17630 274 IV-----GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-674 |
2.78e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.03 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK12467 522 ARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITFNQGLR------GGRVVELKKIVDEaVKHCPtvqhvlvAHRTDnkvhmgdldVPLEqema 272
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAqlpvpaGLRSLCLDEPADL-LCGYS-------GHNPE---------VALD---- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 273 kedpvcaPESMGsedmlFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWITGHsYVVYGPLC 352
Cdd:PRK12467 655 -------PDNLA-----YVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 353 NGATSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLHRVV 432
Cdd:PRK12467 721 SGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEAL---QVDLLARVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 433 GDS-RCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARtiy 511
Cdd:PRK12467 793 ALGpGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGA--GLAR--- 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 512 GDHQR-------FVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 583
Cdd:PRK12467 867 GYHRRpaltaerFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ 946
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 584 PHDiKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGD 661
Cdd:PRK12467 947 PGD-AGLQLVAYLVPAAVADGAEhqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFV 1025
|
570
....*....|...
gi 28416953 662 TTTLEDPSIIAEI 674
Cdd:PRK12467 1026 APQTELEKRLAAI 1038
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
140-649 |
3.27e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 113.26 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGAV-HTV---IFAgfsaESLAGRIN 209
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTInprLFP----EQIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 210 DAKCKVV---ITFnqglrggrvvelKKIVDEAVKHCPTVQHVLVAhrTDnKVHMGDLDVPL---EQEMAKEDPVCAPESM 283
Cdd:PRK07008 109 HAEDRYVlfdLTF------------LPLVDALAPQCPNVKGWVAM--TD-AAHLPAGSTPLlcyETLVGAQDGDYDWPRF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA---ALThklvfdhqpgDIFGCVA-DI-----------GW-------IT 341
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHRSTVLHAygaALP----------DAMGLSArDAvlpvvpmfhvnAWglpysapLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 342 GHSYVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSL-RTL--GSVGE 418
Cdd:PRK07008 244 GAKLVLPGPDLDGKS--------LY-------ELIEAERVTFSAGVPTVWLGLLNHMREAGLRF--STLrRTVigGSACP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 419 PINCEAWEwlhrvvGDSRCTLVDTWWQTET---GGICI-----APRPSEEGAEILPAMAmRPFFGIVPVLMDEKGSvveg 490
Cdd:PRK07008 307 PAMIRTFE------DEYGVEVIHAWGMTEMsplGTLCKlkwkhSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGR---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 491 snvsgalciSQAWPGMArtiYGD-HQR---FVDAYFK--AYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLG 561
Cdd:PRK07008 376 ---------ELPWDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWIS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 562 TAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSG 641
Cdd:PRK07008 444 SIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATG 520
|
....*...
gi 28416953 642 KVMRRLLR 649
Cdd:PRK07008 521 KLQKLKLR 528
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
285-650 |
4.29e-26 |
|
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: 110.26 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 285 SEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAtSVLFESTP 364
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 365 VYPNAGRY---WETVERLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLV 440
Cdd:cd05944 79 GYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVELRARFEDATG---LPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 441 DTWWQTETggICIAPRPSEEGAEILPAMAMR-PFFGIVPVLMDEKGSVVE--GSNVSGALCIsqAWPGMAR-TIYGDHQR 516
Cdd:cd05944 151 EGYGLTEA--TCLVAVNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRdcAPDEVGEICV--AGPGVFGgYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 517 FVDAYfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 596
Cdd:cd05944 227 NAFVA----DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 597 VVKDSAgdsDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05944 303 QLKPGA---VVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-662 |
4.74e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 112.98 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITFNqGLRGGRVVE-LKKIVDEaVKHC----------PTVQHVLvahRTDNKVHMGDL 263
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVAmLYELAPE-LATCepgqlqsarlPELRRVI---FLGDEKHPGML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 264 DVPLEQEMAKEDPVCAPESMGSE----DMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-------LVFDHQ---PGD 329
Cdd:PRK08315 173 NFDELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKG-----------ATLTHRnilnngyFIGEAMkltEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 330 ----------IFGCVadIGwitghsyvVYGPLCNGATSVlfestpvYPNAG----RYWETVERLKINQFYGAPTAVRLLL 395
Cdd:PRK08315 242 rlcipvplyhCFGMV--LG--------NLACVTHGATMV-------YPGEGfdplATLAAVEEERCTALYGVPTMFIAEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 396 KYGDawVKKYDRSSLRT---LGSVGePInceawEWLHRVVGDSRCTLVdT--WWQTETG-GIC-------IAPRPSEEGa 462
Cdd:PRK08315 305 DHPD--FARFDLSSLRTgimAGSPC-PI-----EVMKRVIDKMHMSEV-TiaYGMTETSpVSTqtrtddpLEKRVTTVG- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 463 EILPAMAMR---PFFG-IVPVlmdekgsvvegsNVSGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYY 529
Cdd:PRK08315 375 RALPHLEVKivdPETGeTVPR------------GEQGELCtrgysVMKGYWNDpektAEAIDAD-------------GWM 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 530 FTGDGAYRTEGGYYQITGRMDDVI-----NISGhRlgtaEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagD 604
Cdd:PRK08315 430 HTGDLAVMDEEGYVNIVGRIKDMIirggeNIYP-R----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP---G 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 605 SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQELGDT 662
Cdd:PRK08315 502 ATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM---IEELGLQ 556
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
151-649 |
5.79e-26 |
|
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: 111.70 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 151 CRLANTLKRHGVHRG----DRVAIYMPVSPLAvaamlacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrgg 226
Cdd:cd05929 12 FHQRRLLLLDVYSIAlnrnARAAAAEGVWIAD--------GVYIYLINSILTVFAAAAAWKCGACPAYKSSR-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 227 rvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvh 306
Cdd:cd05929 76 ---APRAEACAIIEIKAAALVCGLF--TGGGALDGLEDYEAAEGGSPETPI-EDEAAGWK----MLYSGGTTGRPKGI-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 307 tqagyllyaalthKLVFDHQPGD---IFGCVADIGWITGHSYVVYGPL-------------CNGATSVLFESTpvypNAG 370
Cdd:cd05929 144 -------------KRGLPGGPPDndtLMAAALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTLVLMEKF----DPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 371 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAW---EWLHrvvgdsrctlvdtWW--- 444
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAP--CPPWvkeQWID-------------WGgpi 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 445 ------QTETGGICIAprpseEGAEILpamamrpffgivpvlmDEKGSVveGSNVSGALCI-----SQAWPGMARTIYgd 513
Cdd:cd05929 272 iweyygGTEGQGLTII-----NGEEWL----------------THPGSV--GRAVLGKVHIldedgNEVPPGEIGEVY-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 514 hqrFVDAYFKAYPGYYF-------------TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 580
Cdd:cd05929 327 ---FANGPGFEYTNDPEktaaarneggwstLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 581 IGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:cd05929 404 VGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-658 |
7.21e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.49 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVElkkivdeavkHCPTVQHVLVAhrtdnkvhmgDLDVPLEQEMAKE 274
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT------QAHLLE----------QLPAPAGDTAL----------TLDRLDLNGYSEN 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPvcAPESMGsEDMLFMLYTSGSTGMPKGI--------VHTQAGYLLYAALTHKLVFDHQPGDIFGCVADigwitghsyv 346
Cdd:PRK12467 3229 NP--STRVMG-ENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSFDGAQER---------- 3295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 347 VYGPLCNGATSVLfestpvypNAGRYW---ETV-----ERLKINQFygAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGE 418
Cdd:PRK12467 3296 FLWTLICGGCLVV--------RDNDLWdpeELWqaihaHRISIACF--PPAYLQQFAEDAGG----ADCASLDIYVFGGE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 419 PINCEAWEWLHRVV---------GDSRCTLVDTWWQTETGGICIAPrpseegaeILPamAMRPFFGIVPVLMDEKGSVVE 489
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDAVCEAP--------YAP--IGRPVAGRSIYVLDGQLNPVP 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 490 gSNVSGALCIsqAWPGMARtiyGDHQ-------RFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLG 561
Cdd:PRK12467 3432 -VGVAGELYI--GGVGLAR---GYHQrpsltaeRFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 562 TAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSG 641
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
570
....*....|....*..
gi 28416953 642 KVMRRLLRKIITSEAQE 658
Cdd:PRK12467 3582 KVDRKALPDPDAKGSRE 3598
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
123-656 |
1.28e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 111.58 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPtVQHVLVAHRTDNK----VHMGDLDvpLEQEMAKEDPVC 278
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDT---------EFAEVAREALALLP-GPKPLVIDVDDPEypggRFIGALD--YEAFLASGDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 APESMGSE-DMLFMLYTSGSTGMPKGIV-HTQAGYLlyAALTHKLVFDHQPGDI-------FGCVadiGWitGHSYVVyg 349
Cdd:PRK08162 174 AWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL--NALSNILAWGMPKHPVylwtlpmFHCN---GW--CFPWTV-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 pLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRS-SLRTLG-----SVGEPINCE 423
Cdd:PRK08162 245 -AARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPvHAMVAGaappaAVIAKMEEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 424 AWEWLHrVVGdsrctLVDTW-------WQTETGGICIAPR-----------PSEEGAEILPAMAMRPffgiVPVLMDEKG 485
Cdd:PRK08162 320 GFDLTH-VYG-----LTETYgpatvcaWQPEWDALPLDERaqlkarqgvryPLQEGVTVLDPDTMQP----VPADGETIG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 486 SVVegsnVSGALCISQawpgmartiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISG-HRLGTAE 564
Cdd:PRK08162 390 EIM----FRGNIVMKG---------YLKNPKATEEAFAG--GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENISSIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 565 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVM 644
Cdd:PRK08162 454 VEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAS---ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQ 529
|
570
....*....|..
gi 28416953 645 RRLLRKIITSEA 656
Cdd:PRK08162 530 KFVLREQAKSLK 541
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
141-650 |
1.46e-25 |
|
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: 109.74 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVvitfn 220
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGM 300
Cdd:cd05912 77 -----------------------------------------------------------------DDIATIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGpLCNGATSVLFESTpvypNAGRYWETVERLK 380
Cdd:cd05912 92 PKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLINSGK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 381 INQFYGAPTAV-RLLLKYGDAWvkkydRSSLRT--LGsvGEPINCEAWEwlhrvvgdsRCT-----LVDTWWQTETGGIC 452
Cdd:cd05912 166 VTIISVVPTMLqRLLEILGEGY-----PNNLRCilLG--GGPAPKPLLE---------QCKekgipVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 453 IAPRPseEGAEILPAMAMRPFFG----IVPVLMDEKGS---VVEGSNVSGALcisqawpgMARTIYGDhQRFVDAYFKay 525
Cdd:cd05912 230 VTLSP--EDALNKIGSAGKPLFPvelkIEDDGQPPYEVgeiLLKGPNVTKGY--------LNRPDATE-ESFENGWFK-- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 526 pgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 605
Cdd:cd05912 297 -----TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-----SER 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 28416953 606 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05912 367 PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-657 |
2.01e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.95 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12467 1580 IEDQAAATPEAVALVF------GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVplEQEMAKE 274
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT--------------------------QSHLQARLPLPDGLRSLVLDQ--EDDWLEG 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPES-MGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH--QPGDIFGCVADIGWITGHSYV----- 346
Cdd:PRK12467 1706 YSDSNPAVnLAPQNLAYVIYTSGSTGRPKG-----------AGNRHGALVNRlcATQEAYQLSAADVVLQFTSFAfdvsv 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 347 --VYGPLCNGAtSVLFESTPVYPNAGRYWETVERLKI----------NQF------YGAPTAVRLLLKYGDAWVKKYDRS 408
Cdd:PRK12467 1775 weLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRP 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 409 SLRTLGSVGepinceawewLHRVVGDSRCTLVDTWWQtetggiciAPRPSEEGAEILPamamrpffgIVPVLMDEKGSVV 488
Cdd:PRK12467 1854 WLERLPDTG----------LFNLYGPTETAVDVTHWT--------CRRKDLEGRDSVP---------IGQPIANLSTYIL 1906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 489 EGS------NVSGALCISQAwpGMARtiyGDH-------QRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVI 553
Cdd:PRK12467 1907 DASlnpvpiGVAGELYLGGV--GLAR---GYLnrpaltaERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQV 1980
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 554 NISGHRLGTAEIEDAIADHPAVPESAVIgyPHD-IKGEAAFAFIVVKDSAGDSDVVVQ-----ELKSMVATKIAKYAVPD 627
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVI--AQDgANGKQLVAYVVPTDPGLVDDDEAQvalraILKNHLKASLPEYMVPA 2058
|
570 580 590
....*....|....*....|....*....|
gi 28416953 628 EILVVKRLPKTRSGKVMRRLLRKIITSEAQ 657
Cdd:PRK12467 2059 HLVFLARMPLTPNGKLDRKALPAPDASELQ 2088
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
123-648 |
2.63e-25 |
|
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: 109.26 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17652 1 PDAPAVVFG------DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapes 282
Cdd:cd17652 75 RIAYMLADARPALLLTT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 mgSEDMLFMLYTSGSTGMPKGIV--HTQAGYLLYAALTHklvFDHQPGDifgCVADIGWITGHSYV--VYGPLCNGATSV 358
Cdd:cd17652 92 --PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGS---RVLQFASPSFDASVweLLMALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 359 LFESTPVYPNAGrYWETVERLKINQFYGAPTAVrlllkygdAWVKKYDRSSLRTLGSVGEPINCE---AWEWLHRVV--- 432
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAAL--------AALPPDDLPDLRTLVVAGEACPAElvdRWAPGRRMInay 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 433 GDSRCTLVDTWWQTETGG--ICIAPRPSEEGAEILPAmAMRPffgiVPVlmdekgsvvegsNVSGALCIsqAWPGMARTi 510
Cdd:cd17652 235 GPTETTVCATMAGPLPGGgvPPIGRPVPGTRVYVLDA-RLRP----VPP------------GVPGELYI--AGAGLARG- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGDH-----QRFVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 583
Cdd:cd17652 295 YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVR 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 584 PHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17652 374 DDRPGDKRLVAYVVPAPGAAPT---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
564-642 |
3.03e-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: 99.54 E-value: 3.03e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 564 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 642
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
142-645 |
7.43e-25 |
|
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: 107.92 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 222 glrgGRVVELKKIVdeavkhcptvqhVLVAHRTdnkvhmgdldvpleqEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 301
Cdd:TIGR01923 78 ----DSLLEEKDFQ------------ADSLDRI---------------EAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 302 KGIVHTQAGYLLYA-ALTHKLVFDhqPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfestpVYPNAgRYWETVERLK 380
Cdd:TIGR01923 127 KAVPHTFRNHYASAvGSKENLGFT--EDDNWLLSLPLYHISGLS-ILFRWLIEGATLRI-----VDKFN-QLLEMIANER 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 381 INQFYGAPTAVRLLLKygdawvKKYDRSSLRTLGSVGEPINCEawewLHRVVGDSRCTLVDTWWQTETGGICIAPRPsee 460
Cdd:TIGR01923 198 VTHISLVPTQLNRLLD------EGGHNENLRKILLGGSAIPAP----LIEEAQQYGLPIYLSYGMTETCSQVTTATP--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 461 gaEILPAM--AMRPFFGI-VPVLMDEKGSVVEgsnvsgalcISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYR 537
Cdd:TIGR01923 265 --EMLHARpdVGRPLAGReIKIKVDNKEGHGE---------IMVKGANLMKG-YLYQGELTPAFEQQ--GWFNTGDIGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 538 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVA 617
Cdd:TIGR01923 331 DGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-----SESDISQAKLIAYLT 405
|
490 500
....*....|....*....|....*...
gi 28416953 618 TKIAKYAVPDEILVVKRLPKTRSGKVMR 645
Cdd:TIGR01923 406 EKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
115-657 |
8.85e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 108.92 E-value: 8.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRksPESVALIW-ERdepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAaMLACARIGAVh 192
Cdd:PRK10946 31 LTRHAA--SDAIAVICgER-------QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYIT-FFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 193 tVIFAGFSAESL-----AGRINDAkckVVItfnqGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLDvpL 267
Cdd:PRK10946 100 -PVNALFSHQRSelnayASQIEPA---LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDD------GEHS--L 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 268 EQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlYAAlthklvfdHQPGDIFGCVADIGWI----TGH 343
Cdd:PRK10946 164 DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSV--------RRSVEICGFTPQTRYLcalpAAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 344 SYVVYGPlcnGATSVLFESTPVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLgSVG-- 417
Cdd:PRK10946 235 NYPMSSP---GALGVFLAGGTVVlapdPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL-QVGga 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 418 -----------EPINCEawewLHRVVGDSRcTLV------DTWWQT-ETGGiciapRPSEEGAEILPAmamrpffgivpv 479
Cdd:PRK10946 311 rlsetlarripAELGCQ----LQQVFGMAE-GLVnytrldDSDERIfTTQG-----RPMSPDDEVWVA------------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 480 lmDEKGS-VVEGSnvSGALcisqawpgMAR---TIYG-----DHQRFVdayFKAyPGYYFTGDGAYRTEGGYYQITGRMD 550
Cdd:PRK10946 369 --DADGNpLPQGE--VGRL--------MTRgpyTFRGyykspQHNASA---FDA-NGFYCSGDLVSIDPDGYITVVGREK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 551 DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagdsdvvvqELKSMVATK------IAKYA 624
Cdd:PRK10946 433 DQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE----------PLKAVQLRRflreqgIAEFK 502
|
570 580 590
....*....|....*....|....*....|...
gi 28416953 625 VPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 657
Cdd:PRK10946 503 LPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-679 |
1.08e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK12316 2013 AARAPEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 199 FSAESLAGRINDAKCKVVITfnqglrggrvvelKKIVDEAVKhCPTVQHVLvahrtdnkvhmgDLDVPLEQEmakEDPVC 278
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT-------------QRHLLERLP-LPAGVARL------------PLDRDAEWA---DYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 279 APE-SMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHQPGDifgCVADIGWIT--GHSYVVYGPLCNGA 355
Cdd:PRK12316 2138 APAvQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 356 tSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDS 435
Cdd:PRK12316 2214 -RVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 436 RctLVDTWWQTETggiCIAPRPSEEGAEILPAMAMRPffgIVPVLMDEKGSVVEGS------NVSGALCISQAwpGMART 509
Cdd:PRK12316 2289 Y--LFNGYGPTEA---VVTPLLWKCRPQDPCGAAYVP---IGRALGNRRAYILDADlnllapGMAGELYLGGE--GLARG 2358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 510 IYG----DHQRFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGyp 584
Cdd:PRK12316 2359 YLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-- 2436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 585 HDIKGEAAFAFIVVKDSAGDSDvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDT 662
Cdd:PRK12316 2437 QDGASGKQLVAYVVPDDAAEDL--LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQayVAPQ 2514
|
570
....*....|....*....
gi 28416953 663 TTLED--PSIIAEILSVYQ 679
Cdd:PRK12316 2515 EGLEQrlAAIWQAVLKVEQ 2533
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
141-649 |
4.13e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 107.81 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfN 220
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 QGLR----GGRVVELKKIVDEAVKHCPTvqhvlvahrtdnkvhmgDLdvpleqemakedpvcapESMGSEDMLFMLYTSG 296
Cdd:PRK06060 110 DALRdrfqPSRVAEAAELMSEAARVAPG-----------------GY-----------------EPMGGDALAYATYTSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfESTPVYPNAGRYWETv 376
Cdd:PRK06060 156 TTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 377 eRLKINQFYGAPTavrLLLKYGDAWVKKYDRSsLRTLGSVGEPINCEAWEWLHRVVGDsrCTLVDTWWQTETGGICIAP- 455
Cdd:PRK06060 234 -RFGPSVLYGVPN---FFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSNr 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 456 ----RPSEEGaEILPAMAMRPffgIVPvlmdekGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAyfkayPGYYFT 531
Cdd:PRK06060 307 vdewRLGTLG-RVLPPYEIRV---VAP------DGTTAGPGVEGDLWVRG--PAIAKGYWNRPDSPVAN-----EGWLDT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 532 GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQE 611
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 28416953 612 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK06060 450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
140-649 |
2.94e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 104.01 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 219
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 NQGLRGgrvveLKKIVDEAVK--HCPTVQHVLVAHRTDN---KVHMGDLDvpLEQEMAKEDPVCAPESMGSEDMLfmlYT 294
Cdd:PRK12406 91 ADLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISPallTPPAGAID--WEGWLAQQEPYDGPPVPQPQSMI---YT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 295 SGSTGMPKGiVHTQAGYLLYAALTHKLVfdhqpGDIFGcvadigWITGHSYVVYGPLcngatsvlFESTP-VYP-NAGRY 372
Cdd:PRK12406 161 SGTTGHPKG-VRRAAPTPEQAAAAEQMR-----ALIYG------LKPGIRALLTGPL--------YHSAPnAYGlRAGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 373 WET---------------VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAwewlhrvvgDSRC 437
Cdd:PRK12406 221 GGVlvlqprfdpeellqlIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAP--CPA---------DVKR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 438 TLVDtWW---------QTETGGICIAprpSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISqawPGMAR 508
Cdd:PRK12406 290 AMIE-WWgpviyeyygSTESGAVTFA---TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI---AGNPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 509 TIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIGYP 584
Cdd:PRK12406 363 FTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMV-ISG---GVniypAEIEAVLHAVPGVHDCAVFGIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 585 HDIKGEAAFAFIVVKDSAG-DSDVVVQELKSMVAtkiaKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK12406 437 DAEFGEALMAVVEPQPGATlDEADIRAQLKARLA----GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-646 |
6.11e-23 |
|
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: 102.29 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 220
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakEDPvcapesmgsEDMLFMLYTSGSTGM 300
Cdd:cd05907 84 -----------------------------------------------------EDP---------DDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnagrywETVERLK 380
Cdd:cd05907 102 PKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL------DDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 381 INQFYGAPtavRLLLK-YGDAWVKK--------YDR---SSLRTLGSVGEPINCEAWEWLHRvVGdsrCTLVDTWWQTET 448
Cdd:cd05907 175 PTVFLAVP---RVWEKvYAAIKVKAvpglkrklFDLavgGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 449 GGICIAPRPSeegaeilpamamRPFFGIVpvlmdekGSVVEGSNV----SGALCISQawPGMARTIYGDHQRFVDAYFKa 524
Cdd:cd05907 248 SAVVTLNPPG------------DNRIGTV-------GKPLPGVEVriadDGEILVRG--PNVMLGYYKNPEATAEALDA- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 525 yPGYYFTGDGAYRTEGGYYQITGRMDDVI-NISGHRLGTAEIEDAIADHPAVPESAVIG--YPH-----DIKGEAAFAFI 596
Cdd:cd05907 306 -DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgRPFlvaliVPDPEALEAWA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 597 VVKDSAGDSDV-------VVQELKSMV---------ATKIAKYAVPDEILVVKRLPKTRSGKVMRR 646
Cdd:cd05907 385 EEHGIAYTDVAelaanpaVRAEIEAAVeaanarlsrYEQIKKFLLLPEPFTIENGELTPTLKLKRP 450
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
124-651 |
6.46e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 103.36 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 124 ESVALIWER------DEPGTE---VRITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAVAAMLacaRIGA 190
Cdd:PRK12492 24 KSVVEVFERsckkfaDRPAFSnlgVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPnvlQYPIAVFGAL---RAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 191 VHTVIFAGFSAESLAGRINDAKCKVVITFNqgLRGGRVVELkkIVDEAVKHC---------PTVQHVLVAHRTDNKVHMg 261
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYLN--MFGKLVQEV--LPDTGIEYLieakmgdllPAAKGWLVNTVVDKVKKM- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 262 dldVP---LEQEMA-------KEDPVCAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTH-KLVFDHQpgDI 330
Cdd:PRK12492 176 ---VPayhLPQAVPfkqalrqGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKG-----------AMLTHgNLVANML--QV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 331 FGCVADIGwITGHsyvvygPLCNGATSVLFESTPVY------------------------P-NAGRYWETVERLKINQFY 385
Cdd:PRK12492 240 RACLSQLG-PDGQ------PLMKEGQEVMIAPLPLYhiyaftancmcmmvsgnhnvlitnPrDIPGFIKELGKWRFSALL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 386 GAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPI---NCEAWEWLhrvvgdSRCTLVDTWWQTETGGICIApRPSEEGA 462
Cdd:PRK12492 313 GLNTLFVALMDHPG--FKDLDFSALKLTNSGGTALvkaTAERWEQL------TGCTIVEGYGLTETSPVAST-NPYGELA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 463 EI------LPAMAMRpffgivpVLMDEKGSVVEGSNvsGALCIS--QAWPGMARTIYGDHQrFVDAyfkayPGYYFTGDG 534
Cdd:PRK12492 384 RLgtvgipVPGTALK-------VIDDDGNELPLGER--GELCIKgpQVMKGYWQQPEATAE-ALDA-----EGWFKTGDI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 535 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKS 614
Cdd:PRK12492 449 AVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG----LSVEELKA 524
|
570 580 590
....*....|....*....|....*....|....*..
gi 28416953 615 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 651
Cdd:PRK12492 525 YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
112-658 |
6.93e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 103.16 E-value: 6.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 112 VNCLDQHVRKSPESVALiwerDEPGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK05605 35 VDLYDNAVARFGDRPAL----DFFGAT--TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 192 ---HTVIFagfSAESLAGRINDAKCKVVITFN------QGLRGGrvVELKKIVD-EAVKHCPTVQHVLV------AHRTD 255
Cdd:PRK05605 109 vveHNPLY---TAHELEHPFEDHGARVAIVWDkvaptvERLRRT--TPLETIVSvNMIAAMPLLQRLALrlpipaLRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 256 NKVHMGDLD-VPLEQ----EMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHklvfdhqpGDI 330
Cdd:PRK05605 184 AALTGPAPGtVPWETlvdaAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKG-----------AQLTH--------RNL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 331 FGCVAD-IGWITG---------------HSY-----VVYGPLCnGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPT 389
Cdd:PRK05605 245 FANAAQgKAWVPGlgdgpervlaalpmfHAYgltlcLTLAVSI-GGELVLLPA----PDIDLILDAMKKHPPTWLPGVPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 390 AVRLLLKygDAWVKKYDRSSLRTL--GSVGEPIN-CEAWEwlhRVVGDSrctLVDTWWQTETGGIcIAPRPSEEGAeilp 466
Cdd:PRK05605 320 LYEKIAE--AAEERGVDLSGVRNAfsGAMALPVStVELWE---KLTGGL---LVEGYGLTETSPI-IVGNPMSDDR---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 467 amamRPFFGIVPvLMDEKGSVVEGSNVSGALCISQAWPGMARtiygDHQRFvDAYFKA--------YPGYYFTGDGAYRT 538
Cdd:PRK05605 387 ----RPGYVGVP-FPDTEVRIVDPEDPDETMPDGEEGELLVR----GPQVF-KGYWNRpeetaksfLDGWFRTGDVVVME 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 539 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVAT 618
Cdd:PRK05605 457 EDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGA---ALDPEGLRAYCRE 533
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 28416953 619 KIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 658
Cdd:PRK05605 534 HLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
115-650 |
7.08e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 103.42 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVELkkiVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKE 274
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIV------GEELVEA---FEEARADLARPPRLWVAGGDTLDDPEGYEDL---AAAAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPESMGS---EDMLFMLYTSGSTGMPKGIVHTQAGYLLY----AALThklvfDHQPGDIFGCVADIGWITGHSYVV 347
Cdd:PRK08279 185 APTTNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAmggfGGLL-----RLTPDDVLYCCLPLYHNTGGTVAW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 348 YGPLCNGATSVLFESTpvypNAGRYWETVERlkinqfYGApTAV-------RLLLkygDAWVKKYDRS-SLRTLgsVGEP 419
Cdd:PRK08279 260 SSVLAAGATLALRRKF----SASRFWDDVRR------YRA-TAFqyigelcRYLL---NQPPKPTDRDhRLRLM--IGNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 420 INCEAW-EWLHRvVGDSRctLVDTWWQTE--TGGICIAPRPSEEGaeILPAMAMRPfFGIVPVlmD-EKGSVVEGSNvsg 495
Cdd:PRK08279 324 LRPDIWdEFQQR-FGIPR--ILEFYAASEgnVGFINVFNFDGTVG--RVPLWLAHP-YAIVKY--DvDTGEPVRDAD--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 ALCI--SQAWPGMARTIYGDHQRFvDAY--------------FKayPG--YYFTGDGAYRTEGGYYQITGRMDDVINISG 557
Cdd:PRK08279 393 GRCIkvKPGEVGLLIGRITDRGPF-DGYtdpeasekkilrdvFK--KGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 558 HRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKR 634
Cdd:PRK08279 470 ENVATTEVENALSGFPGVEEAVVYGVEvpgTD--GRAGMAAIVLADGA---EFDLAALAAHLYERLPAYAVPLFVRLVPE 544
|
570
....*....|....*.
gi 28416953 635 LPKTRSGKVMRRLLRK 650
Cdd:PRK08279 545 LETTGTFKYRKVDLRK 560
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
118-657 |
1.32e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 101.78 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 118 HVRKSPESVALIwERDEpgtevRITYRELLETTCRLANTLkRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK07638 10 HASLQPNKIAIK-ENDR-----VLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 198 GFSAESLAGRINDAKCKVVIT---FNQGLRG--GRVVELKKIvdeavkhcptvqhvlvahrtdnkvhMGDLDVPLEQEMA 272
Cdd:PRK07638 83 KWKQDELKERLAISNADMIVTeryKLNDLPDeeGRVIEIDEW-------------------------KRMIEKYLPTYAP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 273 KEDPVCAPESMGsedmlfmlYTSGSTGMPKGIVHTQAGYLL-YAALTHKLVFDHQ-----PGDIFgcvadigwitgHSYV 346
Cdd:PRK07638 138 IENVQNAPFYMG--------FTSGSTGKPKAFLRAQQSWLHsFDCNVHDFHMKREdsvliAGTLV-----------HSLF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 347 VYGplcngATSVLFESTPVY------PNAGRywETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSvGEPI 420
Cdd:PRK07638 199 LYG-----AISTLYVGQTVHlmrkfiPNQVL--DKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISS-GAKW 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 421 NCEAWE-----WLHrvvgdsrCTLVDTWWQTETGGICIAprpSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEgsnvsg 495
Cdd:PRK07638 266 EAEAKEkikniFPY-------AKLYEFYGASELSFVTAL---VDEESERRPNSVGRPFHNVQVRICNEAGEEVQ------ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 496 alcisqawPGMARTIY-GDHQRFV----DAYFKAYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 567
Cdd:PRK07638 330 --------KGEIGTVYvKSPQFFMgyiiGGVLARELnadGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIES 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 568 AIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSAGdsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 647
Cdd:PRK07638 402 VLHEHPAVDEIVVIGVPDSYWGEKPVA--IIKGSAT-----KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARME 474
|
570
....*....|
gi 28416953 648 LRKIITSEAQ 657
Cdd:PRK07638 475 AKSWIENQEK 484
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
291-645 |
3.56e-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: 98.34 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 291 MLYTSGSTGMPKGIV--HTQAgYLLYAALthklvfdhqpgdifgcvADIGWIT-GHSYVVYGPLCN------GATSVLFE 361
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAAW-----------------ADCADLTeDDRYLIINPFFHtfgykaGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 362 STPVYPNA----GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrc 437
Cdd:cd17638 67 GATVVPVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 438 TLVDTWWQTETGGICIApRPSEEgAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNV-SGALCISQAwpgMARTIYGDhqr 516
Cdd:cd17638 143 TVLTAYGLTEAGVATMC-RPGDD-AETVATTCGRACPGFEVRIADDGEVLVRGYNVmQGYLDDPEA---TAEAIDAD--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 517 fvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 596
Cdd:cd17638 215 ----------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFV 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 28416953 597 VVKDSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMR 645
Cdd:cd17638 285 VARPGVTlTEEDVIAWCRE----RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
133-643 |
4.69e-22 |
|
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: 100.10 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 133 DEPGTEVriTYRELLETTCRLANTLKRhGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAK 212
Cdd:cd05909 2 DTLGTSL--TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 213 CKVVITFNQ-----GLRGGRVVEL-KKIVD-EAVKhcptvqhvlvahrtdNKVHMGD-LDVPLEQEMAKEDPV----CAP 280
Cdd:cd05909 79 IKTVLTSKQfieklKLHHLFDVEYdARIVYlEDLR---------------AKISKADkCKAFLAGKFPPKWLLrifgVAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 281 ESmgSEDMLFMLYTSGSTGMPKGIVHTQAGYL--LYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSV 358
Cdd:cd05909 144 VQ--PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 359 LfestpvYPNAGRYW---ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVGEPINC---EAWEWLHRVV 432
Cdd:cd05909 219 F------HPNPLDYKkipELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGIR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 433 gdsrctLVDTWWQTETG---GICIAPRPSEEGA--EILPAMAMR--PFFGIVPVLMDEKGSV-VEGSNV-SGALcisqAW 503
Cdd:cd05909 289 ------ILEGYGTTECSpviSVNTPQSPNKEGTvgRPLPGMEVKivSVETHEEVPIGEGGLLlVRGPNVmLGYL----NE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 504 PGMARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH-PAVPESAVIG 582
Cdd:cd05909 359 PELTSFAFGD-------------GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVS 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28416953 583 YPHDIKGEAAFAFIVvkDSAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKV 643
Cdd:cd05909 426 VPDGRKGEKIVLLTT--TTDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
287-645 |
4.90e-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: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 287 DMLFMLYTSGSTGMPKGIVHTQAGYLLYaalthklvFDHQPGDIFGCVADIGWITG---HSYVVYGplcngATSVLFEST 363
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYG-----AISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 364 PVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctL 439
Cdd:cd17633 68 TFIgqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKNIFPKAN--L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 440 VDTWWQTETGgiCIAPRPSEEGAEilPAMAMRPFFGIVPVLMDEKGSVVegsnvsGALCISQAwpgMARTIYgdhqrfVD 519
Cdd:cd17633 140 IEFYGTSELS--FITYNFNQESRP--PNSVGRPFPNVEIEIRNADGGEI------GKIFVKSE---MVFSGY------VR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 520 AYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvk 599
Cdd:cd17633 201 GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS-- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 28416953 600 dsaGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 645
Cdd:cd17633 279 ---GDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
116-648 |
5.29e-22 |
|
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: 99.82 E-value: 5.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITfnQGlrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemaked 275
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT--QP----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 pvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPgDIFGCVADIGWITGhSYVVYGPLCNGA 355
Cdd:cd17644 106 ----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 356 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINCEAWEWLHRVVGDs 435
Cdd:cd17644 174 TLVL-RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 436 RCTLVDTWWQTE---TGGICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYG 512
Cdd:cd17644 251 FIQLINVYGPTEatiAATVCRLTQLTER--NITSVPIGRPIANTQVYILDENLQPVP-VGVPGELHIGGV--GLARGYLN 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 513 ----DHQRFVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 586
Cdd:cd17644 326 rpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQ 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 587 IKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17644 406 PGNKRLVAYIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
130-650 |
2.25e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 98.70 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 130 WERDEPGTevrITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:PRK05620 31 WGGAEQEQ---TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 209 NDAKCKVVITFNQglrggrvveLKKIVDEAVKHCPTVQHVLVAHRTD---------NKVHMGDLDVPLEQEMAKEDPVCA 279
Cdd:PRK05620 108 NHAEDEVIVADPR---------LAEQLGEILKECPCVRAVVFIGPSDadsaaahmpEGIKVYSYEALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 280 PESMGSEdmlfMLYTSGSTGMPKGIVHT-QAGYLLYAALTHKLVFDHQPGDIFGCVADI-----------GWITGHSYVV 347
Cdd:PRK05620 179 DETTAAA----ICYSTGTTGAPKGVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPIyhvlswgvplaAFMSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 348 YGPLCNGAT--SVLFESTPvypnagrywetverlkiNQFYGAPTA-VRLLLKYGDawvKKYDRSSLRTL---GSVGEPIN 421
Cdd:PRK05620 255 PGPDLSAPTlaKIIATAMP-----------------RVAHGVPTLwIQLMVHYLK---NPPERMSLQEIyvgGSAVPPIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 CEAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRPSEeGAEILPAMAMRPFFGIVPVLMDEK----GSVVEGSN----- 492
Cdd:PRK05620 315 IKAWEERYGV------DVVHVWGMTETSPVGTVARPPS-GVSGEARWAYRVSQGRFPASLEYRivndGQVMESTDrnege 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 493 --VSGALCI-------SQAWPGMARTIYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTA 563
Cdd:PRK05620 388 iqVRGNWVTasyyhspTEEGGGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 564 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 643
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKF 546
|
....*..
gi 28416953 644 MRRLLRK 650
Cdd:PRK05620 547 DKKDLRQ 553
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
140-650 |
7.10e-21 |
|
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: 96.34 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 219
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKEDPVCAPesMGSEDMLFMLYTSGSTG 299
Cdd:cd05939 82 ------------------------------------------NLLDPLLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 300 MPKGIVHTQAGYLLYAALTHKlVFDHQPGDIFgcvadigWITGHSYVVYGPLCNGATSVLFESTPVYP---NAGRYWETV 376
Cdd:cd05939 118 LPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVV-------YDCLPLYHSAGGIMGVGQALLHGSTVVIRkkfSASNFWDDC 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 377 ERLK--INQFYGapTAVRLLLkygDAWVKKYD-RSSLRTLgsVGEPINCEAWEWLHRVVG-----------DSRCTLVDT 442
Cdd:cd05939 190 VKYNctIVQYIG--EICRYLL---AQPPSEEEqKHNVRLA--VGNGLRPQIWEQFVRRFGipqigefygatEGNSSLVNI 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 443 wwQTETGGICIAPRpseegaeILPAMamrpfFGIVPVLMDE-KGSVVEGSNvsgALCISQAwPG-----MARTIYGDHQR 516
Cdd:cd05939 263 --DNHVGACGFNSR-------ILPSV-----YPIRLIKVDEdTGELIRDSD---GLCIPCQ-PGepgllVGKIIQNDPLR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 517 FVDAY--------------FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 582
Cdd:cd05939 325 RFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYG 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 583 Y--PHdIKGEAAFAFIVVKDSAGDSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05939 405 VevPG-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
112-649 |
7.10e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 97.05 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 112 VNCLDQHVRKSPESVALIwerdEPGtEVrITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAVAAMLacaR 187
Cdd:PRK08974 26 VDMFEQAVARYADQPAFI----NMG-EV-MTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPnllQYPIALFGIL---R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 188 IGAVHTVIFAGFSAESLAGRINDAKCK---VVITFNQglrggrvvELKKIVDE-AVKHC---------PTVQHVLV---- 250
Cdd:PRK08974 97 AGMIVVNVNPLYTPRELEHQLNDSGAKaivIVSNFAH--------TLEKVVFKtPVKHViltrmgdqlSTAKGTLVnfvv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 251 --AHRTDNKVHMGD-------LDVPLEQEMAKEDpvcapesMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHkl 321
Cdd:PRK08974 169 kyIKRLVPKYHLPDaisfrsaLHKGRRMQYVKPE-------LVPEDLAFLQYTGGTTGVAKG-----------AMLTH-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 322 vfdhqpGDIFGCVADIGWItghsyvvYGPLCNGATSVLFESTPVYP------NAGRYWE----------------TVERL 379
Cdd:PRK08974 229 ------RNMLANLEQAKAA-------YGPLLHPGKELVVTALPLYHifaltvNCLLFIElggqnllitnprdipgFVKEL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 380 KINQFYgAPTAVRLLLkygDAWV-----KKYDRSSLRTLGSVGEPInceawewlHRVVGDSrctlvdtwWQTETGGICIa 454
Cdd:PRK08974 296 KKYPFT-AITGVNTLF---NALLnneefQELDFSSLKLSVGGGMAV--------QQAVAER--------WVKLTGQYLL- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 455 prpseEG---AEILPAMAMRPF--------FGiVPV------LMDEKGSVVEGSNvSGALCIS--QAWPGmartiYGDHQ 515
Cdd:PRK08974 355 -----EGyglTECSPLVSVNPYdldyysgsIG-LPVpsteikLVDDDGNEVPPGE-PGELWVKgpQVMLG-----YWQRP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 516 RFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 595
Cdd:PRK08974 423 EATDEVIK--DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIF 500
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 28416953 596 IVVKDSAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK08974 501 VVKKDPSLTEE----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
285-642 |
9.61e-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: 94.37 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 285 SEDMLFMLYTSGSTGMPKGIVHTQA---GYLLYAALTHKLVFDHQPGDIFGCVADigwiTGHSYVVYGPLCNGA------ 355
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFTPSEDAHKAAAAA----AGTVMFPAPPLMHGTgswtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 356 TSVLFESTPVYP----NAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPIN 421
Cdd:cd05924 78 GGLLGGQTVVLPddrfDPEEVWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 CEAWEWLHRVVGDSrcTLVDTWWQTETGGICIApRPSEEGAEilpamaMRPFFGIVP--VLMDEKGSVVE-GSNVSGALc 498
Cdd:cd05924 148 PEVKQGLLELVPNI--TLVDAFGSSETGFTGSG-HSAGSGPE------TGPFTRANPdtVVLDDDGRVVPpGSGGVGWI- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 499 isqAWPG-MARTIYGDHQRfVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 575
Cdd:cd05924 218 ---ARRGhIPLGYYGDEAK-TAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 576 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 642
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
115-648 |
1.10e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.93 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDakCKVVITFNQGLRGGRVvelkkivdeavkhcPTVQHVLVahrtdnkvhmgdldVPLEQEMAKE 274
Cdd:PRK05691 1211 LDPDYPAERLAYMLAD--SGVELLLTQSHLLERL--------------PQAEGVSA--------------IALDSLHLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKL-----VFDHQPGDIFGCVADIGWITGhSYVVY 348
Cdd:PRK05691 1261 WPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNT------HAALAERLqwmqaTYALDDSDVLMQKAPISFDVS-VWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 349 GPLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE-- 426
Cdd:PRK05691 1334 WPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA----AACTSLRRLFSGGEALPAELRNrv 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 427 -------WLHRVVGDSRCTLVDTWWQtetggiCIAprpsEEGaEILPAMamRPFFGIVPVLMDEKGSVVEGSnVSGALCI 499
Cdd:PRK05691 1409 lqrlpqvQLHNRYGPTETAINVTHWQ------CQA----EDG-ERSPIG--RPLGNVLCRVLDAELNLLPPG-VAGELCI 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 500 SQAwpGMARTIYG----DHQRFV-DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPA 574
Cdd:PRK05691 1475 GGA--GLARGYLGrpalTAERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 575 VPESAVIgyphdIKGEAAFAFIVVKDSAGDS-DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:PRK05691 1553 VAQAAVL-----VREGAAGAQLVGYYTGEAGqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
141-649 |
1.81e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.71 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLAN-TLKRHGVHRGDRVAIYMPVS---PLAVAAMLaCARIGAV------------HTVIFAGFSA--- 201
Cdd:PRK08751 51 ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNClqyPIATFGVL-RAGLTVVnvnplytprelkHQLIDSGASVlvv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 202 -----ESLAGRINDAKCKVVITfnQGLrgGRVVELKK--IVDEAVKHcptVQHVLVAHRTDNKVHMGD-LDVPLEQEMAK 273
Cdd:PRK08751 130 idnfgTTVQQVIADTPVKQVIT--TGL--GDMLGFPKaaLVNFVVKY---VKKLVPEYRINGAIRFREaLALGRKHSMPT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 EDpvcapesMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-LVFDHQPGDifgcvadiGWITGHS-------- 344
Cdd:PRK08751 203 LQ-------IEPDDIAFLQYTGGTTGVAKG-----------AMLTHRnLVANMQQAH--------QWLAGTGkleegcev 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 345 -------YVVYGPLCNGATSVLFE------STPvyPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLR 411
Cdd:PRK08751 257 vitalplYHIFALTANGLVFMKIGgcnhliSNP--RDMPGFVKELKKTRFTAFTGVNTLFNGLLN--TPGFDQIDFSSLK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 412 -TLGSvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETG-GICIAPRPSEE--GAEILPamamrpffgiVP----VLMDE 483
Cdd:PRK08751 333 mTLGG-GMAVQRSVAERWKQVTG---LTLVEAYGLTETSpAACINPLTLKEynGSIGLP----------IPstdaCIKDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 484 KGSVVEGSNVsGALCISQAwpgmaRTIYGDHQR------FVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISG 557
Cdd:PRK08751 399 AGTVLAIGEI-GELCIKGP-----QVMKGYWKRpeetakVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 558 HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPK 637
Cdd:PRK08751 468 FNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA----LTAEDVKAHARANLTGYKQPRIIEFRKELPK 543
|
570
....*....|..
gi 28416953 638 TRSGKVMRRLLR 649
Cdd:PRK08751 544 TNVGKILRRELR 555
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
527-649 |
4.42e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 93.90 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 527 GYYFTGDGAYRTEGGYYQITGRMD-DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 605
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-----GAD 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 28416953 606 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
116-648 |
7.13e-20 |
|
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: 93.00 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 116 DQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemaked 275
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 pvcapesmGSEDMLFMLYTSGSTGMPKGI-VHTQAgyLLYAALTHKLVFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNG 354
Cdd:cd17645 102 --------NPDDLAYVIYTSGSTGLPKGVmIEHHN--LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 355 ATsvlfesTPVYPNAGRYweTVERLkiNQFYGAPTAVRLLLKYGDA-WVKKYDRSSLRTLGSVGEPINcEAWEWLHRVV- 432
Cdd:cd17645 171 AA------LHVVPSERRL--DLDAL--NDYFNQEGITISFLPTGAAeQFMQLDNQSLRVLLTGGDKLK-KIERKGYKLVn 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 433 --GDSRCTLVDTWWQTEtggiciaprPSEEGAEILPAMAMrpffgiVPVLMDEKGSVVEGSNVSGALCIsqAWPGMARTI 510
Cdd:cd17645 240 nyGPTENTVVATSFEID---------KPYANIPIGKPIDN------TRVYILDEALQLQPIGVAGELCI--AGEGLARGY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 586
Cdd:cd17645 303 LNrpelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416953 587 IKGEAAFAFIVVKdsagdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd17645 383 DGRKYLVAYVTAP-----EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
138-650 |
1.31e-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: 92.88 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 TFNqglrggrvvELKKIVDEAVKhcptvqhvLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSE-DMLFMLYTSG 296
Cdd:cd05915 102 FDP---------NLLPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVHTQAG-YLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEstpvYPNAGRYWET 375
Cdd:cd05915 164 TTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 376 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinceawEWLHRVVGDSRCTLVDTWWQTETGGICIA- 454
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAP------RSLIARFERMGVEVRQGYGLTETSPVVVQn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 455 ---PR----PSEEGAEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNVSgalCISQAWPGMARTIYGDHQRFVDAYFKAyp 526
Cdd:cd05915 314 fvkSHleslSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPkDGKALG---EVQLKGPWITGGYYGNEEATRSALTPD-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 527 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 606
Cdd:cd05915 389 GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 28416953 607 VVVQELKSMVATkiaKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05915 469 ELNEHLLKAGFA---KWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
141-649 |
1.35e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 92.90 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAV-AAMlacaRIGAVHTVIFAGFSAESLAGRINDAKCKV 215
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPnvlQYPVAVfGAM----RAGLIVVNTNPLYTAREMEHQFNDSGAKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 216 VITF------------NQGLRGGRVVEL--------KKIVDEAVKHcptVQHVLVAHRTDNKVHMGDLdvpleQEMAKED 275
Cdd:PRK05677 126 LVCLanmahlaekvlpKTGVKHVIVTEVadmlpplkRLLINAVVKH---VKKMVPAYHLPQAVKFNDA-----LAKGAGQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 276 PVcAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-LVfdhqpGDIFGCVADIGWITGH-SYVVYGPL-- 351
Cdd:PRK05677 198 PV-TEANPQADDVAVLQYTGGTTGVAKG-----------AMLTHRnLV-----ANMLQCRALMGSNLNEgCEILIAPLpl 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 352 ---------CnGATSVLFESTPVYPNAGRYWETVERL---KINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEP 419
Cdd:PRK05677 261 yhiyaftfhC-MAMMLIGNHNILISNPRDLPAMVKELgkwKFSGFVGLNTLFVALCNNEA--FRKLDFSALKLTLSGGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 420 INCEAWEWLHRVVGdsrCTLVDTWWQTETGGI-CIAPRPSEEGAEI-LPAMAMrpffgIVPVLMDEKGSVVEGSnvSGAL 497
Cdd:PRK05677 338 LQLATAERWKEVTG---CAICEGYGMTETSPVvSVNPSQAIQVGTIgIPVPST-----LCKVIDDDGNELPLGE--VGEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 498 CIS--QAWPGmartiYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 575
Cdd:PRK05677 408 CVKgpQVMKG-----YWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28416953 576 PESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK05677 482 LQCAAIGVPDEKSGEAIKVFVVVKPGET---LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
286-645 |
1.76e-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: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 286 EDMLFMLYTSGSTGMPKGIVhtQAGYLLYAALTH--KLVFDHQPGDIFGCVADIGWITGHSYVvygplcngATSVLFEST 363
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVL--LANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWI--------LTCLIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 364 PVYPNAGRYWETVerLKINQFYGA------PTA---VRLLLKYGDAWVKKydrssLRTLGSVGE-PINCEA--WEWLHRV 431
Cdd:cd17635 71 CVTGGENTTYKSL--FKILTTNAVtttclvPTLlskLVSELKSANATVPS-----LRLIGYGGSrAIAADVrfIEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 432 vgdsrcTLVDTWWQTETGGICIAPrpSEEGAEILPAMAmRPFFGIVPVLMDEKG-SVVEGSNvsGALCISQAWpgMARTI 510
Cdd:cd17635 144 ------NTAQVYGLSETGTALCLP--TDDDSIEINAVG-RPYPGVDVYLAATDGiAGPSASF--GTIWIKSPA--NMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 590
Cdd:cd17635 211 WNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 591 AAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 645
Cdd:cd17635 288 LVGLAVVA--SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
117-648 |
1.09e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.07 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 197 AGFSAESLAgRINDAKCKVVITFNqglRGGRVvelkkivdeAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDP 276
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPAAALVA---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 277 vcapeSMGSEDMLFMLYTSGSTGMPKGIvhtqagyLLyaalthklvfdhqPGDIFGCVADI---------GWITGHSyvV 347
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAV-------LL-------------ANRTFFAVPDIlqkeglnwvTWVVGET--T 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 348 YGPLcnGATSVlfestpvypnAGRYW----------------------ETVERLKINQFYGAPTAVRLL---LKYGDAwv 402
Cdd:PRK05857 218 YSPL--PATHI----------GGLWWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLvseLKSANA-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 403 kkyDRSSLRTLGSVGEPInceawewlhrVVGDSR---CTLVDT---WWQTETG--GICIaPRPSEEGAEILPAMAMRPFF 474
Cdd:PRK05857 284 ---TVPSLRLVGYGGSRA----------IAADVRfieATGVRTaqvYGLSETGctALCL-PTDDGSIVKIEAGAVGRPYP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 475 GIVPVLMDEKGSVVEGSNVSGALCISQAW---PGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDD 551
Cdd:PRK05857 350 GVDVYLAATDGIGPTAPGAGPSASFGTLWiksPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 552 VINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGeaAFAFIVVKDSAGDSDVVVQELKSMVATKIAK----YAVPD 627
Cdd:PRK05857 427 MIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG--ALVGLAVVASAELDESAARALKHTIAARFRResepMARPS 504
|
570 580
....*....|....*....|.
gi 28416953 628 EILVVKRLPKTRSGKVMRRLL 648
Cdd:PRK05857 505 TIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
117-654 |
4.80e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.11 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAAMLACARIGavhtvI 195
Cdd:PLN02330 36 QDAELYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPnVAEYGIVALGIMAAGG-----V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRIND----AKCKVVITfnQGLRGGRVVELKkivdeavkhCPTVqhVLVAHRTDNKVHMGDLdvpLEQEM 271
Cdd:PLN02330 107 FSGANPTALESEIKKqaeaAGAKLIVT--NDTNYGKVKGLG---------LPVI--VLGEEKIEGAVNWKEL---LEAAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 272 AKEDPVcAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLvFDHQPgDIFGCVADIGWITG-HSYVVYGP 350
Cdd:PLN02330 171 RAGDTS-DNEEILQTDLCALPFSSGTTGISKGVMLTHRN--LVANLCSSL-FSVGP-EMIGQVVTLGLIPFfHIYGITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 351 LCngATsvlfestpvYPNAGRYwETVERLKINQFYGA------------PTAVRLLLKygDAWVKKYDRSSL--RTLGSV 416
Cdd:PLN02330 246 CC--AT---------LRNKGKV-VVMSRFELRTFLNAlitqevsfapivPPIILNLVK--NPIVEEFDLSKLklQAIMTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 417 GEPINCE---AWEWLHRVVgdsrcTLVDTWWQTETGGICIAPRPSEEGAEIlpamAMRPFFG-IVPVL----MDEKGSVV 488
Cdd:PLN02330 312 AAPLAPElltAFEAKFPGV-----QVQEAYGLTEHSCITLTHGDPEKGHGI----AKKNSVGfILPNLevkfIDPDTGRS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 489 EGSNVSGALCI-SQAwpgMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 564
Cdd:PLN02330 383 LPKNTPGELCVrSQC---VMQGYYNNKEetdRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 565 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 644
Cdd:PLN02330 455 LEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE---EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIM 531
|
570
....*....|
gi 28416953 645 RRLLRKIITS 654
Cdd:PLN02330 532 RRLLKEKMLS 541
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
138-651 |
1.34e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.61 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 TFNqglrggrvvELKKIVDEAVKHCPTVQH-----VLVAHRTDNKVHMGDLDVPLEQEMAKEDPvcAPESMGS------- 285
Cdd:PLN03102 117 VDR---------SFEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 286 EDMLFMLYTSGSTGMPKGIVHTQAGYLLyAALThkLVFDHQPG---------DIFGCVadiGWItghsyVVYGPLCNGAT 356
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYL-STLS--AIIGWEMGtcpvylwtlPMFHCN---GWT-----FTWGTAARGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 SVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLKyGDAWVKKYDRSSLRTLGSVGEP-------INCEAWEWLH 429
Cdd:PLN03102 255 SVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPPpaalvkkVQRLGFQVMH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 rVVGDSRCT--LVDTWWQTETGGIciaprPSEEGAEILPAMAMRpFFGIVPVLMDEKG---SVVEGSNVSGALCISqawp 504
Cdd:PLN03102 330 -AYGLTEATgpVLFCEWQDEWNRL-----PENQQMELKARQGVS-ILGLADVDVKNKEtqeSVPRDGKTMGEIVIK---- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 505 gmARTIYGDHQRFVDAYFKAYP-GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 583
Cdd:PLN03102 399 --GSSIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAM 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 584 PHDIKGEAAFAFIVVKDS----AGDSDVVVQELKSMVA---TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 651
Cdd:PLN03102 477 PHPTWGETPCAFVVLEKGettkEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
139-660 |
1.38e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 86.44 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 139 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 219 fNQglrggrvvELKKIVDEAVK---------HCPTVQHVLVAHRTDNKV---HMGDLDVPLEQEMAKEDPVCAPESMGSE 286
Cdd:PLN02479 124 -DQ--------EFFTLAEEALKilaekkkssFKPPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 287 -DMLFMLYTSGSTGMPKGIV-HTQAGYLLyaALTHKLVFDHQPGDI-------FGCVadiGWITGHSYVVygpLCngATS 357
Cdd:PLN02479 195 wQSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVylwtlpmFHCN---GWCFTWTLAA---LC--GTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 358 VLF---ESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWL-HRV 431
Cdd:PLN02479 265 ICLrqvTAKAIY-------SAIANYGVTHFCAAPVVLNTIVNApkSETILPLPRVVHVMTAGAAPPPSVLFAMSEKgFRV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 432 VgdsrctlvDTWWQTETGG---ICI-APR----PSEEGAEILPAMAMRpFFGI-----------VPVLMDEK--GSVVEG 490
Cdd:PLN02479 338 T--------HTYGLSETYGpstVCAwKPEwdslPPEEQARLNARQGVR-YIGLegldvvdtktmKPVPADGKtmGEIVMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 491 SNVsgalcisqAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 570
Cdd:PLN02479 409 GNM--------VMKGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 571 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLL 648
Cdd:PLN02479 474 THPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
570
....*....|..
gi 28416953 649 RkiitSEAQELG 660
Cdd:PLN02479 553 R----AKAKEMG 560
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
130-650 |
1.70e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 86.27 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 130 WERDEPG---TEVRITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLA 205
Cdd:PRK07867 15 AEDDDRGlyfEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 206 GRINDAKCKVVITFNqglrggrvvelkkivdeavKHCPTVQHVlvahrtDNKVHMGDLDVPL-EQEMAKEDPVCAPESMG 284
Cdd:PRK07867 95 RDIAHADCQLVLTES-------------------AHAELLDGL------DPGVRVINVDSPAwADELAAHRDAEPPFRVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 285 SEDMLFMLY-TSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIfgCVADIGWItgHSYVV---YGP-LCNGATSVL 359
Cdd:PRK07867 150 DPDDLFMLIfTSGTSGDPKAVRCTH-RKVASAGVMLAQRFGLGPDDV--CYVSMPLF--HSNAVmagWAVaLAAGASIAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 360 ---FestpvypNAGRYWETVERlkinqfYGAPTA--VRLLLKYGDAWVKKYD--RSSLRTL-GSVGEPINCEAWEwlhRV 431
Cdd:PRK07867 225 rrkF-------SASGFLPDVRR------YGATYAnyVGKPLSYVLATPERPDdaDNPLRIVyGNEGAPGDIARFA---RR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 432 VGdsrCTLVDTWWQTEtGGICIAPRPSEegaeilPAMAMRPFFGIVPVLMDEKGS-----------VVEGSNVSGALcIS 500
Cdd:PRK07867 289 FG---CVVVDGFGSTE-GGVAITRTPDT------PPGALGPLPPGVAIVDPDTGTecppaedadgrLLNADEAIGEL-VN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 501 QAWPGMARTIY----GDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 576
Cdd:PRK07867 358 TAGPGGFEGYYndpeADAERMRG-------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416953 577 ESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:PRK07867 431 EVAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
120-464 |
1.76e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.11 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 120 RKSPESVALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 196 FAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKivdEAVKHCPTVqhvlvahrtDNKVHMG--DLDvPLEQEMAK 273
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK---PSVRRLVTV---------GGRLLWGgtTLA-TLLRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 274 EDPVCAPesMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlyAALTH-KLVFDHQPGDIfgcvaDIgwitgHSY---VVYG 349
Cdd:PRK09274 164 APFPMAD--LAPDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEAlREDYGIEPGEI-----DL-----PTFplfALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 350 PLCnGATSVLFESTPVYP---NAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWE 426
Cdd:PRK09274 230 PAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 427 WLHRVVGD--------------------SRCTLVDTWWQTETG-GICIApRPSeEGAEI 464
Cdd:PRK09274 307 RFRAMLPPdaeiltpygatealpissieSREILFATRAATDNGaGICVG-RPV-DGVEV 363
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
142-649 |
6.91e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 84.31 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLKrhGVHRGDR---VAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:PRK13388 28 TWREVLAEAAARAAALI--ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 219 fnqglrggrvvelkkivDEAvkHCPTVQHVLVAhrtdnKVHMGDLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGS 297
Cdd:PRK13388 106 -----------------DAE--HRPLLDGLDLP-----GVRVLDVDTPAYAELVAAAGALTPHReVDAMDPFMLIFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 298 TGMPKGIVHTQAGYLLYA-ALTHKlvFDHQPGDIFGCVADIGwitgHSYVVY---GP-LCNGATSVLfestPVYPNAGRY 372
Cdd:PRK13388 162 TGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPLF----HSNAVMagwAPaVASGAAVAL----PAKFSASGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 373 WETVerlkinQFYGAP--TAVRLLLKYGDAWVKKYDRS--SLRT-LGSVGEPINCEawEWLHRVvgdsRCTLVDTWWQTE 447
Cdd:PRK13388 232 LDDV------RRYGATyfNYVGKPLAYILATPERPDDAdnPLRVaFGNEASPRDIA--EFSRRF----GCQVEDGYGSSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 448 TGGICIAPRPSEEGAeilpamAMRPFFGIV-----------PVLMDEKGSVVEGSNVSGALcISQAWPGMARTIYGDH-- 514
Cdd:PRK13388 300 GAVIVVREPGTPPGS------IGRGAPGVAiynpetltecaVARFDAHGALLNADEAIGEL-VNTAGAGFFEGYYNNPea 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 515 --QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 592
Cdd:PRK13388 373 taERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 593 FAFIVVKDsagDSDVVVQELKSMVATK--IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 649
Cdd:PRK13388 446 MAALVLRD---GATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
123-648 |
1.32e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.12 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK13383 49 PGRTAII---DDDGA---LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 203 SLAGRINDAKCKVVITFNQglrggrvvelkkIVDEAVKhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPES 282
Cdd:PRK13383 123 ALAAALRAHHISTVVADNE------------FAERIAG-------------ADDAVAVIDPATAGAEESGGRPAVAAPGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 283 MgsedmlfMLYTSGSTGMPKGIVHT---QAGYLLYAALTHKLVFDhqpgdifgcvadigwiTGHSYVVYGPLCNG---AT 356
Cdd:PRK13383 178 I-------VLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRLR----------------TGSRISVAMPMFHGlglGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 357 SVLFESTPVYPNAGRYWETVERL------KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHR 430
Cdd:PRK13383 235 LMLTIALGGTVLTHRHFDAEAALaqaslhRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 431 VVGDsrcTLVDTWWQTETGgICIAPRPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGmarti 510
Cdd:PRK13383 315 TYGD---ILYNGYGSTEVG-IGALATPAD--LRDAPETVGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAG----- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 ygdhQRFVDAYFKAY-PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 589
Cdd:PRK13383 383 ----TRYTDGGGKAVvDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFG 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 590 EAAFAFIVVKDSagdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:PRK13383 459 HRLAAFVVLHPG---SGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
115-648 |
2.46e-16 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 83.56 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 195 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkiVDEavkhcptvqhvlVAHRTDNkvhmGDLDVPLEQEMAKE 274
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLIT----------------TAD------------QLPRFAD----VPDLTSLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 275 DPVCAPESMGS-EDMLFMLYTSGSTGMPKGIVHTQagyllyAALTHKLVFDHqpgDIFGCVAD--IGWITGHSYVV---- 347
Cdd:PRK10252 586 PQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQ------TAIVNRLLWMQ---NHYPLTADdvVLQKTPCSFDVsvwe 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 348 -YGPLCNGATSVLFEstpvyPNAGRYWETVERL----KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGE--PI 420
Cdd:PRK10252 657 fFWPFIAGAKLVMAE-----PEAHRDPLAMQQFfaeyGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEalPA 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 421 N-CEAWEW-----LHRVVGDSRCTlVD-TWW--------QTETGGICIAPRPSEEGAEILPAMaMRPffgiVPVlmdekg 485
Cdd:PRK10252 732 DlCREWQQltgapLHNLYGPTEAA-VDvSWYpafgeelaAVRGSSVPIGYPVWNTGLRILDAR-MRP----VPP------ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 486 svvegsNVSGALCIS--QawpgMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHR 559
Cdd:PRK10252 800 ------GVAGDLYLTgiQ----LAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQR 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 560 LGTAEIEDAIADHP----AVPESAVIGYPHDIKGEAA--FAFIVVKDSAG-DSDVvvqeLKSMVATKIAKYAVPDEILVV 632
Cdd:PRK10252 870 IELGEIDRAMQALPdveqAVTHACVINQAAATGGDARqlVGYLVSQSGLPlDTSA----LQAQLRERLPPHMVPVVLLQL 945
|
570
....*....|....*.
gi 28416953 633 KRLPKTRSGKVMRRLL 648
Cdd:PRK10252 946 DQLPLSANGKLDRKAL 961
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
522-653 |
5.78e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.81 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 522 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDS 601
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 28416953 602 AGDsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 653
Cdd:PRK07445 399 SIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
58-114 |
9.26e-16 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 71.73 E-value: 9.26e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 58 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFStGKIGWFLGGQLNVSVNC 114
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
138-648 |
1.84e-15 |
|
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: 79.41 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 TfnqglrggrvvelkkivdeavkhcptvqhvlvahrTDNkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGS 297
Cdd:cd05914 85 V-----------------------------------SDE-----------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 298 TGMPKGIVHTQAG----------YLLYAALTHKLVFdhQP-GDIFGCVADIgwitghsyvVYgPLCNGATSVLFESTP-- 364
Cdd:cd05914 101 TGNSKGVMLTYRNivsnvdgvkeVVLLGKGDKILSI--LPlHHIYPLTFTL---------LL-PLLNGAHVVFLDKIPsa 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 365 ---------VYPNAG--RYWETVERLK---INQFYGAPTAVRLLLKYGDAWVKKYDRSSL--------RTLGSVGEPINC 422
Cdd:cd05914 169 kiialafaqVTPTLGvpVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAWEWLHRVvgdsRCTLVDTWWQTETGGICIAPRPSEE----GAEILPAMAMRPFfgiVPVLMDEKGS-VVEGSNVsgal 497
Cdd:cd05914 249 DVEEFLRTI----GFPYTIGYGMTETAPIISYSPPNRIrlgsAGKVIDGVEVRID---SPDPATGEGEiIVRGPNV---- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 498 cisqawpgMaRTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINI-SGHRLGTAEIEDAIADHPAVP 576
Cdd:cd05914 318 --------M-KGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVL 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 577 ESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYA-VPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:cd05914 387 ESLVVVQEKKLVAlayiDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
530-648 |
2.02e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.92 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 530 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfIVVKDSAGDSDvvv 609
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA-KVISHEEIDPV--- 369
|
90 100 110
....*....|....*....|....*....|....*....
gi 28416953 610 qELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:PRK08308 370 -QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
141-653 |
4.56e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 78.73 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDakCKVVITF 219
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVD--CSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 nqglrggrvvelkkIVDEAVKHCPTVQhVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGS 297
Cdd:PLN02574 145 --------------TSPENVEKLSPLG-VPVIGVPENYDFdSKRIEFPKFYELIKEDFDFVPKPvIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 298 TGMPKGIVHTQAGYL----LYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYW 373
Cdd:PLN02574 210 TGASKGVVLTHRNLIamveLFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 374 ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVgepiNCEAWEWLHRVVGD-----SRCTLVDTWWQTET 448
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKK----AKGVCGEVLKSLKQV----SCGAAPLSGKFIQDfvqtlPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 449 GGICIAPRPSEEGAE------ILPAMAMRpffgivpVLMDEKGSVVEGSNvSGALCISQawPGMARTIYGDHQRFVDAYF 522
Cdd:PLN02574 358 TAVGTRGFNTEKLSKyssvglLAPNMQAK-------VVDWSTGCLLPPGN-CGELWIQG--PGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 523 KayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSA 602
Cdd:PLN02574 428 K--DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 28416953 603 GDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 653
Cdd:PLN02574 506 TLSQ---EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
133-651 |
8.80e-15 |
|
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: 77.71 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 133 DEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAK 212
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 213 cKVVITFNQGL---RGGRVVELKKIVDEAVkhcptvqhvlvahrtdnkvHMGDLDVPLEQEMAKEDPVCAPESmGSEDML 289
Cdd:cd05906 112 -HIWQLLGSPVvltDAELVAEFAGLETLSG-------------------LPGIRVLSIEELLDTAADHDLPQS-RPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 290 FMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFgcvadIGW-----ITGHSYVVYGPLCNGATSVLFESTP 364
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 365 VYPNAGRYWETVERLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLV 440
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLL--EPYGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 441 DT-----WWQTETGGICI------APRPSEE------GAEIlPAMAMRpffgivpvLMDEKGSVVEGSNVsGALCISqaw 503
Cdd:cd05906 320 PDairpaFGMTETCSGVIysrsfpTYDHSQAlefvslGRPI-PGVSMR--------IVDDEGQLLPEGEV-GRLQVR--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 504 pGMARTiygdhqrfvdayfkayPGYY---------FTGDGAYRT------EGGYYQITGRMDDVINISGHRLGTAEIEDA 568
Cdd:cd05906 387 -GPVVT----------------KGYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIVNGVNYYSHEIEAA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 569 IADHPAVPESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAkyAVPDEILVVKR--LPKTRSGK 642
Cdd:cd05906 450 VEEVPGVEPSFTAAFAVRDPGaeteELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLPKeeIPKTSLGK 527
|
....*....
gi 28416953 643 VMRRLLRKI 651
Cdd:cd05906 528 IQRSKLKAA 536
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
524-655 |
1.19e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.85 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 524 AYPGYYFTGD-GAYrtEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsA 602
Cdd:PRK07824 231 AEPGWFRTDDlGAL--DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG---D 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 28416953 603 GDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSE 655
Cdd:PRK07824 306 GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
117-648 |
1.68e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.90 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 117 QHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK05691 2196 AQAARTPQAPALTFAGQT------LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 197 AGFSAESLAGRINDAKCKVVITFNQGLRGgrvveLKKIVDEAVKHCPTVQHVLVAHRTDNKvhMGDLDVPLEQEmakedp 276
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEA-----LGELPAGVARWCLEDDAAALAAYSDAP--LPFLSLPQHQA------ 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 277 vcapesmgsedmlFMLYTSGSTGMPKGIVHTQAGYLLY-AALTHKlvFDHQPGDifgCVADIGWIT--GHSYVVYGPLCN 353
Cdd:PRK05691 2337 -------------YLIYTSGSTGKPKGVVVSHGEIAMHcQAVIER--FGMRADD---CELHFYSINfdAASERLLVPLLC 2398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 354 GATSVLfestpvypNAGRYWETVE--------RLKINQF---YGAPTAVRLllkygdawVKKYDRSSLRTLGSVGEPINC 422
Cdd:PRK05691 2399 GARVVL--------RAQGQWGAEEicqlireqQVSILGFtpsYGSQLAQWL--------AGQGEQLPVRMCITGGEALTG 2462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 423 EAWEWLHRVVGDSrcTLVDTWWQTETGGI---CIAPRPSEEGAEILP---AMAMRpffgiVPVLMDEKGSVVEgSNVSGA 496
Cdd:PRK05691 2463 EHLQRIRQAFAPQ--LFFNAYGPTETVVMplaCLAPEQLEEGAASVPigrVVGAR-----VAYILDADLALVP-QGATGE 2534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 497 LCISQAwpGMARtiyGDHQR-------FVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 568
Cdd:PRK05691 2535 LYVGGA--GLAQ---GYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESR 2609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 569 IADHPAVPESAVIGypHDIKGEAAFAFIVVKDSAGDSDVVVQEL----KSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 644
Cdd:PRK05691 2610 LLEHPAVREAVVLA--LDTPSGKQLAGYLVSAVAGQDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLD 2687
|
....
gi 28416953 645 RRLL 648
Cdd:PRK05691 2688 RRAL 2691
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
123-647 |
5.32e-14 |
|
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: 74.74 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGD-RVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 201
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 202 ESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcape 281
Cdd:cd17648 75 ERIQFILEDTGARVVIT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 282 smGSEDMLFMLYTSGSTGMPKGIVHTQAG-----------YLLYAALTHKL------VFDHQPGDIFgcvadIGWITGHS 344
Cdd:cd17648 92 --NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslserYFGRDNGDEAVlffsnyVFDFFVEQMT-----LALLNGQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 345 YVVYGPlcngatSVLFEStpvypnaGRYWETVERLKINQFYGAPTAVRLllkygdawvkkYD---RSSLRTLGSVGEPIN 421
Cdd:cd17648 165 LVVPPD------EMRFDP-------DRFYAYINREKVTYLSGTPSVLQQ-----------YDlarLPHLKRVDAAGEEFT 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 422 CEAWEWLHrvvGDSRCTLVDTWWQTETGGICI-APRPSEEGAE-------------ILPAmAMRPffgiVPVlmdekGSV 487
Cdd:cd17648 221 APVFEKLR---SRFAGLIINAYGPTETTVTNHkRFFPGDQRFDkslgrpvrntkcyVLND-AMKR----VPV-----GAV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 488 veGSNVSGALCISQAW---PGMARtiygdhQRFVDAYFKA--------YPGYYFTGDGAYRTEGGYYQITGRMDDVINIS 556
Cdd:cd17648 288 --GELYLGGDGVARGYlnrPELTA------ERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 557 GHRLGTAEIEDAIADHPAVPESAVI-GYPHDIKGEAAFAFIV---VKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVV 632
Cdd:cd17648 360 GQRIEPGEVEAALASYPGVRECAVVaKEDASQAQSRIQKYLVgyyLPEPGHVPE---SDLLSFLRAKLPRYMVPARLVRL 436
|
570
....*....|....*.
gi 28416953 633 KRLPKTRSGKV-MRRL 647
Cdd:cd17648 437 EGIPVTINGKLdVRAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
284-677 |
2.94e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYL-------LYAALTHKLVFDHQPGDIFgcvaDIG-WitghsYVVYGPLCNGA 355
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLnnqlskvPYLALSEADVIAQTASQSF----DISvW-----QFLAAPLFGAR 3937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 356 TSVLfestpvyPNA-----GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVkkydrSSLRTLGSVGEPINCE-AWEWLH 429
Cdd:PRK05691 3938 VEIV-------PNAiahdpQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL-----DGLRWMLPTGEAMPPElARQWLQ 4005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RVvgdSRCTLVDTWWQTETGGICIAPRPSEEGAE--ILPAMAmrPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMA 507
Cdd:PRK05691 4006 RY---PQIGLVNAYGPAECSDDVAFFRVDLASTRgsYLPIGS--PTDNNRLYLLDEALELVPLGAV-GELCV--AGTGVG 4077
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 508 RTIYGDHQR----FVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVi 581
Cdd:PRK05691 4078 RGYVGDPLRtalaFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV- 4155
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 582 GYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--- 658
Cdd:PRK05691 4156 AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSqay 4235
|
410 420
....*....|....*....|.
gi 28416953 659 LGDTTTLED--PSIIAEILSV 677
Cdd:PRK05691 4236 LAPRNELEQtlATIWADVLKV 4256
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
138-682 |
9.89e-13 |
|
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: 70.85 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 218 TFNqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGS 297
Cdd:cd17640 83 VEN---------------------------------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 298 TGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIgWitgHSY---VVYGPLCNGAtSVLFESTPVYPN------ 368
Cdd:cd17640 100 TGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAYTSIRTLKDdlkrvk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 369 ------AGRYWETVERLKINQFYGAPTAVRLLLKYgdawvkkydrssLRTLGSVGEPINCeawewlhrvvGDSRCTLVDT 442
Cdd:cd17640 174 phyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGISG----------GGALPPHVDT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 443 WWQ------------TETGGICIAPRPSeegaEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALcisqawpgMARti 510
Cdd:cd17640 232 FFEaigievlngyglTETSPVVSARRLK----CNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIV--------WVR-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 yGDHqrFVDAYFK---------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAV 580
Cdd:cd17640 298 -GPQ--VMKGYYKnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMV 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 581 IGypHDIKgeAAFAFIVvkdsaGDSDVVVQELKSmVATKIAKyaVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG 660
Cdd:cd17640 375 VG--QDQK--RLGALIV-----PNFEELEKWAKE-SGVKLAN--DRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIA 442
|
570 580
....*....|....*....|..
gi 28416953 661 DTTTLEDPSIIAEILSVYQKCK 682
Cdd:cd17640 443 PFALLEEPFIENGEMTQTMKIK 464
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
142-650 |
7.02e-12 |
|
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: 68.23 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfn 220
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKEDPVCApesmgsedmlfMLYTSGSTGM 300
Cdd:cd05937 84 ---------------------------------------------------VDPDDPAI-----------LIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 301 PKGIVHTQAGYLLYAALTHKlVFDHQPGD-IFGCVA---DIGWITGHSYVVYGPLC------------------NGATSV 358
Cdd:cd05937 102 PKAAAISWRRTLVTSNLLSH-DLNLKNGDrTYTCMPlyhGTAAFLGACNCLMSGGTlalsrkfsasqfwkdvrdSGATII 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 359 LFE--------STP------------VYPNAGR--YWETV-ERL---KINQFYGAPTAVRLLLKYG-DAWvkkydrsslr 411
Cdd:cd05937 181 QYVgelcryllSTPpspydrdhkvrvAWGNGLRpdIWERFrERFnvpEIGEFYAATEGVFALTNHNvGDF---------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 412 TLGSVGE--PInceaWEWLHRvvGDSRCTLVDT-----WWQTETGGICIAPRpsEEGAEILpamaMRPFFgivpvlmdek 484
Cdd:cd05937 251 GAGAIGHhgLI----RRWKFE--NQVVLVKMDPetddpIRDPKTGFCVRAPV--GEPGEML----GRVPF---------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 485 gsvvegSNVSgalcisqAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 564
Cdd:cd05937 309 ------KNRE-------AFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTE 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 565 IEDAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAGD-SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 640
Cdd:cd05937 376 VADVLGAHPDIAEANVYGVKvpgHD--GRAGCAAITLEESSAVpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDN 453
|
570
....*....|
gi 28416953 641 GKVMRRLLRK 650
Cdd:cd05937 454 HKQQKGVLRD 463
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
125-361 |
7.35e-12 |
|
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: 68.64 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 125 SVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAES 203
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 204 LAGRINDAKCKVVITFNQGLRGGRvvelkkivdEAVKHCPTVQHVLV-AHRTDNKVHMGDLD------------VPLEQE 270
Cdd:cd17632 132 LAPILAETEPRLLAVSAEHLDLAV---------EAVLEGGTPPRLVVfDHRPEVDAHRAALEsarerlaavgipVTTLTL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 271 MAKED------PVCAPESmgSEDMLFML-YTSGSTGMPKGIVHT--------------QAGYLLYAALTHKLVFDHQPGD 329
Cdd:cd17632 203 IAVRGrdlppaPLFRPEP--DDDPLALLiYTSGSTGTPKGAMYTerlvatfwlkvssiQDIRPPASITLNFMPMSHIAGR 280
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 28416953 330 IfgcvadigwitghsyVVYGPLCNGAT---------SVLFE 361
Cdd:cd17632 281 I---------------SLYGTLARGGTayfaaasdmSTLFD 306
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
141-331 |
1.17e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 67.83 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 QglrggrvvELKKIVDEAvKHCPTVQHVLVAHRTDNKVHMGDLDV--------PLEQEMAKEDPVcAPESMGSEDMLFML 292
Cdd:PLN02387 187 K--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGSsnwtvssfSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170 180 190
....*....|....*....|....*....|....*....
gi 28416953 293 YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF 331
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
140-650 |
1.31e-11 |
|
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: 67.38 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIfagfsaeslagrindakckvvitf 219
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 NQGLRGgrvvelkkivdEAVKHCPTV---QHVLVahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSG 296
Cdd:cd05940 59 NYNLRG-----------ESLAHCLNVssaKHLVV------------------------------------DAALYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVAdIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 376
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLP-LYHSTALIVGWSACLASGATLVIRKKF----SASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 377 --ERLKINQFYGapTAVRLLLKygdAWVKKYDRS-SLRTLgsVGEPINCEAWEWLHRVVGDSRCTlvDTWWQTEtGGICI 453
Cdd:cd05940 167 rkYQATIFQYIG--ELCRYLLN---QPPKPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPRIA--EFYAATE-GNSGF 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 454 APRPSEEGAEILPAMAMRPFFGIVPVLMD-EKGSVVEGSNvsgALCIS--QAWPGMARTIYGDHQRFvDAY--------- 521
Cdd:cd05940 237 INFFGKPGAIGRNPSLLRKVAPLALVKYDlESGEPIRDAE---GRCIKvpRGEPGLLISRINPLEPF-DGYtdpaatekk 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 522 -----FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAF 593
Cdd:cd05940 313 ilrdvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAGM 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 28416953 594 AFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 650
Cdd:cd05940 391 AAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
287-645 |
1.59e-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: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 287 DMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLFESTpvy 366
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 367 pNAGRYWETVERLKINqFYG--APTAVRLLlkygDAWVKK-YDRSSLRTLGSVGEPINCEAWEwlhrVVGDSrctlvdTW 443
Cdd:cd17637 76 -DPAEALELIEEEKVT-LMGsfPPILSNLL----DAAEKSgVDLSSLRHVLGLDAPETIQRFE----ETTGA------TF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 444 W----QTETGG-ICIAP---RPSEEGAEIlPAMAMRpffgIV-----PVLMDEKGSVVegsnVSGALCISQAWPGMARTI 510
Cdd:cd17637 140 WslygQTETSGlVTLSPyreRPGSAGRPG-PLVRVR----IVddndrPVPAGETGEIV----VRGPLVFQGYWNLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGdhqrfvdayFKAypGYYFTGDGAYRTEGGYYQITGRM--DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIK 588
Cdd:cd17637 211 YT---------FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPK 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 589 -GEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 645
Cdd:cd17637 279 wGEGIKAVCVLKPGAT---LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
286-654 |
2.89e-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: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 286 EDMLFMLYTSGSTGMPKGIVHTQagyllyaaltHKLVFDhqpgdIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV 365
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVHN-----MFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 366 YPNAGRY-------------W-ETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPIN---CEAWEW 427
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDyelCHEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 428 LHRVVGDSRCTLVDTWWQTE-TGGICIAPrpseegaeilpamAMRPFFGIV----PVLMDEKGSVVEGSNVSGALCISQA 502
Cdd:cd05908 251 HMSKYGLKRNAILPVYGLAEaSVGASLPK-------------AQSPFKTITlgrrHVTHGEPEPEVDKKDSECLTFVEVG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 503 WP---GMARTIYGDHQRFVDAYF--------KAYPGYY---------FTGDGAYRT------EGGYYQITGRMDDVINIS 556
Cdd:cd05908 318 KPideTDIRICDEDNKILPDGYIghiqirgkNVTPGYYnnpeatakvFTDDGWLKTgdlgfiRNGRLVITGREKDIIFVN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 557 GHRLGTAEIEDAIADHPAVP--ESAVIG-YPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVaTKIAKYAVpDEILVVK 633
Cdd:cd05908 398 GQNVYPHDIERIAEELEGVElgRVVACGvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHL-NKRGGWQI-NEVLPIR 475
|
410 420
....*....|....*....|.
gi 28416953 634 RLPKTRSGKVMRRLLRKIITS 654
Cdd:cd05908 476 RIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
134-654 |
5.09e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 65.79 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIY--MPV--SPLAVAAMLACARIGAVHT----VIFAGFSAESLA 205
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVWAEDTLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 206 grindakckvVItfnqGLRGGRVVELKKIVDEAVkhcPTVQHVLVAHRTdnkvhMGDLDvpleqemaKEDPVcAPESMGS 285
Cdd:PRK07768 103 ----------VI----GMIGAKAVVVGEPFLAAA---PVLEEKGIRVLT-----VADLL--------AADPI-DPVETGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 286 EDMLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVFDHQPGDIFG---CVADIGWItGHSYVvygPLCNGATSVL 359
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGN--LYAnaeAMFVAAEFDVETDVMVSwlpLFHDMGMV-GFLTV---PMYFGAELVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 360 feSTPV-YPNAGRYWETVerlkINQFYGAPTA---------VRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:PRK07768 226 --VTPMdFLRDPLLWAEL----ISKYRGTMTAapnfayallARRLRRQAKP--GAFDLSSLRFALNGAEPIDPADVEDLL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 430 RV---VGDSRCTLVDTWWQTETG-GICIAPR---------------------PSEEGAEILPAMAMRPFFGIVPVLMDEK 484
Cdd:PRK07768 298 DAgarFGLRPEAILPAYGMAEATlAVSFSPCgaglvvdevdadllaalrravPATKGNTRRLATLGPPLPGLEVRVVDED 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 485 GSV----------VEGSNVSgalcisqawPGMaRTIYGdHQRFVDAYfkaypGYYFTGDGAYRTEGGYYQITGRMDDVIN 554
Cdd:PRK07768 378 GQVlpprgvgvieLRGESVT---------PGY-LTMDG-FIPAQDAD-----GWLDTGDLGYLTEEGEVVVCGRVKDVII 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 555 ISGHRLGTAEIEDAIADHPAV-PESAV-IGYPHDIKGEaAFAfIVVKDSAGDSDVVVQELKSMVATKIAKyAV---PDEI 629
Cdd:PRK07768 442 MAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE-GFA-VAVESNAFEDPAEVRRIRHQVAHEVVA-EVgvrPRNV 518
|
570 580
....*....|....*....|....*..
gi 28416953 630 LVVK--RLPKTRSGKVMRRLLRKIITS 654
Cdd:PRK07768 519 VVLGpgSIPKTPSGKLRRANAAELVTP 545
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
136-582 |
8.20e-11 |
|
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: 64.80 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP------VSPLAVaaMLAcariGAVHTVIFAGFSAESLAGRIN 209
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 210 DAKCKVVITfnqglrgGRV---VELKKIVDEAVKHCPTVQH-VLVAHRT-DNKVHMGDldvPLEqemakEDPVCAPESMG 284
Cdd:cd05932 76 HSESKALFV-------GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 285 SedmlfMLYTSGSTGMPKGIVHTQA--GYLLYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFES 362
Cdd:cd05932 141 T-----LIYTSGTTGQPKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 363 TPVYPnagrywETVERLKINQFYGAPtavRLLLK-----YGDAWVKKYDR-------SSL--------------RTLGSV 416
Cdd:cd05932 213 LDTFV------EDVQRARPTLFFSVP---RLWTKfqqgvQDKIPQQKLNLllkipvvNSLvkrkvlkglgldqcRLAGCG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 417 GEPINCEAWEWLHRVVGDsrctLVDTWWQTETGGICIAPRP--SEEG--AEILPAMAMRpffgivpvlMDEKGSVVEGSn 492
Cdd:cd05932 284 SAPVPPALLEWYRSLGLN----ILEAYGMTENFAYSHLNYPgrDKIGtvGNAGPGVEVR---------ISEDGEILVRS- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 493 vsgalcisqawPGMARTIYGDHQRFVDAyFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIAD 571
Cdd:cd05932 350 -----------PALMMGYYKDPEATAEA-FTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAE 416
|
490
....*....|.
gi 28416953 572 HPAVPESAVIG 582
Cdd:cd05932 417 HDRVEMVCVIG 427
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
132-643 |
1.33e-10 |
|
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: 64.03 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 132 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtviFAGFSAESLAGRInda 211
Cdd:cd17654 8 IDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQRS--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 212 kckvvitfnqglrggrvveLKKIVDEAVKHCPTVQHVLVA--HRTDNKVHMgdlDVPLEQEMAkedpvcapesmgsedml 289
Cdd:cd17654 81 -------------------LTVMKKCHVSYLLQNKELDNAplSFTPEHRHF---NIRTDECLA----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 290 FMLYTSGSTGMPKG-----------IVHTQAGYLLYAA----LTHKLVFDHQPGDIFGCVADIG-WITGHSYVVYGPLCn 353
Cdd:cd17654 122 YVIHTSGTTGTPKIvavphkcilpnIQHFRSLFNITSEdilfLTSPLTFDPSVVEIFLSLSSGAtLLIVPTSVKVLPSK- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 354 gATSVLFESTPVypnagryweTVERLkinqfygAPTavrLLLKYGDAWVKKYDRS---SLRTLGSVGE--PINCEAWEWL 428
Cdd:cd17654 201 -LADILFKRHRI---------TVLQA-------TPT---LFRRFGSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 429 HRVVGDSRCTLVDTwwqTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGAL---CISQAWPG 505
Cdd:cd17654 261 GKGNRTRIFNIYGI---TEVSCWALAYKVPEEDS---PVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLnrvCILDDEVT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 506 MARTIYgdhqrfvdayfkaypgyYFTGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYph 585
Cdd:cd17654 335 VPKGTM-----------------RATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS-- 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 586 diKGEAAFAFIVVKDSagdSDVVVQELksmVATKIAKYAVPDEILVVKRLPKTRSGKV 643
Cdd:cd17654 395 --DQQRLIAFIVGESS---SSRIHKEL---QLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
141-582 |
4.14e-10 |
|
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: 62.83 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 QglrgGRVVELKKIVDEAvkhcPTVQHVLVA-------HRTDNKVHMGDLdVPLEQEMAKEDPVCAPESMGS---EDMLF 290
Cdd:cd17641 92 E----EQVDKLLEIADRI----PSVRYVIYCdprgmrkYDDPRLISFEDV-VALGRALDRRDPGLYEREVAAgkgEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 291 MLYTSGSTGMPKGIVhTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG--------ATSVLFES 362
Cdd:cd17641 163 LCTTSGTTGKPKLAM-LSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeePETMMEDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 363 TPVYPN----AGRYWETV---------ERLKINQFY-----------------GAPTAVRLLLKYG--DAWVKK--YDR- 407
Cdd:cd17641 242 REIGPTfvllPPRVWEGIaadvrarmmDATPFKRFMfelgmklglraldrgkrGRPVSLWLRLASWlaDALLFRplRDRl 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 408 --SSLRTLGSVGEPINCEAWEWLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPAMAMRPFFGiVPVLMDEKG 485
Cdd:cd17641 322 gfSRLRSAATGGAALGPDTFRFFHAIGVP----LKQLYGQTELAGAYTVHR----DGDVDPDTVGVPFPG-TEVRIDEVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 486 SVVEGSnvsgalcisqawPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAE 564
Cdd:cd17641 393 EILVRS------------PGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQF 458
|
490
....*....|....*...
gi 28416953 565 IEDAIADHPAVPESAVIG 582
Cdd:cd17641 459 IENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
529-643 |
1.15e-09 |
|
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: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 529 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDIKGEAAFA 594
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSYivPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 595 FIVVKDSAGDSDVVV----------QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 643
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
115-648 |
1.83e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.68 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIG----- 189
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYL------GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 190 -AVHTvifagfSAESLAGRINDAKCKVVITfnqglrggrVVELkkivDEAVKHCPTVQhvlvahrTDNkvhmgdldvpLE 268
Cdd:PRK04813 82 vDVSS------PAERIEMIIEVAKPSLIIA---------TEEL----PLEILGIPVIT-------LDE----------LK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 269 QEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-------ALTHKLVFDHQPGDIFG-CVADIgwi 340
Cdd:PRK04813 126 DIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTnwmledfALPEGPQFLNQAPYSFDlSVMDL--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 341 tghsyvvYGPLCNGATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVR--LLLKYGDAwvKKYdrSSLRTLGSVGE 418
Cdd:PRK04813 203 -------YPTLASGGTLVALPKD-MTANFKQLFETLPQLPINVWVSTPSFADmcLLDPSFNE--EHL--PNLTHFLFCGE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 419 PINCEAWEWLHRVVGDSRctLVDTWWQTETggiCIAPRPSEEGAEI------LPAMAMRPFFGIVpvLMDEKGSVVEGSN 492
Cdd:PRK04813 271 ELPHKTAKKLLERFPSAT--IYNTYGPTEA---TVAVTSIEITDEMldqykrLPIGYAKPDSPLL--IIDEEGTKLPDGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 493 vSGALCISQawPGMARTIYGDHQRfVDAYFKAYPGY--YFTGDGAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 570
Cdd:PRK04813 344 -QGEIVISG--PSVSKGYLNNPEK-TAEAFFTFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLR 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 571 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDV-VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 648
Cdd:PRK04813 419 QSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
112-360 |
7.08e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 59.22 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 112 VNCLDQHVRKSPESVALIWER---DEPgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 188
Cdd:PTZ00216 93 VERVEKEVVKDADGKERTMEVthfNET---RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 189 GAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglRGGRVVELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDVPLE 268
Cdd:PTZ00216 170 SMVAATVYANLGEDALAYALRETECKAIVC-----NGKNVPNLLRLMKSGGMPNTTI------------IYLDSLPASVD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 269 QE----MAKEDPVCAPESMGS----------EDMLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVfdhqpgDIF 331
Cdd:PTZ00216 233 TEgcrlVAWTDVVAKGHSAGShhplnipennDDLALIMYTSGTTGDPKGVMHTHGS--LTAgilALEDRLN------DLI 304
|
250 260 270
....*....|....*....|....*....|...
gi 28416953 332 GCVADigwitGHSYVVYGPLCN----GATSVLF 360
Cdd:PTZ00216 305 GPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
142-657 |
7.84e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.95 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 142 TYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQ 221
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKYSV-EGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 222 GLRGGRVVELKKIVDEAvkhcptvqhvlvahrtdNKVHMGDL--DVPLEQEMAKEDPVCAPE----SMGSEDMLFMLYTS 295
Cdd:PRK08043 312 FLDKGKLWHLPEQLTQV-----------------RWVYLEDLkdDVTTADKLWIFAHLLMPRlaqvKQQPEDAALILFTS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 296 GSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfestpvYPNAGRYwET 375
Cdd:PRK08043 375 GSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL------YPSPLHY-RI 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 376 VERLKINQ----FYGAPTavrLLLKYGdAWVKKYDRSSLRTLGSVGEPINceawewlhrvvgDSRCTLvdtwWQTETG-- 449
Cdd:PRK08043 447 VPELVYDRnctvLFGTST---FLGNYA-RFANPYDFARLRYVVAGAEKLQ------------ESTKQL----WQDKFGlr 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 450 -----GI--C---------IAPRPSEEGaEILPAMAMRpffgIVPVLMDEKGSVVE--GSNV-SGALCISQawPGMARTI 510
Cdd:PRK08043 507 ilegyGVteCapvvsinvpMAAKPGTVG-RILPGMDAR----LLSVPGIEQGGRLQlkGPNImNGYLRVEK--PGVLEVP 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 511 YGDhqrfvDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVIgYPHDIKG 589
Cdd:PRK08043 580 TAE-----NARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKG 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416953 590 EAAFAFivVKDSAGDSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 657
Cdd:PRK08043 654 EALVLF--TTDSELTREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
140-336 |
9.44e-09 |
|
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: 58.46 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 219 fnqglrggrVVELKKIVDEAvkhCPTVQ----HVLVAHRTDNKVHMGDLDVPLEQemAKEDPVcaPESMGSE----DMLF 290
Cdd:cd05938 85 ---------APELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVISLLDKVDA--ASDEPV--PASLRAHvtikSPAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 28416953 291 MLYTSGSTGMPKGIVHTQAGYLLYAALTHklvfdhqpgdIFGCVAD 336
Cdd:cd05938 149 YIYTSGTTGLPKAARISHLRVLQCSGFLS----------LCGVTAD 184
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
529-643 |
2.16e-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: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 529 YFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDiKGEAAF 593
Cdd:TIGR03443 680 YRTGDlGRY-LPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENvtlvrrdkdeepTLVSYivPQD-KSDELE 757
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 594 AFIVVKDSAGDSDVVVQ----------ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 643
Cdd:TIGR03443 758 EFKSEVDDEESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
114-308 |
5.77e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.04 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 114 CLDQHVRKSPESVALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSP----LAVAAMLACARIG 189
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 190 AVHtvifagfSAESLAGRiNDAKCKVVItfnQGLRGGRVvelkkIVDEAVKHCPTVQHVLVAHR---TDNKVHMGDLDVP 266
Cdd:PRK08180 123 PVS-------PAYSLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAATP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 28416953 267 LEQEMAKEDPVCAPESM---GSEDMLFMLYTSGSTGMPKGIVHTQ 308
Cdd:PRK08180 187 FAALLATPPTAAVDAAHaavGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
141-307 |
3.38e-07 |
|
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: 53.37 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfn 220
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 221 qglrggrvvelkkivdeavkhcptvqhvlvahrTDNKvhmgdldvpleqemaKEDPVCapesmgsedmlfMLYTSGSTGM 300
Cdd:cd17639 83 ---------------------------------TDGK---------------PDDLAC------------IMYTSGSTGN 102
|
....*..
gi 28416953 301 PKGIVHT 307
Cdd:cd17639 103 PKGVMLT 109
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
114-659 |
3.64e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 53.26 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 114 CLDQ-HVRKSPESVALIWERdepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PLN02860 12 CLTRlATLRGNAVVTISGNR-------RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 193 TVIFAGFSAEslagrinDAKCKVVITfnqglrggRVVELkkIVDEAVKH---------CPTVQ-HVLVAHRTDNKVHmGD 262
Cdd:PLN02860 85 APLNYRWSFE-------EAKSAMLLV--------RPVML--VTDETCSSwyeelqndrLPSLMwQVFLESPSSSVFI-FL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 263 LDVpLEQEMAKE--------DPVCAPEsmgseDMLFMLYTSGSTGMPKG--IVHTqagyllyAALTHKLvfdhqpgdifG 332
Cdd:PLN02860 147 NSF-LTTEMLKQralgttelDYAWAPD-----DAVLICFTSGTTGRPKGvtISHS-------ALIVQSL----------A 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 333 CVADIGWITGHSYVVYGPLCN-------------GATSVL---FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLK 396
Cdd:PLN02860 204 KIAIVGYGEDDVYLHTAPLCHigglssalamlmvGACHVLlpkFDAKAAL-------QAIKQHNVTSMITVPAMMADLIS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 397 YGDAWVKKYDRSSLRTLGSVGEPINCEAWEwlhrvvgdsrctlvdtwwqtetGGICIAPRpseegAEILPAMAM------ 470
Cdd:PLN02860 277 LTRKSMTWKVFPSVRKILNGGGSLSSRLLP----------------------DAKKLFPN-----AKLFSAYGMteacss 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 471 -------RPFFGIVPVLMDEKGSVVEGSN-VSGALCISQAWPGMARTIY-------------GDH-------QRFVDAYF 522
Cdd:PLN02860 330 ltfmtlhDPTLESPKQTLQTVNQTKSSSVhQPQGVCVGKPAPHVELKIGldessrvgriltrGPHvmlgywgQNSETASV 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 523 KAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD-- 600
Cdd:PLN02860 410 LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgw 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 601 --------SAGDSDVVVQE-LKSMVATK-IAKYAVPDEILV-VKRLPKTRSGKVMRRLLRKIITSEAQEL 659
Cdd:PLN02860 490 iwsdnekeNAKKNLTLSSEtLRHHCREKnLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRREVLSHLQSL 559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-304 |
4.12e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 112 VNCLDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHrGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 192 HTVIFAGFSA-----ESLAGRINDAKCKVVITfNQGLRGGrvveLKKIVDEAVKHCPTVQHVlvahrtdnkvhmGDLDVP 266
Cdd:PRK05691 91 AVPAYPPESArrhhqERLLSIIADAEPRLLLT-VADLRDS----LLQMEELAAANAPELLCV------------DTLDPA 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 28416953 267 LEQEMAKedPVCAPesmgsEDMLFMLYTSGSTGMPKGI 304
Cdd:PRK05691 154 LAEAWQE--PALQP-----DDIAFLQYTSGSTALPKGV 184
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
136-388 |
1.18e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 51.77 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAkcKV 215
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA--EV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 216 VITFnqglrggrvVELKKI--VDEAVKHCPTVQHVLVAhrtdnkvhMGDLDVPLEQEMAKEDPVCAP----ESMGS---- 285
Cdd:PLN02861 151 SIAF---------VQESKIssILSCLPKCSSNLKTIVS--------FGDVSSEQKEEAEELGVSCFSweefSLMGSldce 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 286 ------EDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFdhqpgdifgcVADIGWITGHSYVVYGPLCNGATSVL 359
Cdd:PLN02861 214 lppkqkTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLAHVYDQVI 283
|
250 260 270
....*....|....*....|....*....|....*...
gi 28416953 360 fESTPVYPNAG-RYW--------ETVERLKINQFYGAP 388
Cdd:PLN02861 284 -ETYCISKGASiGFWqgdirylmEDVQALKPTIFCGVP 320
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
289-643 |
1.22e-06 |
|
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: 51.15 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 289 LFMLYTSGSTGMPKGIVHTQAGyLLYAALTHklvfdhqpgdifgcvADIGWITGHS-YVVYGPLCNGATsvLFESTPVYP 367
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQA-LLAQALVL---------------AVLQAIDEGTvFLNSGPLFHIGT--LMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 368 NAGR-----------YWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSvgepinceAWEWLHRVVGDsr 436
Cdd:cd17636 65 AGGTnvfvrrvdaeeVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSSPA--------APEWNDMATVD-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 437 ctlvDTWW--------QTETGG-----------ICIAPRPSeegaeilPAMAMRpffgivpvLMDEKGSVVEGSNVsGAL 497
Cdd:cd17636 133 ----TSPWgrkpggygQTEVMGlatfaalgggaIGGAGRPS-------PLVQVR--------ILDEDGREVPDGEV-GEI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 498 CIsQAWPGMARtiYGDH-----QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 572
Cdd:cd17636 193 VA-RGPTVMAG--YWNRpevnaRRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQH 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28416953 573 PAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 643
Cdd:cd17636 263 PAVADAAVIGVPDPRWAQSVKAIVVLKPGAS---VTEAELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
140-582 |
1.34e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 51.31 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItf 219
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 220 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdlDVPLEQEMAKedpvcapesmgsedmlfMLYTSGSTG 299
Cdd:cd05910 80 --------------------------------------------GIPKADEPAA-----------------ILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 300 MPKGIVHTQAgylLYAALTHKL--VFDHQPGDI----FGCVAdigwitghsyvVYGPLCnGATSVLFESTPVYP---NAG 370
Cdd:cd05910 99 TPKGVVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 371 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD---------------- 434
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSDeaeiltpygatealpv 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 435 ----SRCTLVDTWWQTETG-GICIAPRPSEEGAEILPAMA--MRPFFGIVPVLMDEKGSVVegsnVSGalcisqawPGMA 507
Cdd:cd05910 242 ssigSRELLATTTAATSGGaGTCVGRPIPGVRVRIIEIDDepIAEWDDTLELPRGEIGEIT----VTG--------PTVT 309
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 508 RTIYGDHQrfVDAYFKAYPG----YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 582
Cdd:cd05910 310 PTYVNRPV--ATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
122-312 |
1.48e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 51.03 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 122 SPESVALIwERDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtVIFagfsa 201
Cdd:PRK09029 16 RPQAIALR-LNDE-----VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR--VLP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 202 eslagrINDAkckvvitFNQGLRGGRVVELkkivdeavkhcpTVQHVLVAHRTDNkvhMGDLDVPLEQEMAKEDPVC-AP 280
Cdd:PRK09029 83 ------LNPQ-------LPQPLLEELLPSL------------TLDFALVLEGENT---FSALTSLHLQLVEGAHAVAwQP 134
|
170 180 190
....*....|....*....|....*....|..
gi 28416953 281 ESMGSedmlfMLYTSGSTGMPKGIVHTQAGYL 312
Cdd:PRK09029 135 QRLAT-----MTLTSGSTGLPKAAVHTAQAHL 161
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
108-307 |
2.10e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 50.97 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 108 LNVSVNCLDQHVRKSPESVALIWER--DEP-GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLA 184
Cdd:PLN02430 41 ITTAWDIFSKSVEKYPDNKMLGWRRivDGKvGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 185 CARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRG------GRVVELKKIV-----DEAVKHcPTVQHVLVAHR 253
Cdd:PLN02430 121 CAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEllepdcKSAKRLKAIVsftsvTEEESD-KASQIGVKTYS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28416953 254 TDNKVHMGdldvpleqemaKEDP--VCAPESMgseDMLFMLYTSGSTGMPKGIVHT 307
Cdd:PLN02430 200 WIDFLHMG-----------KENPseTNPPKPL---DICTIMYTSGTSGDPKGVVLT 241
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
134-305 |
2.23e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.79 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 213
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 214 KVVITFNQglrggRVVELKKIVDEAVKHCPTVQHV---------------LVAHRTDNKVHMGD---LDVPLEQEmaked 275
Cdd:PLN02614 153 SIVFVEEK-----KISELFKTCPNSTEYMKTVVSFggvsreqkeeaetfgLVIYAWDEFLKLGEgkqYDLPIKKK----- 222
|
170 180 190
....*....|....*....|....*....|
gi 28416953 276 pvcapesmgsEDMLFMLYTSGSTGMPKGIV 305
Cdd:PLN02614 223 ----------SDICTIMYTSGTTGDPKGVM 242
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
143-308 |
3.96e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 50.00 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 143 YRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT-----VIFAGFSA--ESLAGRINDAKCKV 215
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 216 VITfnqglrggrVVELKKIVDEAVKHCPTVqhvlvahrtdnkvhmgdLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTS 295
Cdd:PRK09192 132 IIT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSS 185
|
170
....*....|...
gi 28416953 296 GSTGMPKGIVHTQ 308
Cdd:PRK09192 186 GSTRFPRGVIITH 198
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
527-659 |
7.29e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 49.54 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 527 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIadHPAVPES----AVIGYPHDIKGEAafafIVV--KD 600
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEK----LVVlhTC 1092
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 28416953 601 SAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitseAQEL 659
Cdd:PRK08633 1093 GAEDVEELKRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL----ALAL 1144
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
115-310 |
9.38e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.97 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 115 LDQHVRKSPESVA---LIWERDEPGTEVRITYRELLETTCRLANTLKRHgVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK12476 40 IERNIANVGDTVAyryLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 192 HTVIFA----GfSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKhcPTVQHVLVAHRTDNKVHMGDLD-VP 266
Cdd:PRK12476 119 AVPLFApelpG-HAERLDTALRDAEPTVVLT-----------------TTAAA--EAVEGFLRNLPRLRRPRVIAIDaIP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 28416953 267 leqEMAKEDPVCAPesMGSEDMLFMLYTSGSTGMPKG--IVHTQAG 310
Cdd:PRK12476 179 ---DSAGESFVPVE--LDTDDVSHLQYTSGSTRPPVGveITHRAVG 219
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
565-675 |
3.04e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 46.68 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 565 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIvvkdsAGDSDVVVQELKSMVATKIAKYAvPDEILVVKRLPKTRSGKVM 644
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|..
gi 28416953 645 RRLLRKIITSEAQELGD-TTTLEDPSIIAEIL 675
Cdd:PRK09188 319 DDILRLIAMNQIDELDDlLREPEIRGLVEAIA 350
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
526-647 |
5.28e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 46.30 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 526 PGYYF-TGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAG- 603
Cdd:PRK05851 394 PDDWFpTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG-EGSARPGLVIAAEFRGp 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 28416953 604 DSDVVVQELKSMVATKIAkyAVPDEILVVK--RLPKTRSGKvMRRL 647
Cdd:PRK05851 472 DEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
140-658 |
7.75e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.11 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 140 RITYRELLETTCRLANTLKrHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIfaGFSAeSLAGRIND---AKCKVV 216
Cdd:PRK06814 658 PLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSA-GIANILSAckaAQVKTV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 217 ITFNQGLRGGRvveLKKIVDEavkhcpTVQHVLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSEDMLFMLYTSG 296
Cdd:PRK06814 734 LTSRAFIEKAR---LGPLIEA------LEFGIRIIYLEDVRAQIGLAD-KIKGLLAGRFPLVYFCNRDPDDPAVILFTSG 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 297 STGMPKGIVHTQAGYLLYAALTHKLVfDHQPGDIFGCVADIGwitgHSYVVYG----PLCNGATSVLfestpvYPNAGRY 372
Cdd:PRK06814 804 SEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPVF----HSFGLTGglvlPLLSGVKVFL------YPSPLHY 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 373 W---ETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE-WLHRVvgdsRCTLVDTWWQTET 448
Cdd:PRK06814 873 RiipELIYDTNATILFGTDTFLNGYARYAHP----YDFRSLRYVFAGAEKVKEETRQtWMEKF----GIRILEGYGVTET 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 449 GGI--CIAP---RPSEEGaEILPAMAMR--PFFGIvpvlmDEKGSV-VEGSNV-SGALCISQawPGMARTIYGdhqrfvd 519
Cdd:PRK06814 945 APViaLNTPmhnKAGTVG-RLLPGIEYRlePVPGI-----DEGGRLfVRGPNVmLGYLRAEN--PGVLEPPAD------- 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416953 520 ayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAafaFIVVK 599
Cdd:PRK06814 1010 -------GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER---IILLT 1079
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28416953 600 DSAgdsDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKV----MRRLLRKIITSEAQE 658
Cdd:PRK06814 1080 TAS---DATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEAA 1140
|
|
| |
