|
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 ... |
54-674 |
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: 1097.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 54 QPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTgKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERD 133
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWEGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 213
Cdd:TIGR02188 82 EPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 214 KVVITFNQGLRGGRVVELKKIVDEAVKHCP-TVQHVLVAHRTDNKV-HMGD-LDVPLEQEMAKEDPVCAPESMGSEDMLF 290
Cdd:TIGR02188 162 KLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVEgRDVWWHDLMAKASAYCEPEPMDSEDPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 291 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAG 370
Cdd:TIGR02188 242 ILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 371 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQ--TGG 448
Cdd:TIGR02188 322 RFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQteTGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 449 ICIAPRPSeeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYF 528
Cdd:TIGR02188 402 IMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 529 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQ 608
Cdd:TIGR02188 480 TGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248205 609 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 674
Cdd:TIGR02188 560 ELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIE 625
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
57-665 |
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: 1085.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 57 SYPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPG 136
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 217 ITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHM-GDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTS 295
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 296 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWET 375
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 376 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQT--GGICIAP 453
Cdd:cd05966 321 VEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTetGGIMITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 454 RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 533
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNEVEG-EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 534 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 613
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 358248205 614 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLED 665
Cdd:cd05966 558 VRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEE-ELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
58-680 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 972.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 58 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDfsTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPGT 137
Cdd:PRK00174 19 YKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIWEGDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 TFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGD-LDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSG 296
Cdd:PRK00174 176 TADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEgRDLWWHELVAGASDECEPEPMDAEDPLFILYTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETV 376
Cdd:PRK00174 256 STGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 377 ERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQT--GGICIAPR 454
Cdd:PRK00174 336 DKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTetGGIMITPL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 455 PseeGA-EILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 533
Cdd:PRK00174 416 P---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEG-GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGA 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 534 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 613
Cdd:PRK00174 492 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNW 571
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 614 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLEDPSIIAEILSVYQKCK 680
Cdd:PRK00174 572 VRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEARQNRK 637
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
102-672 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 820.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 102 WFLGGQLNVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAA 181
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 182 MLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMG 261
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 262 DlDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWIT 341
Cdd:COG0365 161 G-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 342 GHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN 421
Cdd:COG0365 240 GHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 CEAWEWLHRVVGdsrCTLVDTWWQT--GGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQ 499
Cdd:COG0365 320 PEVWEWWYEAVG---VPIVDGWGQTetGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 579
Cdd:COG0365 393 PWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 580 GYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGD 659
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA--EGRPLGD 550
|
570
....*....|...
gi 358248205 660 TTTLEDPSIIAEI 672
Cdd:COG0365 551 TSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
55-675 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 658.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 55 PGSYPALSAQAAREPAAFWGPLArDTLVWDTPYHTVWDC----DFSTG--KIGWFLGGQLNVSVNCLDQHVRK-SPESVA 127
Cdd:PLN02654 29 PQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCLDRNVEAgNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 128 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGR 207
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 208 INDAKCKVVITFNQGLRGGRVVELKKIVDEA----------VKHCPTVQHVLVAHRTDNKVHMGDlDVPLEQEMAKEDPV 277
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-DVWWQDVVPNYPTK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 278 CAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATS 357
Cdd:PLN02654 267 CEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 358 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRC 437
Cdd:PLN02654 347 LVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRC 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 438 TLVDTWWQ--TGGICIAPRPseeGAEIL-PAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAWPGMARTIYGDHQR 514
Cdd:PLN02654 427 PISDTWWQteTGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSWPGAFRTLYGDHER 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 515 FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 594
Cdd:PLN02654 503 YETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFV 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 595 VVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 674
Cdd:PLN02654 583 TLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIA 662
|
.
gi 358248205 675 V 675
Cdd:PLN02654 663 L 663
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
64-642 |
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: 636.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 64 QAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEpGTEVR- 140
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 QGLRGGRVVELKKIVDEAVK-HCPTVQHVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGST 298
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 299 GMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVER 378
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 379 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQT--GGICIAPRPs 456
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTetGGFMITPLP- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 457 eeGAEILPA-MAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYR 535
Cdd:cd17634 404 --GAIELKAgSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 536 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVA 615
Cdd:cd17634 481 DEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
570 580
....*....|....*....|....*..
gi 358248205 616 TKIAKYAVPDEILVVKRLPKTRSGKVM 642
Cdd:cd17634 561 KEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
58-672 |
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: 568.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 58 YPALSAQAAREPAAFWGPLARdTLVWDTPYHTVWDCDfSTGKIGWFLGGQLNVSVNCLDQHVRKS-PESVALIWERDEPG 136
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 217 ITFNQGLRGGRVVELKKIVDEAVK---HCPtvQHVLVAHRTDNKVHMGD--LDVPLEQEMAKEDPV-CAPesMGSEDMLF 290
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALElsgHKP--HHVLVLNRPQVPADLTKpgRDLDWSELLAKAEPVdCVP--VAATDPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 291 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV-YPNA 369
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 370 GRYWETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT- 446
Cdd:cd05967 315 GAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTe 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 447 -------GGICIAPRPSEEGAEILPAMAMRpffgiVPVLmDEKGSVVeGSNVSGALCISQAW-PGMARTIYGDHQRFVDA 518
Cdd:cd05967 392 tgwpitaNPVGLEPLPIKAGSPGKPVPGYQ-----VQVL-DEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 519 YFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD 598
Cdd:cd05967 465 YLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKE 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 599 SAG-DSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTLEDPSIIAEI 672
Cdd:cd05967 545 GVKiTAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
57-672 |
9.49e-179 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 522.97 E-value: 9.49e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 57 SYPALSAQAAREPAAFWGPLARdtLV-WDTPYHTVwdCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVALIWERDE 134
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR--RIdWQTPFTQV--LDYSNPPFArWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 135 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 214
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 215 VVITFNQGLRGGRVVELKKIVDEAV---KHCPtvQHVLVAHR-TDNKVHMGDLDVPLEQEMAK-EDPVCAPESMGSEDML 289
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVDRgLAPMARVAGRDVDYATLRAQhLGARVPVEWLESNEPS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 290 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNA 369
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 370 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQT--G 447
Cdd:PRK10524 317 GIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP---VIDNYWQTetG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 448 GICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAY-PG 525
Cdd:PRK10524 394 WPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 526 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD- 604
Cdd:PRK10524 474 VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADr 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 605 ----VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitSEAQELGDTTTLEDPSIIAEI 672
Cdd:PRK10524 554 earlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI--AEGRDPGDLTTIEDPAALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
56-666 |
6.43e-176 |
|
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: 515.12 E-value: 6.43e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 56 GSYPALSAQAAREPAAFWGPLARDTLVW--DTPYHTVwdcDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWE 131
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIEwyEPPYQTL---DLSGGKpwAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 132 rDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDA 211
Cdd:cd05968 84 -GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 212 KCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSEDMLFM 291
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGR-DLSYDEEKETAGDGAERTESEDPLMI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 292 LYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGR 371
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 372 YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQT---GG 448
Cdd:cd05968 321 LWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTeisGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 449 I--CIAPRPseegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGY 526
Cdd:cd05968 401 IlgNVLIKP------IKPSSFNGPVPGMKADVLDESGKPARPE--VGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 527 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVV 606
Cdd:cd05968 473 WVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEAL 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 607 VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEaqELGDTTTLEDP 666
Cdd:cd05968 553 AEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
102-665 |
1.93e-146 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 438.17 E-value: 1.93e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 102 WFLGGQLNVSVNCLDQHVrKSP--ESVALIWERdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAV 179
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 180 AAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRggrvvelKKIVDEavkhCPTVQHVLVahrTDNKVH 259
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD----LPSLKHVLL---VGEDVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 260 MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQagyllYAALTH----KLVFDHQPGDIFGCVA 335
Cdd:PRK04319 179 EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NAMLQHyqtgKYVLDLHEDDVYWCTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 336 DIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 415
Cdd:PRK04319 254 DPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 416 VGEPINCEAWEWLHRVVGdsrCTLVDTWWQ--TGGICIAPRPSEEgaeILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSG 493
Cdd:PRK04319 331 VGEPLNPEVVRWGMKVFG---LPIHDNWWMteTGGIMIANYPAMD---IKPGSMGKPLPGIEAAIVDDQGNELP-PNRMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 494 ALCISQAWPGMARTIYGDHQRFvDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 573
Cdd:PRK04319 404 NLAIKKGWPSMMRGIWNNPEKY-ESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 574 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRkiitse 653
Cdd:PRK04319 481 AEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK------ 554
|
570
....*....|....*.
gi 358248205 654 AQEL----GDTTTLED 665
Cdd:PRK04319 555 AWELglpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
142-649 |
3.74e-125 |
|
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: 378.77 E-value: 3.74e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 222 glrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvplEQEMAkedpvcapESMGSEDMLFMLYTSGSTGMP 301
Cdd:cd05969 79 ----------------------------------------------TEELY--------ERTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 302 KGIVHTQAGYLLYAaLTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKI 381
Cdd:cd05969 105 KGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 382 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT--GGICIAPRPseeG 459
Cdd:cd05969 181 TVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTetGSIMIANYP---C 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 460 AEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRFvDAYFKAypGYYFTGDGAYRTEGG 539
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELP-PGTKGILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 540 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 619
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLG 410
|
490 500 510
....*....|....*....|....*....|
gi 358248205 620 KYAVPDEILVVKRLPKTRSGKVMRRLLRKI 649
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
142-648 |
1.38e-106 |
|
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: 330.45 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 222 glrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMP 301
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 302 KGIVHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNagRYWETVERLKI 381
Cdd:cd05972 97 KGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 382 NQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT-GGICIAPRPseeGA 460
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTeTGLTVGNFP---DM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 461 EILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGY 540
Cdd:cd05972 245 PVKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTGDRAYRDEDGY 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 541 YQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAK 620
Cdd:cd05972 321 FWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAP 400
|
490 500
....*....|....*....|....*...
gi 358248205 621 YAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05972 401 YKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
115-554 |
4.86e-100 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 313.09 E-value: 4.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHRTDnkvhMGDLDVPLEQEMAKE 274
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITD--------DALKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQ----PGDIFGCVADIGWITGHSYVVYGP 350
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHR 430
Cdd:pfam00501 223 LLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 431 VVGdsrCTLVDTWWQT-GGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIY 509
Cdd:pfam00501 300 LFG---GALVNGYGLTeTTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGYL 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 358248205 510 GDHQRFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINIS 554
Cdd:pfam00501 375 NDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
115-656 |
3.24e-95 |
|
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: 301.73 E-value: 3.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemake 274
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 dpvcapesmgsedmlFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG 354
Cdd:COG0318 104 ---------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 355 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGd 434
Cdd:COG0318 168 ATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 435 srCTLVDTWWQT---GGICIAPrpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD 511
Cdd:COG0318 241 --VRIVEGYGLTetsPVVTVNP---EDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPGEVGEIVVRG--PNVMKGYWND 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 512 ----HQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 587
Cdd:COG0318 313 peatAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWG 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 588 EAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 656
Cdd:COG0318 386 ERVVAFVVLRP---GAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
56-650 |
2.35e-81 |
|
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: 270.30 E-value: 2.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 56 GSYPALSAQAAREPAAFWgplardTLVWD---TPYHTVWDCDFSTGKI----GWFLGGQLNVSVNCLdQHvRKSPESVAL 128
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLL-RH-ADADDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 129 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 209 NDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVP----LEQEMAKE-DPVCAPESM 283
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVvyGPLCNGATSVLFEST 363
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 364 PVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTW 443
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 444 WQ--TGG--IC--------IAP-RPSEEGAEILpAMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMARTIYG 510
Cdd:cd05943 399 LAsiSGGtdIIscfvggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 511 DH--QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 588
Cdd:cd05943 468 DPdgSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDE 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 589 AAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 650
Cdd:cd05943 548 RVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII 609
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
54-678 |
5.87e-77 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 259.29 E-value: 5.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 54 QPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVwdcdFSTGKI--GWFLGGQLNVSVNCLDQHVrKSP---ESVAL 128
Cdd:PTZ00237 6 DPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKV----YSGDEIypDWFKGGELNTCYNVLDIHV-KNPlkrDQDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 129 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:PTZ00237 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 209 NDAKCKVVITFNQGLRGGRVVELKKIVDEAV---KHCPTvqHVLVAHRTD-----NKVHMGD-------LDVPLEQEMAK 273
Cdd:PTZ00237 161 ETITPKLIITTNYGILNDEIITFTPNLKEAIelsTFKPS--NVITLFRNDitsesDLKKIETiptipntLSWYDEIKKIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 ED---PVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYvVYGP 350
Cdd:PTZ00237 239 ENnqsPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF-LYGS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCNGATSVLFESTPVYPNAGR--YWETVERLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPINCEAW 425
Cdd:PTZ00237 318 LSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 426 EWLHRVVGdSRCTLVdtWWQT-GGIC------IAPRPSEegAEILPAmamrPFfgIVPVLMDEKGSVVeGSNVSGALCIS 498
Cdd:PTZ00237 398 EYIENKLK-IKSSRG--YGQTeIGITylycygHINIPYN--ATGVPS----IF--IKPSILSEDGKEL-NVNEIGEVAFK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 499 QAW-PGMARTIYGDHQRFvDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 577
Cdd:PTZ00237 466 LPMpPSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 578 VIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS----MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSE 653
Cdd:PTZ00237 545 SIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDS 624
|
650 660
....*....|....*....|....*
gi 358248205 654 AQELGDTTtlEDPSIIAEILSVYQK 678
Cdd:PTZ00237 625 NYQLPDNV--NDSEIFYKIKELYMK 647
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
56-646 |
1.21e-76 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 258.57 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 56 GSYPALSAQAAREPAAFWgplardTLVWD-------TPYHTVWDcdfSTGKIG--WFLGGQLNVSVNCLDQHvrkSPESV 126
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 127 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAG 206
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 207 RINDAKCKVVITFNqGLR-GGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLD--VPLEQEMAK-EDPVCAPES 282
Cdd:PRK03584 181 RFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF----GCvadiGWITgHSYVVYGPLCnGATSV 358
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 359 LFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrct 438
Cdd:PRK03584 334 LYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA---- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 439 lvDTWW--QTGG--IC---IAprpseeGAEILP-----------AMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQA 500
Cdd:PRK03584 410 --DVWLasISGGtdICscfVG------GNPLLPvyrgeiqcrglGMAVEAW--------DEDGRPVVG--EVGELVCTKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 WPGMArtIY----GDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 576
Cdd:PRK03584 472 FPSMP--LGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDS 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 577 AVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM----RRLL 646
Cdd:PRK03584 550 LVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
287-642 |
1.70e-75 |
|
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: 246.04 E-value: 1.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 287 DMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHqPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFEStpvy 366
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-EGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 367 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT 446
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 447 --GGICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDayfkaYP 524
Cdd:cd04433 150 etGGTVATGPPDDD--ARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVD-----ED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 525 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 604
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---D 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 358248205 605 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 642
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
107-647 |
3.11e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 235.08 E-value: 3.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 107 QLNVSvNCLDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACA 186
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 187 RIGAV-HTV-IFagFSAESLAGRINDAKCKVVItFNQglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKVHmGDLD 264
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS--------EFVPLLAAILPQLPTVRTVIVEGDGPAAPL-APEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 265 VPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTqagyllyaaltHKLVFDHqpgdIFGCVADIGWITGHS 344
Cdd:PRK06187 146 GEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS-----------HRNLFLH----SLAVCAWLKLSRDDV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 345 YVV-------------YGPLCNGATSVL---FESTPVypnagryWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRS 408
Cdd:PRK06187 211 YLVivpmfhvhawglpYLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 409 SLRTLGSVGEPIN---CEAWEWLHRvvgdsrCTLVDTWW--QTGGICIAPRPSEEGAEILPAM--AMRPFFGIVPVLMDE 481
Cdd:PRK06187 282 SLRLVIYGGAALPpalLREFKEKFG------IDLVQGYGmtETSPVVSVLPPEDQLPGQWTKRrsAGRPLPGVEARIVDD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 482 KGSVVEGSNVS-GALCISQAWpgMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGT 560
Cdd:PRK06187 356 DGDELPPDGGEvGEIIVRGPW--LMQGYWNRPEATAETI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 561 AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 640
Cdd:PRK06187 431 RELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP---GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGK 507
|
....*..
gi 358248205 641 VMRRLLR 647
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 ... |
109-647 |
1.13e-68 |
|
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: 233.93 E-value: 1.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 109 NVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 188
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWC-DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 189 GAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGlrggrvvELKKIVDEAVKHCPTVQhVLVahrtdnKVHMGDLD--VP 266
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECPSKP-KLV------WVGDPVPEgwID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 267 LEQEMAKEDPV----CAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITG 342
Cdd:cd05970 162 FRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 343 HSYVVYGPLCNGATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINC 422
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 423 EAWEWLHRVVGDSrctLVDTWWQT-GGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNvSGALCI--SQ 499
Cdd:cd05970 316 EVFNTFKEKTGIK---LMEGFGQTeTTLTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtSK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWP-GMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 578
Cdd:cd05970 389 GKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 579 IGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05970 466 TGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
141-648 |
2.49e-68 |
|
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: 230.48 E-value: 2.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 220
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglrggrvvelkkivDEAVKHcptvqhvlvahrtdnkvhmgDLDvpleqemakedpvcapesmgsEDMLFMLYTSGSTGM 300
Cdd:cd05973 79 ---------------DAANRH--------------------KLD---------------------SDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTQAGYLLYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgryWETVERLK 380
Cdd:cd05973 103 PKGVPVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 381 INQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTG-GICIA-----PR 454
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTElGMVLAnhhalEH 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 455 PSEEGAEILPAMAMRpffgiVPVLMDEKGSVVEGsnVSGALCISQA-WPGMArtiYGDHQRFVDAYFKAypGYYFTGDGA 533
Cdd:cd05973 255 PVHAGSAGRAMPGWR-----VAVLDDDGDELGPG--EPGRLAIDIAnSPLMW---FRGYQLPDTPAIDG--GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 534 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 613
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLH 402
|
490 500 510
....*....|....*....|....*....|....*
gi 358248205 614 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05973 403 VKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
109-648 |
7.55e-65 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 223.50 E-value: 7.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 109 NVSVNCLDQHVRKS-----PESVALIWERDEpGTEVRITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAM 182
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGK-GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 183 LACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVQ-HVLVAHRTDNkvhmG 261
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKtKLLVSEKSRD----G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 262 DLDVPLEQEMAKEDPVCApeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWIT 341
Cdd:cd05928 152 WLNFKELLNEASTEHHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 342 GHSYVVYGPLCNGATsVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPIN 421
Cdd:cd05928 230 SAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 CEAWE-WLHRVVGDSRCTLVDTwwQTGGICIAPRpseeGAEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNVSGALCISQ 499
Cdd:cd05928 305 PEVLEkWKAQTGLDIYEGYGQT--ETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEGDIGIRVKP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 579
Cdd:cd05928 379 IRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248205 580 GYPHDIKGEAAFAFIVVKD--SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05928 457 SSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-647 |
7.04e-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: 218.46 E-value: 7.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 215
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 216 VITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDpvcapesmGSEDMLFMLYTS 295
Cdd:cd05971 82 LVT--------------------------------------------------------D--------GSDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 296 GSTGMPKGIVHTQA---GYLLYAALTHKLVfdHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnaGRY 372
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDP--KAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 373 WETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEW--------LHRVVGDSRCTLVDtww 444
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWareqfgveVNEFYGQTECNLVI--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 445 qtgGICIAPRPSEEGAeilpaMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAyp 524
Cdd:cd05971 249 ---GNCSALFPIKPGS-----MG-KPIPGHRVAIVDDNGTPLP-PGEVGEIAVELPDPVAFLG-YWNNPSATEKKMAG-- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 525 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 604
Cdd:cd05971 316 DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSD 395
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 358248205 605 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05971 396 ALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
140-647 |
1.45e-62 |
|
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: 216.85 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVitf 219
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 nqglrggrVVE---LKKIVDEAVKHCPTVQHVLVAhrtdnKVHMGDLDVP-LEQEMAKEDPVCAPESMGSEDMLFMLYTS 295
Cdd:cd05959 106 --------VVSgelAPVLAAALTKSEHTLVVLIVS-----GGAGPEAGALlLAELVAAEAEQLKPAATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 296 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWET 375
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 376 VERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVgdsrCTLVDTWWQT--GGICIA 452
Cdd:cd05959 250 IRRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGErWKARFG----LDILDGIGSTemLHIFLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 453 PRPSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQawPGMArTIYGdHQRfvDAYFKAYPGYYF-TGD 531
Cdd:cd05959 324 NRPGR----VRYGTTGKPVPGYEVELRDEDGGDVADG-EPGELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTrTGD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 532 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELK 611
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELK 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 358248205 612 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05959 473 EFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
115-643 |
8.20e-62 |
|
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: 212.86 E-value: 8.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVItfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemake 274
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 dpvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG 354
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 355 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinceAWEWLHRVVGD 434
Cdd:cd17631 166 GTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 435 SRCTLVDTWWQT---GGICIAPRpseEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTIYGD 511
Cdd:cd17631 236 RGVKFVQGYGMTetsPGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVPP-GEVGEIVVRG--PHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 512 HQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 591
Cdd:cd17631 310 PEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 358248205 592 AFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
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 ... |
56-683 |
1.11e-61 |
|
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: 217.83 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 56 GSYPALSAQAAREPAAFWGPLARDT-LVWDTPYHTVWDCDFSTGKIgWFLGGQLNVSVNCLdqhvRKSPESVALIWeRDE 134
Cdd:TIGR01217 35 GGYDALHRWSVDELDTFWKAVWEWFdVRFSTPCARVVDDRTMPGAQ-WFPGARLNYAENLL----RAAGTEPALLY-VDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 135 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 214
Cdd:TIGR01217 109 THEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 215 VVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVahrtdnkvhmgdldVPLEQEMAKEDPVcAPESMGSEDM------ 288
Cdd:TIGR01217 189 LLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVH--------------IPYLGPRETEAPK-IDGALDLEDFtaaaqa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 289 -------------LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITgHSYVVYGpLCNGA 355
Cdd:TIGR01217 254 aelvfeqlpfdhpLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM-WNWLVSG-LATGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 356 TSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgds 435
Cdd:TIGR01217 332 TLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY------ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 436 RCTLVDTWWQ--TGGI----CIAPRPSEEGAEILPAMAmrPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIY 509
Cdd:TIGR01217 406 DEIKADVWLAsiSGGTdicsCFAGANPTLPVHIGEIQA--PGLGTAVQSWDPEGKPVTGE--VGELVCTNPMPSMPIRFW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 510 GDHQ--RFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 587
Cdd:TIGR01217 482 NDPDgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 588 EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSeaqelgdtTTLEDPS 667
Cdd:TIGR01217 562 YRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQG--------TPVDNPG 633
|
650
....*....|....*...
gi 358248205 668 IIA--EILSVYQKCKDKQ 683
Cdd:TIGR01217 634 AIDnpELLDLYEELAELR 651
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
137-642 |
1.45e-61 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 213.61 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 217 ITFNQGLrggrvvelkKIVDEAVKHCPTVQHV-LVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTS 295
Cdd:cd05911 87 FTDPDGL---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 296 GSTGMPKGivhtqagyllyAALTHK-LVFDH-----------QPGDIFGCVADIGWITGHSYVVYGPLCnGATSVLFESt 363
Cdd:cd05911 156 GTTGLPKG-----------VCLSHRnLIANLsqvqtflygndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 364 pvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTW 443
Cdd:cd05911 223 ---FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 444 WQT--GGICIAPRPSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS--QAWPG-------MARTI 508
Cdd:cd05911 296 GMTetGGILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyynnpeaTKETF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 509 YGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 588
Cdd:cd05911 368 DED-------------GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 589 AAFAFIVVKDSAGDSDvvvQELKSMVATKIAKY-AVPDEILVVKRLPKTRSGKVM 642
Cdd:cd05911 435 LPRAYVVRKPGEKLTE---KEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
123-646 |
1.17e-58 |
|
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: 204.30 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapes 282
Cdd:cd05930 75 RLAYILEDSGAKLVLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 mGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFES 362
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 363 TPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDT 442
Cdd:cd05930 168 EVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 443 W-------WQTGGICIAPRPSEEGAEIlpamaMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGDH--- 512
Cdd:cd05930 241 YgpteatvDATYYRVPPDDEEDGRVPI-----GRPIPNTRVYVLDENLRPV-PPGVPGELYIGGA--GLARGYLNRPelt 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 513 -QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 591
Cdd:cd05930 313 aERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 592 AFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05930 393 AYVV---PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
141-647 |
2.91e-55 |
|
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: 194.99 E-value: 2.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 220
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGM 300
Cdd:cd05919 89 ---------------------------------------------------------------SADDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADI--GWITGHSyvVYGPLCNGATSVLFestPVYPNAGRYWETVER 378
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 379 LKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVD----TwwQTGGICIAPR 454
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDgigaT--EVGHIFLSNR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 455 PSEegaeILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI--SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDG 532
Cdd:cd05919 254 PGA----WRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVrgPSAAVGYWNNPEKSRATFNG-------GWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 533 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS 612
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHR 401
|
490 500 510
....*....|....*....|....*....|....*
gi 358248205 613 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05919 402 HLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
129-648 |
9.25e-54 |
|
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: 192.85 E-value: 9.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 129 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTvIFAGFSAESLAGR 207
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT-INPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 208 INDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPL---EQEMAKEDPVCAPESMG 284
Cdd:cd12119 93 INHAEDRVVFVDR---------DFLPLLEAIAPRLPTVEHVVVM--TDDAAMPEPAGVGVlayEELLAAESPEYDWPDFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 285 SEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLVFDHQPGDIFGCVADI----GW-------ITGHSYVVYGPLC 352
Cdd:cd12119 162 ENTAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVGAKLVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 353 NGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINCEAWEWLH 429
Cdd:cd12119 242 DPASLA---------------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 -RVVgdsrctlvdTWW---QTGGICIAPRP-------SEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVS-GALCI 497
Cdd:cd12119 305 vRVI---------HAWgmtETSPLGTVARPpsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAvGELQV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 498 SQAWpgMARTIYGDHQR----FVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 573
Cdd:cd12119 376 RGPW--VTKSYYKNDEEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 574 PESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd12119 447 AEAAVIGVPHPKWGERPLAVVVLKE---GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
115-647 |
7.27e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 183.92 E-value: 7.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVI---TFNQGLRGGRVVELKKIVDEavkhcptvqhvlvahrtdnkvhmgdldvpleqem 271
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIvavSFTDLLAAGAPLGERVALTP---------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 272 akedpvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHK--LVFDHQPGDIFGCVADIGWITGHSYVVYG 349
Cdd:cd05936 125 --------------EDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:cd05936 190 PLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 RVVGdsrCTLVdtwwqtggiciaprpseEG---AEILPAMAMRPFFG---------IVP----VLMDEKGSVVEGSNVsG 493
Cdd:cd05936 264 ELTG---VPIV-----------------EGyglTETSPVVAVNPLDGprkpgsigiPLPgtevKIVDDDGEELPPGEV-G 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 494 ALCIS--QAWPGmartiYGDH-----QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 566
Cdd:cd05936 323 ELWVRgpQVMKG-----YWNRpeetaEAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEV 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 567 IADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05936 391 LYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
.
gi 358248205 647 R 647
Cdd:cd05936 468 R 468
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
115-651 |
1.42e-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: 181.50 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtV 194
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFS-----AESLAGRInDAKCKVVITFNQGLRggrvveLKKIVDEAVKHCPTVQHVLVAHRTDNKVhmgDLDVPLEQ 269
Cdd:COG1021 103 VFALPAhrraeISHFAEQS-EAVAYIIPDRHRGFD------YRALARELQAEVPSLRHVLVVGDAGEFT---SLDALLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 270 EMAKEDPVCAPEsmgseDMLFMLYTSGSTGMPKGIVHTQAGYLlYAALTHKLVFDHQPGDIFGCVADIGwitgHSY---- 345
Cdd:COG1021 173 PADLSEPRPDPD-----DVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAEICGLDADTVYLAALPAA----HNFplss 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 346 -VVYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GS------ 415
Cdd:COG1021 243 pGVLGVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLqvgGAklspel 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 416 ---VGEPINCeaweWLHRVVG------------DSRCTLVDTwwQtgGiciapRPSEEGAEILpamamrpffgIVpvlmD 480
Cdd:COG1021 317 arrVRPALGC----TLQQVFGmaeglvnytrldDPEEVILTT--Q--G-----RPISPDDEVR----------IV----D 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 481 EKGS-VVEGSnvSGALcisqawpgMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAYRTEGGYYQITGR 546
Cdd:COG1021 370 EDGNpVPPGE--VGEL--------LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 547 MDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATK-IAKYAVPD 625
Cdd:COG1021 431 AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEP----LTLAELRRFLRERgLAAFKLPD 506
|
570 580
....*....|....*....|....*.
gi 358248205 626 EILVVKRLPKTRSGKVMRRLLRKIIT 651
Cdd:COG1021 507 RLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
57-655 |
8.63e-48 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 179.89 E-value: 8.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 57 SYPALSAQAAREPAAFWgplardTLVWDT---PYHT----VWDCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVAL 128
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW------SIVLDElslVFSVpprcILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 129 IWeRDEPGTEV---RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLA 205
Cdd:PLN03052 195 IW-RDEGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 206 GRINDAKCKVVITFNQGLRGGRVVELKKIVDEAvkHCPTVQhVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPES--- 282
Cdd:PLN03052 274 TRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEyka 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 --MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALT--HklvFDHQPGDIFGCVADIGWITGHsYVVYGPLCNGATSV 358
Cdd:PLN03052 351 veQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLA 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 359 LFESTPVYPNAGRYwetVERLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINCEAWEWLHrvvg 433
Cdd:PLN03052 427 LYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWLM---- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 434 dSRCTLVDTWWQTGGICIAP--------RPSEEGAEILPAMAMRPFfgivpvLMDEKGSVVEgSNVSG----ALCisqaw 501
Cdd:PLN03052 493 -SRAGYKPIIEYCGGTELGGgfvtgsllQPQAFAAFSTPAMGCKLF------ILDDSGNPYP-DDAPCtgelALF----- 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 502 PGM----ARTIYGDHQrfvDAYFKAYPGYYFT-----GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI-ADHP 571
Cdd:PLN03052 560 PLMfgasSTLLNADHY---KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADE 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 572 AVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVP----DEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PLN03052 637 SVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVLR 716
|
....*...
gi 358248205 648 KIITSEAQ 655
Cdd:PLN03052 717 QQLAQELS 724
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-656 |
1.27e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 173.19 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK08316 21 ARRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITfNQGLRGgrvvelkkIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKEDPVC 278
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLV-DPALAP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 APE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVfdhqpgdifGCVADIGWITG----------HS--- 344
Cdd:PRK08316 163 EPDvELADDDLAQILYTSGTESLPKGAMLT------HRALIAEYV---------SCIVAGDMSADdiplhalplyHCaql 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 345 YVVYGP-LCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTlGSVGEPINCE 423
Cdd:PRK08316 228 DVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRK-GYYGASIMPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 424 awEWLHRVvgDSRCTLVDTWWQTGGICIAP-----RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcis 498
Cdd:PRK08316 301 --EVLKEL--RERLPGLRFYNCYGQTEIAPlatvlGPEE--HLRRPGSAGRPVLNVETRVVDDDGNDVA----------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 499 qawPGMARTIYGDHQRFVDAYFK-------AYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 570
Cdd:PRK08316 364 ---PGEVGEIVHRSPQLMLGYWDdpektaeAFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTH 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 571 PAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 650
Cdd:PRK08316 441 PAVAEVAVIGLPDPKWIEAVTAVVVPKAGA---TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
....*.
gi 358248205 651 TSEAQE 656
Cdd:PRK08316 518 AGAFTD 523
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
117-647 |
2.31e-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: 171.76 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 197 AGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqHVLVAHRTDNKVHMGDLDVPLEQEMAKEDP 276
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLT----------------------------HPALAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 277 VCAPESMGseDMLFMLYTSGSTGMPKGIV--HTQAGYLLYAaltHKLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNG 354
Cdd:cd17651 129 PDPALDAD--DLAYVIYTSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 355 ATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCE-------AWEW 427
Cdd:cd17651 203 ATLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTedlrefcAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 428 LHRVV---GDSRCTLVDTWWQTGGICIAPRPSEEGaeilpamamRPFFGIVPVLMDEKGSVVEGsNVSGALCIsqAWPGM 504
Cdd:cd17651 280 GLRLHnhyGPTETHVVTALSLPGDPAAWPAPPPIG---------RPIDNTRVYVLDAALRPVPP-GVPGELYI--GGAGL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 505 ARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 580
Cdd:cd17651 348 ARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 581 YPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd17651 428 REDRPGEKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
123-648 |
1.89e-45 |
|
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: 169.03 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05926 1 PDAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITFNQGL---------RGGRVVELKkiVDEAVKHCPTVQHVLVAHRTDNKVhmgdldvpleqemAK 273
Cdd:cd05926 77 EFEFYLADLGSKLVLTPKGELgpasraaskLGLAILELA--LDVGVLIRAPSAESLSNLLADKKN-------------AK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 EDPVCAPEsmgseDMLFMLYTSGSTGMPKGIVHTQAGYLL---YAALTHKLvfdhQPGDIFGCVADIGWITGHSYVVYGP 350
Cdd:cd05926 142 SEGVPLPD-----DLALILHTSGTTGRPKGVPLTHRNLAAsatNITNTYKL----TPDDRTLVVMPLFHVHGLVASLLST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLH 429
Cdd:cd05926 213 LAAGGSVVL----PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPP--PKLRFIRSCSASLPPAVLEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 RVVGdsrCTLVDTWWQTggiciaprpseegaEILPAMAMRPF------FGIVP-------VLMDEKGSVVEgSNVSGALC 496
Cdd:cd05926 287 ATFG---APVLEAYGMT--------------EAAHQMTSNPLppgprkPGSVGkpvgvevRILDEDGEILP-PGVVGEIC 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 497 ISQawPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 576
Cdd:cd05926 349 LRG--PNVTRGYLNNPEANAEAAFKD--GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEA 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 577 AVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05926 425 VAFGVPDEKYGEEVAAAVVLR---EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-648 |
3.15e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 168.93 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK07656 11 LARAARRFGDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFnQGLRGgrvvelkkiVDEAVKHC-PTVQHVlVAHRTDNKVHMGDLDVPLEQEMAK 273
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVL-GLFLG---------VDYSATTRlPALEHV-VICETEEDDPHTEKMKTFTDFLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 EDPVCAPESMGSEDMLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHKLvfDHQPGD----------IFGCVAdiGWIT 341
Cdd:PRK07656 154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMltHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 342 ghsyvvygPLCNGATsVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPIn 421
Cdd:PRK07656 229 --------PLMRGAT-ILPL--PVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 ceAWEWLHRVVGDSRCTLVDTWW----QTGGICIAPRpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI 497
Cdd:PRK07656 294 --PVALLERFESELGVDIVLTGYglseASGVTTFNRL--DDDRKTVAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 498 S-----QAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 568
Cdd:PRK07656 369 RgpnvmKGYYDDpeatAAAIDAD-------------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 569 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK07656 436 EHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE---LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
138-647 |
3.87e-45 |
|
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: 167.27 E-value: 3.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHR-GDRVAIYMPVSPLAVAAMLACARIGAVhtvifagfsaeslagrindakCKVV 216
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 217 ITFnqgLRGGrvvELKKIVDEAvkhcpTVQHVLVAHRTdnkvhmgdldvpleqemakedpvcapesMGSEDMLFMLYTSG 296
Cdd:cd05958 67 MPL---LRPK---ELAYILDKA-----RITVALCAHAL----------------------------TASDDICILAFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 376
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 377 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTGG--ICIAPR 454
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMfhIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 455 PSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQawPGMARTIYGDHQRfvdAYFKAypGYYFTGDGAY 534
Cdd:cd05958 259 PGD----ARPGATGKPVPGYEAKVVDDEGNPVPDGTI-GRLAVRG--PTGCRYLADKRQR---TYVQG--GWNITGDTYS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 535 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMV 614
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHA 406
|
490 500 510
....*....|....*....|....*....|...
gi 358248205 615 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05958 407 KAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
116-646 |
1.13e-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: 166.61 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITfnQGLRGGRVVELKKIVdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKED 275
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAV--------------------------VIDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 PVCApesmGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlyaalthKLVFDH-----QPGDIFGCVADIGWiTGHSYVVYGP 350
Cdd:cd12117 130 AVPV----SPDDLAYVMYTSGSTGRPKGVAVTHRGVV-------RLVKNTnyvtlGPDDRVLQTSPLAF-DASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCNGATSVLFE-STPVYPNAGRywETVERLKINQFY--------------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 415
Cdd:cd12117 198 LLNGARLVLAPkGTLLDPDALG--ALIAEEGVTVLWltaalfnqladedpECFAGLRELLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 416 vGEPINCeawewlhrvVGDSRCTLVDTWWQTggiciaPRPSEEGAEILPAmamRPFFGIVPVLMDEKGSVVEgSNVSGAL 495
Cdd:cd12117 276 -LRLVNG---------YGPTENTTFTTSHVV------TELDEVAGSIPIG---RPIANTRVYVLDEDGRPVP-PGVPGEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 496 CISQAwpGMARTIYGD----HQRFVDAYFKayPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 569
Cdd:cd12117 336 YVGGD--GLALGYLNRpaltAERFVADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 570 HPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd12117 412 HPGVREAVVVVREDAGGDKRLVAYVV-----AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
140-647 |
6.40e-43 |
|
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: 160.53 E-value: 6.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 219
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPVCapesmgsedmlfMLYTSGSTG 299
Cdd:cd05934 82 -------------------------------------------------------DPAS------------ILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 300 MPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 379
Cdd:cd05934 95 PPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 380 KINQFYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTGGIC--IAPRPs 456
Cdd:cd05934 170 GATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVgvIGPRD- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 457 eegaEILPAMAM-RPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWP-GMARTIYGDHqrfvDAYFKAYP-GYYFTGDGA 533
Cdd:cd05934 241 ----EPRRPGSIgRPAPGYEVRIVDDDGQELP-AGEPGELVIRGLRGwGFFKGYYNMP----EATAEAMRnGWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 534 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSM 613
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD---PEELFAF 388
|
490 500 510
....*....|....*....|....*....|....
gi 358248205 614 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05934 389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
140-648 |
7.45e-43 |
|
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: 162.32 E-value: 7.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 219
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 NqglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNkvhmGDLDvpLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTG 299
Cdd:TIGR02262 110 G---------ALLPVIKAALGKSPHLEHRVVVGRPEA----GEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 300 MPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETVERL 379
Cdd:TIGR02262 175 MPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 380 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVVGDsrctLVDTWWQT--GGICIAPRPS 456
Cdd:TIGR02262 252 QPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTemLHIFLSNLPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 457 eegaEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRT 536
Cdd:TIGR02262 326 ----DVRYGTSGKPVPGYRLRLVGDGGQDV-ADGEPGELLISG---PSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 537 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDIKGEaafAFIVVKDSAGDSDvvvQELKSM 613
Cdd:TIGR02262 396 DDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVAdedGLIKPK---AFVVLRPGQTALE---TELKEH 469
|
490 500 510
....*....|....*....|....*....|....*
gi 358248205 614 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:TIGR02262 470 VKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
116-647 |
9.48e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 159.09 E-value: 9.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITFNQGLrggrvvelkKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLD--VPLEQEMAK 273
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPGVRHRLVLDGD------GELEgfVGYAEAVAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 --EDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvhtqagyllYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPL 351
Cdd:PRK13391 145 lpATPI-ADESLGTD----MLYSSGTTGRPKGI---------KRPLPEQPP-DTPLPLTAFLQRLWGFRSDMVYLSPAPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 352 --------CN-----GATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGE 418
Cdd:PRK13391 210 yhsapqraVMlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 419 PinCEAwewlhrvvgDSRCTLVDtWWqtGGICIAPRPSEEGA--------EIL--PAMAMRPFFGIVPVLMDekgsvveg 488
Cdd:PRK13391 286 P--CPP---------QVKEQMID-WW--GPIIHEYYAATEGLgftacdseEWLahPGTVGRAMFGDLHILDD-------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 489 snvSGALCIsqawPGMARTIYGDHQR-FVdaYFK----------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHR 557
Cdd:PRK13391 344 ---DGAELP----PGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 558 LGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTR 637
Cdd:PRK13391 415 IYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLP 494
|
570
....*....|
gi 358248205 638 SGKVMRRLLR 647
Cdd:PRK13391 495 TGKLYKRLLR 504
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
115-654 |
2.17e-41 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 158.68 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVI---TFnqglrggRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEM 271
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVvpkTF-------RGFDHAAMARRLRPELPALRHVVVVGGDGADSFEALLITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 272 AKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQ----AGYLLYAALthklvFDHQPGDIFGCVADIGWITGHSYVV 347
Cdd:PRK13295 183 PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 348 YGPLCNGATSVLFEStpvypnagryWETVERLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEPI 420
Cdd:PRK13295 258 MMPVMLGATAVLQDI----------WDPARAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 421 NCEAWEWLHRVVGdsrCTLVDTWWQTggiciaprpsEEGAEILpamamrpffgIVPVLMDEKGSVVEGSnvsgalcisqA 500
Cdd:PRK13295 325 PGALVERARAALG---AKIVSAWGMT----------ENGAVTL----------TKLDDPDERASTTDGC----------P 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 WPGMA-RTIYGDHQR----------------FVdAYFK-------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGH 556
Cdd:PRK13295 372 LPGVEvRVVDADGAPlpagqigrlqvrgcsnFG-GYLKrpqlngtDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 557 RLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPK 635
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSlDFEEMVEFLKA---QKVAKQYIPERLVVRDALPR 527
|
570
....*....|....*....
gi 358248205 636 TRSGKVMRRLLRKIITSEA 654
Cdd:PRK13295 528 TPSGKIQKFRLREMLRGED 546
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
140-648 |
5.49e-41 |
|
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: 155.23 E-value: 5.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 219
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 nqglrggrvvelkkivdeavkhcPTVqhvlvaHRTDNKVHMGDldvpleqemakedpvcapesmgseDMLFMLYTSGSTG 299
Cdd:cd05903 80 -----------------------PER------FRQFDPAAMPD------------------------AVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 300 MPKGIVHTqAGYLLYA--ALTHKLVFDhqPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVE 377
Cdd:cd05903 107 EPKGVMHS-HNTLSASirQYAERLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 378 RLKINQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPINC----EAWEWLHRVVgdsrctlVDTWWQT--GGI 449
Cdd:cd05903 180 EHGVTFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVPRslarRAAELLGAKV-------CSAYGSTecPGA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 450 CIAPRPSEEGAeilpAMAM--RPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMartIYGDHQRfVDAYFKAYP-GY 526
Cdd:cd05903 249 VTSITPAPEDR----RLYTdgRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSV---FLGYLDR-PDLTADAAPeGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 527 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDV 605
Cdd:cd05903 318 FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALlTFDE 397
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 358248205 606 VVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05903 398 LVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-646 |
8.04e-41 |
|
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: 155.10 E-value: 8.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmGDldvpleqemakedpvc 278
Cdd:cd05945 75 SPAERIREILDAAKPALLIAD-----------------------------------------GD---------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 apesmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIgwitghS-----YVVYGPLCN 353
Cdd:cd05945 98 --------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 354 GATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINCEAWEWLHRVVG 433
Cdd:cd05945 163 GATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 434 DSR-------------CTLVDTwwqtggiciaPRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVEGsNVSGALCISQa 500
Cdd:cd05945 240 DARiyntygpteatvaVTYIEV----------TPEVLDGYDRLPIG--YAKPGAKLVILDEDGRPVPP-GEKGELVISG- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 wPGMARTiYGDHQRFVDAYFKAYPGY--YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 578
Cdd:cd05945 306 -PSVSKG-YLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 579 IGYPHDIKGEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05945 384 VPKYKGEKVTELIAFVVPKP--GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
139-648 |
1.49e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 157.42 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 139 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgFSAESLAGRINDAKCKVVIT 218
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPL-LEPEQIAELLRAAGAKVLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 219 fnqgLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTD--------------NKVHMGDLDvpLEQEMAKE--DPVCAPES 282
Cdd:PRK07529 136 ----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARylpgpkrlavplirRKAHARILD--FDAELARQpgDRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 MGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGD----------IFGCVAdigwitghsyVVYGPLC 352
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV----------TGLAPLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 353 NGATSVLfeSTPV-YPNAG---RYWETVERLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRTLGSVGEPINCEAWEWL 428
Cdd:PRK07529 279 RGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 429 HRVVGdsrCTLVDTWWQTGGICIAPRPSEEGaEI--------LPAMAMRpffgIVPVlmDEKGSVVEGSNVS--GALCIS 498
Cdd:PRK07529 354 EAATG---VRIVEGYGLTEATCVSSVNPPDG-ERrigsvglrLPYQRVR----VVIL--DDAGRYLRDCAVDevGVLCIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 499 QA--WPGMARtiyGDHQRfvDAYFkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 576
Cdd:PRK07529 424 GPnvFSGYLE---AAHNK--GLWL--EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALA 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248205 577 AVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK07529 497 AAVGRPDAHAGELPVAYVQLKP---GASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
115-675 |
1.19e-39 |
|
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: 157.33 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQEMAKE 274
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLT-----------------QSA----------LAARLPELGVPVLALDALALAAEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPesmGSEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVADIG-----WitghsyVVY 348
Cdd:COG1020 609 NPPVPV---TPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSfdasvW------EIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 349 GPLCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINCEAWEWL 428
Cdd:COG1020 678 GALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 429 HRVVGDsrCTLVD-------TWWQTGGICIAPRPSEEGAEI---LPAMAMRpffgivpVLmDEKGSVV-EGsnVSGALCI 497
Cdd:COG1020 752 RARLPG--ARLVNlygptetTVDSTYYEVTPPDADGGSVPIgrpIANTRVY-------VL-DAHLQPVpVG--VPGELYI 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 498 sqAWPGMARTIYGDH----QRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 571
Cdd:COG1020 820 --GGAGLARGYLNRPeltaERFVADPF-GFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHP 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 572 AVPESAVIGYPhDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 651
Cdd:COG1020 897 GVREAVVVARE-DAPGDKRLVAYVV--PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA 973
|
570 580
....*....|....*....|....
gi 358248205 652 SEAQELGDTTTLEDPSIIAEILSV 675
Cdd:COG1020 974 AAAAAAAAPPAEEEEEEAALALLL 997
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
142-578 |
1.65e-39 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 150.49 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 QglrggrvvelkkivdeavkHCPTVQHVLVAHrtdnkVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTSGSTGM 300
Cdd:TIGR01733 81 A-------------------LASRLAGLVLPV-----ILLDPLELAALDDAPAPPPPDAPS--GPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTQAGyLLYAALTHKLVFDHQPGDIfgcvadigWITGHSYV-------VYGPLCNGATSVLFESTPVYPNAGRYW 373
Cdd:TIGR01733 135 PKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 374 ETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctlvdtWWQTGGI---C 450
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR------LINLYGPtetT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 451 IA------PRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDAYF 520
Cdd:TIGR01733 275 VWstatlvDPDDAPRESPVPIG--RPLANTRLYVLDDDLRPV-PVGVVGELYIGG--PGVARGYLNRpeltAERFVPDPF 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 521 KAYPGY--YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 578
Cdd:TIGR01733 350 AGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
140-646 |
9.63e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 150.88 E-value: 9.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 219 fnqglrggrVVELKKIVDEAVKHCPtVQHVLVAHRTDN-KVHMGD-----LDVPLEQEMAKEDPVCA------------P 280
Cdd:PRK08314 115 ---------GSELAPKVAPAVGNLR-LRHVIVAQYSDYlPAEPEIavpawLRAEPPLQALAPGGVVAwkealaaglappP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 281 ESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF 360
Cdd:PRK08314 185 HTAGPDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 361 -----EStpvypnAGRyweTVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDS 435
Cdd:PRK08314 264 prwdrEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 436 RCT---LVDTWWQTGgicIAP--RPSEEGAEIlpamamrPFFGIVPVLMD----------EKGSVVegsnVSGALCISQA 500
Cdd:PRK08314 333 YVEgygLTETMAQTH---SNPpdRPKLQCLGI-------PTFGVDARVIDpetleelppgEVGEIV----VHGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 WPGMART----IYGDHQRFvdayFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 576
Cdd:PRK08314 399 WNRPEATaeafIEIDGKRF----FR-------TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 577 AVIGYPHDIKGEAAFAFIVVKDSAGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:PRK08314 468 CVIATPDPRRGETVKAVVVLRPEARGK-TTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
120-641 |
1.06e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 151.35 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 120 RKSPESVALIWErdepGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 199
Cdd:PRK06178 44 RERPQRPAIIFY----GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 200 SAESLAGRINDAKCKVVITFNQglrggrvveLKKIVdEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED---- 275
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQ---------LAPVV-EQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAaaga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 ----------PVCAPESMGSEDMLFML-YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHS 344
Cdd:PRK06178 188 idllpalracTAPVPLPPPALDALAALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGEN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 345 YVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVG-----EP 419
Cdd:PRK06178 268 FGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVVSfvkklNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 420 INCEAWewlHRVVGdsrCTLVDTWW---------------QTGGICIAPRPSEEGaeiLPAMAMRpfFGIVpvlmDEKGS 484
Cdd:PRK06178 342 DYRQRW---RALTG---SVLAEAAWgmtethtcdtftagfQDDDFDLLSQPVFVG---LPVPGTE--FKIC----DFETG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 485 VVEGSNVSGALCISQawPGMARTIYG----DHQRFVDayfkaypGYYFTGD-GAYrTEGGYYQITGRMDDVINISGHRLG 559
Cdd:PRK06178 407 ELLPLGAEGEIVVRT--PSLLKGYWNkpeaTAEALRD-------GWLHTGDiGKI-DEQGFLHYLGRRKEMLKVNGMSVF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 560 TAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPdEILVVKRLPKTRSG 639
Cdd:PRK06178 477 PSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP---GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATG 552
|
..
gi 358248205 640 KV 641
Cdd:PRK06178 553 KV 554
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
117-665 |
2.12e-37 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 147.20 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALIwerDEPGTevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 197 AGFSAESLAGRINDAKCKVVIT---FNQGLRGGRVVELKKIVdeavkhcPTVQHVLVAhrtdNKVHMGDLDVPLEQEMAK 273
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlFKQTRPVDLILPLQNQL-------PQLQQIVGV----DKLAPATSSLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 EDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLL----YAALTHkLVFDhqpgDIFGCVADIGWITGHSYVVYG 349
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINC----EAW 425
Cdd:PRK06087 250 PFLIGARSVLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIPKkvarECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 426 EwlHRVVgdsrctLVDTWWQTGGICIAPRPSEEGAEILPAMAMRPFFGI-VPVLMDEKGSV---VEGSNVSGAlcisqaw 501
Cdd:PRK06087 324 Q--RGIK------LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVeIKVVDEARKTLppgCEGEEASRG------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 502 PGMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 578
Cdd:PRK06087 389 PNVFMGYLDEPEltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 579 IGYPHDIKGEAAFAFIVVKDSagDSDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQEL 657
Cdd:PRK06087 464 VAMPDERLGERSCAYVVLKAP--HHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI---MRRL 538
|
....*...
gi 358248205 658 GDTTTLED 665
Cdd:PRK06087 539 TQDVCEEI 546
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
123-646 |
2.17e-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: 145.51 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALiweRDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd12116 1 PDATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivDEAvkhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPES 282
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 MGSEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFdhQPGDIFGCVADIGW-ITGHSyvVYGPLCNGATSVLF 360
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGL--GPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 361 ESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdaWvkkYDRSSLRTL-GsvGEPinceawewLHRVVGDSRCTL 439
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAG--W---QGRAGLTALcG--GEA--------LPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 440 VDTWWQTGGiciaprPSEE-----GAEILPAMAM----RPFFGIVPVLMDEKG-SVVEGsnVSGALCIsqAWPGMARTIY 509
Cdd:cd12116 263 VGSLWNLYG------PTETtiwstAARVTAAAGPipigRPLANTQVYVLDAALrPVPPG--VPGELYI--GGDGVAQGYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 510 GD----HQRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPH 583
Cdd:cd12116 333 GRpaltAERFVPDPF-AGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 584 DIKGEAAfAFIVVKD-SAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd12116 412 GGDRRLV-AYVVLKAgAAPDAA----ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
123-646 |
3.78e-37 |
|
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: 144.76 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapes 282
Cdd:cd17643 75 RIAFILADSGPSLLLT--------------------------------------------------------DP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHQpgdifgcvaDIgWITGHSYV-------VYGPLCNG 354
Cdd:cd17643 93 ---DDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFNED---------DV-WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 355 ATSVLFES----TPVypnagRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINCEAWE-W 427
Cdd:cd17643 160 GRLVVVPYevarSPE-----DFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRpW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 428 LHRVvGDSRCTLVDTWwqtgGI---CIAPRPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEGSnVSGALCISQa 500
Cdd:cd17643 231 AGRF-GLDRPQLVNMY----GItetTVHVTFRPLDAADLPAAAAspigRPLPGLRVYVLDADGRPVPPG-VVGELYVSG- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 wPGMARTIYG----DHQRFVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 574
Cdd:cd17643 304 -AGVARGYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVR 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 575 ESAVIGYpHDIKGEAAFAFIVVKDSAgdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17643 382 DAAVIVR-EDEPGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
119-646 |
7.38e-37 |
|
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: 144.57 E-value: 7.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd05923 11 ASRAPDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRI-NDAKCKVVITFNQG------LRGGRVVELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDVPLEQEM 271
Cdd:cd05923 87 LKAAELAELIeRGEMTAAVIAVDAQvmdaifQSGVRVLALSDLVG--------------------------LGEPESAGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 272 AKEDPVCAPESMGsedmlFMLYTSGSTGMPKGIVHTQAgyllyAALTHKLVFDHQPGDIFGC------VADIGWITGHSY 345
Cdd:cd05923 141 LIEDPPREPEQPA-----FVFYTSGTTGLPKGAVIPQR-----AAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 346 VVYGPLCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAW 425
Cdd:cd05923 211 VLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 426 EWLHRVVGDSRCTLVDTWwQTGGICIAPRPSEEGAeilpamaMRPFFG----IVPVL--MDEKGSVVEGSNVSGALCISQ 499
Cdd:cd05923 285 ERVNQHLPGEKVNIYGTT-EAMNSLYMRDARTGTE-------MRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 579
Cdd:cd05923 357 AFTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 580 GYPHDIKGEAAFAFIVVKDSAGDSDvvvqELKSM-VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05923 430 GVADERWGQSVTACVVPREGTLSAD----ELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
140-646 |
8.74e-37 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 143.00 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 219
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 NqglrggrvvELkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTG 299
Cdd:cd05935 81 S---------EL------------------------------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 300 MPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF-----ESTPvypnagrywE 374
Cdd:cd05935 98 LPKGCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL---------E 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 375 TVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTGGIC---I 451
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTETMSqthT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 452 AP--RPSEEGAEIlpamamrPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAYPGYYF- 528
Cdd:cd05935 243 NPplRPKLQCLGI-------P*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIKGRRFFr 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 529 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsAGDSDVVVQ 608
Cdd:cd05935 314 TGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYRGKVTEE 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 358248205 609 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05935 393 DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
115-646 |
5.29e-36 |
|
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: 142.03 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERdepgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITfNQGLRGGRVVELKKivdeavkhcPTVQHVLVAHRTDnkvhmgdldvpleqemAKE 274
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLT-TADLAARLPAGGDV---------ALLGDEALAAPPA----------------TPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPesmgsEDMLFMLYTSGSTGMPKGIVHTQAG---YLLYaaLTHKlvFDHQPGDIFGCVADIGWITGhSYVVYGPL 351
Cdd:cd17646 132 LVPPRP-----DNLAYVIYTSGSTGRPKGVMVTHAGivnRLLW--MQDE--YPLGPGDRVLQKTPLSFDVS-VWELFWPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 352 CNGATSVLFEstpvyPNAGR---YW-ETVERLKINQFYGAPTAVRLLLkygdAWVKKYDRSSLRTLGSVGEPINCEAWEW 427
Cdd:cd17646 202 VAGARLVVAR-----PGGHRdpaYLaALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 428 LHRVVGdsrCTLVD-----------TWWQTGGiciaprpsEEGAEILPamAMRPFFGIVPVLMDEKGSVVEgSNVSGALC 496
Cdd:cd17646 273 FLALPG---AELHNlygpteaaidvTHWPVRG--------PAETPSVP--IGRPVPNTRLYVLDDALRPVP-VGVPGELY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 497 IsqAWPGMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPA 572
Cdd:cd17646 339 L--GGVQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 573 VPESAVIGYPHDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17646 417 VTHAVVVARAAPAGAARLVGYVVP--AAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
141-648 |
7.14e-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: 140.40 E-value: 7.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINdakckvvitfn 220
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglRGGRVVelkKIVDEAVKhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgSEDMLFMLYTSGSTGM 300
Cdd:cd05974 70 ---RGGAVY---AAVDENTH--------------------------------------------ADDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTQAGYLLyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVypNAGRYWETVERLK 380
Cdd:cd05974 100 PKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 381 INQFYGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTGGICIAPrpSEEGA 460
Cdd:cd05974 177 VTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTALVG--NSPGQ 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 461 EILPAMAMRPFFGIVPVLMDEKGSVVEGSNVsgALCISQAWP-GMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGG 539
Cdd:cd05974 248 PVKAGSMGRPLPGYRVALLDPDGAPATEGEV--ALDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDEDG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 540 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 619
Cdd:cd05974 323 YLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLA 402
|
490 500
....*....|....*....|....*....
gi 358248205 620 KYAVPDEiLVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05974 403 PYKRIRR-LEFAELPKTISGKIRRVELRR 430
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
172-655 |
8.03e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 141.88 E-value: 8.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 172 MPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTV-----Q 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVlpaagE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 247 HVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQ 326
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 327 PGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYwetVERLKINQFYGAPTAVRLLLKYGDAWVKKYD 406
Cdd:PLN03051 159 PGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 407 RSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLV---DTWWQTGGICIAP-RPSEEGAEILPAMAMRpffgivPVLMDEK 482
Cdd:PLN03051 235 WSKLRVFASTGEASAVDDVLWLSSVRGYYKPVIEycgGTELASGYISSTLlQPQAPGAFSTASLGTR------FVLLNDN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 483 G-SVVEGSNVSGALCISQAWPGMA-RTIYGDHQRfvdAYFKAYPGYYFT-------GDGAYRTEGGYYQITGRMDDVINI 553
Cdd:PLN03051 309 GvPYPDDQPCVGEVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 554 SGHRLGTAEIEDAI-ADHPAVPESAVIGYPhDIKGEAAFAFIVVKDS-------AGDSDVVVQELKSMVATKIAKYAVPD 625
Cdd:PLN03051 386 GGIKTSSVEIERACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGeekkgfdQARPEALQKKFQEAIQTNLNPLFKVS 464
|
490 500 510
....*....|....*....|....*....|
gi 358248205 626 EILVVKRLPKTRSGKVMRRLLRKIITSEAQ 655
Cdd:PLN03051 465 RVKIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
117-649 |
4.84e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 140.06 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGA 190
Cdd:PRK07788 57 HAARRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 191 VHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVqHVLVAHrTDNKVHMGDLDVPLEQE 270
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAAREGVKALVYDD---------EFTDLLSALPPDLGRL-RAWGGN-PDDDEPSGSTDETLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 271 MAKED--PVCAPESMGSedmlFMLYTSGSTGMPKGIVHTQAGYLLYAALthklVFDHQP---GDIFGCVADIGWITGHSY 345
Cdd:PRK07788 194 IAGSStaPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLAG----LLSRVPfraGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 346 VVYGpLCNGATSVL---FestpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINC 422
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 423 EAWEWLHRVVGDSRCTLvdtwWQTGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWP 502
Cdd:PRK07788 338 ELATRALEAFGPVLYNL----YGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNGFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 503 gMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP 582
Cdd:PRK07788 413 -FEGYTDGRDKQIID-------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 583 HDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 649
Cdd:PRK07788 485 DEEFGQRLRAFVVKAP---GAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
136-647 |
6.05e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 139.27 E-value: 6.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 215
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 216 VITfnqglrGGRVVELkkiVDEAVKHCPT-VQHVLVAHrtdnkvhmGDLD--VPLEQEMAKEDPV-CAPESMGSEdmlfM 291
Cdd:PRK08276 87 LIV------SAALADT---AAELAAELPAgVPLLLVVA--------GPVPgfRSYEEALAAQPDTpIADETAGAD----M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 292 LYTSGSTGMPKGIVhtqagyllyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGA-------------TSV 358
Cdd:PRK08276 146 LYSSGTTGRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 359 LFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinceawewlhrvvgdsrCT 438
Cdd:PRK08276 217 VMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAP-----------------CP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 439 lVDT------WW-----------QTGGICIAprPSEEGAEiLPAMAMRPFFGIVPVLmDEKGSVVEgsnvsgalcisqaw 501
Cdd:PRK08276 276 -VEVkramidWWgpiiheyyassEGGGVTVI--TSEDWLA-HPGSVGKAVLGEVRIL-DEDGNELP-------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 502 PGMARTIY-----------GDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDA 566
Cdd:PRK08276 337 PGEIGTVYfemdgypfeyhNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 567 IADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:PRK08276 411 LVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
.
gi 358248205 647 R 647
Cdd:PRK08276 491 R 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
123-647 |
1.61e-34 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 137.11 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17649 1 PDAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvQHvlvahrtdnkvhmgdldvpleqemakedpvcaPES 282
Cdd:cd17649 75 RLRYMLEDSGAGLLLT---------------------------HH--------------------------------PRQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 MGsedmlFMLYTSGSTGMPKGIVHTQAgyllyaALTH-----KLVFDHQPGDIFGCVADIGWITGHSYVvYGPLCNGAtS 357
Cdd:cd17649 96 LA-----YVIYTSGSTGTPKGVAVSHG------PLAAhcqatAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-C 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 358 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKyDRSSLRTLGSVGEPINCE-AWEWLhrvvgDSR 436
Cdd:cd17649 163 VVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPElLRRWL-----KAP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 437 CTLVDTWWQTGGI-----CIAPRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG- 510
Cdd:cd17649 237 VRLFNAYGPTEATvtplvWKCEAGAARAGASMPIG--RPLGGRSAYILDADLNPVP-VGVTGELYI--GGEGLARGYLGr 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 511 ---DHQRFV-DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIk 586
Cdd:cd17649 312 pelTAERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG- 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248205 587 GEAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd17649 391 GKQLVAYVVLRAAAAQPE-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
123-646 |
2.14e-34 |
|
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: 137.75 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITFNQG---LRGG--RVVelkkIVDEAVKHCptvqhvlvAHRTDNKVHMGDLDVPleQEMAKEDPV 277
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaekLASLalPVV----LLDSAEFDS--------LSFSDLLFEADEAEPP--VVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 278 CApesmgsedmlfMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT 356
Cdd:cd05904 161 AA-----------LLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGAT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 SVlfestpVYP--NAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGD 434
Cdd:cd05904 230 VV------VMPrfDLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 435 SRctLVDTWWQT--GGICIAPRPSEEGAE-------ILPAMAMRpffgIVpvlmDEKGSVVEGSNVSGALCISQawPGM- 504
Cdd:cd05904 302 VD--LGQGYGMTesTGVVAMCFAPEKDRAkygsvgrLVPNVEAK----IV----DPETGESLPPNQTGELWIRG--PSIm 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 505 ----------ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 574
Cdd:cd05904 370 kgylnnpeatAATIDKE-------------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEIL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 575 ESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05904 437 DAAVIPYPDEEAGEVPMAFVVRK---PGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
115-648 |
1.80e-33 |
|
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: 134.91 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:TIGR03098 6 LEDAAARLPDATALVH------HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFNQGLRggrvvelkkIVDEAVKHCPTVQHVLvahRTDNKVHMGDLDVPLE----QE 270
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLLVTSSERLD---------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEEpaswPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 271 MAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLvfDHQPGDIFGCVADIGWITGHSYVVYG 349
Cdd:TIGR03098 148 LLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAqSVATYL--ENRPDDRLLAVLPLSFDYGFNQLTTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCnGATSVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWvKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:TIGR03098 226 FYV-GATVVLHD----YLLPRDVLKALEKHGITGLAAVPPLWAQLAQ--LDW-PESAAPSLRYLTNSGGAMPRATLSRLR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 RVVGDSRCTLVdtwwqtGGICIAPR----PSEEgaeilpaMAMRPffgivpvlmDEKGSVVEGSNVS-----GALC---- 496
Cdd:TIGR03098 298 SFLPNARLFLM------YGLTEAFRstylPPEE-------VDRRP---------DSIGKAIPNAEVLvlredGSECapge 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 497 ---ISQAWPGMARTIYGDHQRfVDAYFKAYPGYY----------FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEI 563
Cdd:TIGR03098 356 egeLVHRGALVAMGYWNDPEK-TAERFRPLPPFPgelhlpelavWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 564 EDAIADHPAVPESAVIGYPHDIKGEaafAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:TIGR03098 435 EEVAYATGLVAEAVAFGVPDPTLGQ---AIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDR 511
|
....*
gi 358248205 644 RLLRK 648
Cdd:TIGR03098 512 KALAK 516
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
119-646 |
3.11e-33 |
|
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: 133.21 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd12115 9 AARTPDAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvc 278
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 apesmGSEDMLFMLYTSGSTGMPKG--IVHTQAGYLLYAALTH-------------KLVFDHQPGDIFGcvadigwitgh 343
Cdd:cd12115 103 -----DPDDLAYVIYTSGSTGRPKGvaIEHRNAAAFLQWAAAAfsaeelagvlastSICFDLSVFELFG----------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 344 syvvygPLCNGATSVLFESTPVYPNAGRYWETVerlKINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCE 423
Cdd:cd12115 167 ------PLATGGKVVLADNVLALPDLPAAAEVT---LINT---VPSAAAELLRHDAL------PASVRVVNLAGEPLPRD 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 424 AWEWLH------RVV---GDSRctlvDTWWQTGgiCIAPRPSEEGAEIlpamaMRPFFGIVPVLMDEKGSVVeGSNVSGA 494
Cdd:cd12115 229 LVQRLYarlqveRVVnlyGPSE----DTTYSTV--APVPPGASGEVSI-----GRPLANTQAYVLDRALQPV-PLGVPGE 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 495 LCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 570
Cdd:cd12115 297 LYIGGA--GVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 571 PAVPEsAVIGYPHDIKGEAAF-AFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd12115 375 PGVRE-AVVVAIGDAAGERRLvAYIVAEPGAA---GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
123-646 |
1.22e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 131.44 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17650 1 PDAIAVSDA------TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapes 282
Cdd:cd17650 75 RLQYMLEDSGAKLLLT--------------------------------------------------------QP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHQPGDIFGcvadigwITGHSYVVYG-----PLCNGAT 356
Cdd:cd17650 93 ---EDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFDVFAgdfarSLLNGGT 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 SVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPIncEAWEWLHRVVGd 434
Cdd:cd17650 163 LVICPDEVKL-DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QDFKTLAARFG- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 435 SRCTLVDTWWQTGGiCIAPRPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYG 510
Cdd:cd17650 237 QGMRIINSYGVTEA-TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQP-VGVAGELYIGGA--GVARGYLN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 511 D----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgYPHDIK 586
Cdd:cd17650 313 RpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKG 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 587 GEAAFAFIVVKDSAGDSdvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17650 392 GEARLCAYVVAAATLNT----AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
123-640 |
1.43e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 132.70 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVItFNQGLrGGRVVELKkivDEavkhCPTVQHVL-VAHRTDNKVHMGdlDVPLEQEMAKEDPVCAPE 281
Cdd:PRK07798 91 ELRYLLDDSDAVALV-YEREF-APRVAEVL---PR----LPKLRTLVvVEDGSGNDLLPG--AVDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 282 SmGSEDMLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLVFDH--QPGDIFGCVADIGWITGHSYVVYGPLCNGAT--- 356
Cdd:PRK07798 160 E-RSPDDLYLLYTGGTTGMPKGVMWRQED--IFRVLLGGRDFATgePIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 ---------SVLFESTPVYpNAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVG 417
Cdd:PRK07798 237 afaalfsgqTVVLLPDVRF-DADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIASGG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 418 EPINCEAWEWLHRVVGDSrcTLVDTWWQT----GGICIAPRPSEEGAeilpamamRPFFGIVP--VLMDEKGSVVE-GSN 490
Cdd:PRK07798 306 ALFSPSVKEALLELLPNV--VLTDSIGSSetgfGGSGTVAKGAVHTG--------GPRFTIGPrtVVLDEDGNPVEpGSG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 491 VSGALcisqawpgmART------IYGDHQRfVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 562
Cdd:PRK07798 376 EIGWI---------ARRghiplgYYKDPEK-TAETFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEE 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 563 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 640
Cdd:PRK07798 446 VEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
140-648 |
3.08e-32 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 130.10 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIt 218
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 219 fnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSGST 298
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 299 GMPKGIVHTQAGylLYA---ALTHKLVFdhQPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlFESTPvYPNAGRYWET 375
Cdd:cd05941 102 GRPKGVVLTHAN--LAAnvrALVDAWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGAS---VEFLP-KFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 376 VERLKINQFYGAPTAVRLLLKYgdawvkkYDRSSLRTLGSVGEpinceAWEWLHRVVGDSRCTLVDT---WWQTGGICIA 452
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQY-------YEAHFTDPQFARAA-----AAERLRLMVSGSAALPVPTleeWEAITGHTLL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 453 PR--PSEEG--------AEILPAMAMRPFFGI-VPVLMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQRFVDAyFK 521
Cdd:cd05941 242 ERygMTEIGmalsnpldGERRPGTVGMPLPGVqARIVDEETGEPLPRGEV-GEIQV--RGPSVFKEYWNKPEATKEE-FT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 522 AyPGYYFTGDGAYRTEGGYYQITGRM-DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSA 600
Cdd:cd05941 318 D-DGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA--VVVLRA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 358248205 601 GDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05941 395 GAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
115-646 |
3.49e-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: 130.53 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtV 194
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAgfsaeslagrindakckvvitfnqgLRGGRVVELKKIVD--EAVkhcptvqhVLVAHRTdnkvHMGDLDVPLEQEMA 272
Cdd:cd05920 93 VLA-------------------------LPSHRRSELSAFCAhaEAV--------AYIVPDR----HAGFDHRALARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 273 KEDPvcapesmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHQpgDIFGCVADIGwitgHSYV----- 346
Cdd:cd05920 136 ESIP----------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLDQD--TVYLAVLPAA----HNFPlacpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 347 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE 426
Cdd:cd05920 200 VLGTLLAGGRVVLAPD----PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 427 WLHRVVGdsrCTLVDTWWQTGGICIAPRPsEEGAEILPAMAMRPffgIVP----VLMDEKGSVVeGSNVSGALcisqawp 502
Cdd:cd05920 274 RVPPVLG---CTLQQVFGMAEGLLNYTRL-DDPDEVIIHTQGRP---MSPddeiRVVDEEGNPV-PPGEEGEL------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 503 gMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 569
Cdd:cd05920 339 -LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 570 HPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd05920 409 HPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-649 |
8.38e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 130.66 E-value: 8.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFNqGLRGGRVVElkkIVDEAVKHCPTVQHVLVAH----RTDNKVHMGDLDVP---L 267
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTSDYHA---MLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 268 EQEMAKEDPVCAPE-------SMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDHqpgdifgcvadiGWI 340
Cdd:PRK12583 176 WHELQARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKG-----------ATLSHHNILNN------------GYF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 341 TGHS---------------YVVYGPLCNGATSVLFESTPVYPN----AGRYWETVERLKINQFYGAPTAVRLLLKYGDaw 401
Cdd:PRK12583 233 VAESlgltehdrlcvpvplYHCFGMVLANLGCMTVGACLVYPNeafdPLATLQAVEEERCTALYGVPTMFIAELDHPQ-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 402 VKKYDRSSLRTLGSVGEPinCEAwEWLHRVVGDSRCTLVDTWW----------QTGGICIAPRPSEEGAEILPAMAMRpf 471
Cdd:PRK12583 311 RGNFDLSSLRTGIMAGAP--CPI-EVMRRVMDEMHMAEVQIAYgmtetspvslQTTAADDLERRVETVGRTQPHLEVK-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 472 fgivpvLMDEKGSVVEGSNVsGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQ 542
Cdd:PRK12583 386 ------VVDPDGATVPRGEI-GELCtrgysVMKGYWNNpeatAESIDED-------------GWMHTGDLATMDEQGYVR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 543 ITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYA 622
Cdd:PRK12583 446 IVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP---GHAASEEELREFCKARIAHFK 522
|
570 580
....*....|....*....|....*..
gi 358248205 623 VPDEILVVKRLPKTRSGKVMRRLLRKI 649
Cdd:PRK12583 523 VPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
115-662 |
2.23e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 129.38 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFNqgLRGGRVVELKK-------IVDEAVKHCPTVQHVL---VAHRTDNKV------ 258
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLD--LVFPRVTNVQSatkiehvIVTRIADFLPFPKNLLypfVQKKQSNLVvkvses 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 259 HMGDLDVPLEQEM-AKEDPVCAPESmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGD--IFGcVA 335
Cdd:PRK06710 182 ETIHLWNSVEKEVnTGVEVPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEevVLG-VL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 336 DIGWITGHSYVVYGPLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGS 415
Cdd:PRK06710 257 PFFHVYGMTAVMNLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 416 VGEPINCEAWEWLHRVVG-----------DSRCTLVDTWWQT---GGICIaPRPSEEG--AEILPAMAMRPffgivpvlm 479
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGgklvegyglteSSPVTHSNFLWEKrvpGSIGV-PWPDTEAmiMSLETGEALPP--------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 480 DEKGSVVegsnVSGALCISQAW--PGMARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHR 557
Cdd:PRK06710 401 GEIGEIV----VKGPQIMKGYWnkPEETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFN 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 558 LGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTR 637
Cdd:PRK06710 464 VYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE---GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTT 540
|
570 580
....*....|....*....|....*
gi 358248205 638 SGKVMRRLLrkiITSEAQELGDTTT 662
Cdd:PRK06710 541 VGKILRRVL---IEEEKRKNEDEQT 562
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-647 |
8.31e-31 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 127.11 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK08008 14 DDLADVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKivdeavKHCPtvQHVLVAhRTDNKVHMGDLDvpLEQEMAKED 275
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQED------ATPL--RHICLT-RVALPADDGVSS--FTQLKAQQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 P-VCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQ-----AGYllYAALTHKLVFDhqpgDIFGCVADIGWITGHSYVVYG 349
Cdd:PRK08008 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLTVMPAFHIDCQCTAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCNGATSVLFEStpvYpNAGRYWETVERLKINQFYGAPTAVR-LLLKYGDAWvkkyDRS-SLRTLG-----SVGEPinc 422
Cdd:PRK08008 236 AFSAGATFVLLEK---Y-SARAFWGQVCKYRATITECIPMMIRtLMVQPPSAN----DRQhCLREVMfylnlSDQEK--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 423 EAWEWLHRVvgdsrcTLVDTWWQT---GGIcIAPRPSEEgaEILPAMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCIsQ 499
Cdd:PRK08008 305 DAFEERFGV------RLLTSYGMTetiVGI-IGDRPGDK--RRWPSIG-RPGFCYEAEIRDDHNRPLP-AGEIGEICI-K 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWPGmaRTIYGDHQRFVDAYFKAYP--GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 577
Cdd:PRK08008 373 GVPG--KTIFKEYYLDPKATAKVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 578 VIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK08008 451 VVGIKDSIRDEAIKAFVVLNEGE---TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
115-647 |
1.29e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 126.78 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVItFNQGLRGGRVVELKKIVDEAVKhcPTVQHVLVAHRTDNKV---HMGDLDVPLEQEM 271
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLV-VWPGFKGIDFAAILAAVPPDAL--PPLRAIAVVDDAADATpapAPGARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 272 AKEDPVCAPESmGSEDMLFMLY-TSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHQPGDIFGCVADIGWITGHSYVVyGP 350
Cdd:PRK06164 167 PAPPAAAGERA-ADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-GA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVG-EPINCEAWEW-- 427
Cdd:PRK06164 244 LAGGAPLVCE---PVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFGFASfAPALGELAALar 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 428 -----LHRVVGDSRC-TLVDTW---------WQTGGiciapRPSEEGAEilpamamrpffgiVPVLMDEKGSVVEgSNVS 492
Cdd:PRK06164 317 argvpLTGLYGSSEVqALVALQpatdpvsvrIEGGG-----RPASPEAR-------------VRARDPQDGALLP-DGES 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 493 GALCISQawPGMARTiYGDHQrfvDAYFKAYP--GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 570
Cdd:PRK06164 378 GEIEIRA--PSLMRG-YLDNP---DATARALTddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 571 PAVPESAVIGYPHDIKGEAAfAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSG---KVMRRLLR 647
Cdd:PRK06164 452 PGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
113-651 |
1.96e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 125.46 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 113 NCLDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFEEKK------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 193 TVIFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKHcptvqhvlvAHRTDNKVHMGDLdvpleQEMA 272
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLIT-----------------DDDFEA---------KLIPGISVKFAEL-----MNGP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 273 KEDPVcaPESMGSEDMLF-MLYTSGSTGMPKGIVHTQAGYLlYAALTHKLVFDHQPGDIFGCVADIGWITGHSY----VV 347
Cdd:PRK03640 129 KEEAE--IQEEFDLDEVAtIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSIlmrsVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 348 YGplcngATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAV-RLLLKYGDAwvkKYDrSSLRT--LGsvGEPIN--- 421
Cdd:PRK03640 206 YG-----MRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLqRLLERLGEG---TYP-SSFRCmlLG--GGPAPkpl 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 ---CEAWEWlhRVVgdsrctlvdtwwQTGGIC-----IAPRPSEEGAEILPAmAMRPFFGI--------VPVLMDEKGS- 484
Cdd:PRK03640 271 leqCKEKGI--PVY------------QSYGMTetasqIVTLSPEDALTKLGS-AGKPLFPCelkiekdgVVVPPFEEGEi 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 485 VVEGSNV-SGALCISQAwpgmartiygDHQRFVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEI 563
Cdd:PRK03640 336 VVKGPNVtKGYLNREDA----------TRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEI 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 564 EDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:PRK03640 399 EEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-----SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLR 473
|
....*...
gi 358248205 644 RLLRKIIT 651
Cdd:PRK03640 474 HELKQLVE 481
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
115-644 |
2.78e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 125.77 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFNQGLRGGRvvelkkivDEAVKHCPtvqhVLVAHRTDNKVHMGDLDVPLEQEMAKE 274
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRA--------EPTTRWWP----LTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPESMGSEDMLFMlYTSGSTGMPKGIVHTQAGyllYAALTHKLVFDHQPGDIFGCVADIGWITGHSYV--VYGPLC 352
Cdd:PRK05852 166 PATSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 353 NGATSVLfestpvyPNAGR-----YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEW 427
Cdd:PRK05852 242 SGGAVLL-------PARGRfsahtFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 428 LHRVVGDSR-CT--LVDTWWQTGGICIAPRPSEEGAEILPAMAMR---PFFGIV-----PVLMDEKGSV-VEGSNVsgal 495
Cdd:PRK05852 315 LQTEFAAPVvCAfgMTEATHQVTTTQIEGIGQTENPVVSTGLVGRstgAQIRIVgsdglPLPAGAVGEVwLRGTTV---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 496 cisqawpgmARTIYGD----HQRFVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 571
Cdd:PRK05852 391 ---------VRGYLGDptitAANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHP 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248205 572 AVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 644
Cdd:PRK05852 455 NVMEAAVFGVPDQLYGEAVAAVIVPRESAP---PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
137-649 |
2.83e-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: 125.72 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 216
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 217 ITFNQGLRggRVVELKKIVdeavkhcPTVQHVLVahrTDNKVHMGDLDVpLEQEMAKEDPVC-------APESMGSEDML 289
Cdd:cd17642 121 FCSKKGLQ--KVLNVQKKL-------KIIKTIII---LDSKEDYKGYQC-LYTFITQNLPPGfneydfkPPSFDRDEQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 290 FMLYTSGSTGMPKGIvhtqagyllyaALTHKLV---FDHQPGDIFGC-----VADIGWITGHS----YVVYGPLCNGATS 357
Cdd:cd17642 188 LIMNSSGSTGLPKGV-----------QLTHKNIvarFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 358 VL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVG- 433
Cdd:cd17642 257 VLmykFEEE-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 434 ---DSRCTLVDTwwqTGGICIAP----RPSEEGAeilpamaMRPFFGIVPVLMDEKGSVveGSNVSGALCISQawPGMAR 506
Cdd:cd17642 328 pgiRQGYGLTET---TSAILITPegddKPGAVGK-------VVPFFYAKVVDLDTGKTL--GPNERGELCVKG--PMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 507 TIYGDHQRFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 586
Cdd:cd17642 394 GYVNNPEATKALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248205 587 GEAAFAFivvkdsagdsdVVVQELKSMVATKIAKYaVPDEILVVKRL----------PKTRSGKVMRRLLRKI 649
Cdd:cd17642 472 GELPAAV-----------VVLEAGKTMTEKEVMDY-VASQVSTAKRLrggvkfvdevPKGLTGKIDRRKIREI 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-656 |
3.15e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 128.54 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK12316 518 EEQVERTPEAPALAF------GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED 275
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLS--------------------------QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 PvcAPE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVFDHQP-----GDIFGCVADIGWITGHsYVVYG 349
Cdd:PRK12316 646 E--NPGtELNPENLAYVIYTSGSTGKPKGAGNR------HRALSNRLCWMQQAyglgvGDTVLQKTPFSFDVSV-WEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE--- 426
Cdd:PRK12316 717 PLMSGARLVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEALPADAQEqvf 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 427 ---WLHRVV---GDSRCTLVDTWWQtggiCIaprpsEEGAEILPAMamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQA 500
Cdd:PRK12316 792 aklPQAGLYnlyGPTEAAIDVTHWT----CV-----EEGGDSVPIG--RPIANLACYILDANLEPVP-VGVLGELYLAGR 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 wpGMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 576
Cdd:PRK12316 860 --GLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 937
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 577 AVIGyphdIKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 656
Cdd:PRK12316 938 AVLA----VDGKQLVGYVVLESEGGD---WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
123-646 |
8.03e-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: 123.54 E-value: 8.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd12114 1 PDATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITfnqglrggrvvelkkiVDEAVKHCPTVQHVLVahrtdnkvhmgDLDVPLEQEMAKEDPVCAPEs 282
Cdd:cd12114 75 RREAILADAGARLVLT----------------DGPDAQLDVAVFDVLI-----------LDLDALAAPAPPPPVDVAPD- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 mgseDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVA----DIGwitghSYVVYGPLCNGATS 357
Cdd:cd12114 127 ----DLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 358 VLfestpvyPNAGR-----YW-ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRV 431
Cdd:cd12114 196 VL-------PDEARrrdpaHWaELIERHGVTLWNSVPALLEMLLDVLEAAQALL--PSLRLVLLSGDWIPLDLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 432 VGDSR------CTLVDTW--WQTggicIAPRPsEEGAEI-----LPAMAMRpffgivpvLMDEKGS-VVEGsnVSGALCI 497
Cdd:cd12114 267 APDARlislggATEASIWsiYHP----IDEVP-PDWRSIpygrpLANQRYR--------VLDPRGRdCPDW--VPGELWI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 498 SQAwpGMARTIYGDHQRFVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 575
Cdd:cd12114 332 GGR--GVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVAR 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248205 576 SAVIGYPHDikGEAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd12114 410 AVVVVLGDP--GGKRLAAFVVPDNDGTPI-APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-648 |
1.28e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 123.61 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 113 NCLDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 193 TVIFAGFSAESLAGRINDAKCKVVI---TFNQGLRGGRVVELK---KIVDEAVKHCPTVQHVLVAHRtDNKVHMGDLDvp 266
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchaDFPEHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 267 leqemaKEDPvcapesmgsedmLFMLYTSGSTGMPKGIV--HTQAGYLLyaalTHKLVfDHQPGdifgcvadigwITGH- 343
Cdd:PRK07470 162 ------HDDP------------CWFFFTSGTTGRPKAAVltHGQMAFVI----TNHLA-DLMPG-----------TTEQd 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 344 -SYVVyGPL---------CN---GATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSL 410
Cdd:PRK07470 208 aSLVV-APLshgagihqlCQvarGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 411 RTLGSVGEPINCEAWEWLHRVVGDsrcTLVdtwwQ-------TGGICIAPrPSEEGAEILPAMAM----RPFFGIVPVLM 479
Cdd:PRK07470 283 RYVIYAGAPMYRADQKRALAKLGK---VLV----QyfglgevTGNITVLP-PALHDAEDGPDARIgtcgFERTGMEVQIQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 480 DEKGSVVeGSNVSGALCISqawpGMArtIYGDHQRFVDAYFKAYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRL 558
Cdd:PRK07470 355 DDEGREL-PPGETGEICVI----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 559 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 638
Cdd:PRK07470 428 YPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA---PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGY 504
|
570
....*....|
gi 358248205 639 GKVMRRLLRK 648
Cdd:PRK07470 505 GKITKKMVRE 514
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-647 |
1.55e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 123.17 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK06188 22 LKRYPDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVItFNQGLRGGRVVELkkivdeaVKHCPTVQHVLVahrtdnkvhMGDLD--VPLEQEMAKEDP 276
Cdd:PRK06188 96 GSLDDHAYVLEDAGISTLI-VDPAPFVERALAL-------LARVPSLKHVLT---------LGPVPdgVDLLAAAAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 277 VCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALthklvfdhqpgdifgCVADIGWITGHSYVVYGPLCNGAt 356
Cdd:PRK06188 159 APLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI---------------QLAEWEWPADPRFLMCTPLSHAG- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 svlfeSTPVYP--------------NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN- 421
Cdd:PRK06188 223 -----GAFFLPtllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 ---CEAwewlHRVVGDsrcTLVDTWWQT-GGICIAPRPSEEGAEILPAM---AMRPFFGIVPVLMDEKGSVVEGSNVsGA 494
Cdd:PRK06188 296 vrlAEA----IERFGP---IFAQYYGQTeAPMVITYLRKRDHDPDDPKRltsCGRPTPGLRVALLDEDGREVAQGEV-GE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 495 LCISQawPGMArtiygdhqrfvDAYFKAyP---------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 565
Cdd:PRK06188 368 ICVRG--PLVM-----------DGYWNR-PeetaeafrdGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVED 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 566 AIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 645
Cdd:PRK06188 434 VLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP---GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKA 510
|
..
gi 358248205 646 LR 647
Cdd:PRK06188 511 LR 512
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
115-331 |
1.82e-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: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFNQGLrggrvveLKKiVDEAVKHCPTVQHVLVAhrtDNKVHMGDLDV-PLEQEMAK 273
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVL---DPRGLRDDPRLlSLDELLAL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 274 EDPVCAPE-------SMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIF 331
Cdd:COG1022 164 GREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRT 227
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
117-648 |
2.26e-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: 123.12 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 197 A---GFSAESLAGRINDAKCKVVITfnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHrTDNKvhmgDLDVPleqemak 273
Cdd:cd05931 80 PptpGRHAERLAAILADAGPRVVLT---------TAAALAAVRAFAASRPAAGTPRLLV-VDLL----PDTSA------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 eDPVCAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFG----CVADIGWITGhsyvVYG 349
Cdd:cd05931 139 -ADWPPP-SPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCNGATSVLFEstpvyPNA-----GRYWETVERLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPINC 422
Cdd:cd05931 212 PLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 423 EAwewLHR-------------------------------VVGDSRCTLVDTWWQTGGICIAPRPSEEGAEILPAMAmRPF 471
Cdd:cd05931 286 AT---LRRfaeafapfgfrpeafrpsyglaeatlfvsggPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVSCG-RPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 472 FGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDhQRFVDAYFKAYP-----GYYFTGDGAYRTEGGYYqITGR 546
Cdd:cd05931 362 PDQEVRIVDPETGRELPDGEVGEIWVRG--PSVASGYWGR-PEATAETFGALAatdegGWLRTGDLGFLHDGELY-ITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 547 MDDVINISGHRLGTAEIEDAIAD-HPAVPESAVigyphdikgeAAFA---------FIVVKDSAGDSDVVVQELKSMVAT 616
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEaHPALRPGCV----------AAFSvpddgeerlVVVAEVERGADPADLAAIAAAIRA 507
|
570 580 590
....*....|....*....|....*....|....*.
gi 358248205 617 KIAK-YAV-PDEILVVKR--LPKTRSGKVMRRLLRK 648
Cdd:cd05931 508 AVAReHGVaPADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
138-648 |
2.64e-29 |
|
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: 122.02 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 tfnqglrggrvvelkkiVDEAvkhcptvqhvlvaHRTDNKVHMGDLDVPLEQemakedpvcaPESmgSEDMLFMLYTSGS 297
Cdd:cd12118 107 -----------------VDRE-------------FEYEDLLAEGDPDFEWIP----------PAD--EWDPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 298 TGMPKGIVHTQAG-YL--LYAALTHKLvfDHQPG-----DIFGCVadiGWItghsyVVYGPLCNGATSVLFESTpvypNA 369
Cdd:cd12118 145 TGRPKGVVYHHRGaYLnaLANILEWEM--KQHPVylwtlPMFHCN---GWC-----FPWTVAAVGGTNVCLRKV----DA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 370 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRS----------SLRTLGSVGE----------------PINCE 423
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRvhvmtagappPAAVLAKMEElgfdvthvygltetygPATVC 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 424 AW--EWlHRVVGDSRCTL-----VDTwwqtggiciaprPSEEGAEILPAMAMRPffgiVPVLMDEKGSVV-EGSNV-SGA 494
Cdd:cd12118 291 AWkpEW-DELPTEERARLkarqgVRY------------VGLEEVDVLDPETMKP----VPRDGKTIGEIVfRGNIVmKGY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 495 LCISQAwpgmartiygdhqrfVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 574
Cdd:cd12118 354 LKNPEA---------------TAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVL 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 575 ESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd12118 417 EAAVVARPDEKWGEVPCAFVELKEGA---KVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-677 |
3.85e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK12316 4561 ARMTPDAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITFNQGLRGGRVvelkkivdeavkhcPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAkedpvc 278
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRLPI--------------PDGLASLALDRDEDWEGFPAHD-PAVRLHP------ 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 apesmgsEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK--LVFDHQPGDIFGCVADIGWITGHSYV-------VYG 349
Cdd:PRK12316 4694 -------DNLAYVIYTSGSTGRPKG-----------VAVSHGslVNHLHATGERYELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCNGAtSVLFESTPVYPNAGRYWETVE-RLKINQFygAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPIN----CEA 424
Cdd:PRK12316 4756 PLINGA-SVVIRDDSLWDPERLYAEIHEhRVTVLVF--PPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAqasyDLA 4829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 425 WE-----WLHRVVGDSRCTLVDTWWQtggiciAPRPSEEGAEILPAMamRPFFGIVPVLMDEKGSV----VEGSNVSGAL 495
Cdd:PRK12316 4830 WRalkpvYLFNGYGPTETTVTVLLWK------ARDGDACGAAYMPIG--TPLGNRSGYVLDGQLNPlpvgVAGELYLGGE 4901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 496 CISQAW---PGMARtiygdhQRFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 571
Cdd:PRK12316 4902 GVARGYlerPALTA------ERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 572 AVPESAVIGYPHDIkGEAAFAFIVVKDSA-GDSDVV----VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:PRK12316 4976 AVREAVVIAQEGAV-GKQLVGYVVPQDPAlADADEAqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
570 580 590
....*....|....*....|....*....|....*
gi 358248205 647 RKIITSEAQE--LGDTTTLED--PSIIAEILSVYQ 677
Cdd:PRK12316 5055 PQPDASLLQQayVAPRSELEQqvAAIWAEVLQLER 5089
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
117-652 |
4.63e-29 |
|
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: 121.11 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakED 275
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLT-------------------------------------------------------SS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 PvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLLyAALTHKLVFDHQPGD--------IFG-CVADIgwitghsyv 346
Cdd:cd05918 105 P---------SDAAYVIFTSGSTGKPKGVVIEHRALST-SALAHGRALGLTSESrvlqfasyTFDvSILEI--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 347 vYGPLCNGAT------SVLFESTPvypnagrywETVERLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVG 417
Cdd:cd05918 166 -FTTLAAGGClcipseEDRLNDLA---------GFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 418 EPINCEAWE-WLHRVV-----GDSRCTLvdtwwqtGGICIAPRPSEEGAEILPAMAMRPFfgIV-PVLMDE---KGSVve 487
Cdd:cd05918 225 EALTQSDVDtWADRVRlinayGPAECTI-------AATVSPVVPSTDPRNIGRPLGATCW--VVdPDNHDRlvpIGAV-- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 488 gsnvsGALCISQawPGMARTIYGDHQR----FV-DAYFKAYPGY------YFTGDGAYRTEGGYYQITGRMDDVINISGH 556
Cdd:cd05918 294 -----GELLIEG--PILARGYLNDPEKtaaaFIeDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQ 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 557 RLGTAEIEDAIADHPAVPESAVIGY--PHDIKGEAAF-AFIVVKDSAGDSD--------------VVVQELKSMVATKIA 619
Cdd:cd05918 367 RVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLvAFVVLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRLP 446
|
570 580 590
....*....|....*....|....*....|...
gi 358248205 620 KYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 652
Cdd:cd05918 447 SYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
132-648 |
7.65e-29 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 121.40 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 132 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTVIFAGFsAESLAGRIND 210
Cdd:PRK06018 31 RSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 211 AKCKVVI---TFnqglrggrVVELKKIVDeavkHCPTVQHVLVAhrTDnKVHMGDLDVP----LEQEMAKEDPVCAPESM 283
Cdd:PRK06018 110 AEDRVVItdlTF--------VPILEKIAD----KLPSVERYVVL--TD-AAHMPQTTLKnavaYEEWIAEADGDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlvfdhqpGDIFGCVA-DI-----------GW-------ITGHS 344
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANN-------GDALGTSAaDTmlpvvplfhanSWgiafsapSMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 345 YVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPincea 424
Cdd:PRK06018 248 LVMPGAKLDGAS--------VY-------ELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 425 wEWLHRVVGDSRCTLVDTWWQT-----GGICIAPRPSEE--GAEILPAMAM--RPFFGIVPVLMDEKG-SVVEGSNVSGA 494
Cdd:PRK06018 308 -RSMIKAFEDMGVEVRHAWGMTemsplGTLAALKPPFSKlpGDARLDVLQKqgYPPFGVEMKITDDAGkELPWDGKTFGR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 495 LCISQawPGMARTIYGDHQRFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 574
Cdd:PRK06018 387 LKVRG--PAVAAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 575 ESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK06018 460 EAAVIGVYHPKWDERPLLIVQLKP---GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
112-648 |
9.34e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 121.04 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 112 VNCLDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 192 HTVIFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVELKKIVDEAVkhcPTVQHVLVA-HRTDNKVhmgdldVPLEQE 270
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT------EAALAPVATAVRDIV---PLLSTVVVAgGSSDDSV------LGYEDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 271 MAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDifgcvaDIGWITGHSYVVYGp 350
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGADINS------DVGFVGVPLFHIAG- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCNGATSVLFESTPV-YP----NAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSsLRTLGSVGEPinceAW 425
Cdd:PRK07786 231 IGSMLPGLLLGAPTViYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAP----AS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 426 EWLHRVVGDS--RCTLVDTWWQT----------GGICIAPRPSEegAEILPAMAMRpffgIVPVLMDE--KGSVVEgsnv 491
Cdd:PRK07786 304 DTLLRQMAATfpEAQILAAFGQTemspvtcmllGEDAIRKLGSV--GKVIPTVAAR----VVDENMNDvpVGEVGE---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 492 sgalcISQAWPGMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 571
Cdd:PRK07786 374 -----IVYRAPTLMSGYWNNPEATAEAF---AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHP 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 572 AVPESAVIGYPHDIKGEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK07786 446 DIVEVAVIGRADEKWGEVPVAVAAVRN--DDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
116-648 |
1.46e-28 |
|
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: 118.95 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALiwerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKED 275
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLLTTD---------------------------------------------------SPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 PVCApesmgsedmlfmLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGW--ITGhsyVVYGPLCN 353
Cdd:cd17653 107 LAYI------------IFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 354 GATSVLfeSTPVYPnagryWETVERlKINQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPinceawewlhrvvg 433
Cdd:cd17653 171 GGTLVL--ADPSDP-----FAHVAR-TVDALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEA-------------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 434 dsrCT--LVDTWWqtGGICI--APRPSEegAEILPAMA-MRPffgIVPV------------LMDE-KGSVVEGsnVSGAL 495
Cdd:cd17653 221 ---VPpsLLDRWS--PGRRLynAYGPTE--CTISSTMTeLLP---GQPVtigkpipnstcyILDAdLQPVPEG--VVGEI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 496 CISQawPGMARTIYGDHQRFVDAY--FKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADH 570
Cdd:cd17653 289 CISG--VQVARGYLGNPALTASKFvpDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQ 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 571 PAVPESAVIgyphdIKGEAAFAFIVvkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd17653 367 PEVTQAAAI-----VVNGRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
120-647 |
3.43e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 119.48 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 120 RKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 199
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 200 SAESLAGRINDAKCKVVItFNQglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKV-HMGDLDVPLEQEmakedpvc 278
Cdd:PRK13382 128 AGPALAEVVTREGVDTVI-YDE--------EFSATVDRALADCPQATRIVAWTDEDHDLtVEVLIAAHAGQR-------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 aPESMGSEDMLFMLyTSGSTGMPKGIVHTQAGyllyAALTHKLVFDHQPgdifgcvadigWITGHSYVVYGPL------C 352
Cdd:PRK13382 191 -PEPTGRKGRVILL-TSGTTGTPKGARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMfhawgfS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 353 NGATSVLFESTPVYPNAGRYWETVERLKINQFYG---APTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:PRK13382 254 QLVLAASLACTIVTRRRFDPEATLDLIDRHRATGlavVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 RVVGDsrcTLVDTWWQT--GGICIApRPSEEGAEilPAMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMART 507
Cdd:PRK13382 334 DQFGD---VIYNNYNATeaGMIATA-TPADLRAA--PDTAGRPAEGTEIRILDQDFREVP--------------TGEVGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 508 IYGDHQRFVDAYFKA-----YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP 582
Cdd:PRK13382 394 IFVRNDTQFDGYTSGstkdfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 583 HDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK13382 474 DEQYGQRLAAFVVLK---PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
118-655 |
6.74e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.99 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 118 HVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK09088 4 HARLQPQRLAAV----DLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 198 GFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKhcptvqhvlvAHRTDnkvhMGDLDVpLEQEMAKEDPV 277
Cdd:PRK09088 80 RLSASELDALLQDAEPRLLLG-----------------DDAVA----------AGRTD----VEDLAA-FIASADALEPA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 278 CAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT- 356
Cdd:PRK09088 128 DTP-SIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSi 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 --SVLFEstpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvkkYDRSSLRTLGSVgepinceawewlhrvvgd 434
Cdd:PRK09088 206 lvSNGFE-----PKRTLGRLGDPALGITHYFCVPQMAQAFRAQPG-----FDAAALRHLTAL------------------ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 435 srctlvdtwwQTGGiciAPRPSEEGAEILPA-MAMRPFFGivpvlMDEKGSVVeGSNVSGALCISQA------WPGMART 507
Cdd:PRK09088 258 ----------FTGG---APHAAEDILGWLDDgIPMVDGFG-----MSEAGTVF-GMSVDCDVIRAKAgaagipTPTVQTR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 508 IYGDHQRFVDAYFKA---------YPGYY---------FTGDGAYRT-------EGGYYQITGRMDDVINISGHRLGTAE 562
Cdd:PRK09088 319 VVDDQGNDCPAGVPGelllrgpnlSPGYWrrpqataraFTGDGWFRTgdiarrdADGFFWVVDRKKDMFISGGENVYPAE 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 563 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 642
Cdd:PRK09088 399 IEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA---PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQ 475
|
570
....*....|...
gi 358248205 643 RRLLRKIITSEAQ 655
Cdd:PRK09088 476 KARLRDALAAGRK 488
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
141-647 |
8.96e-28 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 118.20 E-value: 8.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 tfnqglrggrVVE-LKKIVDEAVKHCPtVQHVLVAHrtdnkvhMGDL-----------------DVP---LEQEMAKEDP 276
Cdd:PRK07059 126 ----------VLEnFATTVQQVLAKTA-VKHVVVAS-------MGDLlgfkghivnfvvrrvkkMVPawsLPGHVRFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 277 VCA-------PESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYL---LYAALTHKLVFDHQPGD---IFGCVADIgwitgh 343
Cdd:PRK07059 188 LAEgarqtfkPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPL------ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 344 sYVVYGPLCN-------GATSVLFestpvyPN----AGRYWEtVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR- 411
Cdd:PRK07059 262 -YHIFALTVCgllgmrtGGRNILI------PNprdiPGFIKE-LKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 412 TLG---SVGEPInceAWEWLHRV-------VGDSR------CTLVDTWWQTGGICIaPRPSEEgaeilpaMAMRpffgiv 475
Cdd:PRK07059 332 ANGggmAVQRPV---AERWLEMTgcpitegYGLSEtspvatCNPVDATEFSGTIGL-PLPSTE-------VSIR------ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 476 pvlmDEKGSVVEGSNVsGALCIS--QAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGR 546
Cdd:PRK07059 395 ----DDDGNDLPLGEP-GEICIRgpQVMAGywnrpdeTAKVMTAD-------------GFFRTGDVGVMDERGYTKIVDR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 547 MDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDE 626
Cdd:PRK07059 457 KKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA----LTEEDVKAFCKERLTNYKRPKF 532
|
570 580
....*....|....*....|.
gi 358248205 627 ILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK07059 533 VEFRTELPKTNVGKILRRELR 553
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
150-647 |
1.76e-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: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 150 TCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgfsaeslagRINDAKCKVVITFNQGLRGGRVV 229
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV---------PLNPTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 230 elkkIVDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQE--MAKEDPVCAPESMGsEDMLFMLYTSGSTGMPKGIV-- 305
Cdd:cd05922 74 ----LADAG----------AADRLRDALPASPDPGTVLDADgiRAARASAPAHEVSH-EDLALLLYTSGSTGSPKLVRls 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 306 HTQagyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfESTPVYPNAgrYWETVERLKINQFY 385
Cdd:cd05922 139 HQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 386 GAPTAVRLLLKYGdawVKKYDRSSLRTLGSVG-----EPIN--CEAWE-W-LHRVVGDSRCTLVdtwwqtggicIAPRPS 456
Cdd:cd05922 212 GVPSTYAMLTRLG---FDPAKLPSLRYLTQAGgrlpqETIArlRELLPgAqVYVMYGQTEATRR----------MTYLPP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 457 EEGAEILPAMAmRPFFGIVPVLMDEKGS----------VVEGSNVSGALCISQAWPGMARtiygdhqRFVDAYFkaypgy 526
Cdd:cd05922 279 ERILEKPGSIG-LAIPGGEFEILDDDGTptppgepgeiVHRGPNVMKGYWNDPPYRRKEG-------RGGGVLH------ 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 527 yfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIKGEAAFAFIVVKDSAGDSDVV 606
Cdd:cd05922 345 --TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVL 421
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248205 607 VqelksMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05922 422 R-----SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
286-647 |
9.01e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 111.99 E-value: 9.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 286 EDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFD--HQPGD------------------IFGCVADIGWITGHsy 345
Cdd:cd05917 2 DDVINIQFTSGTTGSPKG-----------ATLTHHNIVNngYFIGErlglteqdrlcipvplfhCFGSVLGVLACLTH-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 346 vvygplcnGATSVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAW 425
Cdd:cd05917 69 --------GATMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 426 EWLHRVVGDSRCTLVDTWWQTGGICIAPR---PSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS 498
Cdd:cd05917 136 KRVIEVMNMKDVTIAYGMTETSPVSTQTRtddSIEKRVNtvgrIMPHTEAK--------IVDPEGGIVPPVGVPGELCIR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 499 QAwpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 578
Cdd:cd05917 208 GY--SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 579 IGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05917 284 VGVPDERYGEEVCAWIRLKEGA---ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
122-646 |
1.11e-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: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 122 SPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 201
Cdd:cd17656 1 TPDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 202 ESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavkHCPTVQhvlvahrTDNKVHMgdldVPLEQEMAKEDPVCAPE 281
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQR--------------------HLKSKL-------SFNKSTI----LLEDPSISQEDTSNIDY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 282 SMGSEDMLFMLYTSGSTGMPKGIV--HTQAGYLLyaalthKLVFDHQPGDIFGCVADIgwiTGHSYVV-----YGPLCNG 354
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL------HFEREKTNINFSDKVLQF---ATCSFDVcyqeiFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 355 AT------------SVLFE-------STPVYPNAgrYWETV--ERLKINQFygaPTAVRLLLKYGDAWVKKydrsslRTL 413
Cdd:cd17656 195 GTlyiireetkrdvEQLFDlvkrhniEVVFLPVA--FLKFIfsEREFINRF---PTCVKHIITAGEQLVIT------NEF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 414 GSVGEPINCEawewLHRVVGDSRCTLVDTWwqtggiCIAPRPseEGAEiLPAMAmRPFFGIVPVLMDEKGSVVEgSNVSG 493
Cdd:cd17656 264 KEMLHEHNVH----LHNHYGPSETHVVTTY------TINPEA--EIPE-LPPIG-KPISNTWIYILDQEQQLQP-QGIVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 494 ALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 569
Cdd:cd17656 329 ELYISGA--SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLN 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 570 HPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17656 407 HPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
285-648 |
1.42e-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: 111.80 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 285 SEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAtSVLFESTP 364
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 365 VYPNAGRY---WETVERLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLV 440
Cdd:cd05944 79 GYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVELRARFEDATG---LPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 441 DTWWQTGGICIAPRPSEEGAEILPAMAMR-PFFGIVPVLMDEKGSVVE--GSNVSGALCIsqAWPGMAR-TIYGDHQRFV 516
Cdd:cd05944 151 EGYGLTEATCLVAVNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRdcAPDEVGEICV--AGPGVFGgYLYTEGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 517 DAYfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 596
Cdd:cd05944 229 FVA----DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 358248205 597 KDSAgdsDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05944 305 KPGA---VVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
115-652 |
2.58e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.03 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT 193
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEE------MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 194 VIFAGFSAESLAGRINDAKCKVVitFNQGLRGGRVVELKKIVdeavkhcpTVQHVlvahrtdnkVHMGDLDVPLEQEMAK 273
Cdd:PRK06839 82 PLNIRLTENELIFQLKDSGTTVL--FVEKTFQNMALSMQKVS--------YVQRV---------ISITSLKEIEDRKIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 EDPvcapesmGSEDMLFML-YTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLC 352
Cdd:PRK06839 143 FVE-------KNESASFIIcYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 353 NGATSVL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLH 429
Cdd:PRK06839 215 AGGVIIVprkFEPT-------KALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEE----LM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 RVVGDSRCTLVDTWWQTGGICIAPRPSEEGAEILPAMAMRP-FFGIVPVLMDEKGSVVEGS----NVSGALCISQAW--- 501
Cdd:PRK06839 282 REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPvLFCDYELIDENKNKVEVGEvgelLIRGPNVMKEYWnrp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 502 PGMARTIYGdhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 581
Cdd:PRK06839 362 DATEETIQD--------------GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGR 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248205 582 PHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 652
Cdd:PRK06839 428 QHVKWGEIPIAFIVKKSSS---VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
118-647 |
3.56e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 112.79 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 118 HVRKSPESVALIWErdEPGTEVriTYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK13390 6 HAQIAPDRPAVIVA--ETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 198 GFSAESLAGRINDAKCKVVITfnqglrggrVVELKKIVDEAVKHCPTvqHVLVAHRTDNkvhMGDLdvplEQEMAKEDPV 277
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVA---------SAALDGLAAKVGADLPL--RLSFGGEIDG---FGSF----EAALAGAGPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 278 CAPESMGSedmlFMLYTSGSTGMPKGIvhtqagyllYAALTHKLVfdHQPGDifGCVADIGWITGHSyvvygplcngATS 357
Cdd:PRK13390 144 LTEQPCGA----VMLYSSGTTGFPKGI---------QPDLPGRDV--DAPGD--PIVAIARAFYDIS----------ESD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 358 VLFESTPVYPNAGRYW-----------------------ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLG 414
Cdd:PRK13390 197 IYYSSAPIYHAAPLRWcsmvhalggtvvlakrfdaqatlGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 415 SVGEPinCEAwewlhrvvgDSRCTLVDtwWqTGGICIAPRPSEEgaeilpAMAMRpfFGIVPVLMDEKGSVveGSNVSGA 494
Cdd:PRK13390 277 HAAAP--CPV---------DVKHAMID--W-LGPIVYEYYSSTE------AHGMT--FIDSPDWLAHPGSV--GRSVLGD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 495 LCI-----SQAWPGMARTIY-----------GDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRL 558
Cdd:PRK13390 333 LHIcdddgNELPAGRIGTVYferdrlpfrylNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 559 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 638
Cdd:PRK13390 413 YPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPT 492
|
....*....
gi 358248205 639 GKVMRRLLR 647
Cdd:PRK13390 493 GKLVKGLLR 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-656 |
7.78e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.49 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVElkkivdeavkHCPTVQHVLVAhrtdnkvhmgDLDVPLEQEMAKE 274
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT------QAHLLE----------QLPAPAGDTAL----------TLDRLDLNGYSEN 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPvcAPESMGsEDMLFMLYTSGSTGMPKGI--------VHTQAGYLLYAALTHKLVFDHQPGDIFGCVADigwitghsyv 346
Cdd:PRK12467 3229 NP--STRVMG-ENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSFDGAQER---------- 3295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 347 VYGPLCNGATSVLfestpvypNAGRYW---ETV-----ERLKINQFygAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGE 418
Cdd:PRK12467 3296 FLWTLICGGCLVV--------RDNDLWdpeELWqaihaHRISIACF--PPAYLQQFAEDAGG----ADCASLDIYVFGGE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 419 PINCEAWEWLHRVV---------GDSRCTLVDTWWQTGGiciaprPSEEGAEILPamAMRPFFGIVPVLMDEKGSVVEgS 489
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGG------DAVCEAPYAP--IGRPVAGRSIYVLDGQLNPVP-V 3432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 490 NVSGALCIsqAWPGMARtiyGDHQ-------RFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTA 561
Cdd:PRK12467 3433 GVAGELYI--GGVGLAR---GYHQrpsltaeRFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 3507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 562 EIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:PRK12467 3508 EIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKV 3583
|
570
....*....|....*
gi 358248205 642 MRRLLRKIITSEAQE 656
Cdd:PRK12467 3584 DRKALPDPDAKGSRE 3598
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
118-647 |
1.12e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 111.13 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 118 HVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 198 GFSAESLAGRINDAKCKVVItfnqglrggrvvelkkiVDEAVKHCPTVQH---VLVAHRTDNKVHMGDLDVPleqemake 274
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETpkiVIDAAAQADSRRLAQGGLE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 dpvCAPESMGSEDMLF-MLYTSGSTGMPKGIVHTqagyllYAALTHKlVFDHqpgdifgcVADIGWITGHSYVVYGPLCN 353
Cdd:PRK06145 140 ---IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHS------YGNLHWK-SIDH--------VIALGLTASERLLVVGPLYH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 354 -GA-----TSVL-----------FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWvkKYDRSSLRTLGSV 416
Cdd:PRK06145 202 vGAfdlpgIAVLwvggtlrihreFDPEAVL-------AAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 417 GEPINCEAWEWLHRVVGDSRctLVDTWWQTGGiCIAPRPSEEGAEI---------LPAMAMRpffgivpvLMDEKGSVVE 487
Cdd:PRK06145 273 GEKTPESRIRDFTRVFTRAR--YIDAYGLTET-CSGDTLMEAGREIekigstgraLAHVEIR--------IADGAGRWLP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 488 gSNVSGALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 567
Cdd:PRK06145 342 -PNMKGEICMRG--PKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVI 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 568 ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK06145 416 YELPEVAEAAVIGVHDDRWGERITAVVVLNPGA---TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-655 |
1.14e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.72 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12467 1580 IEDQAAATPEAVALVF------GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVplEQEMAKE 274
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT--------------------------QSHLQARLPLPDGLRSLVLDQ--EDDWLEG 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPES-MGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH--QPGDIFGCVADIGWITGHSYV----- 346
Cdd:PRK12467 1706 YSDSNPAVnLAPQNLAYVIYTSGSTGRPKG-----------AGNRHGALVNRlcATQEAYQLSAADVVLQFTSFAfdvsv 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 347 --VYGPLCNGAtSVLFESTPVYPNAGRYWETVERLKI----------NQF------YGAPTAVRLLLKYGDAWVKKYDRS 408
Cdd:PRK12467 1775 weLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRP 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 409 SLRTLGSVGepinceawewLHRVVGDSRCTLVDTWWQtggiciAPRPSEEGAEILPamamrpffgIVPVLMDEKGSVVEG 488
Cdd:PRK12467 1854 WLERLPDTG----------LFNLYGPTETAVDVTHWT------CRRKDLEGRDSVP---------IGQPIANLSTYILDA 1908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 489 S------NVSGALCISQAwpGMARtiyGDH-------QRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINI 553
Cdd:PRK12467 1909 SlnpvpiGVAGELYLGGV--GLAR---GYLnrpaltaERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKI 1982
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 554 SGHRLGTAEIEDAIADHPAVPESAVIgyPHD-IKGEAAFAFIVVKDSAGDSDVVVQ-----ELKSMVATKIAKYAVPDEI 627
Cdd:PRK12467 1983 RGFRIELGEIEARLREQGGVREAVVI--AQDgANGKQLVAYVVPTDPGLVDDDEAQvalraILKNHLKASLPEYMVPAHL 2060
|
570 580
....*....|....*....|....*...
gi 358248205 628 LVVKRLPKTRSGKVMRRLLRKIITSEAQ 655
Cdd:PRK12467 2061 VFLARMPLTPNGKLDRKALPAPDASELQ 2088
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
142-648 |
1.26e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 111.61 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 222 glrGGRVVElkKIVDEAvkHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAK-----EDPVCAPesmgsedmlfmlYTSG 296
Cdd:PLN02246 129 ---QSCYVD--KLKGLA--EDDGVTVVTIDDPPEGCLHFSELTQADENELPEveispDDVVALP------------YSSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVhtqagyllyaaLTHK-LV-------------FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL--- 359
Cdd:PLN02246 190 TTGLPKGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpk 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 360 FEstpvypnAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHR-----VVGd 434
Cdd:PLN02246 259 FE-------IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKELEDAFRAklpnaVLG- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 435 srctlvdtwwQTGGIciaprpSEEGaeilPAMAM------RPFfgivPVLMDEKGSVVE---------------GSNVSG 493
Cdd:PLN02246 329 ----------QGYGM------TEAG----PVLAMclafakEPF----PVKSGSCGTVVRnaelkivdpetgaslPRNQPG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 494 ALCI--SQAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 564
Cdd:PLN02246 385 EICIrgPQIMKGylndpeaTANTIDKD-------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 565 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 644
Cdd:PLN02246 452 ALLISHPSIADAAVVPMKDEVAGEVPVAFVV---RSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRK 528
|
....
gi 358248205 645 LLRK 648
Cdd:PLN02246 529 DLRA 532
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
290-648 |
1.39e-25 |
|
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: 108.19 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 290 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVfdhqpgdifGCVADIGW--------ITGHSYVVYGPLCNGATSVLFE 361
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---------GFGGGDSWllslplyhVGGLAILVRSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 362 STPVYPNAGRYWETVERLkinqfygAPTAVRLLLKYG--DAWVKkydrsSLRTLGSVGEPINCEawewlhrvvgdsrctl 439
Cdd:cd17630 75 NQALAEDLAPPGVTHVSL-------VPTQLQRLLDSGqgPAALK-----SLRAVLLGGAPIPPE---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 440 vdtwwqtggicIAPRPSEEGAEILPAMAMRPFFGIV---PVLMDEKGSVveGSNVSGA-LCISQA---WPGMARTIYGDH 512
Cdd:cd17630 127 -----------LLERAADRGIPLYTTYGMTETASQVatkRPDGFGRGGV--GVLLPGReLRIVEDgeiWVGGASLAMGYL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 513 Q-RFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 591
Cdd:cd17630 194 RgQLVPEFNE--DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPV 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 592 AFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd17630 272 AVIV-----GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
119-646 |
1.41e-25 |
|
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: 110.88 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:cd17655 7 AEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKHcptvqhvlvahrtdNKVHMGDLDVpLEQEMAKEDPV- 277
Cdd:cd17655 81 YPEERIQYILEDSGADILLT-----------------QSHLQP--------------PIAFIGLIDL-LDEDTIYHEESe 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 278 -CAPESmGSEDMLFMLYTSGSTGMPKGIVHTQAG-------------------YLLYAALThklvFDHQPGDIFGCVadi 337
Cdd:cd17655 129 nLEPVS-KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankviyqgehlrVALFASIS----FDASVTEIFASL--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 338 gwITGHSYVVYG--PLCNGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLlkygdAWVKKYDRSSLRTLGS 415
Cdd:cd17655 201 --LSGNTLYIVRkeTVLDGQALT---------------QYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 416 VGEPINCE-AWEWLHR---------VVGDSRCTLVDTWWQtggiCIAPRPSEEGAEI-LPAMAMRPFfgivpvLMDEKGS 484
Cdd:cd17655 259 GGEALSTElAKKIIELfgtnptitnAYGPTETTVDASIYQ----YEPETDQQVSVPIgKPLGNTRIY------ILDQYGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 485 VV-EGsnVSGALCISQAwpGMARTiYGDH-----QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRL 558
Cdd:cd17655 329 PQpVG--VAGELYIGGE--GVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRI 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 559 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 638
Cdd:cd17655 404 ELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPN 478
|
....*...
gi 358248205 639 GKVMRRLL 646
Cdd:cd17655 479 GKVDRKAL 486
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-647 |
1.67e-25 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 110.74 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 121 KSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 200
Cdd:PRK07514 14 ADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 201 AESLAGRINDAKCKVVItfnqgLRGGRVVELKKIvdeAVKHcpTVQHV--LVAHRTDnkvhmgdldvPLEQEMAKEDPVC 278
Cdd:PRK07514 89 LAELDYFIGDAEPALVV-----CDPANFAWLSKI---AAAA--GAPHVetLDADGTG----------SLLEAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 APESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGD-------IFgcvadigwitgHSYVVY--- 348
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSH-GNLLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvat 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 349 -GPLCNGATSVL---FESTPV---YPNAgryweTVerlkinqFYGAPT-AVRLLlkyGDAWVKKYDRSSLRTLGSVGEPI 420
Cdd:PRK07514 217 nVALLAGASMIFlpkFDPDAVlalMPRA-----TV-------MMGVPTfYTRLL---QEPRLTREAAAHMRLFISGSAPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 421 NCEAwewlHRvvgdsrctlvdTWWQTGGICIAPR--PSE---------EGAEI-------LPAMAMR---PFFGiVPVLM 479
Cdd:PRK07514 282 LAET----HR-----------EFQERTGHAILERygMTEtnmntsnpyDGERRagtvgfpLPGVSLRvtdPETG-AELPP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 480 DEKGSV-VEGSNVsgalcisqawpgmartiygdhqrfvdayFKAY---P----------GYYFTGDGAYRTEGGYYQITG 545
Cdd:PRK07514 346 GEIGMIeVKGPNV----------------------------FKGYwrmPektaeefradGFFITGDLGKIDERGYVHIVG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 546 RMDDVInISG-HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvatKIAKYAV 623
Cdd:PRK07514 398 RGKDLI-ISGgYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAlDEAAILAALKG----RLARFKQ 472
|
570 580
....*....|....*....|....
gi 358248205 624 PDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK07514 473 PKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
123-646 |
1.68e-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: 110.03 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17652 1 PDAPAVVFG------DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapes 282
Cdd:cd17652 75 RIAYMLADARPALLLTT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 mgSEDMLFMLYTSGSTGMPKGIV--HTQAGYLLYAALTHklvFDHQPGDifgCVADIGWITGHSYV--VYGPLCNGATSV 358
Cdd:cd17652 92 --PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGS---RVLQFASPSFDASVweLLMALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 359 LFESTPVYPNAGrYWETVERLKINQFYGAPTAVrlllkygdAWVKKYDRSSLRTLGSVGEPINCE---AWEWLHRVV--- 432
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAAL--------AALPPDDLPDLRTLVVAGEACPAElvdRWAPGRRMInay 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 433 GDSRCTLVDTWwqtggiciaprpseegAEILPAMAM----RPFFGI-VPVLMDEKGSVVEGsnVSGALCIsqAWPGMART 507
Cdd:cd17652 235 GPTETTVCATM----------------AGPLPGGGVppigRPVPGTrVYVLDARLRPVPPG--VPGELYI--AGAGLARG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 508 iYGDH-----QRFVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 580
Cdd:cd17652 295 -YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVV 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248205 581 YPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17652 373 RDDRPGDKRLVAYVVPAPGAAPT---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-677 |
1.95e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.13 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK12316 3064 EEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDldvPLEQEMAKED 275
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLS--------------------------QSHLRLPLAQGVQVLDLD---RGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 PvcaPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNGA 355
Cdd:PRK12316 3189 P---AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 356 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCE------AWEWLH 429
Cdd:PRK12316 3264 RVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA----HRCTSLKRIVCGGEALPADlqqqvfAGLPLY 3338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 RVVGDSRCTLVDTWWQTggiciaprpSEEGAEILPAMamRPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMARtiy 509
Cdd:PRK12316 3339 NLYGPTEATITVTHWQC---------VEEGKDAVPIG--RPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR--- 3401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 510 GDHQR-------FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyp 582
Cdd:PRK12316 3402 GYHNRpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL--- 3478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 583 hDIKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDT 660
Cdd:PRK12316 3479 -AVDGRQLVAYVVPEDEAGD---LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdyVAPV 3554
|
570
....*....|....*....
gi 358248205 661 TTLED--PSIIAEILSVYQ 677
Cdd:PRK12316 3555 NELERrlAAIWADVLKLEQ 3573
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
140-647 |
2.46e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 110.57 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGAV-HTV---IFAgfsaESLAGRIN 209
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTInprLFP----EQIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 210 DAKCKVV---ITFnqglrggrvvelKKIVDEAVKHCPTVQHVLVAhrTDnKVHMGDLDVPL---EQEMAKEDPVCAPESM 283
Cdd:PRK07008 109 HAEDRYVlfdLTF------------LPLVDALAPQCPNVKGWVAM--TD-AAHLPAGSTPLlcyETLVGAQDGDYDWPRF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA---ALThklvfdhqpgDIFGCVA-DI-----------GW-------IT 341
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHRSTVLHAygaALP----------DAMGLSArDAvlpvvpmfhvnAWglpysapLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 342 GHSYVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSL-RTL--GSVGE 418
Cdd:PRK07008 244 GAKLVLPGPDLDGKS--------LY-------ELIEAERVTFSAGVPTVWLGLLNHMREAGLRF--STLrRTVigGSACP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 419 PINCEAWEwlhrvvGDSRCTLVDTWWQT-----GGICI-----APRPSEEGAEILPAMAmRPFFGIVPVLMDEKGSvveg 488
Cdd:PRK07008 307 PAMIRTFE------DEYGVEVIHAWGMTemsplGTLCKlkwkhSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGR---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 489 snvsgalciSQAWPGMArtiYGD-HQR---FVDAYFK--AYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLG 559
Cdd:PRK07008 376 ---------ELPWDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWIS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 560 TAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSG 639
Cdd:PRK07008 444 SIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATG 520
|
....*...
gi 358248205 640 KVMRRLLR 647
Cdd:PRK07008 521 KLQKLKLR 528
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
562-640 |
2.94e-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: 2.94e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 562 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 640
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
123-654 |
3.94e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 110.04 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPtVQHVLVAHRTDNK----VHMGDLDvpLEQEMAKEDPVC 278
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDT---------EFAEVAREALALLP-GPKPLVIDVDDPEypggRFIGALD--YEAFLASGDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 APESMGSE-DMLFMLYTSGSTGMPKGIV-HTQAGYLlyAALTHKLVFDHQPGDI-------FGCVadiGWitGHSYVVyg 349
Cdd:PRK08162 174 AWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL--NALSNILAWGMPKHPVylwtlpmFHCN---GW--CFPWTV-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 pLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDR----------------SSLRTL 413
Cdd:PRK08162 245 -AARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHpvhamvagaappaaviAKMEEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 414 G----------SVGEPINCEAW--EWlHRVVGDSRCTLvdTWWQtgGIciaPRPSEEGAEILPAMAMRPffgiVPVLMDE 481
Cdd:PRK08162 320 GfdlthvygltETYGPATVCAWqpEW-DALPLDERAQL--KARQ--GV---RYPLQEGVTVLDPDTMQP----VPADGET 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 482 KGSVVegsnVSGALCISQawpgmartiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISG-HRLGT 560
Cdd:PRK08162 388 IGEIM----FRGNIVMKG---------YLKNPKATEEAFAG--GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENISS 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 561 AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGK 640
Cdd:PRK08162 452 IEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAS---ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGK 527
|
570
....*....|....
gi 358248205 641 VMRRLLRKIITSEA 654
Cdd:PRK08162 528 IQKFVLREQAKSLK 541
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
138-649 |
9.73e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 108.69 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 TFNQGLrggrvvELKKIVDEAVKHCPTVqhVLVAHRTDNKVHMGDLDVPLEQEMAkedPVCAPESMGSeDMLFMLYTSGS 297
Cdd:PRK06155 124 VEAALL------AALEAADPGDLPLPAV--WLLDAPASVSVPAGWSTAPLPPLDA---PAPAAAVQPG-DTAAILYTSGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 298 TGMPKGIVHTQAGYLLYAALThklvfdhqpgdifgcVADIGWITGHSYVVYGPL-------------CNGATSVLfesTP 364
Cdd:PRK06155 192 TGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVL---EP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 365 VYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvKKYDR-SSLRTLGSVGEPINceawewLHRVVGDsRC--TLVD 441
Cdd:PRK06155 254 RF-SASGFWPAVRRHGATVTYLLGAMVSILLSQPA---RESDRaHRVRVALGPGVPAA------LHAAFRE-RFgvDLLD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 442 TW--WQTGGICIAPRPSEEgaeilPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPG-MARTIYGDHQRFVDA 518
Cdd:PRK06155 323 GYgsTETNFVIAVTHGSQR-----PGSMGRLAPGFEARVVDEHDQELP-DGEPGELLLRADEPFaFATGYFGMPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 519 YFKAYpgyYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD 598
Cdd:PRK06155 397 WRNLW---FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRD 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 358248205 599 -SAGDSDVVVQELKSMvatkIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 649
Cdd:PRK06155 474 gTALEPVALVRHCEPR----LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
115-655 |
1.01e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 108.54 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRksPESVALIW-ERdepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAaMLACARIGAVh 192
Cdd:PRK10946 31 LTRHAA--SDAIAVICgER-------QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYIT-FFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 193 tVIFAGFSAESL-----AGRINDAkckVVItfnqGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLDvpL 267
Cdd:PRK10946 100 -PVNALFSHQRSelnayASQIEPA---LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDD------GEHS--L 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 268 EQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlYAAlthklvfdHQPGDIFGCVADIGWI----TGH 343
Cdd:PRK10946 164 DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSV--------RRSVEICGFTPQTRYLcalpAAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 344 SYVVYGPlcnGATSVLFESTPVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLgSVG-- 417
Cdd:PRK10946 235 NYPMSSP---GALGVFLAGGTVVlapdPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL-QVGga 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 418 -----------EPINCEawewLHRVVGDSRcTLV------DTWWQ---TGGiciapRPSEEGAEILPAmamrpffgivpv 477
Cdd:PRK10946 311 rlsetlarripAELGCQ----LQQVFGMAE-GLVnytrldDSDERiftTQG-----RPMSPDDEVWVA------------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 478 lmDEKGS-VVEGSnvSGALcisqawpgMAR---TIYG-----DHQRFVdayFKAyPGYYFTGDGAYRTEGGYYQITGRMD 548
Cdd:PRK10946 369 --DADGNpLPQGE--VGRL--------MTRgpyTFRGyykspQHNASA---FDA-NGFYCSGDLVSIDPDGYITVVGREK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 549 DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagdsdvvvqELKSMVATK------IAKYA 622
Cdd:PRK10946 433 DQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE----------PLKAVQLRRflreqgIAEFK 502
|
570 580 590
....*....|....*....|....*....|...
gi 358248205 623 VPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 655
Cdd:PRK10946 503 LPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
151-647 |
1.02e-24 |
|
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: 108.23 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 151 CRLANTLKRHGVHRG----DRVAIYMPVSPLAvaamlacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrgg 226
Cdd:cd05929 12 FHQRRLLLLDVYSIAlnrnARAAAAEGVWIAD--------GVYIYLINSILTVFAAAAAWKCGACPAYKSSR-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 227 rvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvh 306
Cdd:cd05929 76 ---APRAEACAIIEIKAAALVCGLF--TGGGALDGLEDYEAAEGGSPETPI-EDEAAGWK----MLYSGGTTGRPKGI-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 307 tqagyllyaalthKLVFDHQPGD---IFGCVADIGWITGHSYVVYGPL-------------CNGATSVLFESTpvypNAG 370
Cdd:cd05929 144 -------------KRGLPGGPPDndtLMAAALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTLVLMEKF----DPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 371 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAW---EWLHrvvgdsrctlvdtWWqtG 447
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAP--CPPWvkeQWID-------------WG--G 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 448 GICIAPRPSEEGAeilpamamrpffGIVPVLMDE----KGSVveGSNVSGALCI-----SQAWPGMARTIYgdhqrFVDA 518
Cdd:cd05929 270 PIIWEYYGGTEGQ------------GLTIINGEEwlthPGSV--GRAVLGKVHIldedgNEVPPGEIGEVY-----FANG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 519 YFKAYPGYYF-------------TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDI 585
Cdd:cd05929 331 PGFEYTNDPEktaaarneggwstLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEE 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 586 KGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:cd05929 411 LGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-672 |
1.69e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 110.25 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK12467 522 ARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITFNQGLR------GGRVVELKKIVDEaVKHCPtvqhvlvAHRTDnkvhmgdldVPLEqema 272
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAqlpvpaGLRSLCLDEPADL-LCGYS-------GHNPE---------VALD---- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 273 kedpvcaPESMGsedmlFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWITGHsYVVYGPLC 352
Cdd:PRK12467 655 -------PDNLA-----YVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 353 NGATSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLHRVV 432
Cdd:PRK12467 721 SGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEAL---QVDLLARVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 433 GDS-RCTLVDTWWQT-GGICIAPRP-SEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARtiy 509
Cdd:PRK12467 793 ALGpGARLINHYGPTeTTVGVSTYElSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGA--GLAR--- 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 510 GDHQR-------FVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 581
Cdd:PRK12467 867 GYHRRpaltaerFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ 946
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 582 PHDiKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGD 659
Cdd:PRK12467 947 PGD-AGLQLVAYLVPAAVADGAEhqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFV 1025
|
570
....*....|...
gi 358248205 660 TTTLEDPSIIAEI 672
Cdd:PRK12467 1026 APQTELEKRLAAI 1038
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-660 |
1.85e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 107.97 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITFNqGLRGGRVVE-LKKIVDEaVKHC----------PTVQHVLvahRTDNKVHMGDL 263
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVAmLYELAPE-LATCepgqlqsarlPELRRVI---FLGDEKHPGML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 264 DVPLEQEMAKEDPVCAPESMGSE----DMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-------LVFDHQ---PGD 329
Cdd:PRK08315 173 NFDELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKG-----------ATLTHRnilnngyFIGEAMkltEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 330 ----------IFGCVadIGwitghsyvVYGPLCNGATSVlfestpvYPNAG----RYWETVERLKINQFYGAPTAVRLLL 395
Cdd:PRK08315 242 rlcipvplyhCFGMV--LG--------NLACVTHGATMV-------YPGEGfdplATLAAVEEERCTALYGVPTMFIAEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 396 KYGDawVKKYDRSSLRT---LGSVGePInceawEWLHRVVGD------------------SRCTLVDTwwqtggiCIAPR 454
Cdd:PRK08315 305 DHPD--FARFDLSSLRTgimAGSPC-PI-----EVMKRVIDKmhmsevtiaygmtetspvSTQTRTDD-------PLEKR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 455 PSEEGaEILPAMAMR---PFFG-IVPVlmdekgsvvegsNVSGALC-----ISQAWPGM----ARTIYGDhqrfvdayfk 521
Cdd:PRK08315 370 VTTVG-RALPHLEVKivdPETGeTVPR------------GEQGELCtrgysVMKGYWNDpektAEAIDAD---------- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 522 aypGYYFTGDGAYRTEGGYYQITGRMDDVI-----NISGhRlgtaEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 596
Cdd:PRK08315 427 ---GWMHTGDLAVMDEEGYVNIVGRIKDMIirggeNIYP-R----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIL 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 597 KDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQELGDT 660
Cdd:PRK08315 499 RP---GATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM---IEELGLQ 556
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-677 |
1.92e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.05 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 119 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 198
Cdd:PRK12316 2013 AARAPEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 199 FSAESLAGRINDAKCKVVITfnqglrggrvvelKKIVDEAVKhCPTVQHVLvahrtdnkvhmgDLDVPLEQEmakEDPVC 278
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT-------------QRHLLERLP-LPAGVARL------------PLDRDAEWA---DYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 279 APE-SMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHQPGDifgCVADIGWIT--GHSYVVYGPLCNGA 355
Cdd:PRK12316 2138 APAvQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 356 tSVLFESTPVYpNAGRYWETVER----------LKINQFY------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGep 419
Cdd:PRK12316 2214 -RVLIRDDELW-DPEQLYDEMERhgvtildfppVYLQQLAehaerdGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY-- 2289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 420 inceawewLHRVVGDSRCTLVDTWWQtggiciAPRPSEEGAEILPamamrpffgIVPVLMDEKGSVVEGS------NVSG 493
Cdd:PRK12316 2290 --------LFNGYGPTEAVVTPLLWK------CRPQDPCGAAYVP---------IGRALGNRRAYILDADlnllapGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 494 ALCISQAwpGMARTIYG----DHQRFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 568
Cdd:PRK12316 2347 ELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQ 2424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 569 DHPAVPESAVIGypHDIKGEAAFAFIVVKDSAGDSDvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK12316 2425 AHPAVREAVVVA--QDGASGKQLVAYVVPDDAAEDL--LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
570 580 590
....*....|....*....|....*....|...
gi 358248205 649 IITSEAQE--LGDTTTLED--PSIIAEILSVYQ 677
Cdd:PRK12316 2501 PDVSQLRQayVAPQEGLEQrlAAIWQAVLKVEQ 2533
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
142-643 |
1.21e-23 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 104.45 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 221
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 222 glrgGRVVELKKIVdeavkhcptvqhVLVAHRTdnkvhmgdldvpleqEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMP 301
Cdd:TIGR01923 78 ----DSLLEEKDFQ------------ADSLDRI---------------EAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 302 KGIVHTQAGYLLYA-ALTHKLVFDhqPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfestpVYPNAgRYWETVERLK 380
Cdd:TIGR01923 127 KAVPHTFRNHYASAvGSKENLGFT--EDDNWLLSLPLYHISGLS-ILFRWLIEGATLRI-----VDKFN-QLLEMIANER 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 381 INQFYGAPTAVRLLLKygdawvKKYDRSSLRTLGSVGEPINCEAWEwlhrvvgDSRCTLVDTWWQTGGICIAPRPSEEGA 460
Cdd:TIGR01923 198 VTHISLVPTQLNRLLD------EGGHNENLRKILLGGSAIPAPLIE-------EAQQYGLPIYLSYGMTETCSQVTTATP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 461 EILPAM--AMRPFFGI-VPVLMDEKGSVVEgsnvsgalcISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAYRTE 537
Cdd:TIGR01923 265 EMLHARpdVGRPLAGReIKIKVDNKEGHGE---------IMVKGANLMKG-YLYQGELTPAFEQQ--GWFNTGDIGELDG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 538 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATK 617
Cdd:TIGR01923 333 EGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-----SESDISQAKLIAYLTEK 407
|
490 500
....*....|....*....|....*.
gi 358248205 618 IAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:TIGR01923 408 LAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
141-648 |
1.35e-23 |
|
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: 103.97 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVvitfn 220
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTGM 300
Cdd:cd05912 77 -----------------------------------------------------------------DDIATIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGpLCNGATSVLFESTpvypNAGRYWETVERLK 380
Cdd:cd05912 92 PKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLINSGK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 381 INQFYGAPTAV-RLLLKYGDAWvkkydRSSLRT--LGsvGEPINCEAWEwlhrvvgdsRCTLVDT-WWQTGGIciaprpS 456
Cdd:cd05912 166 VTIISVVPTMLqRLLEILGEGY-----PNNLRCilLG--GGPAPKPLLE---------QCKEKGIpVYQSYGM------T 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 457 EEGAEIL---PAMAM-------RPFFG----IVPVLMDEKGS---VVEGSNVSGALcisqawpgMARTIYGDhQRFVDAY 519
Cdd:cd05912 224 ETCSQIVtlsPEDALnkigsagKPLFPvelkIEDDGQPPYEVgeiLLKGPNVTKGY--------LNRPDATE-ESFENGW 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 520 FKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkds 599
Cdd:cd05912 295 FK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV---- 363
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 358248205 600 aGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05912 364 -SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
141-647 |
5.64e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 103.96 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfN 220
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 QGLR----GGRVVELKKIVDEAVKHCPTvqhvlvahrtdnkvhmgDLdvpleqemakedpvcapESMGSEDMLFMLYTSG 296
Cdd:PRK06060 110 DALRdrfqPSRVAEAAELMSEAARVAPG-----------------GY-----------------EPMGGDALAYATYTSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfESTPVYPNAGRYWETv 376
Cdd:PRK06060 156 TTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 377 eRLKINQFYGAPTavrLLLKYGDAWVKKYDRSsLRTLGSVGEPINCEAWEWLHRV---------VGDSRC------TLVD 441
Cdd:PRK06060 234 -RFGPSVLYGVPN---FFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFfggipildgIGSTEVgqtfvsNRVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 442 TWwqtggiciapRPSEEGaEILPAMAMRPffgIVPvlmdekGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAyfk 521
Cdd:PRK06060 309 EW----------RLGTLG-RVLPPYEIRV---VAP------DGTTAGPGVEGDLWVRG--PAIAKGYWNRPDSPVAN--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 522 ayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG 601
Cdd:PRK06060 364 --EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAT 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 358248205 602 DSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK06060 442 IDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
115-648 |
8.32e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 103.03 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVELkkiVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKE 274
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIV------GEELVEA---FEEARADLARPPRLWVAGGDTLDDPEGYEDL---AAAAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPESMGS---EDMLFMLYTSGSTGMPKGIVHTQAGYLLY----AALThklvfDHQPGDIFGCVADIGWITGHSYVV 347
Cdd:PRK08279 185 APTTNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAmggfGGLL-----RLTPDDVLYCCLPLYHNTGGTVAW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 348 YGPLCNGATSVLFESTpvypNAGRYWETVERlkinqfYGApTAV-------RLLLkygDAWVKKYDRS-SLRTLgsVGEP 419
Cdd:PRK08279 260 SSVLAAGATLALRRKF----SASRFWDDVRR------YRA-TAFqyigelcRYLL---NQPPKPTDRDhRLRLM--IGNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 420 INCEAW-EWL-----HRVV---GDSRCTL----VDTWWQTGGICiaprpseegaeilPAMAMRPfFGIVPVlmD-EKGSV 485
Cdd:PRK08279 324 LRPDIWdEFQqrfgiPRILefyAASEGNVgfinVFNFDGTVGRV-------------PLWLAHP-YAIVKY--DvDTGEP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 486 VEGSNvsgALCI--SQAWPGMARTIYGDHQRFvDAY--------------FKayPG--YYFTGDGAYRTEGGYYQITGRM 547
Cdd:PRK08279 388 VRDAD---GRCIkvKPGEVGLLIGRITDRGPF-DGYtdpeasekkilrdvFK--KGdaWFNTGDLMRDDGFGHAQFVDRL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 548 DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVP 624
Cdd:PRK08279 462 GDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgTD--GRAGMAAIVLADGA---EFDLAALAAHLYERLPAYAVP 536
|
570 580
....*....|....*....|....
gi 358248205 625 DEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK08279 537 LFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
118-655 |
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 358248205 118 HVRKSPESVALIwERDEpgtevRITYRELLETTCRLANTLkRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 197
Cdd:PRK07638 10 HASLQPNKIAIK-ENDR-----VLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 198 GFSAESLAGRINDAKCKVVIT---FNQGLRG--GRVVELKKIvdeavkhcptvqhvlvahrtdnkvhMGDLDVPLEQEMA 272
Cdd:PRK07638 83 KWKQDELKERLAISNADMIVTeryKLNDLPDeeGRVIEIDEW-------------------------KRMIEKYLPTYAP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 273 KEDPVCAPESMGsedmlfmlYTSGSTGMPKGIVHTQAGYLL-YAALTHKLVFDHQ-----PGDIFgcvadigwitgHSYV 346
Cdd:PRK07638 138 IENVQNAPFYMG--------FTSGSTGKPKAFLRAQQSWLHsFDCNVHDFHMKREdsvliAGTLV-----------HSLF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 347 VYGplcngATSVLFESTPVY------PNAGRywETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEpi 420
Cdd:PRK07638 199 LYG-----AISTLYVGQTVHlmrkfiPNQVL--DKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISSGAK-- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 421 nceaWEwlhrvvGDSRCTLVDTW--------WQTGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEgsnvs 492
Cdd:PRK07638 265 ----WE------AEAKEKIKNIFpyaklyefYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQ----- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 493 galcisqawPGMARTIY-GDHQRFV----DAYFKAYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 564
Cdd:PRK07638 330 ---------KGEIGTVYvKSPQFFMgyiiGGVLARELnadGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 565 DAIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSAGdsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 644
Cdd:PRK07638 401 SVLHEHPAVDEIVVIGVPDSYWGEKPVA--IIKGSAT-----KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473
|
570
....*....|.
gi 358248205 645 LLRKIITSEAQ 655
Cdd:PRK07638 474 EAKSWIENQEK 484
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
112-656 |
2.22e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 101.62 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 112 VNCLDQHVRKSPESVALiwerDEPGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK05605 35 VDLYDNAVARFGDRPAL----DFFGAT--TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 192 ---HTVIFagfSAESLAGRINDAKCKVVITFN------QGLRGGrvVELKKIVD-EAVKHCPTVQHVLV------AHRTD 255
Cdd:PRK05605 109 vveHNPLY---TAHELEHPFEDHGARVAIVWDkvaptvERLRRT--TPLETIVSvNMIAAMPLLQRLALrlpipaLRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 256 NKVHMGDLD-VPLEQ----EMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHklvfdhqpGDI 330
Cdd:PRK05605 184 AALTGPAPGtVPWETlvdaAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKG-----------AQLTH--------RNL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 331 FGCVAD-IGWITG---------------HSY-----VVYGPLCnGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPT 389
Cdd:PRK05605 245 FANAAQgKAWVPGlgdgpervlaalpmfHAYgltlcLTLAVSI-GGELVLLPA----PDIDLILDAMKKHPPTWLPGVPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 390 AVRLLLKygDAWVKKYDRSSLRTL--GSVGEPIN-CEAWEWLhrvvgdsrctlvdtwwqTGGICIAPRPSEEGAEILPAM 466
Cdd:PRK05605 320 LYEKIAE--AAEERGVDLSGVRNAfsGAMALPVStVELWEKL-----------------TGGLLVEGYGLTETSPIIVGN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 467 AM----RPFFGIVPvLMDEKGSVVEGSNVSGALCISQAWPGMARtiygDHQRFvDAYFKA--------YPGYYFTGDGAY 534
Cdd:PRK05605 381 PMsddrRPGYVGVP-FPDTEVRIVDPEDPDETMPDGEEGELLVR----GPQVF-KGYWNRpeetaksfLDGWFRTGDVVV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 535 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMV 614
Cdd:PRK05605 455 MEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGA---ALDPEGLRAYC 531
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 358248205 615 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 656
Cdd:PRK05605 532 REHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
140-648 |
5.62e-22 |
|
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: 99.81 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 219
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKEDPVCAPesMGSEDMLFMLYTSGSTG 299
Cdd:cd05939 82 ------------------------------------------NLLDPLLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 300 MPKGIVHTQAGYLLYAALTHKlVFDHQPGDIFgcvadigWITGHSYVVYGPLCNGATSVLFESTPVYP---NAGRYWETV 376
Cdd:cd05939 118 LPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVV-------YDCLPLYHSAGGIMGVGQALLHGSTVVIRkkfSASNFWDDC 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 377 ERLK--INQFYGapTAVRLLLkygDAWVKKYD-RSSLRTLgsVGEPINCEAWEWLHRVVG-----------DSRCTLVDT 442
Cdd:cd05939 190 VKYNctIVQYIG--EICRYLL---AQPPSEEEqKHNVRLA--VGNGLRPQIWEQFVRRFGipqigefygatEGNSSLVNI 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 443 WWQTGGICIAPRpseegaeILPAMamrpfFGIVPVLMDE-KGSVVEGSNvsgALCISQAwPG-----MARTIYGDHQRFV 516
Cdd:cd05939 263 DNHVGACGFNSR-------ILPSV-----YPIRLIKVDEdTGELIRDSD---GLCIPCQ-PGepgllVGKIIQNDPLRRF 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 517 DAY--------------FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY- 581
Cdd:cd05939 327 DGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVe 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 582 -PHdIKGEAAFAFIVVKDSAGDSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05939 407 vPG-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
133-641 |
6.38e-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: 99.71 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 133 DEPGTEVriTYRELLETTCRLANTLKRhGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAK 212
Cdd:cd05909 2 DTLGTSL--TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 213 CKVVITFNQ-----GLRGGRVVEL-KKIVD-EAVKhcptvqhvlvahrtdNKVHMGD-LDVPLEQEMAKEDPV----CAP 280
Cdd:cd05909 79 IKTVLTSKQfieklKLHHLFDVEYdARIVYlEDLR---------------AKISKADkCKAFLAGKFPPKWLLrifgVAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 281 ESmgSEDMLFMLYTSGSTGMPKGIVHTQAGYL--LYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSV 358
Cdd:cd05909 144 VQ--PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 359 LfestpvYPNAGRYW---ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVGEPINC---EAWEWLHRVV 432
Cdd:cd05909 219 F------HPNPLDYKkipELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGIR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 433 -----GDSRCTLVDTwwqtggICIAPRPSEEGA--EILPAMAMR--PFFGIVPVLMDEKGSV-VEGSNV-SGALcisqAW 501
Cdd:cd05909 289 ilegyGTTECSPVIS------VNTPQSPNKEGTvgRPLPGMEVKivSVETHEEVPIGEGGLLlVRGPNVmLGYL----NE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 502 PGMARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH-PAVPESAVIG 580
Cdd:cd05909 359 PELTSFAFGD-------------GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVS 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248205 581 YPHDIKGEAAFAFIVvkDSAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:cd05909 426 VPDGRKGEKIVLLTT--TTDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
140-647 |
1.26e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 99.00 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 219
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 NQGLRGgrvveLKKIVDEAVK--HCPTVQHVLVAHRTDN---KVHMGDLDvpLEQEMAKEDPVCAPESMGSEDMLfmlYT 294
Cdd:PRK12406 91 ADLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISPallTPPAGAID--WEGWLAQQEPYDGPPVPQPQSMI---YT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 295 SGSTGMPKGiVHTQAGYLLYAALTHKLVfdhqpGDIFgcvadiGWITGHSYVVYGPlcngatsvLFESTP-VYP-NAGRY 372
Cdd:PRK12406 161 SGTTGHPKG-VRRAAPTPEQAAAAEQMR-----ALIY------GLKPGIRALLTGP--------LYHSAPnAYGlRAGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 373 WET---------------VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAwewlhrvvgDSRC 437
Cdd:PRK12406 221 GGVlvlqprfdpeellqlIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAP--CPA---------DVKR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 438 TLVDtWW-----------QTGGICIAprpSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISqawPGMAR 506
Cdd:PRK12406 290 AMIE-WWgpviyeyygstESGAVTFA---TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI---AGNPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 507 TIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIGYP 582
Cdd:PRK12406 363 FTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMV-ISG---GVniypAEIEAVLHAVPGVHDCAVFGIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248205 583 HDIKGEAAFAFIVVKDSAG-DSDVVVQELKSMVatkiAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK12406 437 DAEFGEALMAVVEPQPGATlDEADIRAQLKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-644 |
1.44e-21 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 98.05 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 220
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakEDPvcapesmgsEDMLFMLYTSGSTGM 300
Cdd:cd05907 84 -----------------------------------------------------EDP---------DDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnagrywETVERLK 380
Cdd:cd05907 102 PKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL------DDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 381 INQFYGAPtavRLllkygdaWVKKYDRSSLRTLGSVGEPInceawewLHRVVGDsRCTLVdtwwQTGGICIAPR------ 454
Cdd:cd05907 175 PTVFLAVP---RV-------WEKVYAAIKVKAVPGLKRKL-------FDLAVGG-RLRFA----ASGGAPLPAEllhffr 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 455 ----PSEEG---AEILPAMAMRPFFGIVPvlmDEKGSVVEGSNV----SGALCISQawPGMARTIYGDHQRFVDAYFKay 523
Cdd:cd05907 233 algiPVYEGyglTETSAVVTLNPPGDNRI---GTVGKPLPGVEVriadDGEILVRG--PNVMLGYYKNPEATAEALDA-- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 524 PGYYFTGDGAYRTEGGYYQITGRMDDVI-NISGHRLGTAEIEDAIADHPAVPESAVIG--YPH-----DIKGEAAFAFIV 595
Cdd:cd05907 306 DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgRPFlvaliVPDPEALEAWAE 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 596 VKDSAGDSDV-------VVQELKSMV---------ATKIAKYAVPDEILVVKRLPKTRSGKVMRR 644
Cdd:cd05907 386 EHGIAYTDVAelaanpaVRAEIEAAVeaanarlsrYEQIKKFLLLPEPFTIENGELTPTLKLKRP 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
291-643 |
1.69e-21 |
|
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: 96.03 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 291 MLYTSGSTGMPKGIV--HTQAgYLLYAALthklvfdhqpgdifgcvADIGWIT-GHSYVVYGPLCN------GATSVLFE 361
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAAW-----------------ADCADLTeDDRYLIINPFFHtfgykaGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 362 STPVYPNA----GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrc 437
Cdd:cd17638 67 GATVVPVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 438 TLVDTWWQTGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNV-SGALCISQAwpgMARTIYGDhqrfv 516
Cdd:cd17638 143 TVLTAYGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIADDGEVLVRGYNVmQGYLDDPEA---TAEAIDAD----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 517 dayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 596
Cdd:cd17638 215 --------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 358248205 597 KDSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:cd17638 287 RPGVTlTEEDVIAWCRE----RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
287-643 |
1.81e-21 |
|
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: 95.94 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 287 DMLFMLYTSGSTGMPKGIVHTQAGYLLYaalthklvFDHQPGDIFGCVADIGWITG---HSYVVYGplcngATSVLFEST 363
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYG-----AISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 364 PVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctL 439
Cdd:cd17633 68 TFIgqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKNIFPKAN--L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 440 VDTWWQTGGICIAPRPSEEGAEilPAMAMRPFFGIVPVLMDEKGSVVegsnvsGALCISQAwpgMARTIYgdhqrfVDAY 519
Cdd:cd17633 140 IEFYGTSELSFITYNFNQESRP--PNSVGRPFPNVEIEIRNADGGEI------GKIFVKSE---MVFSGY------VRGG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 520 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkds 599
Cdd:cd17633 203 FSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 358248205 600 aGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:cd17633 279 -GDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
124-649 |
6.23e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.20 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 124 ESVALIWER------DEPGTE---VRITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAVAAMLacaRIGA 190
Cdd:PRK12492 24 KSVVEVFERsckkfaDRPAFSnlgVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPnvlQYPIAVFGAL---RAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 191 VHTVIFAGFSAESLAGRINDAKCKVVITFNqgLRGGRVVELkkIVDEAVKHC---------PTVQHVLVAHRTDNKVHMg 261
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYLN--MFGKLVQEV--LPDTGIEYLieakmgdllPAAKGWLVNTVVDKVKKM- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 262 dldVP---LEQEMA-------KEDPVCAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTH-KLVFDHQpgDI 330
Cdd:PRK12492 176 ---VPayhLPQAVPfkqalrqGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKG-----------AMLTHgNLVANML--QV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 331 FGCVADIGwITGHsyvvygPLCNGATSVLFESTPVY------------------------P-NAGRYWETVERLKINQFY 385
Cdd:PRK12492 240 RACLSQLG-PDGQ------PLMKEGQEVMIAPLPLYhiyaftancmcmmvsgnhnvlitnPrDIPGFIKELGKWRFSALL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 386 GAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPI---NCEAWEWLhrvvgdSRCTLVDTWWQTGGICIA-PRPSEEGAE 461
Cdd:PRK12492 313 GLNTLFVALMDHPG--FKDLDFSALKLTNSGGTALvkaTAERWEQL------TGCTIVEGYGLTETSPVAsTNPYGELAR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 462 I------LPAMAMRpffgivpVLMDEKGSVVEGSNvsGALCIS--QAWPGMARTIYGDHQrFVDAyfkayPGYYFTGDGA 533
Cdd:PRK12492 385 LgtvgipVPGTALK-------VIDDDGNELPLGER--GELCIKgpQVMKGYWQQPEATAE-ALDA-----EGWFKTGDIA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 534 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSM 613
Cdd:PRK12492 450 VIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG----LSVEELKAY 525
|
570 580 590
....*....|....*....|....*....|....*.
gi 358248205 614 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 649
Cdd:PRK12492 526 CKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
115-646 |
6.38e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 98.70 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDakCKVVITFNQGLRGGRVvelkkivdeavkhcPTVQHVLVahrtdnkvhmgdldVPLEQEMAKE 274
Cdd:PRK05691 1211 LDPDYPAERLAYMLAD--SGVELLLTQSHLLERL--------------PQAEGVSA--------------IALDSLHLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKL-----VFDHQPGDIFGCVADIGWITGhSYVVY 348
Cdd:PRK05691 1261 WPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNT------HAALAERLqwmqaTYALDDSDVLMQKAPISFDVS-VWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 349 GPLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE-- 426
Cdd:PRK05691 1334 WPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA----AACTSLRRLFSGGEALPAELRNrv 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 427 -------WLHRVVGDSRCTLVDTWWQtggiCIAprpsEEGaEILPAMamRPFFGIVPVLMDEKGSVVEGSnVSGALCISQ 499
Cdd:PRK05691 1409 lqrlpqvQLHNRYGPTETAINVTHWQ----CQA----EDG-ERSPIG--RPLGNVLCRVLDAELNLLPPG-VAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AwpGMARTIYG----DHQRFV-DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 574
Cdd:PRK05691 1477 A--GLARGYLGrpalTAERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVA 1554
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248205 575 ESAVIgyphdIKGEAAFAFIVVKDSAGDS-DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:PRK05691 1555 QAAVL-----VREGAAGAQLVGYYTGEAGqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
116-646 |
7.59e-21 |
|
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: 95.96 E-value: 7.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITfnQGlrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemaked 275
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT--QP----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 pvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPgDIFGCVADIGWITGhSYVVYGPLCNGA 355
Cdd:cd17644 106 ----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 356 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINCEAWEWLHRVVGDs 435
Cdd:cd17644 174 TLVL-RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 436 RCTLVDTWWQTGG-----ICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYG 510
Cdd:cd17644 251 FIQLINVYGPTEAtiaatVCRLTQLTER--NITSVPIGRPIANTQVYILDENLQPVP-VGVPGELHIGGV--GLARGYLN 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 511 ----DHQRFVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 584
Cdd:cd17644 326 rpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQ 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248205 585 IKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17644 406 PGNKRLVAYIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
525-647 |
4.39e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 93.90 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 525 GYYFTGDGAYRTEGGYYQITGRMD-DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 603
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-----GAD 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 358248205 604 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
138-648 |
7.28e-20 |
|
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: 93.65 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 TFNqglrggrvvELKKIVDEAVKhcptvqhvLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSE-DMLFMLYTSG 296
Cdd:cd05915 102 FDP---------NLLPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVHTQAG-YLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEstpvYPNAGRYWET 375
Cdd:cd05915 164 TTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 376 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWL--HRVVGDSRCTLVdtwWQTGGICI-A 452
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIARFERmgVEVRQGYGLTET---SPVVVQNFvK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 453 PR----PSEEGAEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNVSgalCISQAWPGMARTIYGDHQRFVDAYFKAypGYY 527
Cdd:cd05915 317 SHleslSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPkDGKALG---EVQLKGPWITGGYYGNEEATRSALTPD--GFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 528 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVV 607
Cdd:cd05915 392 RTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELN 471
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 358248205 608 QELKSMVATkiaKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05915 472 EHLLKAGFA---KWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
116-646 |
7.48e-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: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 116 DQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemaked 275
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 pvcapesmGSEDMLFMLYTSGSTGMPKGI-VHTQAgyLLYAALTHKLVFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNG 354
Cdd:cd17645 102 --------NPDDLAYVIYTSGSTGLPKGVmIEHHN--LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 355 ATsvlfesTPVYPNAGRYweTVERLkiNQFYGAPTAVRLLLKYGDA-WVKKYDRSSLRTLGSVGEPINcEAWEWLHRVV- 432
Cdd:cd17645 171 AA------LHVVPSERRL--DLDAL--NDYFNQEGITISFLPTGAAeQFMQLDNQSLRVLLTGGDKLK-KIERKGYKLVn 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 433 --GDSRCTLVDTWWQTggiciapRPSEEGAEILPAMAMrpffgiVPVLMDEKGSVVEGSNVSGALCIsqAWPGMARTIYG 510
Cdd:cd17645 240 nyGPTENTVVATSFEI-------DKPYANIPIGKPIDN------TRVYILDEALQLQPIGVAGELCI--AGEGLARGYLN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 511 ----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 586
Cdd:cd17645 305 rpelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADG 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 587 GEAAFAFIVVKdsagdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:cd17645 385 RKYLVAYVTAP-----EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
112-647 |
7.66e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.58 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 112 VNCLDQHVRKSPESVALIwerdEPGtEVrITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAVAAMLacaR 187
Cdd:PRK08974 26 VDMFEQAVARYADQPAFI----NMG-EV-MTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPnllQYPIALFGIL---R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 188 IGAVHTVIFAGFSAESLAGRINDAKCK---VVITFNQglrggrvvELKKIVDE-AVKHC---------PTVQHVLV---- 250
Cdd:PRK08974 97 AGMIVVNVNPLYTPRELEHQLNDSGAKaivIVSNFAH--------TLEKVVFKtPVKHViltrmgdqlSTAKGTLVnfvv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 251 --AHRTDNKVHMGD-------LDVPLEQEMAKEDpvcapesMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHkl 321
Cdd:PRK08974 169 kyIKRLVPKYHLPDaisfrsaLHKGRRMQYVKPE-------LVPEDLAFLQYTGGTTGVAKG-----------AMLTH-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 322 vfdhqpGDIFGCVADIGWItghsyvvYGPLCNGATSVLFESTPVYP------NAGRYWE----------------TVERL 379
Cdd:PRK08974 229 ------RNMLANLEQAKAA-------YGPLLHPGKELVVTALPLYHifaltvNCLLFIElggqnllitnprdipgFVKEL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 380 KINQFYgAPTAVRLLLkygDAWV-----KKYDRSSLRTLGSVGEPIN---CEAWEWLhrvvgdSRCTLVDTWWQTggici 451
Cdd:PRK08974 296 KKYPFT-AITGVNTLF---NALLnneefQELDFSSLKLSVGGGMAVQqavAERWVKL------TGQYLLEGYGLT----- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 452 aprpseegaEILPAMAMRPF--------FGiVPV------LMDEKGSVVEGSNvSGALCIS--QAWPGmartiYGDHQRF 515
Cdd:PRK08974 361 ---------ECSPLVSVNPYdldyysgsIG-LPVpsteikLVDDDGNEVPPGE-PGELWVKgpQVMLG-----YWQRPEA 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 516 VDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 595
Cdd:PRK08974 425 TDEVIK--DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV 502
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 358248205 596 VKDSAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK08974 503 KKDPSLTEE----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
141-647 |
1.30e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 89.94 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLAN-TLKRHGVHRGDRVAIYMPVS---PLAVAAMLaCARIGAV------------HTVIFAGFSA--- 201
Cdd:PRK08751 51 ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNClqyPIATFGVL-RAGLTVVnvnplytprelkHQLIDSGASVlvv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 202 -----ESLAGRINDAKCKVVITfnQGLrgGRVVELKK--IVDEAVKHcptVQHVLVAHRTDNKVHMGD-LDVPLEQEMAK 273
Cdd:PRK08751 130 idnfgTTVQQVIADTPVKQVIT--TGL--GDMLGFPKaaLVNFVVKY---VKKLVPEYRINGAIRFREaLALGRKHSMPT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 EDpvcapesMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-LVFDHQPGDifgcvadiGWITGHS-------- 344
Cdd:PRK08751 203 LQ-------IEPDDIAFLQYTGGTTGVAKG-----------AMLTHRnLVANMQQAH--------QWLAGTGkleegcev 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 345 -------YVVYGPLCNGATSVLFE------STPvyPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLR 411
Cdd:PRK08751 257 vitalplYHIFALTANGLVFMKIGgcnhliSNP--RDMPGFVKELKKTRFTAFTGVNTLFNGLLN--TPGFDQIDFSSLK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 412 -TLGSvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTG---GICIAPRPSEE--GAEILPamamrpffgiVP----VLMDE 481
Cdd:PRK08751 333 mTLGG-GMAVQRSVAERWKQVTG---LTLVEAYGLTEtspAACINPLTLKEynGSIGLP----------IPstdaCIKDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 482 KGSVVEGSNVsGALCISQAwpgmaRTIYGDHQR------FVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISG 555
Cdd:PRK08751 399 AGTVLAIGEI-GELCIKGP-----QVMKGYWKRpeetakVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 556 HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPK 635
Cdd:PRK08751 468 FNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA----LTAEDVKAHARANLTGYKQPRIIEFRKELPK 543
|
570
....*....|..
gi 358248205 636 TRSGKVMRRLLR 647
Cdd:PRK08751 544 TNVGKILRRELR 555
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
130-648 |
1.33e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 89.84 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 130 WERDEPGTevrITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:PRK05620 31 WGGAEQEQ---TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 209 NDAKCKVVITFNQglrggrvveLKKIVDEAVKHCPTVQHVLVAHRTD---------NKVHMGDLDVPLEQEMAKEDPVCA 279
Cdd:PRK05620 108 NHAEDEVIVADPR---------LAEQLGEILKECPCVRAVVFIGPSDadsaaahmpEGIKVYSYEALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 280 PESMGSEdmlfMLYTSGSTGMPKGIVHT-QAGYLLYAALTHKLVFDHQPGDIFGCVADI-----------GWITGHSYVV 347
Cdd:PRK05620 179 DETTAAA----ICYSTGTTGAPKGVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPIyhvlswgvplaAFMSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 348 YGPLCNGAT--SVLFESTPvypnagrywetverlkiNQFYGAPTA-VRLLLKYGDawvKKYDRSSLRTL---GSVGEPIN 421
Cdd:PRK05620 255 PGPDLSAPTlaKIIATAMP-----------------RVAHGVPTLwIQLMVHYLK---NPPERMSLQEIyvgGSAVPPIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 CEAWEWLHRVvgdsrcTLVDTW--WQTGGICIAPRPSEeGAEILPAMAMRPFFGIVPVLMDEK----GSVVEGSN----- 490
Cdd:PRK05620 315 IKAWEERYGV------DVVHVWgmTETSPVGTVARPPS-GVSGEARWAYRVSQGRFPASLEYRivndGQVMESTDrnege 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 491 --VSGALCI-------SQAWPGMARTIYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTA 561
Cdd:PRK05620 388 iqVRGNWVTasyyhspTEEGGGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 562 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKF 546
|
....*..
gi 358248205 642 MRRLLRK 648
Cdd:PRK05620 547 DKKDLRQ 553
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
286-643 |
1.37e-18 |
|
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: 87.70 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 286 EDMLFMLYTSGSTGMPKGIVhtQAGYLLYAALTH--KLVFDHQPGDIFGCVADIGWITGHSYVvygplcngATSVLFEST 363
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVL--LANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWI--------LTCLIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 364 PVYPNAGRYWETVerLKINQFYGA------PTA---VRLLLKYGDAWVKKydrssLRTLGSVGE-PINCEA--WEWLHRV 431
Cdd:cd17635 71 CVTGGENTTYKSL--FKILTTNAVtttclvPTLlskLVSELKSANATVPS-----LRLIGYGGSrAIAADVrfIEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 432 VGDSRCTLVDTwwqTGGICIaprPSEEGAEILPAMAmRPFFGIVPVLMDEKG-SVVEGSNvsGALCISQAWpgMARTIYG 510
Cdd:cd17635 144 NTAQVYGLSET---GTALCL---PTDDDSIEINAVG-RPYPGVDVYLAATDGiAGPSASF--GTIWIKSPA--NMLGYWN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 511 DHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 590
Cdd:cd17635 213 NPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 358248205 591 FAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:cd17635 290 GLAVVA--SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
141-647 |
2.82e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 88.67 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAV-AAMlacaRIGAVHTVIFAGFSAESLAGRINDAKCKV 215
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPnvlQYPVAVfGAM----RAGLIVVNTNPLYTAREMEHQFNDSGAKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 216 VITF------------NQGLRGGRVVEL--------KKIVDEAVKHcptVQHVLVAHRTDNKVHMGDLdvpleQEMAKED 275
Cdd:PRK05677 126 LVCLanmahlaekvlpKTGVKHVIVTEVadmlpplkRLLINAVVKH---VKKMVPAYHLPQAVKFNDA-----LAKGAGQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 276 PVcAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-LVfdhqpGDIFGCVADIGWITGH-SYVVYGPL-- 351
Cdd:PRK05677 198 PV-TEANPQADDVAVLQYTGGTTGVAKG-----------AMLTHRnLV-----ANMLQCRALMGSNLNEgCEILIAPLpl 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 352 ---------CnGATSVLFESTPVYPNAGRYWETVERL---KINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEP 419
Cdd:PRK05677 261 yhiyaftfhC-MAMMLIGNHNILISNPRDLPAMVKELgkwKFSGFVGLNTLFVALCNNEA--FRKLDFSALKLTLSGGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 420 INCEAWEWLHRVVGdsrCTLVDTWWQTggiciaprpseegaEILPAMAMRPFFGI--------VP-----VLMDEKGSVV 486
Cdd:PRK05677 338 LQLATAERWKEVTG---CAICEGYGMT--------------ETSPVVSVNPSQAIqvgtigipVPstlckVIDDDGNELP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 487 EGSnvSGALCIS--QAWPGmartiYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 564
Cdd:PRK05677 401 LGE--VGELCVKgpQVMKG-----YWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 565 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 644
Cdd:PRK05677 473 DVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET---LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRR 549
|
...
gi 358248205 645 LLR 647
Cdd:PRK05677 550 ELR 552
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
285-640 |
2.87e-18 |
|
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: 87.05 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 285 SEDMLFMLYTSGSTGMPKGIVHTQA---GYLLYAALTHKLVFDHQPGDIFGCVADigwiTGHSYVVYGPLCNGA------ 355
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFTPSEDAHKAAAAA----AGTVMFPAPPLMHGTgswtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 356 TSVLFESTPVYP----NAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPIN 421
Cdd:cd05924 78 GGLLGGQTVVLPddrfDPEEVWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 CEAWEWLHRVVGDSrcTLVDTWW--QTGGICIApRPSEEGAEilpamaMRPFFGIVP--VLMDEKGSVVE-GSNVSGALc 496
Cdd:cd05924 148 PEVKQGLLELVPNI--TLVDAFGssETGFTGSG-HSAGSGPE------TGPFTRANPdtVVLDDDGRVVPpGSGGVGWI- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 497 isqAWPG-MARTIYGDHQRfVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 573
Cdd:cd05924 218 ---ARRGhIPLGYYGDEAK-TAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 574 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 640
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
117-646 |
5.81e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 87.76 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 197 AGFSAESLAgRINDAKCKVVITFNqglRGGRVvelkkivdeAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDP 276
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPAAALVA---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 277 vcapeSMGSEDMLFMLYTSGSTGMPKGIvhtqagyLLyaalthklvfdhqPGDIFGCVADI---------GWITGHSyvV 347
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAV-------LL-------------ANRTFFAVPDIlqkeglnwvTWVVGET--T 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 348 YGPLcnGATSVlfestpvypnAGRYW----------------------ETVERLKINQFYGAPTAVRLL---LKYGDAwv 402
Cdd:PRK05857 218 YSPL--PATHI----------GGLWWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLvseLKSANA-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 403 kkyDRSSLRTLGSVGEPINCEAWEWLHrvVGDSRCTLVDTWWQTG--GICIaPRPSEEGAEILPAMAMRPFFGIVPVLMD 480
Cdd:PRK05857 284 ---TVPSLRLVGYGGSRAIAADVRFIE--ATGVRTAQVYGLSETGctALCL-PTDDGSIVKIEAGAVGRPYPGVDVYLAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 481 EKGSVVEGSNVSGALCISQAW---PGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHR 557
Cdd:PRK05857 358 TDGIGPTAPGAGPSASFGTLWiksPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVN 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 558 LGTAEIEDAIADHPAVPESAVIGYPHDIKGeaAFAFIVVKDSAGDSDVVVQELKSMVATKIAK----YAVPDEILVVKRL 633
Cdd:PRK05857 435 IAPDEVDRIAEGVSGVREAACYEIPDEEFG--ALVGLAVVASAELDESAARALKHTIAARFRResepMARPSTIVIVTDI 512
|
570
....*....|...
gi 358248205 634 PKTRSGKVMRRLL 646
Cdd:PRK05857 513 PRTQSGKVMRASL 525
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
117-652 |
1.43e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.57 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAAMLACARIGavhtvI 195
Cdd:PLN02330 36 QDAELYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPnVAEYGIVALGIMAAGG-----V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRIND----AKCKVVITfnQGLRGGRVVELKkivdeavkhCPTVqhVLVAHRTDNKVHMGDLdvpLEQEM 271
Cdd:PLN02330 107 FSGANPTALESEIKKqaeaAGAKLIVT--NDTNYGKVKGLG---------LPVI--VLGEEKIEGAVNWKEL---LEAAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 272 AKEDPVcAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLvFDHQPgDIFGCVADIGWITG-HSYVVYGP 350
Cdd:PLN02330 171 RAGDTS-DNEEILQTDLCALPFSSGTTGISKGVMLTHRN--LVANLCSSL-FSVGP-EMIGQVVTLGLIPFfHIYGITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 351 LCngATsvlfestpvYPNAGRYwETVERLKINQFYGA------------PTAVRLLLKygDAWVKKYDRSSL--RTLGSV 416
Cdd:PLN02330 246 CC--AT---------LRNKGKV-VVMSRFELRTFLNAlitqevsfapivPPIILNLVK--NPIVEEFDLSKLklQAIMTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 417 GEPINCE---AWE------WLHRVVG--DSRCTLVDTWWQTGGICIAPRPSEegAEILPAMAMRpffgivpvLMDEKGSV 485
Cdd:PLN02330 312 AAPLAPElltAFEakfpgvQVQEAYGltEHSCITLTHGDPEKGHGIAKKNSV--GFILPNLEVK--------FIDPDTGR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 486 VEGSNVSGALCI-SQAwpgMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTA 561
Cdd:PLN02330 382 SLPKNTPGELCVrSQC---VMQGYYNNKEetdRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 562 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:PLN02330 454 ELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE---EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKI 530
|
570
....*....|.
gi 358248205 642 MRRLLRKIITS 652
Cdd:PLN02330 531 MRRLLKEKMLS 541
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
115-646 |
1.66e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.41 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 195 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkiVDEavkhcptvqhvlVAHRTDNkvhmGDLDVPLEQEMAKE 274
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLIT----------------TAD------------QLPRFAD----VPDLTSLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 275 DPVCAPESMGS-EDMLFMLYTSGSTGMPKGIVHTQagyllyAALTHKLVFDHqpgDIFGCVAD--IGWITGHSYVV---- 347
Cdd:PRK10252 586 PQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQ------TAIVNRLLWMQ---NHYPLTADdvVLQKTPCSFDVsvwe 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 348 -YGPLCNGATSVLFEstpvyPNAGRYWETVERL----KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGE--PI 420
Cdd:PRK10252 657 fFWPFIAGAKLVMAE-----PEAHRDPLAMQQFfaeyGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEalPA 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 421 N-CEAWEW-----LHRVVGDSRCTlVD-TWWQTGGICIAPRPSEE----------GAEILPAMaMRPffgiVPVlmdekg 483
Cdd:PRK10252 732 DlCREWQQltgapLHNLYGPTEAA-VDvSWYPAFGEELAAVRGSSvpigypvwntGLRILDAR-MRP----VPP------ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 484 svvegsNVSGALCIS--QawpgMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHR 557
Cdd:PRK10252 800 ------GVAGDLYLTgiQ----LAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQR 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 558 LGTAEIEDAIADHP----AVPESAVIGYPHDIKGEAA--FAFIVVKDSAG-DSDVvvqeLKSMVATKIAKYAVPDEILVV 630
Cdd:PRK10252 870 IELGEIDRAMQALPdveqAVTHACVINQAAATGGDARqlVGYLVSQSGLPlDTSA----LQAQLRERLPPHMVPVVLLQL 945
|
570
....*....|....*.
gi 358248205 631 KRLPKTRSGKVMRRLL 646
Cdd:PRK10252 946 DQLPLSANGKLDRKAL 961
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
138-649 |
6.02e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.69 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 TFNqglrggrvvELKKIVDEAVKHCPTVQH-----VLVAHRTDNKVHMGDLDVPLEQEMAKEDPvcAPESMGS------- 285
Cdd:PLN03102 117 VDR---------SFEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 286 EDMLFMLYTSGSTGMPKGIVHTQAGYLLyAALThkLVFDHQPG---------DIFGCVadiGWItghsyVVYGPLCNGAT 356
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYL-STLS--AIIGWEMGtcpvylwtlPMFHCN---GWT-----FTWGTAARGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 SVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLKyGD----------------------AWVKKYDRSSLRTLG 414
Cdd:PLN03102 255 SVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNsldlsprsgpvhvltggspppaALVKKVQRLGFQVMH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 415 SVGE-----PI-NCEaWEwlhrvvgdsrctlvDTWWQTggiciaprPSEEGAEILPAMAMRpFFGIVPVLMDEKG---SV 485
Cdd:PLN03102 330 AYGLteatgPVlFCE-WQ--------------DEWNRL--------PENQQMELKARQGVS-ILGLADVDVKNKEtqeSV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 486 VEGSNVSGALCISqawpgmARTIYGDHQRFVDAYFKAYP-GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 564
Cdd:PLN03102 386 PRDGKTMGEIVIK------GSSIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 565 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDS----AGDSDVVVQELKSMVA---TKIAKYAVPDEILVVKRLPKTR 637
Cdd:PLN03102 460 NVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGettkEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELPKNG 539
|
570
....*....|..
gi 358248205 638 SGKVMRRLLRKI 649
Cdd:PLN03102 540 NGKILKPKLRDI 551
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
130-648 |
1.18e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 83.58 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 130 WERDEPG---TEVRITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLA 205
Cdd:PRK07867 15 AEDDDRGlyfEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 206 GRINDAKCKVVITFNqglrggrvvelkkivdeavKHCPTVQHVlvahrtDNKVHMGDLDVPL-EQEMAKEDPVCAPESMG 284
Cdd:PRK07867 95 RDIAHADCQLVLTES-------------------AHAELLDGL------DPGVRVINVDSPAwADELAAHRDAEPPFRVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 285 SEDMLFMLY-TSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIfgCVADIGWItgHSYVV---YGP-LCNGATSVL 359
Cdd:PRK07867 150 DPDDLFMLIfTSGTSGDPKAVRCTH-RKVASAGVMLAQRFGLGPDDV--CYVSMPLF--HSNAVmagWAVaLAAGASIAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 360 ---FestpvypNAGRYWETVERlkinqfYGAPTA--VRLLLKYGDAWVKKYD--RSSLRTL-GSVGEPINCEAWEwlhRV 431
Cdd:PRK07867 225 rrkF-------SASGFLPDVRR------YGATYAnyVGKPLSYVLATPERPDdaDNPLRIVyGNEGAPGDIARFA---RR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 432 VGdsrCTLVDTWWQT-GGICIAPRPSEegaeilPAMAMRPFFGIVPVLMDEKGS-----------VVEGSNVSGALcISQ 499
Cdd:PRK07867 289 FG---CVVVDGFGSTeGGVAITRTPDT------PPGALGPLPPGVAIVDPDTGTecppaedadgrLLNADEAIGEL-VNT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWPGMARTIY----GDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 575
Cdd:PRK07867 359 AGPGGFEGYYndpeADAERMRG-------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 576 SAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:PRK07867 432 VAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
139-658 |
1.22e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 83.74 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 139 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 219 fNQglrggrvvELKKIVDEAVK---------HCPTVQHVLVAHRTDNKV---HMGDLDVPLEQEMAKEDPVCAPESMGSE 286
Cdd:PLN02479 124 -DQ--------EFFTLAEEALKilaekkkssFKPPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 287 -DMLFMLYTSGSTGMPKGIV-HTQAGYLLyaALTHKLVFDHQPGDI-------FGCVadiGWITGHSYVVygpLCngATS 357
Cdd:PLN02479 195 wQSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVylwtlpmFHCN---GWCFTWTLAA---LC--GTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 358 VLF---ESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWE------ 426
Cdd:PLN02479 265 ICLrqvTAKAIY-------SAIANYGVTHFCAAPVVLNTIVNApkSETILPLPRVVHVMTAGAAPPPSVLFAMSekgfrv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 427 ----WLHRVVGDSR-CTLVDTWWQTGGICIAPRPSE--------EGAEILPAMAMRPffgiVPVLMDEKGSVVEGSNVsg 493
Cdd:PLN02479 338 thtyGLSETYGPSTvCAWKPEWDSLPPEEQARLNARqgvryiglEGLDVVDTKTMKP----VPADGKTMGEIVMRGNM-- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 494 alcisqAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 573
Cdd:PLN02479 412 ------VMKGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 574 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRkiit 651
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKPGVDKSDeaALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR---- 553
|
....*..
gi 358248205 652 SEAQELG 658
Cdd:PLN02479 554 AKAKEMG 560
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
120-462 |
2.83e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 82.25 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 120 RKSPESVALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 196 FAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKivdEAVKHCPTVqhvlvahrtDNKVHMG--DLDvPLEQEMAK 273
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK---PSVRRLVTV---------GGRLLWGgtTLA-TLLRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 274 EDPVCAPesMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlyAALTH-KLVFDHQPGDIfgcvaDIgwitgHSY---VVYG 349
Cdd:PRK09274 164 APFPMAD--LAPDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEAlREDYGIEPGEI-----DL-----PTFplfALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 350 PLCnGATSVLFESTPVYP---NAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWE 426
Cdd:PRK09274 230 PAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 427 WLHRVVGD--------------------SRCTLVDTWWQT---GGICIApRPSeEGAEI 462
Cdd:PRK09274 307 RFRAMLPPdaeiltpygatealpissieSREILFATRAATdngAGICVG-RPV-DGVEV 363
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
520-651 |
5.75e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.81 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 520 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDS 599
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 358248205 600 AGDsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 651
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 |
9.24e-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: 9.24e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 58 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFStGKIGWFLGGQLNVSVNC 114
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
123-646 |
1.34e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 80.04 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK13383 49 PGRTAII---DDDGA---LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 203 SLAGRINDAKCKVVITFNQglrggrvvelkkIVDEAVKhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPES 282
Cdd:PRK13383 123 ALAAALRAHHISTVVADNE------------FAERIAG-------------ADDAVAVIDPATAGAEESGGRPAVAAPGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 283 MgsedmlfMLYTSGSTGMPKGIVHT---QAGYLLYAALTHKLVFDhqpgdifgcvadigwiTGHSYVVYGPLCNG---AT 356
Cdd:PRK13383 178 I-------VLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRLR----------------TGSRISVAMPMFHGlglGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 357 SVLFESTPVYPNAGRYWETVERL------KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHR 430
Cdd:PRK13383 235 LMLTIALGGTVLTHRHFDAEAALaqaslhRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 431 VVGDsrcTLVDTWWQTG-GICIAPRPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGmartiy 509
Cdd:PRK13383 315 TYGD---ILYNGYGSTEvGIGALATPAD--LRDAPETVGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAG------ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 510 gdhQRFVDAYFKAY-PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 588
Cdd:PRK13383 383 ---TRYTDGGGKAVvDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGH 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 589 AAFAFIVVKDSagdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:PRK13383 460 RLAAFVVLHPG---SGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
142-647 |
1.93e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 79.69 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLKrhGVHRGDR---VAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:PRK13388 28 TWREVLAEAAARAAALI--ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 219 fnqglrggrvvelkkivDEAvkHCPTVQHVLVAhrtdnKVHMGDLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGS 297
Cdd:PRK13388 106 -----------------DAE--HRPLLDGLDLP-----GVRVLDVDTPAYAELVAAAGALTPHReVDAMDPFMLIFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 298 TGMPKGIVHTQAGYLLYA-ALTHKlvFDHQPGDIFGCVADIGwitgHSYVVY---GP-LCNGATSVLfestPVYPNAGRY 372
Cdd:PRK13388 162 TGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPLF----HSNAVMagwAPaVASGAAVAL----PAKFSASGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 373 WETVerlkinQFYGAP--TAVRLLLKYGDAWVKKYDRS--SLRT-LGSVGEPINCEawEWLHRVvgdsRCTLVDTWWQTG 447
Cdd:PRK13388 232 LDDV------RRYGATyfNYVGKPLAYILATPERPDDAdnPLRVaFGNEASPRDIA--EFSRRF----GCQVEDGYGSSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 448 GICIAPRpsEEGAeilPAMAM-RPFFGIV-----------PVLMDEKGSVVEGSNVSGALcISQAWPGMARTIYGDH--- 512
Cdd:PRK13388 300 GAVIVVR--EPGT---PPGSIgRGAPGVAiynpetltecaVARFDAHGALLNADEAIGEL-VNTAGAGFFEGYYNNPeat 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 513 -QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 591
Cdd:PRK13388 374 aERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVM 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 592 AFIVVKDsagDSDVVVQELKSMVATK--IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 647
Cdd:PRK13388 447 AALVLRD---GATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
528-646 |
1.95e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.92 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 528 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfIVVKDSAGDSDvvv 607
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA-KVISHEEIDPV--- 369
|
90 100 110
....*....|....*....|....*....|....*....
gi 358248205 608 qELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 646
Cdd:PRK08308 370 -QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
522-653 |
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 358248205 522 AYPGYYFTGD-GAYrtEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsA 600
Cdd:PRK07824 231 AEPGWFRTDDlGAL--DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG---D 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 358248205 601 GDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSE 653
Cdd:PRK07824 306 GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
133-649 |
1.72e-14 |
|
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: 76.55 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 133 DEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAK 212
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 213 cKVVITFNQGL---RGGRVVELKKIVDEAVkhcptvqhvlvahrtdnkvHMGDLDVPLEQEMAKEDPVCAPESmGSEDML 289
Cdd:cd05906 112 -HIWQLLGSPVvltDAELVAEFAGLETLSG-------------------LPGIRVLSIEELLDTAADHDLPQS-RPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 290 FMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFgcvadIGW-----ITGHSYVVYGPLCNGATSVLFESTP 364
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 365 VYPNAGRYWETVERLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdsrctlv 440
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLL-------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 441 dtwwqtggiciaprpSEEGaeiLPAMAMRPFFGivpvlMDEKGSVVEGSNVSGALCISQAWPGMA--RTIYGDHQRFVDA 518
Cdd:cd05906 314 ---------------EPYG---LPPDAIRPAFG-----MTETCSGVIYSRSFPTYDHSQALEFVSlgRPIPGVSMRIVDD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 519 YFKAYP----------------GYY---------FTGDGAYRT------EGGYYQITGRMDDVINISGHRLGTAEIEDAI 567
Cdd:cd05906 371 EGQLLPegevgrlqvrgpvvtkGYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIVNGVNYYSHEIEAAV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 568 ADHPAVPESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAkyAVPDEILVVKR--LPKTRSGKV 641
Cdd:cd05906 451 EEVPGVEPSFTAAFAVRDPGaeteELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLPKeeIPKTSLGKI 528
|
....*...
gi 358248205 642 MRRLLRKI 649
Cdd:cd05906 529 QRSKLKAA 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
141-651 |
2.93e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 76.03 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDakCKVVITF 219
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVD--CSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 nqglrggrvvelkkIVDEAVKHCPTVQhVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGS 297
Cdd:PLN02574 145 --------------TSPENVEKLSPLG-VPVIGVPENYDFdSKRIEFPKFYELIKEDFDFVPKPvIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 298 TGMPKGIVHTQAGYL----LYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYW 373
Cdd:PLN02574 210 TGASKGVVLTHRNLIamveLFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 374 ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVgepiNCEAWEWLHRVVGD-----SRCTLVDTWWQTGG 448
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKK----AKGVCGEVLKSLKQV----SCGAAPLSGKFIQDfvqtlPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 449 ICIAPR--PSEEGAE------ILPAMAMRpffgivpVLMDEKGSVVEGSNvSGALCISQawPGMARTIYGDHQRFVDAYF 520
Cdd:PLN02574 358 TAVGTRgfNTEKLSKyssvglLAPNMQAK-------VVDWSTGCLLPPGN-CGELWIQG--PGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 521 KayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSA 600
Cdd:PLN02574 428 K--DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 358248205 601 GDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 651
Cdd:PLN02574 506 TLSQ---EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
138-646 |
7.56e-14 |
|
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: 74.40 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 TfnqglrggrvvelkkivdeavkhcptvqhvlvahrTDNkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGS 297
Cdd:cd05914 85 V-----------------------------------SDE-----------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 298 TGMPKGIVHTQAG----------YLLYAALTHKLVFdhQP-GDIFGCVADIgwitghsyvVYgPLCNGATSVLFESTP-- 364
Cdd:cd05914 101 TGNSKGVMLTYRNivsnvdgvkeVVLLGKGDKILSI--LPlHHIYPLTFTL---------LL-PLLNGAHVVFLDKIPsa 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 365 ---------VYPNAG--RYWETVERLK---INQFYGAPTAVRLLLKYGDAWVKKYDRSSL--------RTLGSVGEPINC 422
Cdd:cd05914 169 kiialafaqVTPTLGvpVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 423 EAWEWLHrvvgdsrctlvdtwwqTGGICIAprpseEG---AEILPAMAMRPFFGIVpvlMDEKGSVVEGSNVSGALCISQ 499
Cdd:cd05914 249 DVEEFLR----------------TIGFPYT-----IGygmTETAPIISYSPPNRIR---LGSAGKVIDGVEVRIDSPDPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 500 AWPG--------MARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINI-SGHRLGTAEIEDAIADH 570
Cdd:cd05914 305 TGEGeiivrgpnVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNM 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 571 PAVPESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYA-VPDEILVVKRLPKTRSGKVMRRL 645
Cdd:cd05914 383 PFVLESLVVVQEKKLVAlayiDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKRFL 462
|
.
gi 358248205 646 L 646
Cdd:cd05914 463 Y 463
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
117-646 |
2.74e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 117 QHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK05691 2196 AQAARTPQAPALTFAGQT------LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 197 AGFSAESLAGRINDAKCKVVITFNQGLRGgrvveLKKIVDEAVKHCPTVQHVLVAHRTDNKvhMGDLDVPLEQEmakedp 276
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEA-----LGELPAGVARWCLEDDAAALAAYSDAP--LPFLSLPQHQA------ 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 277 vcapesmgsedmlFMLYTSGSTGMPKGIVHTQAGYLLY-AALTHKlvFDHQPGDifgCVADIGWIT--GHSYVVYGPLCN 353
Cdd:PRK05691 2337 -------------YLIYTSGSTGKPKGVVVSHGEIAMHcQAVIER--FGMRADD---CELHFYSINfdAASERLLVPLLC 2398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 354 GATSVLfestpvypNAGRYWETVE--------RLKINQF---YGAPTAVRLllkygdawVKKYDRSSLRTLGSVGEPINC 422
Cdd:PRK05691 2399 GARVVL--------RAQGQWGAEEicqlireqQVSILGFtpsYGSQLAQWL--------AGQGEQLPVRMCITGGEALTG 2462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 423 EAWEWLHRVVGDSrcTLVDTWWQTGGI-----CIAPRPSEEGAEILP---AMAMRpffgiVPVLMDEKGSVVEgSNVSGA 494
Cdd:PRK05691 2463 EHLQRIRQAFAPQ--LFFNAYGPTETVvmplaCLAPEQLEEGAASVPigrVVGAR-----VAYILDADLALVP-QGATGE 2534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 495 LCISQAwpGMARtiyGDHQR-------FVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 566
Cdd:PRK05691 2535 LYVGGA--GLAQ---GYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESR 2609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 567 IADHPAVPESAVIGypHDIKGEAAFAFIVVKDSAGDSDVVVQEL----KSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 642
Cdd:PRK05691 2610 LLEHPAVREAVVLA--LDTPSGKQLAGYLVSAVAGQDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLD 2687
|
....
gi 358248205 643 RRLL 646
Cdd:PRK05691 2688 RRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
284-675 |
4.92e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.89 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 284 GSEDMLFMLYTSGSTGMPKGIVHTQAGYL-------LYAALTHKLVFDHQPGDIFgcvaDIG-WitghsYVVYGPLCNGA 355
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLnnqlskvPYLALSEADVIAQTASQSF----DISvW-----QFLAAPLFGAR 3937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 356 TSVLfestpvyPNA-----GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVkkydrSSLRTLGSVGEPINCE-AWEWLH 429
Cdd:PRK05691 3938 VEIV-------PNAiahdpQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL-----DGLRWMLPTGEAMPPElARQWLQ 4005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 R--------VVGDSRCT------LVDTWWQTGGICIAPRPSEEGaeilpamamRPFfgivpvLMDEKGSVVEGSNVsGAL 495
Cdd:PRK05691 4006 RypqiglvnAYGPAECSddvaffRVDLASTRGSYLPIGSPTDNN---------RLY------LLDEALELVPLGAV-GEL 4069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 496 CIsqAWPGMARTIYGDHQR----FVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 569
Cdd:PRK05691 4070 CV--AGTGVGRGYVGDPLRtalaFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE 4146
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 570 HPAVPESAViGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 649
Cdd:PRK05691 4147 QAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
410 420 430
....*....|....*....|....*....|.
gi 358248205 650 ITSEAQE---LGDTTTLED--PSIIAEILSV 675
Cdd:PRK05691 4226 DIGQLQSqayLAPRNELEQtlATIWADVLKV 4256
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
123-645 |
5.08e-13 |
|
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: 71.66 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGD-RVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 201
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 202 ESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcape 281
Cdd:cd17648 75 ERIQFILEDTGARVVIT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 282 smGSEDMLFMLYTSGSTGMPKGIVHTQAG-----------YLLYAALTHKL------VFDHQPGDIFgcvadIGWITGHS 344
Cdd:cd17648 92 --NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslserYFGRDNGDEAVlffsnyVFDFFVEQMT-----LALLNGQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 345 YVVYGPlcngatSVLFEStpvypnaGRYWETVERLKINQFYGAPTAVRLllkygdawvkkYD---RSSLRTLGSVGEPIN 421
Cdd:cd17648 165 LVVPPD------EMRFDP-------DRFYAYINREKVTYLSGTPSVLQQ-----------YDlarLPHLKRVDAAGEEFT 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 422 CEAWEWL-----------------------HRVVGDSRctlvdtwwQTGGICiapRPSEEGAEILPAMAMRPffgiVPVl 478
Cdd:cd17648 221 APVFEKLrsrfagliinaygptettvtnhkRFFPGDQR--------FDKSLG---RPVRNTKCYVLNDAMKR----VPV- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 479 mdekGSVveGSNVSGALCISQAW---PGMARtiygdhQRFVDAYFKA--------YPGYYFTGDGAYRTEGGYYQITGRM 547
Cdd:cd17648 285 ----GAV--GELYLGGDGVARGYlnrPELTA------ERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRN 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 548 DDVINISGHRLGTAEIEDAIADHPAVPESAVI-GYPHDIKGEAAFAFIV---VKDSAGDSDvvvQELKSMVATKIAKYAV 623
Cdd:cd17648 353 DFQVKIRGQRIEPGEVEAALASYPGVRECAVVaKEDASQAQSRIQKYLVgyyLPEPGHVPE---SDLLSFLRAKLPRYMV 429
|
570 580
....*....|....*....|...
gi 358248205 624 PDEILVVKRLPKTRSGKV-MRRL 645
Cdd:cd17648 430 PARLVRLEGIPVTINGKLdVRAL 452
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
140-648 |
4.35e-12 |
|
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: 68.92 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIfagfsaeslagrindakckvvitf 219
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 NQGLRGgrvvelkkivdEAVKHCPTV---QHVLVahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSG 296
Cdd:cd05940 59 NYNLRG-----------ESLAHCLNVssaKHLVV------------------------------------DAALYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVAdIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 376
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLP-LYHSTALIVGWSACLASGATLVIRKKF----SASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 377 --ERLKINQFYGapTAVRLLLKygdAWVKKYDRS-SLRTLgsVGEPINCEAWEWLHRVVGDSR-----------CTLVDT 442
Cdd:cd05940 167 rkYQATIFQYIG--ELCRYLLN---QPPKPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPRiaefyaategnSGFINF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 443 WWQTGGICIAPRPSEEGAEI----LPAMAMRPffgivpvLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQ----R 514
Cdd:cd05940 240 FGKPGAIGRNPSLLRKVAPLalvkYDLESGEP-------IRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAatekK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 515 FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAF 591
Cdd:cd05940 313 ILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAGM 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248205 592 AFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 648
Cdd:cd05940 391 AAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
125-361 |
7.26e-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: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 125 SVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAES 203
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 204 LAGRINDAKCKVVITFNQGLRGGRvvelkkivdEAVKHCPTVQHVLV-AHRTDNKVHMGDLD------------VPLEQE 270
Cdd:cd17632 132 LAPILAETEPRLLAVSAEHLDLAV---------EAVLEGGTPPRLVVfDHRPEVDAHRAALEsarerlaavgipVTTLTL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 271 MAKED------PVCAPESmgSEDMLFML-YTSGSTGMPKGIVHT--------------QAGYLLYAALTHKLVFDHQPGD 329
Cdd:cd17632 203 IAVRGrdlppaPLFRPEP--DDDPLALLiYTSGSTGTPKGAMYTerlvatfwlkvssiQDIRPPASITLNFMPMSHIAGR 280
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 358248205 330 IfgcvadigwitghsyVVYGPLCNGAT---------SVLFE 361
Cdd:cd17632 281 I---------------SLYGTLARGGTayfaaasdmSTLFD 306
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
141-331 |
1.16e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 67.83 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 QglrggrvvELKKIVDEAvKHCPTVQHVLVAHRTDNKVHMGDLDV--------PLEQEMAKEDPVcAPESMGSEDMLFML 292
Cdd:PLN02387 187 K--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGSsnwtvssfSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170 180 190
....*....|....*....|....*....|....*....
gi 358248205 293 YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF 331
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
142-648 |
2.14e-11 |
|
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: 66.69 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfn 220
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKEDPVCApesmgsedmlfMLYTSGSTGM 300
Cdd:cd05937 84 ---------------------------------------------------VDPDDPAI-----------LIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 301 PKGIVHTQAGYLLYAALTHKlVFDHQPGD-IFGCVA---DIGWITGHSYVVYGPLC------------------NGATSV 358
Cdd:cd05937 102 PKAAAISWRRTLVTSNLLSH-DLNLKNGDrTYTCMPlyhGTAAFLGACNCLMSGGTlalsrkfsasqfwkdvrdSGATII 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 359 LFE--------STP------------VYPNAGR--YWETV-ERL---KINQFYGAPTAVRLLLKYG-DAWvkkydrsslr 411
Cdd:cd05937 181 QYVgelcryllSTPpspydrdhkvrvAWGNGLRpdIWERFrERFnvpEIGEFYAATEGVFALTNHNvGDF---------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 412 TLGSVGE--PInceaWEWLHRvvGDSRCTLVDTwwQTGGICIAPR-------PSEEGAEILpamaMRPFFgivpvlmdek 482
Cdd:cd05937 251 GAGAIGHhgLI----RRWKFE--NQVVLVKMDP--ETDDPIRDPKtgfcvraPVGEPGEML----GRVPF---------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 483 gsvvegSNVSgalcisqAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 562
Cdd:cd05937 309 ------KNRE-------AFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTE 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 563 IEDAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAGD-SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 638
Cdd:cd05937 376 VADVLGAHPDIAEANVYGVKvpgHD--GRAGCAAITLEESSAVpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDN 453
|
570
....*....|
gi 358248205 639 GKVMRRLLRK 648
Cdd:cd05937 454 HKQQKGVLRD 463
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
138-680 |
5.96e-11 |
|
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: 65.07 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 217
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 218 TFNqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGS 297
Cdd:cd17640 83 VEN---------------------------------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 298 TGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIgWitgHSY---VVYGPLCNGAtSVLFESTPVYPN------ 368
Cdd:cd17640 100 TGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAYTSIRTLKDdlkrvk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 369 ------AGRYWETVERLKINQFYGAPTAVRLLLKYgdawvkkydrssLRTLGSVGEPINCeawewlhrvvGDSRCTLVDT 442
Cdd:cd17640 174 phyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGISG----------GGALPPHVDT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 443 WWQTGGICIAprpseEG---AEILPAMAMR------------PFFGIVPVLMDEKGSVVEGSNVSGALcisqawpgMARt 507
Cdd:cd17640 232 FFEAIGIEVL-----NGyglTETSPVVSARrlkcnvrgsvgrPLPGTEIKIVDPEGNVVLPPGEKGIV--------WVR- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 508 iyGDHqrFVDAYFK---------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESA 577
Cdd:cd17640 298 --GPQ--VMKGYYKnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIM 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 578 VIGypHDIKgeAAFAFIVvkdsaGDSDVVVQELKSmVATKIAKyaVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQEL 657
Cdd:cd17640 374 VVG--QDQK--RLGALIV-----PNFEELEKWAKE-SGVKLAN--DRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQI 441
|
570 580
....*....|....*....|...
gi 358248205 658 GDTTTLEDPSIIAEILSVYQKCK 680
Cdd:cd17640 442 APFALLEEPFIENGEMTQTMKIK 464
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
134-652 |
1.42e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.25 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIY--MPV--SPLAVAAMLACARIGAVHT----VIFAGFSAESLA 205
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVWAEDTLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 206 grindakckvVItfnqGLRGGRVVELKKIVDEAVkhcPTVQHVLVAHRTdnkvhMGDLDvpleqemaKEDPVcAPESMGS 285
Cdd:PRK07768 103 ----------VI----GMIGAKAVVVGEPFLAAA---PVLEEKGIRVLT-----VADLL--------AADPI-DPVETGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 286 EDMLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVFDHQPGDIFG---CVADIGWItGHSYVvygPLCNGATSVL 359
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGN--LYAnaeAMFVAAEFDVETDVMVSwlpLFHDMGMV-GFLTV---PMYFGAELVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 360 feSTPV-YPNAGRYWETVerlkINQFYGAPTA---------VRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLH 429
Cdd:PRK07768 226 --VTPMdFLRDPLLWAEL----ISKYRGTMTAapnfayallARRLRRQAKP--GAFDLSSLRFALNGAEPIDPADVEDLL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 430 R--------------VVGDSRCTLVDTWWQTGGiciAPRPSEEGAEILPAM---------AMRPFFGIVPVL-------M 479
Cdd:PRK07768 298 DagarfglrpeailpAYGMAEATLAVSFSPCGA---GLVVDEVDADLLAALrravpatkgNTRRLATLGPPLpglevrvV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 480 DEKGSV----------VEGSNVSgalcisqawPGMaRTIYGdHQRFVDAYfkaypGYYFTGDGAYRTEGGYYQITGRMDD 549
Cdd:PRK07768 375 DEDGQVlpprgvgvieLRGESVT---------PGY-LTMDG-FIPAQDAD-----GWLDTGDLGYLTEEGEVVVCGRVKD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 550 VINISGHRLGTAEIEDAIADHPAV-PESAV-IGYPHDIKGEaAFAfIVVKDSAGDSDVVVQELKSMVATKIAKyAV---P 624
Cdd:PRK07768 439 VIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE-GFA-VAVESNAFEDPAEVRRIRHQVAHEVVA-EVgvrP 515
|
570 580 590
....*....|....*....|....*....|
gi 358248205 625 DEILVVK--RLPKTRSGKVMRRLLRKIITS 652
Cdd:PRK07768 516 RNVVVLGpgSIPKTPSGKLRRANAAELVTP 545
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
286-652 |
1.49e-10 |
|
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: 64.05 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 286 EDMLFMLYTSGSTGMPKGIVHTQagyllyaaltHKLVFDhqpgdIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV 365
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVHN-----MFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 366 YPNAGRY-------------W-ETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPIN---CEAWEW 427
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDyelCHEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 428 LHRVVGDSRCTLVDTWW---QTGGICIAPrpseegaeilpamAMRPFFGIV----PVLMDEKGSVVEGSNVSGALCISQA 500
Cdd:cd05908 251 HMSKYGLKRNAILPVYGlaeASVGASLPK-------------AQSPFKTITlgrrHVTHGEPEPEVDKKDSECLTFVEVG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 WP---GMARTIYGDHQRFVDAYF--------KAYPGYY---------FTGDGAYRT------EGGYYQITGRMDDVINIS 554
Cdd:cd05908 318 KPideTDIRICDEDNKILPDGYIghiqirgkNVTPGYYnnpeatakvFTDDGWLKTgdlgfiRNGRLVITGREKDIIFVN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 555 GHRLGTAEIEDAIADHPAVP--ESAVIG-YPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVaTKIAKYAVpDEILVVK 631
Cdd:cd05908 398 GQNVYPHDIERIAEELEGVElgRVVACGvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHL-NKRGGWQI-NEVLPIR 475
|
410 420
....*....|....*....|.
gi 358248205 632 RLPKTRSGKVMRRLLRKIITS 652
Cdd:cd05908 476 RIPKTTSGKVKRYELAQRYQS 496
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
136-580 |
3.34e-10 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 62.87 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP------VSPLAVaaMLAcariGAVHTVIFAGFSAESLAGRIN 209
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 210 DAKCKVVITfnqglrgGRV---VELKKIVDEAVKHCPTVQH-VLVAHRT-DNKVHMGDldvPLEqemakEDPVCAPESMG 284
Cdd:cd05932 76 HSESKALFV-------GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 285 SedmlfMLYTSGSTGMPKGIVHTQA--GYLLYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFES 362
Cdd:cd05932 141 T-----LIYTSGTTGQPKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 363 TPVYPnagrywETVERLKINQFYGAPtavRLLLKYGDAWVKKYDRSSLRTLGSVgeP-INCEAWEWLHRVVGDSRCTLVd 441
Cdd:cd05932 213 LDTFV------EDVQRARPTLFFSVP---RLWTKFQQGVQDKIPQQKLNLLLKI--PvVNSLVKRKVLKGLGLDQCRLA- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 442 twwqtgGICIAPRPS-------EEGAEILPAMAMRPFFGIVPVlmdekgsVVEGSNVSGAlcISQAWPGMARTIYGDHQR 514
Cdd:cd05932 281 ------GCGSAPVPPallewyrSLGLNILEAYGMTENFAYSHL-------NYPGRDKIGT--VGNAGPGVEVRISEDGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 515 FVDAyfKA-YPGYY---------FTGDGAYRT-------EGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPES 576
Cdd:cd05932 346 LVRS--PAlMMGYYkdpeataeaFTADGFLRTgdkgeldADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMV 423
|
....
gi 358248205 577 AVIG 580
Cdd:cd05932 424 CVIG 427
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
132-641 |
4.13e-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: 62.49 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 132 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtviFAGFSAESLAGRInda 211
Cdd:cd17654 8 IDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQRS--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 212 kckvvitfnqglrggrvveLKKIVDEAVKHCPTVQHVLVA--HRTDNKVHMgdlDVPLEQEMAkedpvcapesmgsedml 289
Cdd:cd17654 81 -------------------LTVMKKCHVSYLLQNKELDNAplSFTPEHRHF---NIRTDECLA----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 290 FMLYTSGSTGMPKG-----------IVHTQAGYLLYAA----LTHKLVFDHQPGDIFGCVADIG-WITGHSYVVYGPLCn 353
Cdd:cd17654 122 YVIHTSGTTGTPKIvavphkcilpnIQHFRSLFNITSEdilfLTSPLTFDPSVVEIFLSLSSGAtLLIVPTSVKVLPSK- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 354 gATSVLFESTPVypnagryweTVERLkinqfygAPTavrLLLKYGDAWVKKYDRS---SLRTLGSVGE--PINCEAWEWL 428
Cdd:cd17654 201 -LADILFKRHRI---------TVLQA-------TPT---LFRRFGSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 429 HRVVGDSRC-----TLVDTWWQTGGICIAPRPSEEGAEILpamamrpffGIVPVLMDEKGSVVEGSNVSGAL---CISQA 500
Cdd:cd17654 261 GKGNRTRIFniygiTEVSCWALAYKVPEEDSPVQLGSPLL---------GTVIEVRDQNGSEGTGQVFLGGLnrvCILDD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 501 WPGMARTIYgdhqrfvdayfkaypgyYFTGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 580
Cdd:cd17654 332 EVTVPKGTM-----------------RATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTL 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248205 581 YphdiKGEAAFAFIVVKDSagdSDVVVQELksmVATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:cd17654 394 S----DQQRLIAFIVGESS---SSRIHKEL---QLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
525-643 |
6.26e-10 |
|
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: 61.13 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 525 GYYFTGDGAYRTEGGYYQITGRM--DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIK-GEAAFAFIVVKDSAG 601
Cdd:cd17637 216 GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPKwGEGIKAVCVLKPGAT 294
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 358248205 602 dsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:cd17637 295 ---LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
527-641 |
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 358248205 527 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDIKGEAAFA 592
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSYivPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 593 FIVVKDSAGDSDVVV----------QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
142-655 |
5.93e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.34 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 142 TYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQ 221
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKYSV-EGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 222 GLRGGRVVELKKIVDEAvkhcptvqhvlvahrtdNKVHMGDL--DVPLEQEMAKEDPVCAPE----SMGSEDMLFMLYTS 295
Cdd:PRK08043 312 FLDKGKLWHLPEQLTQV-----------------RWVYLEDLkdDVTTADKLWIFAHLLMPRlaqvKQQPEDAALILFTS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 296 GSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfestpvYPNAGRYwET 375
Cdd:PRK08043 375 GSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL------YPSPLHY-RI 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 376 VERLKINQ----FYGAPTavrLLLKYGdAWVKKYDRSSLRTLGSVGEPINCEAWE-WLH----RVV---GDSRCTLVDTW 443
Cdd:PRK08043 447 VPELVYDRnctvLFGTST---FLGNYA-RFANPYDFARLRYVVAGAEKLQESTKQlWQDkfglRILegyGVTECAPVVSI 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 444 wqtgGICIAPRPSEEGaEILPAMAMRpffgIVPVLMDEKGSVVE--GSNV-SGALCISQawPGMARTIYGDhqrfvDAYF 520
Cdd:PRK08043 523 ----NVPMAAKPGTVG-RILPGMDAR----LLSVPGIEQGGRLQlkGPNImNGYLRVEK--PGVLEVPTAE-----NARG 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 521 KAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVIgYPHDIKGEAAFAFivVKDS 599
Cdd:PRK08043 587 EMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGEALVLF--TTDS 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 358248205 600 AGDSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 655
Cdd:PRK08043 664 ELTREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
112-360 |
6.87e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 59.22 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 112 VNCLDQHVRKSPESVALIWER---DEPgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 188
Cdd:PTZ00216 93 VERVEKEVVKDADGKERTMEVthfNET---RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 189 GAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglRGGRVVELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDVPLE 268
Cdd:PTZ00216 170 SMVAATVYANLGEDALAYALRETECKAIVC-----NGKNVPNLLRLMKSGGMPNTTI------------IYLDSLPASVD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 269 QE----MAKEDPVCAPESMGS----------EDMLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVfdhqpgDIF 331
Cdd:PTZ00216 233 TEgcrlVAWTDVVAKGHSAGShhplnipennDDLALIMYTSGTTGDPKGVMHTHGS--LTAgilALEDRLN------DLI 304
|
250 260 270
....*....|....*....|....*....|...
gi 358248205 332 GCVADigwitGHSYVVYGPLCN----GATSVLF 360
Cdd:PTZ00216 305 GPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
140-336 |
9.57e-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: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 218
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 219 fnqglrggrVVELKKIVDEAvkhCPTVQ----HVLVAHRTDNKVHMGDLDVPLEQemAKEDPVcaPESMGSE----DMLF 290
Cdd:cd05938 85 ---------APELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVISLLDKVDA--ASDEPV--PASLRAHvtikSPAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 358248205 291 MLYTSGSTGMPKGIVHTQAGYLLYAALTHklvfdhqpgdIFGCVAD 336
Cdd:cd05938 149 YIYTSGTTGLPKAARISHLRVLQCSGFLS----------LCGVTAD 184
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
141-356 |
1.56e-08 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 57.82 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 220
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 QglrgGRVVELKKIVDEAvkhcPTVQHVLVA-------HRTDNKVHMGDLdVPLEQEMAKEDPVCAPESMGS---EDMLF 290
Cdd:cd17641 92 E----EQVDKLLEIADRI----PSVRYVIYCdprgmrkYDDPRLISFEDV-VALGRALDRRDPGLYEREVAAgkgEDVAV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248205 291 MLYTSGSTGMPKGIVhTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT 356
Cdd:cd17641 163 LCTTSGTTGKPKLAM-LSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFI 227
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
527-641 |
2.15e-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: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 527 YFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDiKGEAAF 591
Cdd:TIGR03443 680 YRTGDlGRY-LPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENvtlvrrdkdeepTLVSYivPQD-KSDELE 757
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 592 AFIVVKDSAGDSDVVVQ----------ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 641
Cdd:TIGR03443 758 EFKSEVDDEESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
114-308 |
5.89e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.04 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 114 CLDQHVRKSPESVALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSP----LAVAAMLACARIG 189
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 190 AVHtvifagfSAESLAGRiNDAKCKVVItfnQGLRGGRVvelkkIVDEAVKHCPTVQHVLVAHR---TDNKVHMGDLDVP 266
Cdd:PRK08180 123 PVS-------PAYSLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAATP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 358248205 267 LEQEMAKEDPVCAPESM---GSEDMLFMLYTSGSTGMPKGIVHTQ 308
Cdd:PRK08180 187 FAALLATPPTAAVDAAHaavGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
115-646 |
9.05e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 55.29 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIG----- 189
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYL------GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 190 -AVHTvifagfSAESLAGRINDAKCKVVITfnqglrggrVVELkkivDEAVKHCPTVQhvlvahrTDNkvhmgdldvpLE 268
Cdd:PRK04813 82 vDVSS------PAERIEMIIEVAKPSLIIA---------TEEL----PLEILGIPVIT-------LDE----------LK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 269 QEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-------ALTHKLVFDHQPGDIFG-CVADIgwi 340
Cdd:PRK04813 126 DIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTnwmledfALPEGPQFLNQAPYSFDlSVMDL--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 341 tghsyvvYGPLCNGATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVR--LLLKYGDAwvKKYdrSSLRTLGSVGE 418
Cdd:PRK04813 203 -------YPTLASGGTLVALPKD-MTANFKQLFETLPQLPINVWVSTPSFADmcLLDPSFNE--EHL--PNLTHFLFCGE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 419 PINCEAWEWLHRVVGDSRctLVDTWWQT------GGICIAPrpseegaEI------LPAMAMRPFFGIVpvLMDEKGSVV 486
Cdd:PRK04813 271 ELPHKTAKKLLERFPSAT--IYNTYGPTeatvavTSIEITD-------EMldqykrLPIGYAKPDSPLL--IIDEEGTKL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 487 EGSNvSGALCISQawPGMARTIYGDHQRfVDAYFKAYPGY--YFTGDGAYrTEGGYYQITGRMDDVINISGHRLGTAEIE 564
Cdd:PRK04813 340 PDGE-QGEIVISG--PSVSKGYLNNPEK-TAEAFFTFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIE 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 565 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDV-VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 643
Cdd:PRK04813 415 QNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
...
gi 358248205 644 RLL 646
Cdd:PRK04813 495 KAL 497
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
114-657 |
2.10e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 54.03 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 114 CLDQ-HVRKSPESVALIWERdepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PLN02860 12 CLTRlATLRGNAVVTISGNR-------RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 193 TVIFAGFSAEslagrinDAKCKVVITfnqglrggRVVELkkIVDEAVKH---------CPTVQ-HVLVAHRTDNKVHmGD 262
Cdd:PLN02860 85 APLNYRWSFE-------EAKSAMLLV--------RPVML--VTDETCSSwyeelqndrLPSLMwQVFLESPSSSVFI-FL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 263 LDVpLEQEMAKE--------DPVCAPEsmgseDMLFMLYTSGSTGMPKG--IVHTqagyllyAALTHKLvfdhqpgdifG 332
Cdd:PLN02860 147 NSF-LTTEMLKQralgttelDYAWAPD-----DAVLICFTSGTTGRPKGvtISHS-------ALIVQSL----------A 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 333 CVADIGWITGHSYVVYGPLCN-------------GATSVL---FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLK 396
Cdd:PLN02860 204 KIAIVGYGEDDVYLHTAPLCHigglssalamlmvGACHVLlpkFDAKAAL-------QAIKQHNVTSMITVPAMMADLIS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 397 YGDAWVKKYDRSSLRTLGSVGEPINCEAWEwlhrvvgdsrctlvdtwwqtGGICIAPRpseegAEILPAMAM-------- 468
Cdd:PLN02860 277 LTRKSMTWKVFPSVRKILNGGGSLSSRLLP--------------------DAKKLFPN-----AKLFSAYGMteacsslt 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 469 -----RPFFGIVPVLMDEKGSVVEGSN-VSGALCISQAWPGMARTIY-------------GDH-------QRFVDAYFKA 522
Cdd:PLN02860 332 fmtlhDPTLESPKQTLQTVNQTKSSSVhQPQGVCVGKPAPHVELKIGldessrvgriltrGPHvmlgywgQNSETASVLS 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 523 YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD---- 598
Cdd:PLN02860 412 NDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiw 491
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248205 599 ------SAGDSDVVVQE-LKSMVATK-IAKYAVPDEILV-VKRLPKTRSGKVMRRLLRKIITSEAQEL 657
Cdd:PLN02860 492 sdnekeNAKKNLTLSSEtLRHHCREKnLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRREVLSHLQSL 559
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
141-307 |
3.34e-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: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfn 220
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 221 qglrggrvvelkkivdeavkhcptvqhvlvahrTDNKvhmgdldvpleqemaKEDPVCapesmgsedmlfMLYTSGSTGM 300
Cdd:cd17639 83 ---------------------------------TDGK---------------PDDLAC------------IMYTSGSTGN 102
|
....*..
gi 358248205 301 PKGIVHT 307
Cdd:cd17639 103 PKGVMLT 109
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-304 |
4.10e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 112 VNCLDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHrGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 192 HTVIFAGFSA-----ESLAGRINDAKCKVVITfNQGLRGGrvveLKKIVDEAVKHCPTVQHVlvahrtdnkvhmGDLDVP 266
Cdd:PRK05691 91 AVPAYPPESArrhhqERLLSIIADAEPRLLLT-VADLRDS----LLQMEELAAANAPELLCV------------DTLDPA 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 358248205 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 358248205 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAkcKV 215
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA--EV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 216 VITFnqglrggrvVELKKI--VDEAVKHCPTVQHVLVAhrtdnkvhMGDLDVPLEQEMAKEDPVCAP----ESMGS---- 285
Cdd:PLN02861 151 SIAF---------VQESKIssILSCLPKCSSNLKTIVS--------FGDVSSEQKEEAEELGVSCFSweefSLMGSldce 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 286 ------EDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFdhqpgdifgcVADIGWITGHSYVVYGPLCNGATSVL 359
Cdd:PLN02861 214 lppkqkTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLAHVYDQVI 283
|
250 260 270
....*....|....*....|....*....|....*...
gi 358248205 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, ... |
561-641 |
1.21e-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: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 561 AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 640
Cdd:cd17636 253 AEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS---VTEAELIEHCRARIASYKKPKSVEFADALPRTAGGA 329
|
.
gi 358248205 641 V 641
Cdd:cd17636 330 D 330
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
122-312 |
1.47e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 51.03 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 122 SPESVALIwERDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtVIFagfsa 201
Cdd:PRK09029 16 RPQAIALR-LNDE-----VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR--VLP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 202 eslagrINDAkckvvitFNQGLRGGRVVELkkivdeavkhcpTVQHVLVAHRTDNkvhMGDLDVPLEQEMAKEDPVC-AP 280
Cdd:PRK09029 83 ------LNPQ-------LPQPLLEELLPSL------------TLDFALVLEGENT---FSALTSLHLQLVEGAHAVAwQP 134
|
170 180 190
....*....|....*....|....*....|..
gi 358248205 281 ESMGSedmlfMLYTSGSTGMPKGIVHTQAGYL 312
Cdd:PRK09029 135 QRLAT-----MTLTSGSTGLPKAAVHTAQAHL 161
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
108-307 |
2.09e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 50.97 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 108 LNVSVNCLDQHVRKSPESVALIWER--DEP-GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLA 184
Cdd:PLN02430 41 ITTAWDIFSKSVEKYPDNKMLGWRRivDGKvGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 185 CARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRG------GRVVELKKIV-----DEAVKHcPTVQHVLVAHR 253
Cdd:PLN02430 121 CAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEllepdcKSAKRLKAIVsftsvTEEESD-KASQIGVKTYS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 358248205 254 TDNKVHMGdldvpleqemaKEDP--VCAPESMgseDMLFMLYTSGSTGMPKGIVHT 307
Cdd:PLN02430 200 WIDFLHMG-----------KENPseTNPPKPL---DICTIMYTSGTSGDPKGVVLT 241
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
134-305 |
2.22e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.79 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 213
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 214 KVVITFNQglrggRVVELKKIVDEAVKHCPTVQHV---------------LVAHRTDNKVHMGD---LDVPLEQEmaked 275
Cdd:PLN02614 153 SIVFVEEK-----KISELFKTCPNSTEYMKTVVSFggvsreqkeeaetfgLVIYAWDEFLKLGEgkqYDLPIKKK----- 222
|
170 180 190
....*....|....*....|....*....|
gi 358248205 276 pvcapesmgsEDMLFMLYTSGSTGMPKGIV 305
Cdd:PLN02614 223 ----------SDICTIMYTSGTTGDPKGVM 242
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
143-308 |
3.98e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 50.00 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 143 YRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT-----VIFAGFSA--ESLAGRINDAKCKV 215
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 216 VITfnqglrggrVVELKKIVDEAVKHCPTVqhvlvahrtdnkvhmgdLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTS 295
Cdd:PRK09192 132 IIT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSS 185
|
170
....*....|...
gi 358248205 296 GSTGMPKGIVHTQ 308
Cdd:PRK09192 186 GSTRFPRGVIITH 198
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
140-434 |
4.08e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.77 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItf 219
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 220 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdlDVPLEQEMAKedpvcapesmgsedmlfMLYTSGSTG 299
Cdd:cd05910 80 --------------------------------------------GIPKADEPAA-----------------ILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 300 MPKGIVHTQAgylLYAALTHKL--VFDHQPGDI----FGCVAdigwitghsyvVYGPLCnGATSVLFESTPVYP---NAG 370
Cdd:cd05910 99 TPKGVVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQ 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358248205 371 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD 434
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSD 225
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
525-657 |
7.32e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 49.54 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 525 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIadHPAVPES----AVIGYPHDIKGEAafafIVV--KD 598
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEK----LVVlhTC 1092
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 358248205 599 SAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitseAQEL 657
Cdd:PRK08633 1093 GAEDVEELKRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL----ALAL 1144
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
115-310 |
9.43e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.97 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 115 LDQHVRKSPESVA---LIWERDEPGTEVRITYRELLETTCRLANTLKRHgVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK12476 40 IERNIANVGDTVAyryLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 192 HTVIFA----GfSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKhcPTVQHVLVAHRTDNKVHMGDLD-VP 266
Cdd:PRK12476 119 AVPLFApelpG-HAERLDTALRDAEPTVVLT-----------------TTAAA--EAVEGFLRNLPRLRRPRVIAIDaIP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 358248205 267 leqEMAKEDPVCAPesMGSEDMLFMLYTSGSTGMPKG--IVHTQAG 310
Cdd:PRK12476 179 ---DSAGESFVPVE--LDTDDVSHLQYTSGSTRPPVGveITHRAVG 219
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
563-673 |
3.05e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 46.68 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 563 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIvvkdsAGDSDVVVQELKSMVATKIAKYAvPDEILVVKRLPKTRSGKVM 642
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|..
gi 358248205 643 RRLLRKIITSEAQELGD-TTTLEDPSIIAEIL 673
Cdd:PRK09188 319 DDILRLIAMNQIDELDDlLREPEIRGLVEAIA 350
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
524-645 |
5.26e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 46.30 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 524 PGYYF-TGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAG- 601
Cdd:PRK05851 394 PDDWFpTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG-EGSARPGLVIAAEFRGp 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 358248205 602 DSDVVVQELKSMVATKIAkyAVPDEILVVK--RLPKTRSGKvMRRL 645
Cdd:PRK05851 472 DEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
140-656 |
5.48e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 43.42 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 140 RITYRELLETTCRLANTLKrHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIfaGFSAeSLAGRIND---AKCKVV 216
Cdd:PRK06814 658 PLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSA-GIANILSAckaAQVKTV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 217 ITFNQGLRGGRvveLKKIVDEavkhcpTVQHVLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSEDMLFMLYTSG 296
Cdd:PRK06814 734 LTSRAFIEKAR---LGPLIEA------LEFGIRIIYLEDVRAQIGLAD-KIKGLLAGRFPLVYFCNRDPDDPAVILFTSG 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 297 STGMPKGIVHTQAGYLLYAALTHKLVfDHQPGDIFGCVADIGwitgHSYVVYG----PLCNGATSVLfestpvYPNAGRY 372
Cdd:PRK06814 804 SEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPVF----HSFGLTGglvlPLLSGVKVFL------YPSPLHY 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 373 W---ETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWEwlhrvvgdsrctlvdTWWQTGGI 449
Cdd:PRK06814 873 RiipELIYDTNATILFGTDTFLNGYARYAHP----YDFRSLRYVFAGAEKVKEETRQ---------------TWMEKFGI 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 450 CIAprpseEG---AEILPAMA----MRPFFGIVPVL---MDEKGSVVEGSNVSGALCISqawpG---MARTIYGDHQRFV 516
Cdd:PRK06814 934 RIL-----EGygvTETAPVIAlntpMHNKAGTVGRLlpgIEYRLEPVPGIDEGGRLFVR----GpnvMLGYLRAENPGVL 1004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248205 517 DAyfkAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAafaFIVV 596
Cdd:PRK06814 1005 EP---PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER---IILL 1078
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248205 597 KDSAgdsDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKV----MRRLLRKIITSEAQE 656
Cdd:PRK06814 1079 TTAS---DATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEAA 1140
|
|
| |
