|
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 ... |
51-676 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 1101.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 51 ASQPGSYPALSAQAAREPAAFWGPLARDTLLWDTPYHTVWDCDFSTgKIGWFLGGQLNVSVNCLDQHVQKSPESVALIWE 130
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 131 RDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDA 210
Cdd:TIGR02188 80 GDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 211 KCKVVITFNQGLRGGRVMELKKIVDEAVKHCP-TVQHVLVAHRTDNKV-HMGD-LDIPLEQEMAKEDPVCAPESMGSEDV 287
Cdd:TIGR02188 160 GAKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVEgRDVWWHDLMAKASAYCEPEPMDSEDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 288 LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPN 367
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 368 AGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTET 447
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 448 GGICIAPRPSeeGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGY 527
Cdd:TIGR02188 400 GGIMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 528 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVV 607
Cdd:TIGR02188 478 YFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDEL 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 608 VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIITEILSA 676
Cdd:TIGR02188 558 RKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
56-666 |
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: 1088.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 56 SYPALSAQAAREPAAFWGPLARDtLLWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVQKSPESVALIWERDEPG 135
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 136 TEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVV 215
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 216 ITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHM-GDLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTS 294
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 295 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWET 374
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 375 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAP 454
Cdd:cd05966 321 VEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 455 RPSEegAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 534
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNEVEG-EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 535 HRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 614
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 615 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLED 666
Cdd:cd05966 558 VRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEE-ELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
57-681 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 979.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 57 YPALSAQAAREPAAFWGPLARDtLLWDTPYHTVWDCDfsTGKIGWFLGGQLNVSVNCLDQHVQKSPESVALIWERDEPGT 136
Cdd:PRK00174 19 YKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIWEGDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGD-LDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSG 295
Cdd:PRK00174 176 TADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEgRDLWWHELVAGASDECEPEPMDAEDPLFILYTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETV 375
Cdd:PRK00174 256 STGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 376 ERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPR 455
Cdd:PRK00174 336 DKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 456 PseeGA-EILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 534
Cdd:PRK00174 416 P---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEG-GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGA 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 535 HRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 614
Cdd:PRK00174 492 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNW 571
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 615 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLEDPSIITEILSAYQKCK 681
Cdd:PRK00174 572 VRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEARQNRK 637
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
101-673 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 824.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 101 WFLGGQLNVSVNCLDQHVQKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAA 180
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 181 MLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMG 260
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 261 DlDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWIT 340
Cdd:COG0365 161 G-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 341 GHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN 420
Cdd:COG0365 240 GHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 421 CEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQ 500
Cdd:COG0365 320 PEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 501 AWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 580
Cdd:COG0365 393 PWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 581 GYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGD 660
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA--EGRPLGD 550
|
570
....*....|...
gi 1622839330 661 TTTLEDPSIITEI 673
Cdd:COG0365 551 TSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
41-675 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 671.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 41 PSGSAPAVAAASQPGSYPALSAQAAREPAAFWGPLArDTLLWDTPYHTVWDC----DFSTG--KIGWFLGGQLNVSVNCL 114
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQK-SPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PLN02654 95 DRNVEAgNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKIVDEA----------VKHCPTVQHVLVAHRTDNKVHMGDlD 263
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-D 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 264 IPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHS 343
Cdd:PLN02654 254 VWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 344 YVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEA 423
Cdd:PLN02654 334 YVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 424 WEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPseeGAEIL-PGMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAW 502
Cdd:PLN02654 414 WRWFFNVVGDSRCPISDTWWQTETGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSW 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 503 PGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 582
Cdd:PLN02654 490 PGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGI 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 583 PHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTT 662
Cdd:PLN02654 570 EHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTS 649
|
650
....*....|...
gi 1622839330 663 TLEDPSIITEILS 675
Cdd:PLN02654 650 TLADPGVVDQLIA 662
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
63-643 |
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: 640.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 63 QAAREPAAFWGPLARDtLLWDTPYHTVWDCDFSTGK--IGWFLGGQLNVSVNCLDQHVQKSPESVALIWERDEpGTEVR- 139
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFN 219
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 QGLRGGRVMELKKIVDEAVK-HCPTVQHVLVAHRTDNKVH-MGDLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGST 297
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 298 GMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVER 377
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 378 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPS 457
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 458 EEgaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRT 537
Cdd:cd17634 405 AI--ELKAGSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 538 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVAT 617
Cdd:cd17634 482 EDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRK 561
|
570 580
....*....|....*....|....*.
gi 1622839330 618 KIAKYAVPDEILVVKRLPKTRSGKVM 643
Cdd:cd17634 562 EIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
57-673 |
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: 568.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 57 YPALSAQAAREPAAFWGPLARdTLLWDTPYHTVWDCDfSTGKIGWFLGGQLNVSVNCLDQHVQKS-PESVALIWERDEPG 135
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 136 TEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVV 215
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 216 ITFNQGLRGGRVMELKKIVDEAVK---HCPtvQHVLVAHRTDNKVHMGD--LDIPLEQEMAKEDPV-CAPesMGSEDVLF 289
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALElsgHKP--HHVLVLNRPQVPADLTKpgRDLDWSELLAKAEPVdCVP--VAATDPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 290 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV-YPNA 368
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 369 GRYWETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTE 446
Cdd:cd05967 315 GAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 447 TGGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAYP 525
Cdd:cd05967 392 TGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DS 604
Cdd:cd05967 471 GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKiTA 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 605 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTLEDPSIITEI 673
Cdd:cd05967 551 EELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
56-676 |
1.17e-180 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 527.98 E-value: 1.17e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 56 SYPALSAQAAREPAAFWGPLARdTLLWDTPYHTVwdCDFSTGKIG-WFLGGQLNVSVNCLDQHVQKSPESVALIWERDEP 134
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR-RIDWQTPFTQV--LDYSNPPFArWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:PRK10524 80 DEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 215 VITFNQGLRGGRVMELKKIVDEAV---KHCPtvQHVLVAHR---TDNKVHMGDLDIPLEQEmAKEDPVCAPESMGSEDVL 288
Cdd:PRK10524 160 IVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVDRglaPMARVAGRDVDYATLRA-QHLGARVPVEWLESNEPS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 289 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNA 368
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 369 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG 448
Cdd:PRK10524 317 GIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP---VIDNYWQTETG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 449 GICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAY-PG 526
Cdd:PRK10524 394 WPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 527 YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD- 605
Cdd:PRK10524 474 VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADr 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 606 ----VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitSEAQELGDTTTLEDPSIITEILSA 676
Cdd:PRK10524 554 earlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI--AEGRDPGDLTTIEDPAALQQIRQA 626
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
55-667 |
3.11e-174 |
|
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: 510.88 E-value: 3.11e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 55 GSYPALSAQAAREPAAFWGPLARDTLLW--DTPYHTVwdcDFSTGK--IGWFLGGQLNVSVNCLDQHVQKSPESVALIWE 130
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIEwyEPPYQTL---DLSGGKpwAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 131 rDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDA 210
Cdd:cd05968 84 -GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 211 KCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKV--HMGDlDIPLEQEMAKEDPvcAPESMGSEDVL 288
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFtpAKGR-DLSYDEEKETAGD--GAERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 289 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNA 368
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 369 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTE-T 447
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 448 GGI--CIAPRPSEEGA--EILPGMAmrpffgivPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQRFVDAYFKA 523
Cdd:cd05968 399 GGIlgNVLIKPIKPSSfnGPVPGMK--------ADVLDESGKPARPE--VGELVLLAPWPGMTRGFWRDEDRYLETYWSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 524 YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGD 603
Cdd:cd05968 469 FDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 604 SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEaqELGDTTTLEDP 667
Cdd:cd05968 549 TEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
101-666 |
3.33e-147 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 440.10 E-value: 3.33e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 101 WFLGGQLNVSVNCLDQHVqKSP--ESVALIWERdePGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAV 178
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 179 AAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGLRggrvmelKKIVDEAvkhcPTVQHVLVahrTDNKVH 258
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDL----PSLKHVLL---VGEDVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 259 MGDLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQagyllYAALTH----KLVFDHRPGDIFGCVA 334
Cdd:PRK04319 179 EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NAMLQHyqtgKYVLDLHEDDVYWCTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 335 DIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 414
Cdd:PRK04319 254 DPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 415 VGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEEgaeILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSG 494
Cdd:PRK04319 331 VGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAMD---IKPGSMGKPLPGIEAAIVDDQGNELP-PNRMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 495 ALCISQAWPGMARTIYGDHQRFvDAYFKayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 574
Cdd:PRK04319 404 NLAIKKGWPSMMRGIWNNPEKY-ESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 575 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRkiitse 654
Cdd:PRK04319 481 AEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK------ 554
|
570
....*....|....*.
gi 1622839330 655 AQEL----GDTTTLED 666
Cdd:PRK04319 555 AWELglpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
141-650 |
2.78e-126 |
|
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: 381.85 E-value: 2.78e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQ 220
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 221 glrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipLEQEMAKEDPvcapesmgsedvLFMLYTSGSTGMP 300
Cdd:cd05969 82 ---------------------------------------------LYERTDPEDP------------TLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 301 KGIVHTQAGYLLYAaLTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKI 380
Cdd:cd05969 105 KGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 381 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeG 460
Cdd:cd05969 181 TVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP---C 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 461 AEILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRFvDAYFKAypGYYFTGDGAHRTEGG 540
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELP-PGTKGILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 541 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 620
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLG 410
|
490 500 510
....*....|....*....|....*....|
gi 1622839330 621 KYAVPDEILVVKRLPKTRSGKVMRRLLRKI 650
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
141-649 |
7.21e-107 |
|
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: 331.22 E-value: 7.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnq 220
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 221 glrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmGSEDVLFMLYTSGSTGMP 300
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 301 KGIVHTqAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNagRYWETVERLKI 380
Cdd:cd05972 97 KGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 381 NQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgICIAPRPseeG 460
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP---D 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 461 AEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAHRTEGG 540
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 541 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 620
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
gi 1622839330 621 KYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
114-555 |
6.01e-102 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 318.10 E-value: 6.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNQglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDnkvhMGDLDIPLEQEMAKE 273
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLV----FDHRPGDIFGCVADIGWITGHSYVVYGP 349
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 350 LCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHR 429
Cdd:pfam00501 223 LLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 430 VVGdsrCTLVDTWWQTETGGICIAPRPsEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTI 509
Cdd:pfam00501 300 LFG---GALVNGYGLTETTGVVTTPLP-LDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622839330 510 YGDHQRFVDAYFKayPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 555
Cdd:pfam00501 374 LNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
114-657 |
1.10e-97 |
|
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: 307.89 E-value: 1.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemake 273
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 dpvcapesmgsedvlFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNG 353
Cdd:COG0318 104 ---------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGd 433
Cdd:COG0318 168 ATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 srCTLVDTWWQTETGGICIAPRpsEEGAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD- 512
Cdd:COG0318 241 --VRIVEGYGLTETSPVVTVNP--EDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPGEVGEIVVRG--PNVMKGYWNDp 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 513 ---HQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 589
Cdd:COG0318 314 eatAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 590 AAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 657
Cdd:COG0318 387 RVVAFVVLRP---GAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
55-651 |
7.67e-82 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 271.84 E-value: 7.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 55 GSYPALSAQAAREPAAFWgplardTLLWD---TPYHTVWDCDFSTGKI----GWFLGGQLNVSVNCLDQHVQksPESVAL 127
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLLRHADA--DDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 128 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRI 207
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 208 NDAKCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDIP----LEQEMAKE-DPVCAPESM 282
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 283 GSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVvyGPLCNGATSVLFEST 362
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 363 PVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTW 442
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 443 WQTETGG--IC--------IAP-RPSEEGAEILpGMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMARTIYG 511
Cdd:cd05943 399 LASISGGtdIIscfvggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 512 DH--QRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 589
Cdd:cd05943 468 DPdgSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDE 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 590 AAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 651
Cdd:cd05943 548 RVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII 609
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
286-643 |
7.55e-81 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 259.91 E-value: 7.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDhRPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFEStpvy 365
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL-TEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 366 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT 445
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 446 ETGGICIAPRPSEEgaEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDayfkaYP 525
Cdd:cd04433 150 ETGGTVATGPPDDD--ARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVD-----ED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 605
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---D 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622839330 606 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 643
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
52-679 |
8.96e-78 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 261.60 E-value: 8.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 52 SQPGSYPALSAQAAREPAAFWGPLARDTLLWDTPYHTVwdcdFSTGKI--GWFLGGQLNVSVNCLDQHVqKSP---ESVA 126
Cdd:PTZ00237 5 SDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKV----YSGDEIypDWFKGGELNTCYNVLDIHV-KNPlkrDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 127 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGR 206
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 207 INDAKCKVVITFNQGLRGGRVMELKKIVDEAV---KHCPTvqHVLVAHRTD-------NKVHmgdlDIPL-------EQE 269
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIelsTFKPS--NVITLFRNDitsesdlKKIE----TIPTipntlswYDE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 270 MAK-----EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSY 344
Cdd:PTZ00237 234 IKKikennQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 345 VvYGPLCNGATSVLFESTPVYPNAGR--YWETVERLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPI 419
Cdd:PTZ00237 314 L-YGSLSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 420 NCEAWEWLHRVVGdSRCTLVdtWWQTETGG---ICIAPRPSEEGAEILPGmamrPFfgIVPVLMDEKGSVVeGSNVSGAL 496
Cdd:PTZ00237 393 EESIPEYIENKLK-IKSSRG--YGQTEIGItylYCYGHINIPYNATGVPS----IF--IKPSILSEDGKEL-NVNEIGEV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 497 CISQAWP-GMARTIYGDHQRFvDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 575
Cdd:PTZ00237 463 AFKLPMPpSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 576 ESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS----MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 651
Cdd:PTZ00237 542 ECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFL 621
|
650 660
....*....|....*....|....*...
gi 1622839330 652 TSEAQELGDTTtlEDPSIITEILSAYQK 679
Cdd:PTZ00237 622 NDSNYQLPDNV--NDSEIFYKIKELYMK 647
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
55-647 |
1.23e-76 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 258.57 E-value: 1.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 55 GSYPALSAQAAREPAAFWgplardTLLWD-------TPYHTVWDcdfSTGKIG--WFLGGQLNVSVNCLDQHvqkSPESV 125
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 126 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAG 205
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 206 RINDAKCKVVITFNqGLR-GGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLD--IPLEQEMAK-EDPVCAPES 281
Cdd:PRK03584 181 RFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIF----GCvadiGWITgHSYVVYGPLCnGATSV 357
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 358 LFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrct 437
Cdd:PRK03584 334 LYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA---- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 438 lvDTWWQTETGG--IC---IAprpseeGAEILP-----------GMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQA 501
Cdd:PRK03584 410 --DVWLASISGGtdICscfVG------GNPLLPvyrgeiqcrglGMAVEAW--------DEDGRPVVG--EVGELVCTKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 502 WPGMArtIY----GDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 577
Cdd:PRK03584 472 FPSMP--LGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDS 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 578 AVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM----RRLL 647
Cdd:PRK03584 550 LVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
140-649 |
6.31e-71 |
|
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: 237.42 E-value: 6.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglrggrvmelkkivDEAVKHcptvqhvlvahrtdnkvhmgDLDipleqemakedpvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05973 79 ---------------DAANRH--------------------KLD---------------------SDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKGIVHTQAGYLLYAALTHKLVfDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgryWETVERLK 379
Cdd:cd05973 103 PKGVPVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 380 INQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgICIA-----P 454
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELG-MVLAnhhalE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 455 RPSEEGAE--ILPGMAmrpffgiVPVLMDEKGSVVEGsnVSGALCISQA-WPGMArtiYGDHQRFVDAYFKAypGYYFTG 531
Cdd:cd05973 254 HPVHAGSAgrAMPGWR-------VAVLDDDGDELGPG--EPGRLAIDIAnSPLMW---FRGYQLPDTPAIDG--GYYLTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 532 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQEL 611
Cdd:cd05973 320 DTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADEL 399
|
490 500 510
....*....|....*....|....*....|....*...
gi 1622839330 612 KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05973 400 QLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
108-648 |
1.09e-70 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 239.70 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 108 NVSVNCLDQHVQKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARI 187
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWC-DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 188 GAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGlrggrvmELKKIVDEAVKHCPTVQhVLVahrtdnKVHMGDLD--IP 265
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECPSKP-KLV------WVGDPVPEgwID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 266 LEQEMAKEDPV----CAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAgYLLYAALTHKLVFDHRPGDIFGCVADIGWITG 341
Cdd:cd05970 162 FRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 342 HSYVVYGPLCNGATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINC 421
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 422 EAWEWLHRVVGDSrctLVDTWWQTETGgICIAPRPseeGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNvSGALCI--S 499
Cdd:cd05970 316 EVFNTFKEKTGIK---LMEGFGQTETT-LTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 500 QAWP-GMARTIYGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 578
Cdd:cd05970 388 KGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 579 VIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05970 465 VTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
106-648 |
1.44e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 238.55 E-value: 1.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 106 QLNVSvNCLDQHVQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACA 185
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 186 RIGAV-HTV-IFagFSAASLAGRINDAKCKVVItFNQglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDNKVHmGDLD 263
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS--------EFVPLLAAILPQLPTVRTVIVEGDGPAAPL-APEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 264 IPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDI-------FGCVAdI 336
Cdd:PRK06187 146 GEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA-WLKLSRDDVylvivpmFHVHA-W 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 337 GWItghsyvvYGPLCNGATSVL---FESTPVypnagryWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLG 413
Cdd:PRK06187 224 GLP-------YLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFSSLRLVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 414 SVGEPIN---CEAWEWLHRvvgdsrCTLVDTWWQTETGGI--CIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVE 488
Cdd:PRK06187 288 YGGAALPpalLREFKEKFG------IDLVQGYGMTETSPVvsVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 489 GSNVS-GALCISQAWpgMARTIYGDHQRFVDAYfkaYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 567
Cdd:PRK06187 362 PDGGEvGEIIVRGPW--LMQGYWNRPEATAETI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 568 IADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK06187 437 LYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP---GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
.
gi 1622839330 648 R 648
Cdd:PRK06187 514 R 514
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
108-649 |
1.23e-66 |
|
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: 228.50 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 108 NVSVNCLDQHVQKS-----PESVALIWERDEpGTEVRITYRELLETTCRLANTLKrhGVC---RGDCVAIYMPVSPLAVA 179
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGK-GDEVKWSFRELGSLSRKAANVLS--GACglqRGDRVAVILPRVPEWWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 180 AMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPTVQ-HVLVAHRTDNkvh 258
Cdd:cd05928 83 VNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKtKLLVSEKSRD--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 259 mGDLDIPLEQEMAKEDPVCApeSMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGW 338
Cdd:cd05928 151 -GWLNFKELLNEASTEHHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 339 ITGHSYVVYGPLCNGATsVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEP 418
Cdd:cd05928 228 IKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 419 INCEAWE-WLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPGMAMRPFFGIVPVLMDEKGSVV-EGSNVSGAL 496
Cdd:cd05928 303 LNPEVLEkWKAQTGLD----IYEGYGQTETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEGDIGI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 497 CISQAWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 576
Cdd:cd05928 375 RVKPIRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVE 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 577 SAVIGYPHDIKGEAAFAFIVVKD--SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05928 453 SAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
136-643 |
1.26e-64 |
|
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: 221.70 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 136 TEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVV 215
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 216 ITFNQGLrggrvmelkKIVDEAVKHCPTVQHV-LVAHRTDNKVHMGDLDIPLEQEMAKEDPVCAPEsmGSEDVLFMLYTS 294
Cdd:cd05911 87 FTDPDGL---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 295 GSTGMPKGivhtqagyllyAALTHK-LVFDH-----------RPGDIFGCVADIGWITGHSYVVYGPLCnGATSVLFESt 362
Cdd:cd05911 156 GTTGLPKG-----------VCLSHRnLIANLsqvqtflygndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 363 pvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTW 442
Cdd:cd05911 223 ---FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 443 WQTETGGICIAPRPSEEGAE----ILPGMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS--QAWPG-------MARTI 509
Cdd:cd05911 296 GMTETGGILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyynnpeaTKETF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 510 YGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 589
Cdd:cd05911 368 DED-------------GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 590 AAFAFIVVKDSAGDSDvvvQELKSMVATKIAKY-AVPDEILVVKRLPKTRSGKVM 643
Cdd:cd05911 435 LPRAYVVRKPGEKLTE---KEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
114-644 |
6.05e-63 |
|
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: 215.94 E-value: 6.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVItfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemake 273
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 dpvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNG 353
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinceAWEWLHRVVGD 433
Cdd:cd17631 166 GTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 SRCTLVDTWWQTETG-GICIAPRpseEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTIYGD 512
Cdd:cd17631 236 RGVKFVQGYGMTETSpGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVPP-GEVGEIVVRG--PHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 513 HQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAF 592
Cdd:cd17631 310 PEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 593 AFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:cd17631 387 AVVVPRPGA---ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
135-648 |
1.71e-62 |
|
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: 214.60 E-value: 1.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 215 VITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDpvcapesmGSEDVLFMLYTS 294
Cdd:cd05971 82 LVT--------------------------------------------------------D--------GSDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 295 GSTGMPKGIVHTQA---GYLLYAALTHKLVfdHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnaGRY 371
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDP--KAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 372 WETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG--- 448
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFGVE---VNEFYGQTECNlvi 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 449 GICIAPRPseegaeILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYY 528
Cdd:cd05971 249 GNCSALFP------IKPGSMGKPIPGHRVAIVDDNGTPLP-PGEVGEIAVELPDPVAFLG-YWNNPSATEKKMAG--DWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 529 FTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVV 608
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1622839330 609 QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05971 399 REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
139-648 |
2.17e-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: 216.47 E-value: 2.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 NqglrggrvmELKKIVDEAV-KHCPTVQHVLVA--HRTDNKVHMgdldipLEQEMAKEDPVCAPESMGSEDVLFMLYTSG 295
Cdd:cd05959 109 G---------ELAPVLAAALtKSEHTLVVLIVSggAGPEAGALL------LAELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETV 375
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 376 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVgdsrCTLVDTWWQTETGGICIAP 454
Cdd:cd05959 251 RRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGErWKARFG----LDILDGIGSTEMLHIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 455 RPSEegaeILPGMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQawPGMArTIYGdHQRfvDAYFKAYPGYYF-TGDG 533
Cdd:cd05959 325 RPGR----VRYGTTGKPVPGYEVELRDEDGGDVADG-EPGELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTrTGDK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 534 AHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS 613
Cdd:cd05959 394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKE 473
|
490 500 510
....*....|....*....|....*....|....*
gi 1622839330 614 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05959 474 FVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
122-647 |
1.23e-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: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapes 281
Cdd:cd05930 75 RLAYILEDSGAKLVLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 mGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFES 361
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 362 TPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDT 441
Cdd:cd05930 168 EVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 442 WWQTETGGICIA---PRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGDH----Q 514
Cdd:cd05930 241 YGPTEATVDATYyrvPPDDEEDGRVPIG---RPIPNTRVYVLDENLRPV-PPGVPGELYIGGA--GLARGYLNRPeltaE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 515 RFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 594
Cdd:cd05930 315 RFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAY 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622839330 595 IVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05930 395 VV---PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
140-648 |
2.40e-58 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 203.46 E-value: 2.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmGSEDVLFMLYTSGSTGM 299
Cdd:cd05919 89 ---------------------------------------------------------------SADDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADI--GWITGHSyvVYGPLCNGATSVLFestPVYPNAGRYWETVER 377
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 378 LKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPS 457
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 458 EegaeILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI--SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAH 535
Cdd:cd05919 256 A----WRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVrgPSAAVGYWNNPEKSRATFNG-------GWYRTGDKFC 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 536 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMV 615
Cdd:cd05919 324 RDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHL 403
|
490 500 510
....*....|....*....|....*....|...
gi 1622839330 616 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05919 404 LERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
128-649 |
2.01e-53 |
|
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: 192.08 E-value: 2.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 128 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV-HTvIFAGFSAASLAGR 206
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT-INPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 207 INDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPTVQHVLV-AHRTDNKVHMGDLDIPLEQEMAKEDPVCAPESMGSE 285
Cdd:cd12119 93 INHAEDRVVFVDR---------DFLPLLEAIAPRLPTVEHVVVmTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLVFDHRPGDIFGCVADI----GW-------ITGHSYVVYGPLCNG 353
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVGAKLVLPGPYLDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINCEAWEWLHrv 430
Cdd:cd12119 244 ASLA---------------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 431 vgdsrctlVDT---WWQTETGGICIAPRPSEEGAEILPGMAM-------RPFFGIVPVLMDEKGSVVEGSNVS-GALCIS 499
Cdd:cd12119 305 --------VRVihaWGMTETSPLGTVARPPSEHSNLSEDEQLalrakqgRPVPGVELRIVDDDGRELPWDGKAvGELQVR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 500 QAWpgMARTIYGDHQR----FVDAYFKaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 575
Cdd:cd12119 377 GPW--VTKSYYKNDEEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 576 ESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd12119 448 EAAVIGVPHPKWGERPLAVVVLKE---GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
114-648 |
1.92e-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: 185.46 E-value: 1.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVI---TFNQGLRGGRVMELKKIVDEavkhcptvqhvlvahrtdnkvhmgdldipleqem 270
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIvavSFTDLLAAGAPLGERVALTP---------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 271 akedpvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHK--LVFDHRPGDIFGCVADIGWITGHSYVVYG 348
Cdd:cd05936 125 --------------EDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:cd05936 190 PLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 429 RVVGdsrCTLVDTWWQTETGGIcIAPRPSEEgaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCIS--QAWPGma 506
Cdd:cd05936 264 ELTG---VPIVEGYGLTETSPV-VAVNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEV-GELWVRgpQVMKG-- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 507 rtiYGDH-----QRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 581
Cdd:cd05936 335 ---YWNRpeetaEAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 582 YPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05936 405 VPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
56-656 |
1.80e-48 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 181.82 E-value: 1.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 56 SYPALSAQAAREPAAFWgPLARDTL--LWDTPYHTVWDCDFSTGKIG-WFLGGQLNVSVNCLDQHVQKSPESVALIWeRD 132
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW-SIVLDELslVFSVPPRCILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAIIW-RD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 133 EPGTEV---RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRIND 209
Cdd:PLN03052 199 EGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 210 AKCKVVITFNQGLRGGRVMELKKIVDEAvkHCPTVQhVLVAHRTDNKVHMGDLDIPLEQEMAKEDPVCAPES-----MGS 284
Cdd:PLN03052 279 SKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEykaveQPV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 EDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALT--HklvFDHRPGDIFGCVADIGWITGHsYVVYGPLCNGATSVLFEST 362
Cdd:PLN03052 356 EAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLALYNGS 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 363 PVYPNAGRYwetVERLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgdSRCT 437
Cdd:PLN03052 432 PLGRGFAKF---VQDAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWLM-----SRAG 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 438 ---LVDTWWQTETGGICIAP---RPSEEGAEILPGMAMRPFfgivpvLMDEKGSVVEgSNVSG----ALCisqawPGM-- 505
Cdd:PLN03052 497 ykpIIEYCGGTELGGGFVTGsllQPQAFAAFSTPAMGCKLF------ILDDSGNPYP-DDAPCtgelALF-----PLMfg 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 --ARTIYGDHQrfvDAYFKAYPGYYFT-----GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI-ADHPAVPES 577
Cdd:PLN03052 565 asSTLLNADHY---KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLET 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 578 AVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVP----DEILVVKRLPKTRSGKVMRRLLRKIITS 653
Cdd:PLN03052 642 AAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVLRQQLAQ 721
|
...
gi 1622839330 654 EAQ 656
Cdd:PLN03052 722 ELS 724
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
114-652 |
2.24e-48 |
|
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: 178.42 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtV 193
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFS--AASLAGRINDAKCKVVITfnqgLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTDNKVhmgDLDIPLEQEMA 271
Cdd:COG1021 103 VFALPAhrRAEISHFAEQSEAVAYII----PDRHRGFDYRALARELQAEVPSLRHVLVVGDAGEFT---SLDALLAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 272 KEDPVCAPEsmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDhrPGDIFGCVADIGwitgHSY-----V 345
Cdd:COG1021 176 LSEPRPDPD-----DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICgLD--ADTVYLAALPAA----HNFplsspG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GS-------- 414
Cdd:COG1021 245 VLGVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLqvgGAklspelar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 415 -VGEPINCeaweWLHRVVG------------DSRCTLVDTwwQtetgGiciapRPSEEGAEILpgmamrpffgIVpvlmD 481
Cdd:COG1021 319 rVRPALGC----TLQQVFGmaeglvnytrldDPEEVILTT--Q----G-----RPISPDDEVR----------IV----D 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 482 EKGS-VVEGSnvSGALcisqawpgMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAHRTEGGYYQITGR 547
Cdd:COG1021 370 EDGNpVPPGE--VGEL--------LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 548 MDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATK-IAKYAVPD 626
Cdd:COG1021 431 AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEP----LTLAELRRFLRERgLAAFKLPD 506
|
570 580
....*....|....*....|....*.
gi 1622839330 627 EILVVKRLPKTRSGKVMRRLLRKIIT 652
Cdd:COG1021 507 RLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
137-648 |
2.40e-48 |
|
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: 176.13 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCR-GDCVAIYMPVSPLAVAAMLACARIGAVhtvifagfsaaslagrindakCKVV 215
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 216 ITFnqgLRGGrvmELKKIVDEAvkhcpTVQHVLVAHRTdnkvhmgdldipleqemakedpvcapesMGSEDVLFMLYTSG 295
Cdd:cd05958 67 MPL---LRPK---ELAYILDKA-----RITVALCAHAL----------------------------TASDDICILAFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 375
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 376 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPR 455
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 456 PSEegaeILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQawPGMARTIYGDHQRfvdAYFKAypGYYFTGDGAH 535
Cdd:cd05958 259 PGD----ARPGATGKPVPGYEAKVVDDEGNPVPDGTI-GRLAVRG--PTGCRYLADKRQR---TYVQG--GWNITGDTYS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 536 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMV 615
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHA 406
|
490 500 510
....*....|....*....|....*....|...
gi 1622839330 616 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05958 407 KAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
114-649 |
4.76e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 174.32 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK07656 11 LARAARRFGDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFnQGLRGgrvmelkkiVDEAVKHC-PTVQHVlVAHRTDNKVHMGDLDIPLEQEMAK 272
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVL-GLFLG---------VDYSATTRlPALEHV-VICETEEDDPHTEKMKTFTDFLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 273 EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHKLvfDHRPGD----------IFGCVAdiGWIT 340
Cdd:PRK07656 154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMltHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 341 ghsyvvygPLCNGATsVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPIn 420
Cdd:PRK07656 229 --------PLMRGAT-ILPL--PVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 421 ceAWEWLHRVVGDSRCTLVDTWWQ-TETGGI-CIAPRpsEEGAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCI 498
Cdd:PRK07656 294 --PVALLERFESELGVDIVLTGYGlSEASGVtTFNRL--DDDRKTVAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 499 S-----QAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 569
Cdd:PRK07656 369 RgpnvmKGYYDDpeatAAAIDAD-------------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 570 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PRK07656 436 EHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE---LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
139-649 |
1.12e-45 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 170.02 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 NqglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDNkvhmGDLDipLEQEMAKEDPVCAPESMGSEDVLFMLYTSGSTG 298
Cdd:TIGR02262 110 G---------ALLPVIKAALGKSPHLEHRVVVGRPEA----GEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETVERL 378
Cdd:TIGR02262 175 MPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 379 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVVGDsrctLVDTWWQTETGGICIAPRPS 457
Cdd:TIGR02262 252 QPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTEMLHIFLSNLPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 458 EegaeILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRT 537
Cdd:TIGR02262 326 D----VRYGTSGKPVPGYRLRLVGDGGQDV-ADGEPGELLISG---PSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 538 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDIKGEaafAFIVVKDSAGDSDvvvQELKSM 614
Cdd:TIGR02262 396 DDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVAdedGLIKPK---AFVVLRPGQTALE---TELKEH 469
|
490 500 510
....*....|....*....|....*....|....*
gi 1622839330 615 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:TIGR02262 470 VKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
114-655 |
3.07e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 169.85 E-value: 3.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVI---TFnqglrggRVMELKKIVDEAVKHCPTVQHVLVAHrTDNKVHMGDLDIPLEQEM 270
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVvpkTF-------RGFDHAAMARRLRPELPALRHVVVVG-GDGADSFEALLITPAWEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 271 AKEDP-VCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQ----AGYLLYAALthklvFDHRPGDIFGCVADIGWITGHSYV 345
Cdd:PRK13295 182 EPDAPaILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 VYGPLCNGATSVLFEStpvypnagryWETVERLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEP 418
Cdd:PRK13295 257 LMMPVMLGATAVLQDI----------WDPARAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 419 INCEAWEWLHRVVGdsrCTLVDTWWQTETGGIC-IAPRPSEEGAEI-----LPGMAMRpffgIV-----PVLMDEKGS-V 486
Cdd:PRK13295 324 IPGALVERARAALG---AKIVSAWGMTENGAVTlTKLDDPDERASTtdgcpLPGVEVR----VVdadgaPLPAGQIGRlQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 487 VEG-SNVSGALcisqAWPGMARTiygdhqrfvDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIE 565
Cdd:PRK13295 397 VRGcSNFGGYL----KRPQLNGT---------DA-----DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 566 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:PRK13295 459 ALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSlDFEEMVEFLKA---QKVAKQYIPERLVVRDALPRTPSGKIQK 535
|
570
....*....|.
gi 1622839330 645 RLLRKIITSEA 655
Cdd:PRK13295 536 FRLREMLRGED 546
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-648 |
9.12e-45 |
|
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: 165.54 E-value: 9.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 nqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDPVCapesmgsedvlfMLYTSGSTG 298
Cdd:cd05934 82 -------------------------------------------------------DPAS------------ILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHTQAgYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 378
Cdd:cd05934 95 PPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 379 KINQFYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPS 457
Cdd:cd05934 170 GATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 458 EEGaeilPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWP-GMARTIYGDHqrfvDAYFKAYP-GYYFTGDGAH 535
Cdd:cd05934 242 PRR----PGSIGRPAPGYEVRIVDDDGQELP-AGEPGELVIRGLRGwGFFKGYYNMP----EATAEAMRnGWFHTGDLGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 536 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMV 615
Cdd:cd05934 313 RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD---PEELFAFC 389
|
490 500 510
....*....|....*....|....*....|...
gi 1622839330 616 ATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05934 390 EGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
122-649 |
1.19e-44 |
|
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: 167.10 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd05926 1 PDAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglRGGRVMElkkiVDEAVKHcPTVQHVLVAHRTDNKVHMGDLDiPLEQEMAKEDPVCAPES 281
Cdd:cd05926 77 EFEFYLADLGSKLVLT-----PKGELGP----ASRAASK-LGLAILELALDVGVLIRAPSAE-SLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGYLL---YAALTHKLVfdhrPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL 358
Cdd:cd05926 146 PLPDDLALILHTSGTTGRPKGVPLTHRNLAAsatNITNTYKLT----PDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 359 festPVYPNAGRYWETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGdsrCT 437
Cdd:cd05926 222 ----PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFG---AP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 438 LVDTWWQTETGG------ICIAPRPseegaeilPGMAMRPFfGIVPVLMDEKGSVVEgSNVSGALCISQawPGMARTIYG 511
Cdd:cd05926 293 VLEAYGMTEAAHqmtsnpLPPGPRK--------PGSVGKPV-GVEVRILDEDGEILP-PGVVGEICLRG--PNVTRGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 512 DHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 591
Cdd:cd05926 361 NPEANAEAAFKD--GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 592 FAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05926 439 AAAVVLR---EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
118-657 |
4.35e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 165.88 E-value: 4.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK08316 21 ARRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITfNQGLRGgrvmelkkIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDIpleQEMAKEDPVC 277
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLV-DPALAP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 APE-SMGSEDVLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVfdhrpgdifGCVADIGWITG----------HS--- 343
Cdd:PRK08316 163 EPDvELADDDLAQILYTSGTESLPKGAMLT------HRALIAEYV---------SCIVAGDMSADdiplhalplyHCaql 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 344 YVVYGP-LCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTlGSVGEPI-NC 421
Cdd:PRK08316 228 DVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRK-GYYGASImPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 422 EAWEWLHRVVGDSRctLVDTWWQTEtggicIAP-----RPSEegAEILPGMAMRPFFGIVPVLMDEKGSVVEgsnvsgal 496
Cdd:PRK08316 301 EVLKELRERLPGLR--FYNCYGQTE-----IAPlatvlGPEE--HLRRPGSAGRPVLNVETRVVDDDGNDVA-------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 497 cisqawPGMARTIYGDHQRFVDAYFK-------AYPGYYF-TGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 568
Cdd:PRK08316 364 ------PGEVGEIVHRSPQLMLGYWDdpektaeAFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEAL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 569 ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK08316 438 YTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA---TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
....*....
gi 1622839330 649 KIITSEAQE 657
Cdd:PRK08316 515 ERYAGAFTD 523
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
116-648 |
4.67e-44 |
|
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: 165.21 E-value: 4.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 196 AGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqHVLVAHRTDNKVHMGDLDIPLEQEMAKEDP 275
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLT----------------------------HPALAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 276 VCAPESMGseDVLFMLYTSGSTGMPKGIV--HTQAGYLLYAaltHKLVFDHRPGDIFGCVADIGWITGHSYVvYGPLCNG 353
Cdd:cd17651 129 PDPALDAD--DLAYVIYTSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAW--EWLHRVV 431
Cdd:cd17651 203 ATLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTEDlrEFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 432 GdsrCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCIsqAWPGMARTIYG 511
Cdd:cd17651 280 G---LRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPP-GVPGELYI--GGAGLARGYLN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 512 D----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 587
Cdd:cd17651 354 RpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 588 GEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd17651 434 EKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-647 |
6.24e-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: 164.68 E-value: 6.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITfnQGLRGGRVMELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDIPLEQEMAKED 274
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAVV--------------------------IDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 PVCApesmGSEDVLFMLYTSGSTGMPKGIVHTQAGYLlyaalthKLVFDHR-----PGDIFGCVADIGWiTGHSYVVYGP 349
Cdd:cd12117 130 AVPV----SPDDLAYVMYTSGSTGRPKGVAVTHRGVV-------RLVKNTNyvtlgPDDRVLQTSPLAF-DASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 350 LCNGATSVLFE-STPVYPNAGRywETVERLKINQFY--------------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 414
Cdd:cd12117 198 LLNGARLVLAPkGTLLDPDALG--ALIAEEGVTVLWltaalfnqladedpECFAGLRELLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 415 VgEPINCeawewlhrvVGDSRCTLVDTWWQTetggiciaPRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVE-GsnVS 493
Cdd:cd12117 276 L-RLVNG---------YGPTENTTFTTSHVV--------TELDEVAGSIPIG---RPIANTRVYVLDEDGRPVPpG--VP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 494 GALCISQAwpGMARTIYGD----HQRFVDAYFKayPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 567
Cdd:cd12117 333 GELYVGGD--GLALGYLNRpaltAERFVADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 568 IADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd12117 409 LRAHPGVREAVVVVREDAGGDKRLVAYVV-----AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
139-649 |
1.22e-43 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 162.94 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 nqglrggrvmelkkivdeavkhcPTVqhvlvaHRTDNKVHMGDldipleqemakedpvcapesmgseDVLFMLYTSGSTG 298
Cdd:cd05903 80 -----------------------PER------FRQFDPAAMPD------------------------AVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHTqAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 378
Cdd:cd05903 107 EPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 379 KINQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPINC----EAWEWLHRVVgdsrctlVDTWWQTETGGICI 452
Cdd:cd05903 182 GVTFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVPRslarRAAELLGAKV-------CSAYGSTECPGAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 453 APRPSEEGAEIlpGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMartIYGDHQRfVDAYFKAYP-GYYFTG 531
Cdd:cd05903 251 SITPAPEDRRL--YTDGRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSV---FLGYLDR-PDLTADAAPeGWFRTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 532 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQE 610
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALlTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622839330 611 LKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05903 402 LD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
115-648 |
1.39e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 161.40 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWerdePGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITFNQGLrggrvmelkKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDIPLEQEMAkeD 274
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPA--T 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 PVcAPESMGSEdvlfMLYTSGSTGMPKGI--------VHTQAGYLlyaALTHKLvFDHRPGDIFGCVADIGwitgHSyvv 346
Cdd:PRK13391 149 PI-ADESLGTD----MLYSSGTTGRPKGIkrplpeqpPDTPLPLT---AFLQRL-WGFRSDMVYLSPAPLY----HS--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 yGPL--CN-----GATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPi 419
Cdd:PRK13391 213 -APQraVMlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAP- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 420 nCEAwewlhrvvgDSRCTLVDtWW---------QTETGGICiAPRPSEEGAEilPGMAMRPFFGIVPVLMDekgsvvegs 490
Cdd:PRK13391 287 -CPP---------QVKEQMID-WWgpiiheyyaATEGLGFT-ACDSEEWLAH--PGTVGRAMFGDLHILDD--------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 491 nvSGALCIsqawPGMARTIYGDHQR-FVdaYFK----------AYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRL 559
Cdd:PRK13391 344 --DGAELP----PGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNI 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 560 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 639
Cdd:PRK13391 416 YPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPT 495
|
....*....
gi 1622839330 640 GKVMRRLLR 648
Cdd:PRK13391 496 GKLYKRLLR 504
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
118-647 |
2.89e-42 |
|
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: 159.33 E-value: 2.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITFnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmGDldipleqemakedpvc 277
Cdd:cd05945 75 SPAERIREILDAAKPALLIAD-----------------------------------------GD---------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 apesmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIgwitghS-----YVVYGPLCN 352
Cdd:cd05945 98 --------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 353 GATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINCEAWEWLHRVVG 432
Cdd:cd05945 163 GATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 433 DSRctLVDTWWQTETGGICIAPRPSEE---GAEILP-GmamRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMART 508
Cdd:cd05945 240 DAR--IYNTYGPTEATVAVTYIEVTPEvldGYDRLPiG---YAKPGAKLVILDEDGRPVPP-GEKGELVISG--PSVSKG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 509 iYGDHQRFVDAYFKAYPGY--YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDI 586
Cdd:cd05945 312 -YLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 587 KGEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05945 391 KVTELIAFVVPKP--GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
141-579 |
4.18e-41 |
|
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: 155.12 E-value: 4.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFn 219
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 QGLRGGRVMELKKIVDEAvkhcptvqhvlvahrtdnkvhmgDLDIPLEQEMAKEDPVCAPEsmGSEDVLFMLYTSGSTGM 299
Cdd:TIGR01733 80 SALASRLAGLVLPVILLD-----------------------PLELAALDDAPAPPPPDAPS--GPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKGIVHTQAGyLLYAALTHKLVFDHRPGDIfgcvadigWITGHSYV-------VYGPLCNGATSVLFESTPVYPNAGRYW 372
Cdd:TIGR01733 135 PKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 373 ETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICI 452
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTVWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 453 A---PRPSEEGAEILP-GmamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDAYFKAY 524
Cdd:TIGR01733 279 AtlvDPDDAPRESPVPiG---RPLANTRLYVLDDDLRPV-PVGVVGELYIGG--PGVARGYLNRpeltAERFVPDPFAGG 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 525 PGY--YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 579
Cdd:TIGR01733 353 DGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
138-649 |
9.24e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.19 E-value: 9.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 138 VRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAgFSAASLAGRINDAKCKVVIT 217
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPL-LEPEQIAELLRAAGAKVLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 218 fnqgLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRTD--------------NKVHMGDLDipLEQEMAKE--DPVCAPES 281
Cdd:PRK07529 136 ----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARylpgpkrlavplirRKAHARILD--FDAELARQpgDRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGD----------IFGCVAdigwitghsyVVYGPLC 351
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV----------TGLAPLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 352 NGATSVLfeSTPV-YPNAG---RYWETVERLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRTLGSVGEPINCEAWEWL 427
Cdd:PRK07529 279 RGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 428 HRVVGdsrCTLVDTWWQTE-TGGICIAPR--PSEEGA--EILPGMAMRpffgIVPVlmDEKGSVVEGSNVS--GALCISQ 500
Cdd:PRK07529 354 EAATG---VRIVEGYGLTEaTCVSSVNPPdgERRIGSvgLRLPYQRVR----VVIL--DDAGRYLRDCAVDevGVLCIAG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 501 A--WPGMARtiyGDHQRfvDAYFkaYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 578
Cdd:PRK07529 425 PnvFSGYLE---AAHNK--GLWL--EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAA 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 579 VIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PRK07529 498 AVGRPDAHAGELPVAYVQLKP---GASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
114-674 |
1.40e-38 |
|
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: 153.86 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvQHVLVAHRTDNKVHMGDLDIPLEQEMAKE 273
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLT---------------------------QSALAARLPELGVPVLALDALALAAEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPesmGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhrPGDIFGCVADIG-----WitghsyVVY 347
Cdd:COG1020 609 NPPVPV---TPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSfdasvW------EIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 348 GPLCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINCEAWEWL 427
Cdd:COG1020 678 GALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 428 HRVVGDSR---------CTLVDTWWQTETGGICIAP----RPseegaeiLPGMAMRpffgivpVLmDEKGSVV-EGsnVS 493
Cdd:COG1020 752 RARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSvpigRP-------IANTRVY-------VL-DAHLQPVpVG--VP 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 494 GALCIsqAWPGMARTIYGDH----QRFVDAYFkAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 567
Cdd:COG1020 815 GELYI--GGAGLARGYLNRPeltaERFVADPF-GFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAA 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 568 IADHPAVPESAVIGYPhDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:COG1020 892 LLQHPGVREAVVVARE-DAPGDKRLVAYVV--PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
570 580
....*....|....*....|....*..
gi 1622839330 648 RKIITSEAQELGDTTTLEDPSIITEIL 674
Cdd:COG1020 969 PAPAAAAAAAAAAPPAEEEEEEAALAL 995
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-642 |
2.83e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 149.81 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 119 QKSPESVALIWErdepGTEvrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 198
Cdd:PRK06178 44 RERPQRPAIIFY----GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 199 SAASLAGRINDAKCKVVITFNQglrggrvmeLKKIVdEAVKHCPTVQHVLVAHRTD-----------------NKVHMGD 261
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQ---------LAPVV-EQVRAETSLRHVIVTSLADvlpaeptlplpdslrapRLAAAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 262 LDI-PLEQEMAKEDPVCAPESmgseDVLFML-YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWI 339
Cdd:PRK06178 188 IDLlPALRACTAPVPLPPPAL----DALAALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 340 TGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVG--- 416
Cdd:PRK06178 264 AGENFGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVVSfvk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 417 --EPINCEAWewlHRVVGdsrCTLVDT-WWQTETGGICIAPRPSEEGAEILPGmamRPFFGIVPV------LMDEKGSVV 487
Cdd:PRK06178 338 klNPDYRQRW---RALTG---SVLAEAaWGMTETHTCDTFTAGFQDDDFDLLS---QPVFVGLPVpgtefkICDFETGEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 488 EGSNVSGALCISQawPGMARTIYG----DHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAE 563
Cdd:PRK06178 409 LPLGAEGEIVVRT--PSLLKGYWNkpeaTAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 564 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPdEILVVKRLPKTRSGKV 642
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP---GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV 554
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
122-647 |
4.08e-38 |
|
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: 147.82 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALiweRDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd12116 1 PDATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivDEAvkhcptvqhvlvahrTDNKVHMGDLDIPLEQEMAKEDPVCAPES 281
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 MGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFdhRPGDIFGCVADIGW-ITGHSyvVYGPLCNGATSVLF 359
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGL--GPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 360 ESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdaWvkkYDRSSLRTL-GsvGEPinceawewLHRVVGDSRCTL 438
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAG--W---QGRAGLTALcG--GEA--------LPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 439 VDTWWQ----TETGGICIAPRPSEEGAEILPGmamRPFFGIVPVLMDEKG-SVVEGsnVSGALCIsqAWPGMARTIYGD- 512
Cdd:cd12116 263 VGSLWNlygpTETTIWSTAARVTAAAGPIPIG---RPLANTQVYVLDAALrPVPPG--VPGELYI--GGDGVAQGYLGRp 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 513 ---HQRFVDAYFkAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIK 587
Cdd:cd12116 336 altAERFVPDPF-AGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGD 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 588 GEAAfAFIVVKD-SAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd12116 415 RRLV-AYVVLKAgAAPDAA----ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
122-647 |
7.64e-38 |
|
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: 147.77 E-value: 7.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITFNQG---LRGG--RVMelkkIVDEAVKHCptvqhvlvahrtdnkVHMGDLDIPleqemAKEDPV 276
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaekLASLalPVV----LLDSAEFDS---------------LSFSDLLFE-----ADEAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 277 CAPEsMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHRPGDIFGCVADIGWITGHSYVVYGPLCNGAT 355
Cdd:cd05904 151 PVVV-IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGAT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 356 SVlfestpVYP--NAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGD 433
Cdd:cd05904 230 VV------VMPrfDLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 SRctLVDTWWQTETGGICIAPRPSEEGAE-------ILPGMAMRpffgIVpvlmDEKGSVVEGSNVSGALCISQawPGM- 505
Cdd:cd05904 302 VD--LGQGYGMTESTGVVAMCFAPEKDRAkygsvgrLVPNVEAK----IV----DPETGESLPPNQTGELWIRG--PSIm 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 ----------ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 575
Cdd:cd05904 370 kgylnnpeatAATIDKE-------------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEIL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 576 ESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05904 437 DAAVIPYPDEEAGEVPMAFVVRK---PGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
171-656 |
4.24e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 145.34 E-value: 4.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 171 MPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKIVDEAVKHCPTV-----Q 245
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVlpaagE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 246 HVLVAHRTDNKVHMGDLDIPLEQEMAKEDPVcAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHR 325
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 326 PGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYwetVERLKINQFYGAPTAVRLLLKYGDAWVKKYD 405
Cdd:PLN03051 159 PGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 406 RSSLRTLGSVGEPINCEAWEWLHRVVGDSRcTLVDTWWQTETGGICIAPRPSEEGAeilPGMAMRPFFGIVPVLMDEKG- 484
Cdd:PLN03051 235 WSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQA---PGAFSTASLGTRFVLLNDNGv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 485 SVVEGSNVSGALCISQAWPGMA-RTIYGDHQRfvdAYFKAYPGYYFT-------GDGAHRTEGGYYQITGRMDDVINISG 556
Cdd:PLN03051 311 PYPDDQPCVGEVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 557 HRLGTAEIEDAI-ADHPAVPESAVIGYPhDIKGEAAFAFIVVKDS-------AGDSDVVVQELKSMVATKIAKYAVPDEI 628
Cdd:PLN03051 388 IKTSSVEIERACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGeekkgfdQARPEALQKKFQEAIQTNLNPLFKVSRV 466
|
490 500
....*....|....*....|....*...
gi 1622839330 629 LVVKRLPKTRSGKVMRRLLRKIITSEAQ 656
Cdd:PLN03051 467 KIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
139-647 |
8.41e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 145.49 E-value: 8.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRH-GVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIT 217
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 218 fnqglrggrVMELKKIVDEAVKHCPtVQHVLVAHRTD-------NKVH------------MGDLDIPLEQEMAKEDPVcA 278
Cdd:PRK08314 115 ---------GSELAPKVAPAVGNLR-LRHVIVAQYSDylpaepeIAVPawlraepplqalAPGGVVAWKEALAAGLAP-P 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 279 PESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL 358
Cdd:PRK08314 184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 359 F-----EStpvypnAGRyweTVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGd 433
Cdd:PRK08314 263 MprwdrEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTG- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 srCTLVDTWWQTETggicIAP-------RPSEEGAEIlpgmamrPFFGIVPVLMD----------EKGSVVegsnVSGAL 496
Cdd:PRK08314 331 --LDYVEGYGLTET----MAQthsnppdRPKLQCLGI-------PTFGVDARVIDpetleelppgEVGEIV----VHGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 497 CISQAWPGMART----IYGDHQRFvdayFKaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 572
Cdd:PRK08314 394 VFKGYWNRPEATaeafIEIDGKRF----FR-------TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 573 AVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK08314 463 AIQEACVIATPDPRRGETVKAVVVLRPEARGK-TTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
135-648 |
1.59e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 143.89 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 215 VITfnqglrGGRVMELkkiVDEAVKHCPT-VQHVLVAHrtdnkvhmGDLD--IPLEQEMAKEDPV-CAPESMGSEdvlfM 290
Cdd:PRK08276 87 LIV------SAALADT---AAELAAELPAgVPLLLVVA--------GPVPgfRSYEEALAAQPDTpIADETAGAD----M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 291 LYTSGSTGMPKGIVhtqagyllyAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGA-------------TSV 357
Cdd:PRK08276 146 LYSSGTTGRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 358 LFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP----INCEAWEWLHRVVgd 433
Cdd:PRK08276 217 VMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPcpveVKRAMIDWWGPII-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 srctlVDTWWQTETGGICIAPrpSEEGAEiLPGMAMRPFFGIVPVLmDEKGSVVEgsnvsgalcisqawPGMARTIY--- 510
Cdd:PRK08276 291 -----HEYYASSEGGGVTVIT--SEDWLA-HPGSVGKAVLGEVRIL-DEDGNELP--------------PGEIGTVYfem 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 511 --------GDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESA 578
Cdd:PRK08276 348 dgypfeyhNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVA 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 579 VIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK08276 422 VFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
139-647 |
2.25e-36 |
|
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: 141.85 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 NqglrggrvmELkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGSTG 298
Cdd:cd05935 81 S---------EL------------------------------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF-----ESTPvypnagrywE 373
Cdd:cd05935 98 LPKGCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL---------E 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 374 TVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETggicIA 453
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTET----MS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 454 P-------RPSEEGAEIlpgmamrPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAYPG 526
Cdd:cd05935 239 QthtnpplRPKLQCLGI-------P*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIKGR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 527 YYF-TGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsAGDSD 605
Cdd:cd05935 310 RFFrTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYRGK 388
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622839330 606 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05935 389 VTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
118-647 |
3.23e-36 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 142.65 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd05923 11 ASRAPDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRI-NDAKCKVVITFNQG------LRGGRVMELKKIVDeavkhcptvqhvlvahrtdnkvhmgdLDIPLEQEM 270
Cdd:cd05923 87 LKAAELAELIeRGEMTAAVIAVDAQvmdaifQSGVRVLALSDLVG--------------------------LGEPESAGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 271 AKEDPVCAPESMGsedvlFMLYTSGSTGMPKGIVHTQAgyllyAALTHKLVFDHRPGDIFGC------VADIGWITGHSY 344
Cdd:cd05923 141 LIEDPPREPEQPA-----FVFYTSGTTGLPKGAVIPQR-----AAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 345 VVYGPLCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAW 424
Cdd:cd05923 211 VLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 425 EWLHRVVGDSRctlVDTWWQTETGGICIAPRPSeegaeilPGMAMRPFFG----IVPVL--MDEKGSVVEGSNVSGALCI 498
Cdd:cd05923 285 ERVNQHLPGEK---VNIYGTTEAMNSLYMRDAR-------TGTEMRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 499 SQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 578
Cdd:cd05923 355 DAAFTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 579 VIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqELKSM-VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05923 428 VIGVADERWGQSVTACVVPREGTLSAD----ELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
122-647 |
6.04e-36 |
|
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: 141.29 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDPvcapes 281
Cdd:cd17643 75 RIAFILADSGPSLLLT--------------------------------------------------------DP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 mgsEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHRpgdifgcvaDIgWITGHSYV-------VYGPLCNG 353
Cdd:cd17643 93 ---DDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFNED---------DV-WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATSVLFES----TPVypnagRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINCEAWE-W 426
Cdd:cd17643 160 GRLVVVPYevarSPE-----DFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRpW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 427 LHRVvGDSRCTLVDTWWQTETggiCIAPRPSEEGAEILPGMAM----RPFFGIVPVLMDEKGSVVEGSnVSGALCISQaw 502
Cdd:cd17643 231 AGRF-GLDRPQLVNMYGITET---TVHVTFRPLDAADLPAAAAspigRPLPGLRVYVLDADGRPVPPG-VVGELYVSG-- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 503 PGMARTIYG----DHQRFVDAYFKAyPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 576
Cdd:cd17643 304 AGVARGYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRD 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 577 SAVIGYpHDIKGEAAFAFIVVKDSAgdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17643 383 AAVIVR-EDEPGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
116-666 |
9.70e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 142.19 E-value: 9.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVALIwerDEPGTevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 196 AGFSAASLAGRINDAKCKVVIT---FNQGLRGGRVMELKKIVdeavkhcPTVQHVLVAhrtdNKVHMGDLDIPLEQEMAK 272
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlFKQTRPVDLILPLQNQL-------PQLQQIVGV----DKLAPATSSLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 273 EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLL----YAALTHkLVFDhrpgDIFGCVADIGWITGHSYVVYG 348
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINC----EAW 424
Cdd:PRK06087 250 PFLIGARSVLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIPKkvarECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 425 EwlHRVVgdsrctLVDTWWQTETggiciAPR---PSEEGAEILPGMAMRPFFGI-VPVLMDEKGSV---VEGSNVSGAlc 497
Cdd:PRK06087 324 Q--RGIK------LLSVYGSTES-----SPHavvNLDDPLSRFMHTDGYAAAGVeIKVVDEARKTLppgCEGEEASRG-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 498 isqawPGMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 574
Cdd:PRK06087 389 -----PNVFMGYLDEPEltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 575 PESAVIGYPHDIKGEAAFAFIVVKDSagDSDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIts 653
Cdd:PRK06087 459 HDACVVAMPDERLGERSCAYVVLKAP--HHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI-- 534
|
570
....*....|...
gi 1622839330 654 eAQELGDTTTLED 666
Cdd:PRK06087 535 -MRRLTQDVCEEI 546
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
140-649 |
1.54e-35 |
|
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: 139.63 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINdakckvvitfn 219
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglRGGRVMelkKIVDEAVKhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgSEDVLFMLYTSGSTGM 299
Cdd:cd05974 70 ---RGGAVY---AAVDENTH--------------------------------------------ADDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKGIVHTQAGYLLyAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVypNAGRYWETVERLK 379
Cdd:cd05974 100 PKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 380 INQFYGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGIcIAPRPsee 459
Cdd:cd05974 177 VTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP--- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 460 GAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsgALCISQAWP-GMARTIYGDHQRFVDAYfkaYPGYYFTGDGAHRTE 538
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGAPATEGEV--ALDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 539 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATK 618
Cdd:cd05974 321 DGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRER 400
|
490 500 510
....*....|....*....|....*....|.
gi 1622839330 619 IAKYAVPDEiLVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05974 401 LAPYKRIRR-LEFAELPKTISGKIRRVELRR 430
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
139-649 |
9.12e-35 |
|
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: 137.42 E-value: 9.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTL-KRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIt 217
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 218 fnqglrggrvmelkkivDEAVkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsedvlfMLYTSGST 297
Cdd:cd05941 90 -----------------DPAL---------------------------------------------------ILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 298 GMPKGIVHTQAGylLYA---ALTHKLVFdhRPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlFESTPvYPNAGRYWET 374
Cdd:cd05941 102 GRPKGVVLTHAN--LAAnvrALVDAWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGAS---VEFLP-KFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 375 VERLKINQFYGAPTAVRLLLKYGDAWVKKYD---RSSLRTL-----GSVGEPINC-EAWEWL--HRvvgdsrctLVDTWW 443
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQYYEAHFTDPQfarAAAAERLrlmvsGSAALPVPTlEEWEAItgHT--------LLERYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 444 QTETGGICIAP-----RPSEEGAEiLPGMAMRpffgivpVLMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQRFVD 518
Cdd:cd05941 246 MTEIGMALSNPldgerRPGTVGMP-LPGVQAR-------IVDEETGEPLPRGEV-GEIQV--RGPSVFKEYWNKPEATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 519 AyFKAyPGYYFTGDGAHRTEGGYYQITGRM-DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfiVV 597
Cdd:cd05941 315 E-FTD-DGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA--VV 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 598 KDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05941 391 VLRAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
122-648 |
1.35e-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: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17649 1 PDAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvQHvlvahrtdnkvhmgdldipleqemakedpvcaPES 281
Cdd:cd17649 75 RLRYMLEDSGAGLLLT---------------------------HH--------------------------------PRQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 MGsedvlFMLYTSGSTGMPKGIVHTQAgyllyaALTH-----KLVFDHRPGDIFGCVADIGWITGHSYVvYGPLCNGAtS 356
Cdd:cd17649 96 LA-----YVIYTSGSTGTPKGVAVSHG------PLAAhcqatAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-C 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 357 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKyDRSSLRTLGSVGEPINCE-AWEWLhrvvgDSR 435
Cdd:cd17649 163 VVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPElLRRWL-----KAP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 436 CTLVDTWWQTE---TGGICIAPRPSEEGAEILP-GmamRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG 511
Cdd:cd17649 237 VRLFNAYGPTEatvTPLVWKCEAGAARAGASMPiG---RPLGGRSAYILDADLNPVP-VGVTGELYI--GGEGLARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 512 ----DHQRFV-DAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDI 586
Cdd:cd17649 311 rpelTAERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 587 kGEAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd17649 391 -GKQLVAYVVLRAAAAQPE-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
116-650 |
1.78e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 138.52 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIympvspLA------VAAMLACARIGA 189
Cdd:PRK07788 57 HAARRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 190 VHTVIFAGFSAASLAGRINDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPTVqHVLVAHrTDNKVHMGDLDIPLEQE 269
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAAREGVKALVYDD---------EFTDLLSALPPDLGRL-RAWGGN-PDDDEPSGSTDETLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 270 MAKED--PVCAPESMGSedvlFMLYTSGSTGMPKGIVHTQAGYLLYAALthklVFDHRP---GDIFGCVADIGWITGHSY 344
Cdd:PRK07788 194 IAGSStaPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLAG----LLSRVPfraGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 345 VVYGpLCNGATSVL---FestpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINC 421
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 422 EAWEWLHRVVGDSRCTLvdtWWQTETGGICIApRPSEegAEILPGMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQA 501
Cdd:PRK07788 338 ELATRALEAFGPVLYNL---YGSTEVAFATIA-TPED--LAEAPGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 502 WPgMARTIYGDHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 581
Cdd:PRK07788 411 FP-FEGYTDGRDKQIID-------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 582 YPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 650
Cdd:PRK07788 483 VDDEEFGQRLRAFVVKAP---GAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
114-647 |
1.79e-34 |
|
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: 137.41 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERdepgteVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITfnQGLRGGRvmelkkIVDEAVKhcPTVQHVLVAHRTDnkvhmgdldipleqemAKE 273
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLT--TADLAAR------LPAGGDV--ALLGDEALAAPPA----------------TPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPEsmgseDVLFMLYTSGSTGMPKGIVHTQAG---YLLYaaLTHKlvFDHRPGDIFGCVADIGWITGhSYVVYGPL 350
Cdd:cd17646 132 LVPPRPD-----NLAYVIYTSGSTGRPKGVMVTHAGivnRLLW--MQDE--YPLGPGDRVLQKTPLSFDVS-VWELFWPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 351 CNGATSVLFEstpvyPNAGR---YW-ETVERLKINQFYGAPTAVRLLLkygdAWVKKYDRSSLRTLGSVGEPINCEAWEW 426
Cdd:cd17646 202 VAGARLVVAR-----PGGHRdpaYLaALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 427 LHRVVGdsrCTLVDTWWQTETGgICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMA 506
Cdd:cd17646 273 FLALPG---AELHNLYGPTEAA-IDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVP-VGVPGELYL--GGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 507 RTIYG----DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY 582
Cdd:cd17646 346 RGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 583 PHDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17646 426 AAPAGAARLVGYVVP--AAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
122-647 |
2.11e-34 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 136.44 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17650 1 PDAIAVSDA------TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakeDPvcapes 281
Cdd:cd17650 75 RLQYMLEDSGAKLLLT--------------------------------------------------------QP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 mgsEDVLFMLYTSGSTGMPKGIVHTQAGYL--------LY--AALTHKLV------FDHRPGDIfgCVAdigwitghsyv 345
Cdd:cd17650 93 ---EDLAYVIYTSGTTGKPKGVMVEHRNVAhaahawrrEYelDSFPVRLLqmasfsFDVFAGDF--ARS----------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 vygpLCNGATSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPIncEA 423
Cdd:cd17650 157 ----LLNGGTLVICPDEVKL-DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 424 WEWLHRVVGdSRCTLVDTWWQTETggiCIAPRPSEEGAEILPGMAM----RPFFGIVPVLMDEKGSVVEgSNVSGALCIS 499
Cdd:cd17650 228 FKTLAARFG-QGMRIINSYGVTEA---TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQP-VGVAGELYIG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 500 QAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 575
Cdd:cd17650 303 GA--GVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAID 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 576 ESAVIgYPHDIKGEAAFAFIVVKDSAGDSdvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17650 381 EAVVA-VREDKGGEARLCAYVVAAATLNT----AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
122-641 |
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 1622839330 122 PESVALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVItFNQGLrGGRVMELKkivDEavkhCPTVQHVL-VAHRTDNKVHMGdlDIPLEQEMAKEDPVCAPE 280
Cdd:PRK07798 91 ELRYLLDDSDAVALV-YEREF-APRVAEVL---PR----LPKLRTLVvVEDGSGNDLLPG--AVDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 281 SmGSEDVLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLvfDHRPG----DIFGCVADIGWITGHSYVVYGPLCNGAT- 355
Cdd:PRK07798 160 E-RSPDDLYLLYTGGTTGMPKGVMWRQED--IFRVLLGGR--DFATGepieDEEELAKRAAAGPGMRRFPAPPLMHGAGq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 356 -----------SVLFESTPVYpNAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGS 414
Cdd:PRK07798 235 waafaalfsgqTVVLLPDVRF-DADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 415 VGEPINCEAWEWLHRVVGDSrcTLVDTWWQTETG--GICIAPRPSEEGAeilpgmamRPFFGIVP--VLMDEKGSVVE-G 489
Cdd:PRK07798 304 GGALFSPSVKEALLELLPNV--VLTDSIGSSETGfgGSGTVAKGAVHTG--------GPRFTIGPrtVVLDEDGNPVEpG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 490 SNVSGALcisqawpgmART------IYGDHQRfVDAYFKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGT 561
Cdd:PRK07798 374 SGEIGWI---------ARRghiplgYYKDPEK-TAETFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 562 AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 641
Cdd:PRK07798 444 EEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
118-647 |
6.55e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 129.36 E-value: 6.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd12115 9 AARTPDAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvc 277
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 apesmGSEDVLFMLYTSGSTGMPKG--IVHTQAGYLLYAALTHklvFdhrPGDIFGCVADIGWITGHSYV--VYGPLCNG 353
Cdd:cd12115 103 -----DPDDLAYVIYTSGSTGRPKGvaIEHRNAAAFLQWAAAA---F---SAEELAGVLASTSICFDLSVfeLFGPLATG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATSVLFESTPVYPNAGRYWETVerlKINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLH----- 428
Cdd:cd12115 172 GKVVLADNVLALPDLPAAAEVT---LINT---VPSAAAELLRHDAL------PASVRVVNLAGEPLPRDLVQRLYarlqv 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 429 -RVV---GDSRctlvDTWWQTetggicIAPRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpG 504
Cdd:cd12115 240 eRVVnlyGPSE----DTTYST------VAPVPPGASGEVSIG---RPLANTQAYVLDRALQPV-PLGVPGELYIGGA--G 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 505 MARTIYGD----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVpESAVI 580
Cdd:cd12115 304 VARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV-REAVV 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 581 GYPHDIKGEAAF-AFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd12115 383 VAIGDAAGERRLvAYIVAEPGAA---GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
112-652 |
2.50e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 128.16 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 112 NCLDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVH 191
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFEEKK------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 192 TVIFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivDEAVKHcptvqhvlvAHRTDNKVHMGDLdipleQEMA 271
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLIT-----------------DDDFEA---------KLIPGISVKFAEL-----MNGP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 272 KEDPVcaPESMGSED-VLFMLYTSGSTGMPKGIVHTQAGYLlYAALTHKLVFDHRPGDIFGCVADIGWITGHSY----VV 346
Cdd:PRK03640 129 KEEAE--IQEEFDLDeVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSIlmrsVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 YGplcngATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAV-RLLLKYGDAwvkKYDrSSLRT--LGsvGEPIN--- 420
Cdd:PRK03640 206 YG-----MRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLqRLLERLGEG---TYP-SSFRCmlLG--GGPAPkpl 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 421 ---CEAWewlhrvvgdsRCTLVDTWWQTETggiC--IAPRPSEEGAEILpGMAMRPFFGI--------VPVLMDEKGS-V 486
Cdd:PRK03640 271 leqCKEK----------GIPVYQSYGMTET---AsqIVTLSPEDALTKL-GSAGKPLFPCelkiekdgVVVPPFEEGEiV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 487 VEGSNV-SGALCISQAwpgmartiygDHQRFVDAYFKaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIE 565
Cdd:PRK03640 337 VKGPNVtKGYLNREDA----------TRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 566 DAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 645
Cdd:PRK03640 400 EVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-----SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
....*..
gi 1622839330 646 LLRKIIT 652
Cdd:PRK03640 475 ELKQLVE 481
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
114-647 |
3.64e-31 |
|
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: 127.44 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtV 193
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAgfsaaslagrindakckvvitfnqgLRGGRVMELKKIVD--EAVkhcptvqhVLVAHRTdnkvHMGDLDIPLEQEMA 271
Cdd:cd05920 93 VLA-------------------------LPSHRRSELSAFCAhaEAV--------AYIVPDR----HAGFDHRALARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 272 KEDPvcapesmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHRpgDIFGCVADIGwitgHSYV----- 345
Cdd:cd05920 136 ESIP----------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLDQD--TVYLAVLPAA----HNFPlacpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE 425
Cdd:cd05920 200 VLGTLLAGGRVVLAPD----PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 426 WLHRVVGdsrCTLVDTWWQTEtGGICIApRPSEEGAEIL--PGMAMRPFFGIVPVlmDEKGSVVeGSNVSGALcisqawp 503
Cdd:cd05920 274 RVPPVLG---CTLQQVFGMAE-GLLNYT-RLDDPDEVIIhtQGRPMSPDDEIRVV--DEEGNPV-PPGEEGEL------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 504 gMAR---TIYGdhqrfvdaYFKAyP----------GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 570
Cdd:cd05920 339 -LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 571 HPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05920 409 HPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-657 |
4.41e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.23 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK12316 518 EEQVERTPEAPALAF------GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDIPLEQEMAKED 274
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLS--------------------------QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 PvcAPE-SMGSEDVLFMLYTSGSTGMPKGIVHTqagyllYAALTHKL-----VFDHRPGDIFGCVADIGWITGHsYVVYG 348
Cdd:PRK12316 646 E--NPGtELNPENLAYVIYTSGSTGKPKGAGNR------HRALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSV-WEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLH 428
Cdd:PRK12316 717 PLMSGARLVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEAL---PADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 429 RVVGD-SRCTLVDTWWQTE-TGGICIAPRPSEEGAEILPGmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMA 506
Cdd:PRK12316 789 QVFAKlPQAGLYNLYGPTEaAIDVTHWTCVEEGGDSVPIG---RPIANLACYILDANLEPVP-VGVLGELYLAGR--GLA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 507 RTIYG----DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGy 582
Cdd:PRK12316 863 RGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA- 941
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 583 phdIKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 657
Cdd:PRK12316 942 ---VDGKQLVGYVVLESEGGD---WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
114-663 |
5.61e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 128.23 E-value: 5.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNqglrggrvMELKKIVDeaVKHCPTVQHVLVAHRTD------------------- 254
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLD--------LVFPRVTN--VQSATKIEHVIVTRIADflpfpknllypfvqkkqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 255 -----NKVHMGDLDIPLEQEM-AKEDPVCAPESmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGD 328
Cdd:PRK06710 174 lvvkvSESETIHLWNSVEKEVnTGVEVPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 329 --IFGcVADIGWITGHSYVVYGPLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDR 406
Cdd:PRK06710 250 evVLG-VLPFFHVYGMTAVMNLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 407 SSLRTLGSVGEPINCEAWEWLHRVVG-----------DSRCTLVDTWWQTETGGICIAPRPSEEG--AEILPGMAMRPff 473
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETVTGgklvegyglteSSPVTHSNFLWEKRVPGSIGVPWPDTEAmiMSLETGEALPP-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 474 givpvlmDEKGSVVegsnVSGALCISQAW--PGMARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDV 551
Cdd:PRK06710 401 -------GEIGEIV----VKGPQIMKGYWnkPEETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 552 INISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVV 631
Cdd:PRK06710 457 IVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE---GTECSEEELNQFARKYLAAYKVPKVYEFR 533
|
570 580 590
....*....|....*....|....*....|..
gi 1622839330 632 KRLPKTRSGKVMRRLLrkiITSEAQELGDTTT 663
Cdd:PRK06710 534 DELPKTTVGKILRRVL---IEEEKRKNEDEQT 562
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
112-649 |
7.33e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 127.46 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 112 NCLDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVH 191
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 192 TVIFAGFSAASLAGRINDAKCKVVI---TFNQGLRGGRVMELK---KIVDEAVKHCPTVQHVLVAHRtDNKVHMGDLDip 265
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchaDFPEHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 266 leqemaKEDPvcapesmgsedvLFMLYTSGSTGMPKGIV--HTQAGYLLyaalTHKLVfDHRPGdifgcvadigwITGH- 342
Cdd:PRK07470 162 ------HDDP------------CWFFFTSGTTGRPKAAVltHGQMAFVI----TNHLA-DLMPG-----------TTEQd 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 343 -SYVVyGPL---------CN---GATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSL 409
Cdd:PRK07470 208 aSLVV-APLshgagihqlCQvarGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 410 RTLGSVGEPINCEAWEWLHRVVGDsrcTLVDTWWQTE-TGGICIAPRP---SEEGAEILPGMAMRPFFGIVPVLMDEKGS 485
Cdd:PRK07470 283 RYVIYAGAPMYRADQKRALAKLGK---VLVQYFGLGEvTGNITVLPPAlhdAEDGPDARIGTCGFERTGMEVQIQDDEGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 486 VVeGSNVSGALCISqawpGMArtIYGDHQRFVDAYFKAYPGYYF-TGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEI 564
Cdd:PRK07470 360 EL-PPGETGEICVI----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 565 EDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:PRK07470 433 EEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA---PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
....*
gi 1622839330 645 RLLRK 649
Cdd:PRK07470 510 KMVRE 514
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
115-649 |
1.13e-30 |
|
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: 125.50 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALiwerdePGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVItfnqglrggrvmelkkivdeavkhCPTVQHvlvahrtdnkvhmgdldipleqemaked 274
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLL------------------------TTDSPD---------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 pvcapesmgseDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIGW--ITGhsyVVYGPLCN 352
Cdd:cd17653 106 -----------DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 353 GATSVLfeSTPVYPnagryWETVERlKINQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPINCE-AWEWLHRVV 431
Cdd:cd17653 171 GGTLVL--ADPSDP-----FAHVAR-TVDALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEAVPPSlLDRWSPGRR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 432 -----GDSRCTLVDTWWQTETGgiciapRPSEEGAEIlPGMAMRpffgivpvLMDE-KGSVVEGsnVSGALCISQawPGM 505
Cdd:cd17653 235 lynayGPTECTISSTMTELLPG------QPVTIGKPI-PNSTCY--------ILDAdLQPVPEG--VVGEICISG--VQV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 ARTIYGDHQRFVDAY--FKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVI 580
Cdd:cd17653 296 ARGYLGNPALTASKFvpDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 581 gyphdIKGEAAFAFIVvkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd17653 376 -----VVNGRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
114-645 |
1.39e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 126.54 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNQGLRGGRvmelkkivDEAVKHCPtvqhVLVAHRTDNKVHMGDLDIPLEQEMAKE 273
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRA--------EPTTRWWP----LTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPESMGSEDVLFMlYTSGSTGMPKGIVHTQAGyllYAALTHKLVFDHRPGDIFGCVADIGWITGHSYV--VYGPLC 351
Cdd:PRK05852 166 PATSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 352 NGATSVLfestpvyPNAGR-----YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEW 426
Cdd:PRK05852 242 SGGAVLL-------PARGRfsahtFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 427 LHRVVG--------------DSRCTLVDTWWQTETGGICIAPRPSEEGAEIlpgMAMRPFFGIVPVlmDEKGSV-VEGSN 491
Cdd:PRK05852 315 LQTEFAapvvcafgmteathQVTTTQIEGIGQTENPVVSTGLVGRSTGAQI---RIVGSDGLPLPA--GAVGEVwLRGTT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 492 VsgalcisqawpgmARTIYGD----HQRFVDAYFKaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 567
Cdd:PRK05852 390 V-------------VRGYLGDptitAANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 568 IADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 645
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP---PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
120-649 |
1.53e-30 |
|
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: 126.44 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 120 KSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 199
Cdd:TIGR03098 12 RLPDATALVH------HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 200 AASLAGRINDAKCKVVITFNQGLRggrvmelkkIVDEAVKHCPTVQHVLvahRTDNKVHMGDLDIPLE----QEMAKEDP 275
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLD---------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEEpaswPKLLALGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 276 VCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLvfDHRPGDIFGCVADIGWITGHSYVVYGPLCnGA 354
Cdd:TIGR03098 154 ADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAqSVATYL--ENRPDDRLLAVLPLSFDYGFNQLTTAFYV-GA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 355 TSVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDS 434
Cdd:TIGR03098 231 TVVLHD----YLLPRDVLKALEKHGITGLAAVPPLWAQLAQ--LDW-PESAAPSLRYLTNSGGAMPRATLSRLRSFLPNA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 435 RCTLVdtWWQTETGGICIAP------RPSEEGAEIlpgmamrPFFGIvpVLMDEKGSVVEgSNVSGALCisQAWPGMART 508
Cdd:TIGR03098 304 RLFLM--YGLTEAFRSTYLPpeevdrRPDSIGKAI-------PNAEV--LVLREDGSECA-PGEEGELV--HRGALVAMG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 509 IYGDHQRfVDAYFKAYPGYY----------FTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 578
Cdd:TIGR03098 370 YWNDPEK-TAERFRPLPPFPgelhlpelavWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 579 VIGYPHDIKGEaafAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:TIGR03098 449 AFGVPDPTLGQ---AIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
114-650 |
2.70e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 126.04 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNqglrGGRVMELKKIVDEAVKHCPTVQHVLVAH----RTDNKVHMGDLDIP---L 266
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD----AFKTSDYHAMLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 267 EQEMAKEDPVCAPE-------SMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDHrpgdifgcvadiGWI 339
Cdd:PRK12583 176 WHELQARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKG-----------ATLSHHNILNN------------GYF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 340 TGHS---------------YVVYGPLCNGATSVLFESTPVYPN----AGRYWETVERLKINQFYGAPTAVRLLLKYGDaw 400
Cdd:PRK12583 233 VAESlgltehdrlcvpvplYHCFGMVLANLGCMTVGACLVYPNeafdPLATLQAVEEERCTALYGVPTMFIAELDHPQ-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 401 VKKYDRSSLRTLGSVGEPinCEAwEWLHRVVGDSRCTLVD-TWWQTETGGICIA-------PRPSEEGAEILPGMAMRpf 472
Cdd:PRK12583 311 RGNFDLSSLRTGIMAGAP--CPI-EVMRRVMDEMHMAEVQiAYGMTETSPVSLQttaaddlERRVETVGRTQPHLEVK-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 473 fgivpvLMDEKGSVVEGSNVsGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQ 543
Cdd:PRK12583 386 ------VVDPDGATVPRGEI-GELCtrgysVMKGYWNNpeatAESIDED-------------GWMHTGDLATMDEQGYVR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 544 ITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYA 623
Cdd:PRK12583 446 IVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP---GHAASEEELREFCKARIAHFK 522
|
570 580
....*....|....*....|....*..
gi 1622839330 624 VPDEILVVKRLPKTRSGKVMRRLLRKI 650
Cdd:PRK12583 523 VPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
115-648 |
2.95e-30 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 125.57 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK08008 14 DDLADVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKivdeavKHCPtvQHVLVAhRTDNKVHMGDLDipLEQEMAKED 274
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQED------ATPL--RHICLT-RVALPADDGVSS--FTQLKAQQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 P-VCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQ-----AGYllYAALTHKLVFDHR-----PG---DiFGCVADIGWIT 340
Cdd:PRK08008 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDDDVyltvmPAfhiD-CQCTAAMAAFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 341 GhsyvvygplcnGATSVLFEStpvYpNAGRYWETVERLKINQFYGAPTAVR-LLLKYGDAWvkkyDRS-SLRTLG----- 413
Cdd:PRK08008 239 A-----------GATFVLLEK---Y-SARAFWGQVCKYRATITECIPMMIRtLMVQPPSAN----DRQhCLREVMfylnl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 414 SVGEPincEAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRPSEEgaEILPGMAmRPFFGIVPVLMDEKGSVVEgSNVS 493
Cdd:PRK08008 300 SDQEK---DAFEERFGV------RLLTSYGMTETIVGIIGDRPGDK--RRWPSIG-RPGFCYEAEIRDDHNRPLP-AGEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 494 GALCIsQAWPGmaRTIYGDHQRFVDAYFKAYP--GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 571
Cdd:PRK08008 367 GEICI-KGVPG--KTIFKEYYLDPKATAKVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 572 PAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGE---TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
114-648 |
4.25e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 125.24 E-value: 4.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVItFNQGLRGgrvMELKKIVDEAVKHC-PTVQHVLVAHRTDNKVH---MGDLDIPLEQE 269
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLV-VWPGFKG---IDFAAILAAVPPDAlPPLRAIAVVDDAADATPapaPGARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 270 MAKEDPVCAPESmGSEDVLFMLY-TSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDIFGCVADIGWITGHSYVVyG 348
Cdd:PRK06164 166 DPAPPAAAGERA-ADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-G 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVG-EPINCEAWEW- 426
Cdd:PRK06164 243 ALAGGAPLVCE---PVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFGFASfAPALGELAALa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 427 ------LHRVVGDSRC-TLVDTWwqtetggiciaPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCIS 499
Cdd:PRK06164 316 rargvpLTGLYGSSEVqALVALQ-----------PATDPVSVRIEGGGRPASPEARVRARDPQDGALLP-DGESGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 500 QawPGMARTiYGDHQrfvDAYFKAYP--GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 577
Cdd:PRK06164 384 A--PSLMRG-YLDNP---DATARALTddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 578 AVIGYPHDIKGEAAfAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSG---KVMRRLLR 648
Cdd:PRK06164 458 QVVGATRDGKTVPV-AFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
285-648 |
6.98e-30 |
|
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: 121.23 E-value: 6.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 EDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH----------RPGDI----------FGCVADIGWITGHsy 344
Cdd:cd05917 2 DDVINIQFTSGTTGSPKG-----------ATLTHHNIVNNgyfigerlglTEQDRlcipvplfhcFGSVLGVLACLTH-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 345 vvygplcnGATSVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAW 424
Cdd:cd05917 69 --------GATMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 425 EWLHRVVGDSRCTLVdtWWQTETGGICIAPR---PSEEGAE----ILPGMAMRpffgivpvLMDEKGSVVEGSNVSGALC 497
Cdd:cd05917 136 KRVIEVMNMKDVTIA--YGMTETSPVSTQTRtddSIEKRVNtvgrIMPHTEAK--------IVDPEGGIVPPVGVPGELC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 498 ISQAwpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES 577
Cdd:cd05917 206 IRGY--SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDV 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 578 AVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05917 282 QVVGVPDERYGEEVCAWIRLKEGA---ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-649 |
8.85e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 124.12 E-value: 8.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 111 VNCLDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV 190
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 191 HTVIFAGFSAASLAGRINDAKCKVVITfnQGLRGGRVMELKKIVdeavkhcPTVQHVLVA-HRTDNKVhmgdldIPLEQE 269
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALAPVATAVRDIV-------PLLSTVVVAgGSSDDSV------LGYEDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 270 MAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDifgcvaDIGWITGHSYVVYGp 349
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGADINS------DVGFVGVPLFHIAG- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 350 LCNGATSVLFESTPV-YP----NAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSsLRTLGSVGEPinceAW 424
Cdd:PRK07786 231 IGSMLPGLLLGAPTViYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAP----AS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 425 EWLHRVVGDS--RCTLVDTWWQTETGGI-CI-----APRPSEEGAEILPGMAMRpffgIVPVLMDE--KGSVVEgsnvsg 494
Cdd:PRK07786 304 DTLLRQMAATfpEAQILAAFGQTEMSPVtCMllgedAIRKLGSVGKVIPTVAAR----VVDENMNDvpVGEVGE------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 495 alcISQAWPGMARTIYGDHQRFVDAYfkaYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 574
Cdd:PRK07786 374 ---IVYRAPTLMSGYWNNPEATAEAF---AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDI 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 575 PESAVIGYPHDIKGEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PRK07786 448 VEVAVIGRADEKWGEVPVAVAAVRN--DDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
122-648 |
1.87e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 123.17 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK06188 26 PDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVItFNQGLRGGRVMELkkivdeaVKHCPTVQHVLVahrtdnkvhMGDLDI--PLEQEMAKEDPVCAP 279
Cdd:PRK06188 100 DHAYVLEDAGISTLI-VDPAPFVERALAL-------LARVPSLKHVLT---------LGPVPDgvDLLAAAAKFGPAPLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 280 ESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALthklvfdhrpgdifgCVADIGWITGHSYVVYGPLCNGAtsvlf 359
Cdd:PRK06188 163 AAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI---------------QLAEWEWPADPRFLMCTPLSHAG----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 360 eSTPVYP--------------NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN----C 421
Cdd:PRK06188 223 -GAFFLPtllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSpvrlA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 422 EAwewlHRVVGDsrcTLVDTWWQTETGgICIAPRPSEEGAEILPGM---AMRPFFGIVPVLMDEKGSVVEGSNVsGALCI 498
Cdd:PRK06188 300 EA----IERFGP---IFAQYYGQTEAP-MVITYLRKRDHDPDDPKRltsCGRPTPGLRVALLDEDGREVAQGEV-GEICV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 499 SQawPGMArtiygdhqrfvDAYFKAyP---------GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 569
Cdd:PRK06188 371 RG--PLVM-----------DGYWNR-PeetaeafrdGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLA 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 570 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK06188 437 EHPAVAQVAVIGVPDEKWGEAVTAVVVLRP---GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
116-653 |
2.77e-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: 121.88 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakED 274
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLT-------------------------------------------------------SS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 PvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQAGYLLyAALTHKLVFDHRPGD--------IFG-CVADIgwitghsyv 345
Cdd:cd05918 105 P---------SDAAYVIFTSGSTGKPKGVVIEHRALST-SALAHGRALGLTSESrvlqfasyTFDvSILEI--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 vYGPLCNGAT------SVLFESTPvypnagrywETVERLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVG 416
Cdd:cd05918 166 -FTTLAAGGClcipseEDRLNDLA---------GFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 417 EPIN---CEAWEwlhrvvgdSRCTLVDTWWQTET--GGICIAPRPSEEGAEILPGMAMRPFfgIV-PVLMDE---KGSVv 487
Cdd:cd05918 225 EALTqsdVDTWA--------DRVRLINAYGPAECtiAATVSPVVPSTDPRNIGRPLGATCW--VVdPDNHDRlvpIGAV- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 488 egsnvsGALCISQawPGMARTIYGDHQR----FV-DAYFKAYPGY------YFTGDGAHRTEGGYYQITGRMDDVINISG 556
Cdd:cd05918 294 ------GELLIEG--PILARGYLNDPEKtaaaFIeDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRG 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 557 HRLGTAEIEDAIADHPAVPESAVIGY--PHDIKGEAAF-AFIVVKDSAGDSD--------------VVVQELKSMVATKI 619
Cdd:cd05918 366 QRVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLvAFVVLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRL 445
|
570 580 590
....*....|....*....|....*....|....
gi 1622839330 620 AKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 653
Cdd:cd05918 446 PSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
131-649 |
8.41e-29 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 121.40 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 131 RDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV-HTVIFAGFsAASLAGRIND 209
Cdd:PRK06018 31 RSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 210 AKCKVVI---TFnqglrggrVMELKKIVDeavkHCPTVQHVLVAhrTDnKVHMGDLDIP----LEQEMAKEDPVCAPESM 282
Cdd:PRK06018 110 AEDRVVItdlTF--------VPILEKIAD----KLPSVERYVVL--TD-AAHMPQTTLKnavaYEEWIAEADGDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 283 GSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlvfdhrpGDIFGCVA-DI-----------GW-------ITGHS 343
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANN-------GDALGTSAaDTmlpvvplfhanSWgiafsapSMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 344 YVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPincea 423
Cdd:PRK06018 248 LVMPGAKLDGAS--------VY-------ELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 424 wEWLHRVVGDSRCTLVDTWWQTET---GGICIAPRPSEEgaeiLPG--------MAMRPFFGIVPVLMDEKG-SVVEGSN 491
Cdd:PRK06018 308 -RSMIKAFEDMGVEVRHAWGMTEMsplGTLAALKPPFSK----LPGdarldvlqKQGYPPFGVEMKITDDAGkELPWDGK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 492 VSGALCISQawPGMARTIYGDHQRFVDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 571
Cdd:PRK06018 383 TFGRLKVRG--PAVAAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGH 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 572 PAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PRK06018 456 PKVAEAAVIGVYHPKWDERPLLIVQLKP---GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
137-649 |
1.74e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 119.71 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 tfnqglrggrvmelkkiVDEAvkhcptvqhvlvaHRTDNKVHMGDLDIPLEQEMAKEDPVCapesmgsedvlfMLYTSGS 296
Cdd:cd12118 107 -----------------VDRE-------------FEYEDLLAEGDPDFEWIPPADEWDPIA------------LNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 297 TGMPKGIVHTQAG-YL--LYAALTHKLvfDHRPG-----DIFGCVadiGWItghsyVVYGPLCNGATSVLFESTpvypNA 368
Cdd:cd12118 145 TGRPKGVVYHHRGaYLnaLANILEWEM--KQHPVylwtlPMFHCN---GWC-----FPWTVAAVGGTNVCLRKV----DA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 369 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYD-RSSLRTLGSVGEPINCEAWEWLHRVVgdsrctlVDTWWQTET 447
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDV-------THVYGLTET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 448 GG---ICIAPR-----PSEEGAEILP--GMAMRPFFGI--------VPVLMDEK--GSVV-EGSNV-SGALCISQAwpgm 505
Cdd:cd12118 284 YGpatVCAWKPewdelPTEERARLKArqGVRYVGLEEVdvldpetmKPVPRDGKtiGEIVfRGNIVmKGYLKNPEA---- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 artiygdhqrfVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 585
Cdd:cd12118 360 -----------TAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDE 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 586 IKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd12118 427 KWGEVPCAFVELKEGA---KVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
139-656 |
2.01e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 119.53 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 nqglrggrvmelkkivDEAVKhcptvqhvlvAHRTDnkvhMGDLDIpLEQEMAKEDPVCAPeSMGSEDVLFMLYTSGSTG 298
Cdd:PRK09088 101 ----------------DDAVA----------AGRTD----VEDLAA-FIASADALEPADTP-SIPPERVSLILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHT----QAGYLLYAALTHklvFDHRpgDIFGCVADIGWITGHSYVVYGPLCNGATSVLfeSTPVYPNAGRYWET 374
Cdd:PRK09088 149 QPKGVMLSernlQQTAHNFGVLGR---VDAH--SSFLCDAPMFHIIGLITSVRPVLAVGGSILV--SNGFEPKRTLGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 375 VERLKINQFYGAPTAVRLLLKYGDawvkkYDRSSLRTLGSV---GEPINCEAWE-WLhrvvgDSRCTLVDTWWQTETGGI 450
Cdd:PRK09088 222 DPALGITHYFCVPQMAQAFRAQPG-----FDAAALRHLTALftgGAPHAAEDILgWL-----DDGIPMVDGFGMSEAGTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 451 CIAPRPSEEGAEILpGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAypGYYFT 530
Cdd:PRK09088 292 FGMSVDCDVIRAKA-GAAGIPTPTVQTRVVDDQGNDCP-AGVPGELLLRG--PNLSPGYWRRPQATARAFTGD--GWFRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 531 GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQE 610
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA---PLDLER 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622839330 611 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 656
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
286-649 |
4.74e-28 |
|
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: 115.51 E-value: 4.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVfdhrpgdifGCVADIGW--------ITGHSYVVYGPLCNGATSV 357
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---------GFGGGDSWllslplyhVGGLAILVRSLLAGAELVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 358 LFESTPVYPNAGRYWETVERLkinqfygAPTAVRLLLKYG--DAWVKkydrsSLRTLGSVGEPINCEawewLHRVVGDSR 435
Cdd:cd17630 72 LERNQALAEDLAPPGVTHVSL-------VPTQLQRLLDSGqgPAALK-----SLRAVLLGGAPIPPE----LLERAADRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 436 CTLVDTWWQTETGGICIAPRPSEEGA----EILPGMAMRpffgivpvlmdekgsVVEGsnvsGALCISQAWPGMARTIYG 511
Cdd:cd17630 136 IPLYTTYGMTETASQVATKRPDGFGRggvgVLLPGRELR---------------IVED----GEIWVGGASLAMGYLRGQ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 512 DHQRFVDayfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 591
Cdd:cd17630 197 LVPEFNE------DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 592 FAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd17630 271 VAVIV-----GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
136-650 |
5.41e-28 |
|
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: 118.78 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 136 TEVRITYRELLETTCRLANTLKRHG--------VCRGDCVAIYMPvsplavaaMLACARIGAVHTVIFAGFSAASLAGRI 207
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGlkqndriaVCSENSLQFFLP--------VIAGLFIGVGVAPTNDIYNERELDHSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 208 NDAKCKVVITFNQGLRggRVMELKKIVdeavkhcPTVQHVLVahrTDNKVHMGDLDiPLEQEMAKEDPVC-------APE 280
Cdd:cd17642 113 NISKPTIVFCSKKGLQ--KVLNVQKKL-------KIIKTIII---LDSKEDYKGYQ-CLYTFITQNLPPGfneydfkPPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 281 SMGSEDVLFMLYTSGSTGMPKGIvhtqagyllyaALTHKLV---FDHRPGDIFGC-----VADIGWITGHS----YVVYG 348
Cdd:cd17642 180 FDRDEQVALIMNSSGSTGLPKGV-----------QLTHKNIvarFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGATSVL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINCEAWE 425
Cdd:cd17642 249 YLICGFRVVLmykFEEE-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 426 WLHRVVGDSrcTLVDTWWQTE-TGGICIAP----RPSEEGAeilpgmaMRPFFGIVPVLMDEKGSVveGSNVSGALCISQ 500
Cdd:cd17642 320 AVAKRFKLP--GIRQGYGLTEtTSAILITPegddKPGAVGK-------VVPFFYAKVVDLDTGKTL--GPNERGELCVKG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 501 awPGMARTIYGDHQRFVDAYFKayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 580
Cdd:cd17642 389 --PMIMKGYVNNPEATKALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 581 GYPHDIKGEAAFAFivvkdsagdsdVVVQELKSMVATKIAKYaVPDEILVVKRL----------PKTRSGKVMRRLLRKI 650
Cdd:cd17642 465 GIPDEDAGELPAAV-----------VVLEAGKTMTEKEVMDY-VASQVSTAKRLrggvkfvdevPKGLTGKIDRRKIREI 532
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
120-648 |
6.63e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 118.05 E-value: 6.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 120 KSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 199
Cdd:PRK07514 14 ADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 200 AASLAGRINDAKCKVVItfnqgLRGGRVMELKKIvdeAVKHcpTVQHV--LVAHRTDnkvhmgdldiPLEQEMAKEDPVC 277
Cdd:PRK07514 89 LAELDYFIGDAEPALVV-----CDPANFAWLSKI---AAAA--GAPHVetLDADGTG----------SLLEAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 APESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGD-------IFgcvadigwitgHSYVVY--- 347
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSH-GNLLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvat 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 348 -GPLCNGATSVL---FESTPV---YPNAgryweTVerlkinqFYGAPT-AVRLLlkyGDAWVKKYDRSSLRTLGSVGEPI 419
Cdd:PRK07514 217 nVALLAGASMIFlpkFDPDAVlalMPRA-----TV-------MMGVPTfYTRLL---QEPRLTREAAAHMRLFISGSAPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 420 NCEAW-EWLHRVvGDsrcTLVDTWWQTETGGICIAPRpseEGAEI-------LPGMAMR---PFFGiVPVLMDEKGSV-V 487
Cdd:PRK07514 282 LAETHrEFQERT-GH---AILERYGMTETNMNTSNPY---DGERRagtvgfpLPGVSLRvtdPETG-AELPPGEIGMIeV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 488 EGSNVsgalcisqawpgmartiygdhqrfvdayFKAY---P----------GYYFTGDGAHRTEGGYYQITGRMDDVInI 554
Cdd:PRK07514 354 KGPNV----------------------------FKGYwrmPektaeefradGFFITGDLGKIDERGYVHIVGRGKDLI-I 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 555 SG-HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVK 632
Cdd:PRK07514 405 SGgYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAlDEAAILAALKG----RLARFKQPKRVFFVD 480
|
570
....*....|....*.
gi 1622839330 633 RLPKTRSGKVMRRLLR 648
Cdd:PRK07514 481 ELPRNTMGKVQKNLLR 496
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
122-653 |
7.38e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 118.04 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 200
Cdd:PRK06839 16 PDRIAIITEEEE------MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 201 ASLAGRINDAKCKVVitFNQGLRGGRVMELKKIVdeavkhcpTVQHVlvahrtdnkVHMGDLDIPLEQEMAKEDPvcape 280
Cdd:PRK06839 90 NELIFQLKDSGTTVL--FVEKTFQNMALSMQKVS--------YVQRV---------ISITSLKEIEDRKIDNFVE----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 281 smGSEDVLFML-YTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL- 358
Cdd:PRK06839 146 --KNESASFIIcYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVp 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 359 --FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLHRVVGDSRC 436
Cdd:PRK06839 223 rkFEPT-------KALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEE----LMREFIDRGF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 437 TLVDTWWQTETggiciAPRP---SEEGAEILPGMAMRP-FFGIVPVLMDEKGSVVEGS----NVSGALCISQAW---PGM 505
Cdd:PRK06839 290 LFGQGFGMTET-----SPTVfmlSEEDARRKVGSIGKPvLFCDYELIDENKNKVEVGEvgelLIRGPNVMKEYWnrpDAT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 ARTIYGdhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHD 585
Cdd:PRK06839 365 EETIQD--------------GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHV 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 586 IKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 653
Cdd:PRK06839 431 KWGEIPIAFIVKKSSS---VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
119-648 |
7.65e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 118.32 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 119 QKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 198
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 199 SAASLAGRINDAKCKVVItFNQglrggrvmELKKIVDEAVKHCPTVQHVLVAHRTDNKV-HMGDLDIPLEQEmakedpvc 277
Cdd:PRK13382 128 AGPALAEVVTREGVDTVI-YDE--------EFSATVDRALADCPQATRIVAWTDEDHDLtVEVLIAAHAGQR-------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 aPESMGSEDVLFMLyTSGSTGMPKGIVHTQAGyllyAALTHKLVFDHRPgdifgcvadigWITGHSYVVYGPL------C 351
Cdd:PRK13382 191 -PEPTGRKGRVILL-TSGTTGTPKGARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMfhawgfS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 352 NGATSVLFESTPVYPNAGRYWETVERLKINQFYG---APTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:PRK13382 254 QLVLAASLACTIVTRRRFDPEATLDLIDRHRATGlavVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 429 RVVGDsrcTLVDTWWQTETGGICIApRPSEEGAEilPGMAMRPFFGIVPVLMDEKGSVVEgsnvsgalcisqawPGMART 508
Cdd:PRK13382 334 DQFGD---VIYNNYNATEAGMIATA-TPADLRAA--PDTAGRPAEGTEIRILDQDFREVP--------------TGEVGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 509 IYGDHQRFVDAYFKA-----YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP 583
Cdd:PRK13382 394 IFVRNDTQFDGYTSGstkdfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 584 HDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK13382 474 DEQYGQRLAAFVVLK---PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
122-647 |
7.68e-28 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 117.76 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd12114 1 PDATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvQHVLVAHRTDNkvhmGDLDIPLEQEMAKEDPVCAPES 281
Cdd:cd12114 75 RREAILADAGARLVLT---------------------------DGPDAQLDVAV----FDVLILDLDALAAPAPPPPVDV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 mGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhrPGDIFGCVA----DIGwitghSYVVYGPLCNGATS 356
Cdd:cd12114 124 -APDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 357 VLfestpvyPNAGR-----YW-ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRV 430
Cdd:cd12114 196 VL-------PDEARrrdpaHWaELIERHGVTLWNSVPALLEMLLDVLEAAQALL--PSLRLVLLSGDWIPLDLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 431 VGDsrCTLVDTWWQTETGGICIA---PRPSEEGAEI-----LPGMAMRpffgivpvLMDEKGS-VVEGsnVSGALCISQA 501
Cdd:cd12114 267 APD--ARLISLGGATEASIWSIYhpiDEVPPDWRSIpygrpLANQRYR--------VLDPRGRdCPDW--VPGELWIGGR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 502 wpGMARTIYGDHQRFVDAYFKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 579
Cdd:cd12114 335 --GVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVV 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 580 IGYPHDikGEAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd12114 413 VVLGDP--GGKRLAAFVVPDNDGTPI-APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
114-581 |
9.85e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 118.66 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDepGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNQGLrggrvmeLKKiVDEAVKHCPTVQHVLVAhrtDNKVHMGDLD-IPLEQEMAK 272
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVL---DPRGLRDDPRlLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 273 EDPVCAPE-------SMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYV 345
Cdd:COG1022 164 GREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTLSFLPLAHVFERTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 VYGpLCNGATSVLFESTP------------VYPNAGRYWETV--------------------------ERLKINQFYGAP 387
Cdd:COG1022 243 YYA-LAAGATVAFAESPDtlaedlrevkptFMLAVPRVWEKVyagiqakaeeagglkrklfrwalavgRRYARARLAGKS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 388 TAVRLLLKY--GDAWVkkydRSSLR-TLG-------SVGEPINCEAWEWLHRV-VgdsrcTLVDTWWQTETGGICIAPRP 456
Cdd:COG1022 322 PSLLLRLKHalADKLV----FSKLReALGgrlrfavSGGAALGPELARFFRALgI-----PVLEGYGLTETSPVITVNRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 457 SeegaEILPGMAMRPFFGiVPVLMDEKGSV-VEGSNVsgalcisqawpgM----------ARTIYGDhqrfvdayfkayp 525
Cdd:COG1022 393 G----DNRIGTVGPPLPG-VEVKIAEDGEIlVRGPNV------------MkgyyknpeatAEAFDAD------------- 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMDDVINISGhrlGT----AEIEDAIADHPAVPESAVIG 581
Cdd:COG1022 443 GWLHTGDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
141-649 |
1.84e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 117.00 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnQ 220
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT--Q 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 221 GLRGGRVMELkkivdeavKHCPTVQHVLVAHRTDNKVHMGDLdipleqeMAKEDPVCAPESMGSEDVLFMLYTSGSTGMP 300
Cdd:PLN02246 130 SCYVDKLKGL--------AEDDGVTVVTIDDPPEGCLHFSEL-------TQADENELPEVEISPDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 301 KGIVhtqagyllyaaLTHK-LV-------------FDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL---FEstp 363
Cdd:PLN02246 195 KGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpkFE--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 364 vypnAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEawewLHRVVGDS--RCTLVDT 441
Cdd:PLN02246 261 ----IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKE----LEDAFRAKlpNAVLGQG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 442 WWQTETG---GICIAprpseegaeilpgMAMRPFfgivPVLMDEKGSVVE---------------GSNVSGALCI--SQA 501
Cdd:PLN02246 331 YGMTEAGpvlAMCLA-------------FAKEPF----PVKSGSCGTVVRnaelkivdpetgaslPRNQPGEICIrgPQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 502 WPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 574
Cdd:PLN02246 394 MKGylndpeaTANTIDKD-------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSI 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 575 PESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PLN02246 461 ADAAVVPMKDEVAGEVPVAFVV---RSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
137-650 |
2.96e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 116.40 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TFNQGLrggrvmELKKIVDEAVKHCPTVqhVLVAHRTDNKVHMGDLDIPLEQEMAkedPVCAPESMGSeDVLFMLYTSGS 296
Cdd:PRK06155 124 VEAALL------AALEAADPGDLPLPAV--WLLDAPASVSVPAGWSTAPLPPLDA---PAPAAAVQPG-DTAAILYTSGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 297 TGMPKGIVHTQAGYLLYAALTHKLVfDHRPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfesTPVYpNAGRYWETVE 376
Cdd:PRK06155 192 TGPSKGVCCPHAQFYWWGRNSAEDL-EIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVL---EPRF-SASGFWPAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 377 RLKINQFYGAPTAVRLLLKYGDawvKKYDR-SSLRTLGSVGEPINceawewLHRVVGDsRC--TLVDTWWQTETGGICIA 453
Cdd:PRK06155 266 RHGATVTYLLGAMVSILLSQPA---RESDRaHRVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 454 PRPSEEgaeilPGMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPG-MARTIYGDHQRFVDAYFKAYpgyYFTGD 532
Cdd:PRK06155 336 THGSQR-----PGSMGRLAPGFEARVVDEHDQELP-DGEPGELLLRADEPFaFATGYFGMPEKTVEAWRNLW---FHTGD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 533 GAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD-SAGDSDVVVQEL 611
Cdd:PRK06155 407 RVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgTALEPVALVRHC 486
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622839330 612 KSMvatkIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 650
Cdd:PRK06155 487 EPR----LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
117-648 |
5.15e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 115.49 E-value: 5.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 117 HVQKSPESVALIWErdEPGTEVriTYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFA 196
Cdd:PRK13390 6 HAQIAPDRPAVIVA--ETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 197 GFSAASLAGRINDAKCKVVITfNQGLRGgrvmelkkIVDEAVKHCPTvqHVLVAHRTDNkvhMGDLdiplEQEMAKEDPV 276
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVA-SAALDG--------LAAKVGADLPL--RLSFGGEIDG---FGSF----EAALAGAGPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 277 CAPESMGSedvlFMLYTSGSTGMPKGIVHTQAGYLLYAalthklvfdhrPGDifGCVADIGWITGHSyvvygplcngATS 356
Cdd:PRK13390 144 LTEQPCGA----VMLYSSGTTGFPKGIQPDLPGRDVDA-----------PGD--PIVAIARAFYDIS----------ESD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 357 VLFESTPVYPNAGRYW-----------------------ETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLG 413
Cdd:PRK13390 197 IYYSSAPIYHAAPLRWcsmvhalggtvvlakrfdaqatlGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 414 SVGEP----INCEAWEWLHRVVgdsrctlVDTWWQTETGGICIAPRPSEEGAeilPGMAMRPFFGIVPVLmDEKGSVVEG 489
Cdd:PRK13390 277 HAAAPcpvdVKHAMIDWLGPIV-------YEYYSSTEAHGMTFIDSPDWLAH---PGSVGRSVLGDLHIC-DDDGNELPA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 490 SNVSGALCISQAWPgmaRTIYGDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 569
Cdd:PRK13390 346 GRIGTVYFERDRLP---FRYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 570 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK13390 423 MHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-648 |
8.44e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 114.07 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 149 TCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF----AGFSAASLAGRINDAKCKVVITfnqglrg 224
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVLA------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 225 grVMELKKIVDEAVKHCPTVQHVLvahRTDNKVHMGDlDIPlEQEMAKEDPVCapesmgsedvlfMLYTSGSTGMPKGIV 304
Cdd:cd05922 76 --DAGAADRLRDALPASPDPGTVL---DADGIRAARA-SAP-AHEVSHEDLAL------------LLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 305 --HTQagyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfESTPVYPNAgrYWETVERLKINQ 382
Cdd:cd05922 137 lsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 383 FYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTE-TGGICIAPrPSEEGA 461
Cdd:cd05922 210 LAGVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEaTRRMTYLP-PERILE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 462 EilPGMAMRPFFGIVPVLMDEKGS----------VVEGSNVSGALCISQAWPGMARtiygdhqRFVDAYFkaypgyyfTG 531
Cdd:cd05922 284 K--PGSIGLAIPGGEFEILDDDGTptppgepgeiVHRGPNVMKGYWNDPPYRRKEG-------RGGGVLH--------TG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 532 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIKGEAAFAFIVVKDSAGDSDVVVqel 611
Cdd:cd05922 347 DLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLR--- 422
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622839330 612 ksMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05922 423 --SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
118-657 |
1.46e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.60 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK12316 4561 ARMTPDAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITFNQGLRGGRVmelkkivdeavkhcPTVQHVLVAHRTDNKVHMGDLDiPLEQEMAkedpvc 277
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRLPI--------------PDGLASLALDRDEDWEGFPAHD-PAVRLHP------ 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 apesmgsEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHK--LVFDHRPGDIFGCVADIGWITGHSYV-------VYG 348
Cdd:PRK12316 4694 -------DNLAYVIYTSGSTGRPKG-----------VAVSHGslVNHLHATGERYELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGAtSVLFESTPVYPNAGRYWETVE-RLKINQFygAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPIN----CEA 423
Cdd:PRK12316 4756 PLINGA-SVVIRDDSLWDPERLYAEIHEhRVTVLVF--PPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAqasyDLA 4829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 424 WE-----WLHRVVGDSRCTLVDTWWQTETGGICiaprpseeGAEILPgmAMRPFFGIVPVLMDEKGSV----VEGSNVSG 494
Cdd:PRK12316 4830 WRalkpvYLFNGYGPTETTVTVLLWKARDGDAC--------GAAYMP--IGTPLGNRSGYVLDGQLNPlpvgVAGELYLG 4899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 495 ALCISQAW---PGMARtiygdhQRFVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 570
Cdd:PRK12316 4900 GEGVARGYlerPALTA------ERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE 4973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 571 HPAVPESAVIGYPHDIkGEAAFAFIVVKDSA-GDSDVV----VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 645
Cdd:PRK12316 4974 HPAVREAVVIAQEGAV-GKQLVGYVVPQDPAlADADEAqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
570
....*....|..
gi 1622839330 646 LLRKIITSEAQE 657
Cdd:PRK12316 5053 ALPQPDASLLQQ 5064
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-657 |
2.44e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.03 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITfnqglrGGRVMElkkivdeavkHCPTVQHVLVAhrtdnkvhmgDLDIPLEQEMAKE 273
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT------QAHLLE----------QLPAPAGDTAL----------TLDRLDLNGYSEN 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPvcAPESMGsEDVLFMLYTSGSTGMPKGI--------VHTQAGYLLYAALTHKLVFDHRPGDIFGCVADigwitghsyv 345
Cdd:PRK12467 3229 NP--STRVMG-ENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSFDGAQER---------- 3295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 VYGPLCNGATSVLfestpvypNAGRYW---ETV-----ERLKINQFygAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGE 417
Cdd:PRK12467 3296 FLWTLICGGCLVV--------RDNDLWdpeELWqaihaHRISIACF--PPAYLQQFAEDAGG----ADCASLDIYVFGGE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 418 PINCEAWEWLHRVV---------GDSRCTLVDTWWQTETGGICIAP-----RP-SEEGAEILPGmAMRPffgiVPVlmde 482
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDAVCEAPyapigRPvAGRSIYVLDG-QLNP----VPV---- 3432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 483 kgsvvegsNVSGALCIsqAWPGMARtiyGDHQ-------RFVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK12467 3433 --------GVAGELYI--GGVGLAR---GYHQrpsltaeRFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKI 3499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 555 SGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRL 634
Cdd:PRK12467 3500 RGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAM 3575
|
570 580
....*....|....*....|...
gi 1622839330 635 PKTRSGKVMRRLLRKIITSEAQE 657
Cdd:PRK12467 3576 PLGPNGKVDRKALPDPDAKGSRE 3598
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
140-648 |
2.86e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 113.58 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 tfnqglrggrVME-LKKIVDEAVKHCPtVQHVLVAHrtdnkvhMGDL----------------------DIP----LEQE 269
Cdd:PRK07059 126 ----------VLEnFATTVQQVLAKTA-VKHVVVAS-------MGDLlgfkghivnfvvrrvkkmvpawSLPghvrFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 270 MAK-EDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYL---LYAALTHKLVFDHRPGD---IFGCVADIgwitgh 342
Cdd:PRK07059 188 LAEgARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPL------ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 343 sYVVYGPLCN-------GATSVLFestpvyPN----AGRYWEtVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR- 410
Cdd:PRK07059 262 -YHIFALTVCgllgmrtGGRNILI------PNprdiPGFIKE-LKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 411 TLG---SVGEPInceAWEWLHRvvgdSRCTLVDTWWQTETGGICIA--------------PRPSEEgaeilpgMAMRpff 473
Cdd:PRK07059 332 ANGggmAVQRPV---AERWLEM----TGCPITEGYGLSETSPVATCnpvdatefsgtiglPLPSTE-------VSIR--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 474 givpvlmDEKGSVVEGSNVsGALCIS--QAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQI 544
Cdd:PRK07059 395 -------DDDGNDLPLGEP-GEICIRgpQVMAGywnrpdeTAKVMTAD-------------GFFRTGDVGVMDERGYTKI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 545 TGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAV 624
Cdd:PRK07059 454 VDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA----LTEEDVKAFCKERLTNYKR 529
|
570 580
....*....|....*....|....
gi 1622839330 625 PDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK07059 530 PKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
117-648 |
4.12e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 112.67 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 117 HVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFA 196
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 197 GFSAASLAGRINDAKCKVVItfnqglrggrvmelkkiVDEAVKHCPTVQH---VLVAHRTDNKVHMGDLDIPleqemake 273
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETpkiVIDAAAQADSRRLAQGGLE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 dpvCAPESMGSEDVLF-MLYTSGSTGMPKGIVHTqagyllYAALTHKlVFDHrpgdifgcVADIGWITGHSYVVYGPLCN 352
Cdd:PRK06145 140 ---IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHS------YGNLHWK-SIDH--------VIALGLTASERLLVVGPLYH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 353 -GA-----TSVL-----------FESTPVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWvkKYDRSSLRTLGSV 415
Cdd:PRK06145 202 vGAfdlpgIAVLwvggtlrihreFDPEAVL-------AAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 416 GEPINCEAWEWLHRVVGDSRctLVDTWWQTETggiCIAPRPSEEGAEILP-GMAMRPFFGIVPVLMDEKGSVVEgSNVSG 494
Cdd:PRK06145 273 GEKTPESRIRDFTRVFTRAR--YIDAYGLTET---CSGDTLMEAGREIEKiGSTGRALAHVEIRIADGAGRWLP-PNMKG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 495 ALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 574
Cdd:PRK06145 347 EICMRG--PKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 575 PESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK06145 422 AEAAVIGVHDDRWGERITAVVVLNPGA---TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-657 |
5.43e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.05 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK12316 3064 EEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptVQHVLVAHRTDNKVHMGDldiPLEQEMAKED 274
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLS--------------------------QSHLRLPLAQGVQVLDLD---RGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 PvcaPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHRPGDIFGCVADIGWiTGHSYVVYGPLCNGA 354
Cdd:PRK12316 3189 P---AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 355 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEpinceAWEWLHRVVGDS 434
Cdd:PRK12316 3264 RVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA----HRCTSLKRIVCGGE-----ALPADLQQQVFA 3333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 435 RCTLVDTWWQTETGGICIAPRPSEEGAEILPgmAMRPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMARtiyGDHQ 514
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAVP--IGRPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR---GYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 515 R-------FVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyphDIK 587
Cdd:PRK12316 3406 RpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVD 3481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 588 GEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 657
Cdd:PRK12316 3482 GRQLVAYVVPEDEAGD---LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
114-656 |
5.93e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 112.39 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQksPESVALIW-ERdepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMP-VSPLAVAaMLACARIGAVh 191
Cdd:PRK10946 31 LTRHAA--SDAIAVICgER-------QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYIT-FFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 192 tVIFAGFSAASL-----AGRINDAkckVVItfnqGLRGGRVMELKKIVDEAVKHCPTVQHVLVAHRtdnkvhmgDLDIPL 266
Cdd:PRK10946 100 -PVNALFSHQRSelnayASQIEPA---LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLND--------DGEHSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 267 EQEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLlYAAlthklvfdHRPGDIFGCVADIGWI----TGH 342
Cdd:PRK10946 164 DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSV--------RRSVEICGFTPQTRYLcalpAAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 343 SYVVYGPlcnGATSVLFESTPVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLgSVG-- 416
Cdd:PRK10946 235 NYPMSSP---GALGVFLAGGTVVlapdPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL-QVGga 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 417 -----------EPINCEawewLHRVVGDSRcTLV------DTWWQT-ETGGiciapRPSEEGAEIlpgmamrpffGIVpv 478
Cdd:PRK10946 311 rlsetlarripAELGCQ----LQQVFGMAE-GLVnytrldDSDERIfTTQG-----RPMSPDDEV----------WVA-- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 479 lmDEKGS-VVEGSnvSGALcisqawpgMAR---TIYG-----DHQRFVdayFKAyPGYYFTGDGAHRTEGGYYQITGRMD 549
Cdd:PRK10946 369 --DADGNpLPQGE--VGRL--------MTRgpyTFRGyykspQHNASA---FDA-NGFYCSGDLVSIDPDGYITVVGREK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 550 DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagdsdvvvqELKSMVATK------IAKYA 623
Cdd:PRK10946 433 DQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE----------PLKAVQLRRflreqgIAEFK 502
|
570 580 590
....*....|....*....|....*....|...
gi 1622839330 624 VPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 656
Cdd:PRK10946 503 LPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-649 |
6.17e-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: 109.88 E-value: 6.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 284 SEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGAtSVLFESTP 363
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 364 VYPNAGRY---WETVERLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLV 439
Cdd:cd05944 79 GYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVELRARFEDATG---LPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 440 DTWWQTETggICIAPRPSEEGAEILPGMAMR-PFFGIVPVLMDEKGSVVE--GSNVSGALCIsqAWPGMAR-TIYGDHQR 515
Cdd:cd05944 151 EGYGLTEA--TCLVAVNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRdcAPDEVGEICV--AGPGVFGgYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 516 FVDAYfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 595
Cdd:cd05944 227 NAFVA----DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 596 VVKDSAgdsDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05944 303 QLKPGA---VVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
121-647 |
1.52e-25 |
|
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: 110.64 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 121 SPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 200
Cdd:cd17656 1 TPDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 201 ASLAGRINDAKCKVVITFNqglrggrvmelkkivdeavkHCPTVQhvlvahrTDNKVHMgDLDIPLEqemAKEDPVCAPE 280
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQR--------------------HLKSKL-------SFNKSTI-LLEDPSI---SQEDTSNIDY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 281 SMGSEDVLFMLYTSGSTGMPKGIV--HTQAGYLLyaalthKLVFDHRPGDIFGCVADIgwiTGHSYVV-----YGPLCNG 353
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL------HFEREKTNINFSDKVLQF---ATCSFDVcyqeiFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 AT------------SVLFE-------STPVYPNAgrYWETV--ERLKINQFygaPTAVRLLLKYGDAWVkkydrsslrtl 412
Cdd:cd17656 195 GTlyiireetkrdvEQLFDlvkrhniEVVFLPVA--FLKFIfsEREFINRF---PTCVKHIITAGEQLV----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 413 gsvgepINCEAWEWLHRvvgdSRCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAmRPFFGIVPVLMDEKGSVVEgSNV 492
Cdd:cd17656 259 ------ITNEFKEMLHE----HNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIG-KPISNTWIYILDQEQQLQP-QGI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 493 SGALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI 568
Cdd:cd17656 327 VGELYISGA--SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQL 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 569 ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17656 405 LNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
116-649 |
2.03e-25 |
|
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: 110.79 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVcRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 196 A---GFSAASLAGRINDAKCKVVITfNQGLRGGrvmelkkiVDEAVKHCPTVQHVLVAHrTDNKvhmgDLDIPleqemak 272
Cdd:cd05931 80 PptpGRHAERLAAILADAGPRVVLT-TAAALAA--------VRAFAASRPAAGTPRLLV-VDLL----PDTSA------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 273 eDPVCAPeSMGSEDVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFG----CVADIGWITGhsyvVYG 348
Cdd:cd05931 139 -ADWPPP-SPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCNGATSVLFEstpvyPNA-----GRYWETVERLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPINC 421
Cdd:cd05931 212 PLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 422 EAwewLHRVV-----------------GDSRCTL------------VDTWWQTETGGICIAPRPSEEGAEILPGMAmRPF 472
Cdd:cd05931 286 AT---LRRFAeafapfgfrpeafrpsyGLAEATLfvsggppgtgpvVLRVDRDALAGRAVAVAADDPAARELVSCG-RPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 473 FGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDhQRFVDAYFKAYP-----GYYFTGDGAHRTEGGYYqITGR 547
Cdd:cd05931 362 PDQEVRIVDPETGRELPDGEVGEIWVRG--PSVASGYWGR-PEATAETFGALAatdegGWLRTGDLGFLHDGELY-ITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 548 MDDVINISGHRLGTAEIEDAIAD-HPAVPESAVigyphdikgeAAFA---------FIVVKDSAGDSDVVVQELKSMVAT 617
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEaHPALRPGCV----------AAFSvpddgeerlVVVAEVERGADPADLAAIAAAIRA 507
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622839330 618 KIAK-YAV-PDEILVVKR--LPKTRSGKVMRRLLRK 649
Cdd:cd05931 508 AVAReHGVaPADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
178-648 |
2.23e-25 |
|
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: 110.16 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 178 VAAMLACA---RIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnqglrggrvmELKKIVDEAVKHCPTVQHVLVAhrTD 254
Cdd:cd05929 33 AAAAEGVWiadGVYIYLINSILTVFAAAAAWKCGACPAYKSSR-----------APRAEACAIIEIKAAALVCGLF--TG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 255 NKVHMGDLDIPLEQEMAKEDPVcAPESMGSEdvlfMLYTSGSTGMPKGIvhtqagyllyaalthKLVFDHRPGD---IFG 331
Cdd:cd05929 100 GGALDGLEDYEAAEGGSPETPI-EDEAAGWK----MLYSGGTTGRPKGI---------------KRGLPGGPPDndtLMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 332 CVADIGWITGHSYVVYGPL-------------CNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGD 398
Cdd:cd05929 160 AALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTLVLMEKF----DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 399 AWVKKYDRSSLRTLGSVGEPinCEAW---EWLHrvvgdsrctlvdtWW---------QTETGGICIAprpseEGAEIL-- 464
Cdd:cd05929 236 AVRNAYDLSSLKRVIHAAAP--CPPWvkeQWID-------------WGgpiiweyygGTEGQGLTII-----NGEEWLth 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 465 PGMAMRPFFGIVPVLmDEKGSVVEgsnvsgalcisqawPGMARTIYgdhqrFVDAYFKAYPGYYF-------------TG 531
Cdd:cd05929 296 PGSVGRAVLGKVHIL-DEDGNEVP--------------PGEIGEVY-----FANGPGFEYTNDPEktaaarneggwstLG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 532 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQEL 611
Cdd:cd05929 356 DVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEEL 435
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622839330 612 KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:cd05929 436 IAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
563-641 |
2.31e-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: 2.31e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 563 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 641
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
118-647 |
2.39e-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: 110.11 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:cd17655 7 AEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITfnqglrggrvmelkkivDEAVKHcptvqhvlvahrtdNKVHMGDLDIpLEQEMAKEDPV- 276
Cdd:cd17655 81 YPEERIQYILEDSGADILLT-----------------QSHLQP--------------PIAFIGLIDL-LDEDTIYHEESe 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 277 -CAPESmGSEDVLFMLYTSGSTGMPKGIVHTQAG-------------------YLLYAALThklvFDHRPGDIFGCVadi 336
Cdd:cd17655 129 nLEPVS-KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankviyqgehlrVALFASIS----FDASVTEIFASL--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 337 gwITGHSYVVYG--PLCNGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLlkygdAWVKKYDRSSLRTLGS 414
Cdd:cd17655 201 --LSGNTLYIVRkeTVLDGQALT---------------QYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 415 VGEPINCE-AWEWLHRVvgDSRCTLVDTWWQTETggiCIaprpseeGAEILPGMAMRPFFGIVPV----------LMDEK 483
Cdd:cd17655 259 GGEALSTElAKKIIELF--GTNPTITNAYGPTET---TV-------DASIYQYEPETDQQVSVPIgkplgntriyILDQY 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 484 GSVV-EGsnVSGALCISQAwpGMARTiYGDH-----QRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGH 557
Cdd:cd17655 327 GRPQpVG--VAGELYIGGE--GVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 558 RLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKT 637
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
570
....*....|
gi 1622839330 638 RSGKVMRRLL 647
Cdd:cd17655 477 PNGKVDRKAL 486
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
122-647 |
4.22e-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: 108.88 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:cd17652 1 PDAPAVVFG------DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITFnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapes 281
Cdd:cd17652 75 RIAYMLADARPALLLTT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 mgSEDVLFMLYTSGSTGMPKGIV--HTQAGYLLYAALTHklvFDHRPGDifgCVADIGWITGHSYV--VYGPLCNGATSV 357
Cdd:cd17652 92 --PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGS---RVLQFASPSFDASVweLLMALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 358 LFESTPVYPNAGrYWETVERLKINQFYGAPTAVrlllkygdAWVKKYDRSSLRTLGSVGEPINCE---AWEWLHRVV--- 431
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAAL--------AALPPDDLPDLRTLVVAGEACPAElvdRWAPGRRMInay 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 432 GDSRCTLVDTWwqtetggiciaprpseegAEILPGMAM----RPFFGI-VPVLMDEKGSVVEGsnVSGALCIsqAWPGMA 506
Cdd:cd17652 235 GPTETTVCATM------------------AGPLPGGGVppigRPVPGTrVYVLDARLRPVPPG--VPGELYI--AGAGLA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 507 RTiYGDH-----QRFVDAYFKAyPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 579
Cdd:cd17652 293 RG-YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVV 370
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 580 IGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17652 371 VVRDDRPGDKRLVAYVVPAPGAAPT---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
122-655 |
8.40e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 108.88 E-value: 8.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITFNqglrggrvmELKKIVDEAVKHCPtVQHVLVAHRTDNK----VHMGDLDipLEQEMAKEDPVC 277
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDT---------EFAEVAREALALLP-GPKPLVIDVDDPEypggRFIGALD--YEAFLASGDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 APESMGSE-DVLFMLYTSGSTGMPKGIV-HTQAGYLlyAALTHKLVFD--HRPG-----DIFGCVadiGWitGHSYVVyg 348
Cdd:PRK08162 174 AWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL--NALSNILAWGmpKHPVylwtlPMFHCN---GW--CFPWTV-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 pLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRS-SLRTLG-----SVGEPINCE 422
Cdd:PRK08162 245 -AARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPvHAMVAGaappaAVIAKMEEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 423 AWEWLHrVVGdsrctLVDTW-------WQTETGGICIAPR-----------PSEEGAEILPGMAMRPffgiVPVLMDEKG 484
Cdd:PRK08162 320 GFDLTH-VYG-----LTETYgpatvcaWQPEWDALPLDERaqlkarqgvryPLQEGVTVLDPDTMQP----VPADGETIG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 485 SVVegsnVSGALCISQawpgmartiYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVInISG-HRLGTAE 563
Cdd:PRK08162 390 EIM----FRGNIVMKG---------YLKNPKATEEAFAG--GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENISSIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 564 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVM 643
Cdd:PRK08162 454 VEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAS---ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQ 529
|
570
....*....|..
gi 1622839330 644 RRLLRKIITSEA 655
Cdd:PRK08162 530 KFVLREQAKSLK 541
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-661 |
1.00e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 108.74 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITFNqGLRGGRVME-LKKIVDEaVKHC----------PTVQHVLvahRTDNKVHMGDL 262
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVAmLYELAPE-LATCepgqlqsarlPELRRVI---FLGDEKHPGML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 263 DIPLEQEMAKEDPVCAPESMGSE----DVLFMLYTSGSTGMPKGivhtqagyllyAALTHK-------LVFDH---RPGD 328
Cdd:PRK08315 173 NFDELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKG-----------ATLTHRnilnngyFIGEAmklTEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 329 ----------IFGCVadIGwitghsyvVYGPLCNGATSVlfestpvYPNAG----RYWETVERLKINQFYGAPTAVRLLL 394
Cdd:PRK08315 242 rlcipvplyhCFGMV--LG--------NLACVTHGATMV-------YPGEGfdplATLAAVEEERCTALYGVPTMFIAEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 395 KYGDawVKKYDRSSLRT---LGSVGePInceawEWLHRVVGDSRCTLVdT--WWQTETG-GIC-------IAPRPSEEGa 461
Cdd:PRK08315 305 DHPD--FARFDLSSLRTgimAGSPC-PI-----EVMKRVIDKMHMSEV-TiaYGMTETSpVSTqtrtddpLEKRVTTVG- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 462 EILPGMAMR---PFFG-IVPVlmdekgsvvegsNVSGALC-----ISQAWPGM----ARTIYGDhqrfvdayfkaypGYY 528
Cdd:PRK08315 375 RALPHLEVKivdPETGeTVPR------------GEQGELCtrgysVMKGYWNDpektAEAIDAD-------------GWM 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 529 FTGDGAHRTEGGYYQITGRMDDVI-----NISGhRlgtaEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagD 603
Cdd:PRK08315 430 HTGDLAVMDEEGYVNIVGRIKDMIirggeNIYP-R----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP---G 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 604 SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQELGDT 661
Cdd:PRK08315 502 ATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM---IEELGLQ 556
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
114-649 |
1.75e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 108.42 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITfnqglrGGrvmELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDipLEQeMAKE 273
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIV------GE---ELVEAFEEARADLARPPRLWVAGGDTLDDPEGYED--LAA-AAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPESMGS---EDVLFMLYTSGSTGMPKGIVHTQAGYLLY----AALThklvfDHRPGDIFGCVADIGWITGHSYVV 346
Cdd:PRK08279 185 APTTNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAmggfGGLL-----RLTPDDVLYCCLPLYHNTGGTVAW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 YGPLCNGATSVLFESTpvypNAGRYWETVERlkinqfYGApTAV-------RLLLkygDAWVKKYDRS-SLRTLgsVGEP 418
Cdd:PRK08279 260 SSVLAAGATLALRRKF----SASRFWDDVRR------YRA-TAFqyigelcRYLL---NQPPKPTDRDhRLRLM--IGNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 419 INCEAW-EWLHRVvgdsrctlvdtwwqtetgGIciaPRPSE-----EG------AEILPGMAmrpffGIVPVLMDEKGSV 486
Cdd:PRK08279 324 LRPDIWdEFQQRF------------------GI---PRILEfyaasEGnvgfinVFNFDGTV-----GRVPLWLAHPYAI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 487 VE-----GSNVSGA--LCI--SQAWPGMARTIYGDHQRFvDAY--------------FKayPG--YYFTGDGAHRTEGGY 541
Cdd:PRK08279 378 VKydvdtGEPVRDAdgRCIkvKPGEVGLLIGRITDRGPF-DGYtdpeasekkilrdvFK--KGdaWFNTGDLMRDDGFGH 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 542 YQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAgdsDVVVQELKSMVATK 618
Cdd:PRK08279 455 AQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgTD--GRAGMAAIVLADGA---EFDLAALAAHLYER 529
|
570 580 590
....*....|....*....|....*....|.
gi 1622839330 619 IAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PRK08279 530 LPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
118-656 |
2.03e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.87 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK12467 522 ARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITFNQGLRGGRVmelkkivdeavkhCPTVQHVLVahrtdnkvhmgDLDIPLEQEMAKEDPvc 277
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------------PAGLRSLCL-----------DEPADLLCGYSGHNP-- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 aPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvfdhrpgdiFGCVADIGWITGHSY-------VVYGPL 350
Cdd:PRK12467 650 -EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGAL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 351 CNGATSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLHRV 430
Cdd:PRK12467 720 ASGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEAL---QVDLLARV 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 431 VGDS-RCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARti 509
Cdd:PRK12467 792 RALGpGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGA--GLAR-- 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 510 yGDHQR-------FVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 581
Cdd:PRK12467 867 -GYHRRpaltaerFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA 945
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 582 YPHDiKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 656
Cdd:PRK12467 946 QPGD-AGLQLVAYLVPAAVADGAEhqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQ 1021
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
139-648 |
3.73e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 106.71 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITF 218
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 NQGLRGgrvmeLKKIVDEAVK--HCPTVQHVLVAHRTDN---KVHMGDLDipLEQEMAKEDPVCAPESMGSEDvlfMLYT 293
Cdd:PRK12406 91 ADLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISPallTPPAGAID--WEGWLAQQEPYDGPPVPQPQS---MIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 294 SGSTGMPKGIVHtqagyllyAALT--HKLVFDHRPGDIFGcvadigWITGHSYVVYGPLcngatsvlFESTP-VYP-NAG 369
Cdd:PRK12406 161 SGTTGHPKGVRR--------AAPTpeQAAAAEQMRALIYG------LKPGIRALLTGPL--------YHSAPnAYGlRAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 370 RYWET---------------VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAwewlhrvvgDS 434
Cdd:PRK12406 219 RLGGVlvlqprfdpeellqlIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAP--CPA---------DV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 435 RCTLVDtWW---------QTETGGICIAprpSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISqawPGM 505
Cdd:PRK12406 288 KRAMIE-WWgpviyeyygSTESGAVTFA---TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI---AGN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 ARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIG 581
Cdd:PRK12406 361 PDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMV-ISG---GVniypAEIEAVLHAVPGVHDCAVFG 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 582 YPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSMVAtkiaKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK12406 435 IPDAEFGEALMAVVEPQPGATlDEADIRAQLKARLA----GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
140-649 |
4.00e-24 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 105.51 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVvitfn 219
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05912 77 -----------------------------------------------------------------DDIATIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKGIVHTqAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGpLCNGATSVLFESTpvypNAGRYWETVERLK 379
Cdd:cd05912 92 PKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLINSGK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 380 INQFYGAPTAV-RLLLKYGDAWvkkydRSSLRT--LGsvGEPINCEAWEwlhrvvgdsRCT-----LVDTWWQTETGGIC 451
Cdd:cd05912 166 VTIISVVPTMLqRLLEILGEGY-----PNNLRCilLG--GGPAPKPLLE---------QCKekgipVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 452 IAPRPseEGAEILPGMAMRPFFG----IVPVLMDEKGS---VVEGSNVSGALcisqawpgMARTIYGDhQRFVDAYFKay 524
Cdd:cd05912 230 VTLSP--EDALNKIGSAGKPLFPvelkIEDDGQPPYEVgeiLLKGPNVTKGY--------LNRPDATE-ESFENGWFK-- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 525 pgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 604
Cdd:cd05912 297 -----TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-----SER 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622839330 605 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05912 367 PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
139-648 |
8.84e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 105.94 E-value: 8.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIympvspLA------VAAMLACARIGAV-HTV---IFAgfsaASLAGRIN 208
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTInprLFP----EQIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 209 DAKCKVV---ITFnqglrggrvmelKKIVDEAVKHCPTVQHVLVAhrTDnKVHMGDLDIPL---EQEMAKEDPVCAPESM 282
Cdd:PRK07008 109 HAEDRYVlfdLTF------------LPLVDALAPQCPNVKGWVAM--TD-AAHLPAGSTPLlcyETLVGAQDGDYDWPRF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 283 GSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYA---ALThklvfdhrpgDIFGCVA-DI-----------GW-------IT 340
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHRSTVLHAygaALP----------DAMGLSArDAvlpvvpmfhvnAWglpysapLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 341 GHSYVVYGPLCNGATsvlfestpVYpnagrywETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSL-RTL--GSVGE 417
Cdd:PRK07008 244 GAKLVLPGPDLDGKS--------LY-------ELIEAERVTFSAGVPTVWLGLLNHMREAGLRF--STLrRTVigGSACP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 418 PINCEAWEwlhrvvGDSRCTLVDTWWQTET---GGICI-----APRPSEEGAEILPGMAmRPFFGIVPVLMDEKGSvveg 489
Cdd:PRK07008 307 PAMIRTFE------DEYGVEVIHAWGMTEMsplGTLCKlkwkhSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGR---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 490 snvsgalciSQAWPGMArtiYGD-HQR---FVDAYFK--AYP---GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLG 560
Cdd:PRK07008 376 ---------ELPWDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWIS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 561 TAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSG 640
Cdd:PRK07008 444 SIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATG 520
|
....*...
gi 1622839330 641 KVMRRLLR 648
Cdd:PRK07008 521 KLQKLKLR 528
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
140-645 |
3.02e-23 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 103.44 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakEDPvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05907 84 -----------------------------------------------------EDP---------DDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnagrywETVERLK 379
Cdd:cd05907 102 PKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL------DDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 380 INQFYGAPtavRLLLK-YGDAWVKK--------YDR---SSLRTLGSVGEPINCEAWEWLHRvVGdsrCTLVDTWWQTET 447
Cdd:cd05907 175 PTVFLAVP---RVWEKvYAAIKVKAvpglkrklFDLavgGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 448 GGICIAPRPsEEGAEILPGMAMRPffgiVPVLMDEKGSVVegsnVSGalcisqawPGMARTIYGDHQRFVDAYFKayPGY 527
Cdd:cd05907 248 SAVVTLNPP-GDNRIGTVGKPLPG----VEVRIADDGEIL----VRG--------PNVMLGYYKNPEATAEALDA--DGW 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 528 YFTGDGAHRTEGGYYQITGRMDDVI-NISGHRLGTAEIEDAIADHPAVPESAVIG--YPH-----DIKGEAAFAFIVVKD 599
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgRPFlvaliVPDPEALEAWAEEHG 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 600 SAGDSDV-------VVQELKSMV---------ATKIAKYAVPDEILVVKRLPKTRSGKVMRR 645
Cdd:cd05907 389 IAYTDVAelaanpaVRAEIEAAVeaanarlsrYEQIKKFLLLPEPFTIENGELTPTLKLKRP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-656 |
4.21e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.63 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK12467 1580 IEDQAAATPEAVALVF------GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDipLEQEMAKE 273
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT--------------------------QSHLQARLPLPDGLRSLVLD--QEDDWLEG 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPES-MGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH--RPGDIFGCVADIGWITGHSYV----- 345
Cdd:PRK12467 1706 YSDSNPAVnLAPQNLAYVIYTSGSTGRPKG-----------AGNRHGALVNRlcATQEAYQLSAADVVLQFTSFAfdvsv 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 --VYGPLCNGAtSVLFESTPVYPNAGRYWETVERLKI----------NQF------YGAPTAVRLLLKYGDAWVKKYDRS 407
Cdd:PRK12467 1775 weLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRP 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 408 SLRTLGSVGepinceawewLHRVVGDSRCTLVDTWWQtetggiciAPRPSEEGAEILPgmamrpffgIVPVLMDEKGSVV 487
Cdd:PRK12467 1854 WLERLPDTG----------LFNLYGPTETAVDVTHWT--------CRRKDLEGRDSVP---------IGQPIANLSTYIL 1906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 488 EGS------NVSGALCISQAwpGMARtiyGDH-------QRFVDAYFkAYPG--YYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK12467 1907 DASlnpvpiGVAGELYLGGV--GLAR---GYLnrpaltaERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQV 1980
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 553 NISGHRLGTAEIEDAIADHPAVPESAVIgyPHD-IKGEAAFAFIVVKDSAGDSDVVVQ-----ELKSMVATKIAKYAVPD 626
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVI--AQDgANGKQLVAYVVPTDPGLVDDDEAQvalraILKNHLKASLPEYMVPA 2058
|
570 580 590
....*....|....*....|....*....|
gi 1622839330 627 EILVVKRLPKTRSGKVMRRLLRKIITSEAQ 656
Cdd:PRK12467 2059 HLVFLARMPLTPNGKLDRKALPAPDASELQ 2088
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
141-644 |
4.55e-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: 102.53 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfnq 220
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 221 glrgGRVMELKKIVdeavkhcptvqhVLVAHRTdnkvhmgdldipleqEMAKEDPVCAPESMGSEDVLFMLYTSGSTGMP 300
Cdd:TIGR01923 78 ----DSLLEEKDFQ------------ADSLDRI---------------EAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 301 KGIVHTQAGYLLYA-ALTHKLVFDhrPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfestpVYPNAgRYWETVERLK 379
Cdd:TIGR01923 127 KAVPHTFRNHYASAvGSKENLGFT--EDDNWLLSLPLYHISGLS-ILFRWLIEGATLRI-----VDKFN-QLLEMIANER 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 380 INQFYGAPTAVRLLLKygdawvKKYDRSSLRTLGSVGEPINCEawewLHRVVGDSRCTLVDTWWQTETGGICIAPRPsee 459
Cdd:TIGR01923 198 VTHISLVPTQLNRLLD------EGGHNENLRKILLGGSAIPAP----LIEEAQQYGLPIYLSYGMTETCSQVTTATP--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 460 gaEILPGM--AMRPFFGI-VPVLMDEKGSVVEgsnvsgalcISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTGDGAHR 536
Cdd:TIGR01923 265 --EMLHARpdVGRPLAGReIKIKVDNKEGHGE---------IMVKGANLMKG-YLYQGELTPAFEQQ--GWFNTGDIGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 537 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVA 616
Cdd:TIGR01923 331 DGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-----SESDISQAKLIAYLT 405
|
490 500
....*....|....*....|....*...
gi 1622839330 617 TKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:TIGR01923 406 EKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
140-648 |
4.84e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 104.34 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfN 219
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 QGLR----GGRVMELKKIVDEAVKHCPTvqhvlvahrtdnkvhmgDLDIpleqemakedpvcapesMGSEDVLFMLYTSG 295
Cdd:PRK06060 110 DALRdrfqPSRVAEAAELMSEAARVAPG-----------------GYEP-----------------MGGDALAYATYTSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfESTPVYPNAGRYWETv 375
Cdd:PRK06060 156 TTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 376 eRLKINQFYGAPTavrLLLKYGDAWVKKYDRSsLRTLGSVGEPINCEAWEWLHRVVGDsrCTLVDTWWQTETGGICIAP- 454
Cdd:PRK06060 234 -RFGPSVLYGVPN---FFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSNr 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 455 ----RPSEEGaEILPGMAMRPffgIVPvlmdekGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAyfkayPGYYFT 530
Cdd:PRK06060 307 vdewRLGTLG-RVLPPYEIRV---VAP------DGTTAGPGVEGDLWVRG--PAIAKGYWNRPDSPVAN-----EGWLDT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 531 GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQE 610
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 1622839330 611 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK06060 450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
286-644 |
5.58e-23 |
|
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: 100.65 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHklVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATsvlfestp 363
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMcaHRQT-LRAAAAWAD--CADLTEDDRYLIINPFFHTFGYKAGIVACLLTGAT-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 364 VYPNA----GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrcTLV 439
Cdd:cd17638 70 VVPVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE--TVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 440 DTWWQTETGGICIApRPSEEgAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNV-SGALCISQAwpgMARTIYGDhqrfvd 518
Cdd:cd17638 146 TAYGLTEAGVATMC-RPGDD-AETVATTCGRACPGFEVRIADDGEVLVRGYNVmQGYLDDPEA---TAEAIDAD------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 519 ayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVK 598
Cdd:cd17638 215 -------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622839330 599 DSAG-DSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:cd17638 288 PGVTlTEEDVIAWCRE----RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
132-642 |
1.11e-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: 102.02 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 132 DEPGTEVriTYRELLETTCRLANTLKRhGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIfaGFSAASLAGR--IND 209
Cdd:cd05909 2 DTLGTSL--TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVML--NYTAGLRELRacIKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 210 AKCKVVITFNQGLRGGRVMELKKIVDEAvkhcptvqHVLVAHRTDNKVHMGD-------LDIPLEQEMAKEDPVCAPesm 282
Cdd:cd05909 77 AGIKTVLTSKQFIEKLKLHHLFDVEYDA--------RIVYLEDLRAKISKADkckaflaGKFPPKWLLRIFGVAPVQ--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 283 gSEDVLFMLYTSGSTGMPKGIVHTQAGYL--LYAALTHklvFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfe 360
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 361 stpvYPNAGRYW---ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVGEPINC---EAWEWLHRVVgds 434
Cdd:cd05909 220 ----HPNPLDYKkipELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGIR--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 435 rctLVDTWWQTETG---GICIAPRPSEEGA--EILPGMAMR--PFFGIVPVLMDEKGSV-VEGSNV-SGALcisqAWPGM 505
Cdd:cd05909 289 ---ILEGYGTTECSpviSVNTPQSPNKEGTvgRPLPGMEVKivSVETHEEVPIGEGGLLlVRGPNVmLGYL----NEPEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 ARTIYGDhqrfvdayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH-PAVPESAVIGYPH 584
Cdd:cd05909 362 TSFAFGD-------------GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPD 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 585 DIKGEAAFAFIVvkDSAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKV 642
Cdd:cd05909 429 GRKGEKIVLLTT--TTDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
118-659 |
1.71e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 118 VQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 197
Cdd:PRK12316 2013 AARAPEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 198 FSAASLAGRINDAKCKVVITfnqglrggrvmelKKIVDEAVKhCPTVQHVLvahrtdnkvhmgDLDIPLEQEmakEDPVC 277
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT-------------QRHLLERLP-LPAGVARL------------PLDRDAEWA---DYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 APE-SMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDifgCVADIGWIT--GHSYVVYGPLCNGA 354
Cdd:PRK12316 2138 APAvQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 355 tSVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDS 434
Cdd:PRK12316 2214 -RVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 435 RctLVDTWWQTETggiCIAPRPSEEGAEILPGMAMRPffgIVPVLMDEKGSVVEGS------NVSGALCISQAwpGMART 508
Cdd:PRK12316 2289 Y--LFNGYGPTEA---VVTPLLWKCRPQDPCGAAYVP---IGRALGNRRAYILDADlnllapGMAGELYLGGE--GLARG 2358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 509 IYG----DHQRFVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGyp 583
Cdd:PRK12316 2359 YLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-- 2436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839330 584 HDIKGEAAFAFIVVKDSAGDSDvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG 659
Cdd:PRK12316 2437 QDGASGKQLVAYVVPDDAAEDL--LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAY 2510
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
286-644 |
3.01e-22 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 98.25 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFgcvadigwitghsyvVYGPLC-----NGATSVLFE 360
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAIL---------------APGPLShslflYGAISALYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 361 STPVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINCEAWEWLHRVVGDSRc 436
Cdd:cd17633 66 GGTFIgqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKNIFPKAN- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 437 tLVDTWWQTETGgiCIAPRPSEEGAEilPGMAMRPFFGIVPVLMDEKGSVVegsnvsGALCISQAwpgMARTIYgdhqrf 516
Cdd:cd17633 139 -LIEFYGTSELS--FITYNFNQESRP--PNSVGRPFPNVEIEIRNADGGEI------GKIFVKSE---MVFSGY------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 517 VDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 596
Cdd:cd17633 199 VRGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622839330 597 vkdsaGDSdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:cd17633 279 -----GDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
139-649 |
3.90e-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: 100.19 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITf 218
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 nqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgDLDIPLEQEMAKEDPVCAPesMGSEDVLFMLYTSGSTG 298
Cdd:cd05939 82 ------------------------------------------NLLDPLLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHTQAGYLLYAALTHKlVFDHRPGDIFgcvadigWITGHSYVVYGPLCNGATSVLFESTPVYP---NAGRYWETV 375
Cdd:cd05939 118 LPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVV-------YDCLPLYHSAGGIMGVGQALLHGSTVVIRkkfSASNFWDDC 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 376 ERLK--INQFYG--------APTA-------VRLLLKYG---DAWVKKYDRSSLRTLGSV--GEPINCEAWEWLHRV--- 430
Cdd:cd05939 190 VKYNctIVQYIGeicryllaQPPSeeeqkhnVRLAVGNGlrpQIWEQFVRRFGIPQIGEFygATEGNSSLVNIDNHVgac 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 431 ---------VGDSRCTLVDtwwqTETG-------GICIAPRPSEEGA---EILPGMAMRPFFGIVpvlmDEKGSvvegsn 491
Cdd:cd05939 270 gfnsrilpsVYPIRLIKVD----EDTGelirdsdGLCIPCQPGEPGLlvgKIIQNDPLRRFDGYV----NEGAT------ 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 492 vsgalcisqawpgmartiygdHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 571
Cdd:cd05939 336 ---------------------NKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNV 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 572 PAVPESAVIGY--PHdIKGEAAFAFIVVKDSAGDSDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05939 395 LGLEDVVVYGVevPG-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
123-650 |
1.53e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 99.13 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 123 ESVALIWER------DEPGTE---VRITYRELLETTCRLANTLKRH-GVCRGDCVAIYMP---VSPLAVAAMLacaRIGA 189
Cdd:PRK12492 24 KSVVEVFERsckkfaDRPAFSnlgVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPnvlQYPIAVFGAL---RAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 190 VHTVIFAGFSAASLAGRINDAKCKVVITFNqgLRGGRVMELkkIVDEAVKHC---------PTVQHVLVAHRTDnKVHMG 260
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYLN--MFGKLVQEV--LPDTGIEYLieakmgdllPAAKGWLVNTVVD-KVKKM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 261 DLDIPLEQEMA-------KEDPVCAPESMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTH-KLVFDHRpgDIFGC 332
Cdd:PRK12492 176 VPAYHLPQAVPfkqalrqGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKG-----------AMLTHgNLVANML--QVRAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 333 VADIGwITGHsyvvygPLCNGATSVLFESTPVY------------------------P-NAGRYWETVERLKINQFYGAP 387
Cdd:PRK12492 243 LSQLG-PDGQ------PLMKEGQEVMIAPLPLYhiyaftancmcmmvsgnhnvlitnPrDIPGFIKELGKWRFSALLGLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 388 TAVRLLLKYGDawVKKYDRSSLRTLGSVGEPI---NCEAWEWLhrvvgdSRCTLVDTWWQTETGGICIApRPSEEGAEI- 463
Cdd:PRK12492 316 TLFVALMDHPG--FKDLDFSALKLTNSGGTALvkaTAERWEQL------TGCTIVEGYGLTETSPVAST-NPYGELARLg 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 464 -----LPGMAMRpffgivpVLMDEKGSVVEGSNvsGALCIS--QAWPGMARTIYGDHQrFVDAyfkayPGYYFTGDGAHR 536
Cdd:PRK12492 387 tvgipVPGTALK-------VIDDDGNELPLGER--GELCIKgpQVMKGYWQQPEATAE-ALDA-----EGWFKTGDIAVI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 537 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVA 616
Cdd:PRK12492 452 DPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG----LSVEELKAYCK 527
|
570 580 590
....*....|....*....|....*....|....
gi 1622839330 617 TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 650
Cdd:PRK12492 528 ENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
111-657 |
1.97e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 98.92 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 111 VNCLDQHVQKSPESVALiwerDEPGTEvrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAV 190
Cdd:PRK05605 35 VDLYDNAVARFGDRPAL----DFFGAT--TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 191 ---HTVIFagfSAASLAGRINDAKCKVVITFN------QGLRGGrvMELKKIVD-EAVKHCPTVQHVLV------AHRTD 254
Cdd:PRK05605 109 vveHNPLY---TAHELEHPFEDHGARVAIVWDkvaptvERLRRT--TPLETIVSvNMIAAMPLLQRLALrlpipaLRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 255 NKVHMGDLD-IPLEQ----EMAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHklvfdhrpGDI 329
Cdd:PRK05605 184 AALTGPAPGtVPWETlvdaAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKG-----------AQLTH--------RNL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 330 FGCVAD-IGWITG---------------HSY-----VVYGPLCnGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPT 388
Cdd:PRK05605 245 FANAAQgKAWVPGlgdgpervlaalpmfHAYgltlcLTLAVSI-GGELVLLPA----PDIDLILDAMKKHPPTWLPGVPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 389 AVRLLLKygDAWVKKYDRSSLRTL--GSVGEPIN-CEAWEwlhRVVGDSrctLVDTWWQTETGGIcIAPRPSEEGAEilP 465
Cdd:PRK05605 320 LYEKIAE--AAEERGVDLSGVRNAfsGAMALPVStVELWE---KLTGGL---LVEGYGLTETSPI-IVGNPMSDDRR--P 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 466 GMAMRPFfgivPvlmDEKGSVVEGSNVSGALCISQAWPGMARtiygDHQRFvDAYFKA--------YPGYYFTGDGAHRT 537
Cdd:PRK05605 389 GYVGVPF----P---DTEVRIVDPEDPDETMPDGEEGELLVR----GPQVF-KGYWNRpeetaksfLDGWFRTGDVVVME 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 538 EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVAT 617
Cdd:PRK05605 457 EDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGA---ALDPEGLRAYCRE 533
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622839330 618 KIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 657
Cdd:PRK05605 534 HLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
115-647 |
4.13e-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: 97.12 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITfnQGlrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemaked 274
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT--QP----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 pvcapesmgsEDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPgDIFGCVADIGWITGhSYVVYGPLCNGA 354
Cdd:cd17644 106 ----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 355 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINCEAWEWLHRVVGDs 434
Cdd:cd17644 174 TLVL-RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 435 RCTLVDTWWQTE---TGGICIAPRPSEEGA-EILPGmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIY 510
Cdd:cd17644 251 FIQLINVYGPTEatiAATVCRLTQLTERNItSVPIG---RPIANTQVYILDENLQPVP-VGVPGELHIGGV--GLARGYL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 511 G----DHQRFVDAYFKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPH 584
Cdd:cd17644 325 NrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRED 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839330 585 DIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17644 405 QPGNKRLVAYIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
114-647 |
6.63e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 98.70 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDakCKVVITFNQGLRGGRVmelkkivdeavkhcPTVQHVLVahrtdnkvhmgdldIPLEQEMAKE 273
Cdd:PRK05691 1211 LDPDYPAERLAYMLAD--SGVELLLTQSHLLERL--------------PQAEGVSA--------------IALDSLHLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPE-SMGSEDVLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVFDHRP-----GDIFGCVADIGWITGhSYVVY 347
Cdd:PRK05691 1261 WPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNT------HAALAERLQWMQATyalddSDVLMQKAPISFDVS-VWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 348 GPLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE-- 425
Cdd:PRK05691 1334 WPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA----AACTSLRRLFSGGEALPAELRNrv 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 426 -------WLHRVVGDSRCTLVDTWWQtetggiCIAprpsEEGAEILPGmamRPFFGIVPVLMDEKGSVVEGSnVSGALCI 498
Cdd:PRK05691 1409 lqrlpqvQLHNRYGPTETAINVTHWQ------CQA----EDGERSPIG---RPLGNVLCRVLDAELNLLPPG-VAGELCI 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 499 SQAwpGMARTIYG----DHQRFV-DAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPA 573
Cdd:PRK05691 1475 GGA--GLARGYLGrpalTAERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 574 VPESAVIgyphdIKGEAAFAFIVVKDSAGDS-DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK05691 1553 VAQAAVL-----VREGAAGAQLVGYYTGEAGqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-641 |
7.33e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 94.76 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 284 SEDVLFMLYTSGSTGMPKGIVHTQA---GYLLYAALTHKLVFDhrPGDIFGCVADIGwiTGHSYVVYGPLCNGA------ 354
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFT--PSEDAHKAAAAA--AGTVMFPAPPLMHGTgswtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 355 TSVLFESTPVYP----NAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPIN 420
Cdd:cd05924 78 GGLLGGQTVVLPddrfDPEEVWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 421 CEAWEWLHRVVGDSrcTLVDTWWQTETGGICIApRPSEEGAEilpgmaMRPFFGIVP--VLMDEKGSVVE-GSNVSGALc 497
Cdd:cd05924 148 PEVKQGLLELVPNI--TLVDAFGSSETGFTGSG-HSAGSGPE------TGPFTRANPdtVVLDDDGRVVPpGSGGVGWI- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 498 isqAWPG-MARTIYGDHQRfVDAYFKAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 574
Cdd:cd05924 218 ---ARRGhIPLGYYGDEAK-TAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 575 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 641
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
117-656 |
4.90e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 93.69 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 117 HVQKSPESVALIwERDEpgtevRITYRELLETTCRLANTLkRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFA 196
Cdd:PRK07638 10 HASLQPNKIAIK-ENDR-----VLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 197 GFSAASLAGRINDAKCKVVIT---FNQGLRG--GRVMELKKIvdeavkhcptvqhvlvahrtdnkvhMGDLDIPLEQEMA 271
Cdd:PRK07638 83 KWKQDELKERLAISNADMIVTeryKLNDLPDeeGRVIEIDEW-------------------------KRMIEKYLPTYAP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 272 KEDPVCAPESMGsedvlfmlYTSGSTGMPKGIVHTQAGYLLY---AALTHKLVFDHR---PGDIFgcvadigwitgHSYV 345
Cdd:PRK07638 138 IENVQNAPFYMG--------FTSGSTGKPKAFLRAQQSWLHSfdcNVHDFHMKREDSvliAGTLV-----------HSLF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 346 VYGplcngATSVLFESTPVY------PNAGRywETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSvGEPI 419
Cdd:PRK07638 199 LYG-----AISTLYVGQTVHlmrkfiPNQVL--DKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISS-GAKW 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 420 NCEAWE-----WLHrvvgdsrCTLVDTWWQTETGGICIAprpSEEGAEILPGMAMRPFFGIVPVLMDEKGSVVEgsnvsg 494
Cdd:PRK07638 266 EAEAKEkikniFPY-------AKLYEFYGASELSFVTAL---VDEESERRPNSVGRPFHNVQVRICNEAGEEVQ------ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 495 alcisqawPGMARTIY-GDHQRFV----DAYFKAYP---GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIED 566
Cdd:PRK07638 330 --------KGEIGTVYvKSPQFFMgyiiGGVLARELnadGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIES 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 567 AIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSAGdsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 646
Cdd:PRK07638 402 VLHEHPAVDEIVVIGVPDSYWGEKPVA--IIKGSAT-----KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARME 474
|
570
....*....|
gi 1622839330 647 LRKIITSEAQ 656
Cdd:PRK07638 475 AKSWIENQEK 484
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
526-648 |
7.28e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 93.13 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMD-DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 604
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-----GAD 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622839330 605 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
116-647 |
1.39e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 92.76 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIF 195
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 196 AGFSAASLAgRINDAKCKVVITFNqglRGGRVmelkkivdeAVKHCPTVQHVLVAHRTDNKVHMGDLDIPLEQEMAKEDP 275
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPAAALVA---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 276 vcapeSMGSEDVLFMLYTSGSTGMPKGIvhtqagyLLyaalthklvfdhrPGDIFGCVADI---------GWITGHSyvV 346
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAV-------LL-------------ANRTFFAVPDIlqkeglnwvTWVVGET--T 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 YGPLcnGATSVlfestpvypnAGRYW----------------------ETVERLKINQFYGAPTAVRLL---LKYGDAwv 401
Cdd:PRK05857 218 YSPL--PATHI----------GGLWWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLvseLKSANA-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 402 kkyDRSSLRTLGSVGEPInceawewlhrVVGDSR---CTLVDT---WWQTETG--GICIaPRPSEEGAEILPGMAMRPFF 473
Cdd:PRK05857 284 ---TVPSLRLVGYGGSRA----------IAADVRfieATGVRTaqvYGLSETGctALCL-PTDDGSIVKIEAGAVGRPYP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 474 GIVPVLMDEKGSVVEGSNVSGALCISQAW---PGMARTIYGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDD 550
Cdd:PRK05857 350 GVDVYLAATDGIGPTAPGAGPSASFGTLWiksPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 551 VINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGeaAFAFIVVKDSAGDSDVVVQELKSMVATKIAK----YAVPD 626
Cdd:PRK05857 427 MIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG--ALVGLAVVASAELDESAARALKHTIAARFRResepMARPS 504
|
570 580
....*....|....*....|.
gi 1622839330 627 EILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK05857 505 TIVIVTDIPRTQSGKVMRASL 525
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
137-649 |
2.95e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 91.72 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TFNqglrggrvmELKKIVDEAVKhcptvqhvLVAHRTDNKVHMGDLDiPLEQEMAKEDPVCAPESMGSE-DVLFMLYTSG 295
Cdd:cd05915 102 FDP---------NLLPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 296 STGMPKGIVHTQAG-YLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEstpvYPNAGRYWET 374
Cdd:cd05915 164 TTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 375 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinceawEWLHRVVGDSRCTLVDTWWQTETGGICIA- 453
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAP------RSLIARFERMGVEVRQGYGLTETSPVVVQn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 454 ---PR----PSEEGAEILPGMAMRPFFGIVPVLMDEKGSVV-EGSNVSgalCISQAWPGMARTIYGDHQRFVDAYFKAyp 525
Cdd:cd05915 314 fvkSHleslSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPkDGKALG---EVQLKGPWITGGYYGNEEATRSALTPD-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 605
Cdd:cd05915 389 GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1622839330 606 VVVQELKSMVATkiaKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05915 469 ELNEHLLKAGFA---KWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
129-649 |
3.50e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.77 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 129 WERDEPGTevrITYRELLETTCRLANTLKRH-GVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRI 207
Cdd:PRK05620 31 WGGAEQEQ---TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 208 NDAKCKVVITFNQglrggrvmeLKKIVDEAVKHCPTVQHVLVAHRTD---------NKVHMGDLDIPLEQEMAKEDPVCA 278
Cdd:PRK05620 108 NHAEDEVIVADPR---------LAEQLGEILKECPCVRAVVFIGPSDadsaaahmpEGIKVYSYEALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 279 PESmgseDVLFMLYTSGSTGMPKGIVHT-QAGYLLYAALTHKLVFDHRPGDIFGCVADI-----------GWITGHSYVV 346
Cdd:PRK05620 179 DET----TAAAICYSTGTTGAPKGVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPIyhvlswgvplaAFMSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 YGPLCNGAT--SVLFESTPvypnagrywetverlkiNQFYGAPTA-VRLLLKYGDawvKKYDRSSLRTL---GSVGEPIN 420
Cdd:PRK05620 255 PGPDLSAPTlaKIIATAMP-----------------RVAHGVPTLwIQLMVHYLK---NPPERMSLQEIyvgGSAVPPIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 421 CEAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRPSEeGAEILPGMAMRPFFGIVPVLMDEK----GSVVEGSN----- 491
Cdd:PRK05620 315 IKAWEERYGV------DVVHVWGMTETSPVGTVARPPS-GVSGEARWAYRVSQGRFPASLEYRivndGQVMESTDrnege 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 492 --VSGALCI-------SQAWPGMARTIYGDHQRFVDAYFKAyPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTA 562
Cdd:PRK05620 388 iqVRGNWVTasyyhspTEEGGGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 563 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 642
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKF 546
|
....*..
gi 1622839330 643 MRRLLRK 649
Cdd:PRK05620 547 DKKDLRQ 553
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
285-644 |
3.90e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 89.24 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 EDVLFMLYTSGSTGMPKGIVhtQAGYLLYAALTH--KLVFDHRPGDIFGCVADIGWITGHSYVvygplcngATSVLFEST 362
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVL--LANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWI--------LTCLIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 363 PVYPNAGRYWETVerLKINQFYGA------PTA---VRLLLKYGDAWVKKydrssLRTLGSVGE-PINCEA--WEWLHRV 430
Cdd:cd17635 71 CVTGGENTTYKSL--FKILTTNAVtttclvPTLlskLVSELKSANATVPS-----LRLIGYGGSrAIAADVrfIEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 431 vgdsrcTLVDTWWQTETGGICIAPRpSEEGAEIlpGMAMRPFFGIVPVLMDEKG-SVVEGSNvsGALCISQAWpgMARTI 509
Cdd:cd17635 144 ------NTAQVYGLSETGTALCLPT-DDDSIEI--NAVGRPYPGVDVYLAATDGiAGPSASF--GTIWIKSPA--NMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 510 YGDHQRFVDAYFKaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 589
Cdd:cd17635 211 WNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 590 AAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:cd17635 288 LVGLAVVA--SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
140-648 |
5.81e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.09 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLAN-TLKRHGVCRGDCVAIYMPVS---PLAVAAMLaCARIGAV------------HTVIFAGFSA--- 200
Cdd:PRK08751 51 ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNClqyPIATFGVL-RAGLTVVnvnplytprelkHQLIDSGASVlvv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 201 -----ASLAGRINDAKCKVVITfnQGLrgGRVMELKK--IVDEAVKHcptVQHVLVAHRTDNKVHMGD-LDIPLEQEMAK 272
Cdd:PRK08751 130 idnfgTTVQQVIADTPVKQVIT--TGL--GDMLGFPKaaLVNFVVKY---VKKLVPEYRINGAIRFREaLALGRKHSMPT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 273 EDpvcapesMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHKlvfdhrpgdifGCVADI----GWITGHS----- 343
Cdd:PRK08751 203 LQ-------IEPDDIAFLQYTGGTTGVAKG-----------AMLTHR-----------NLVANMqqahQWLAGTGkleeg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 344 ----------YVVYGPLCNGATSVLFE------STPvyPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRS 407
Cdd:PRK08751 254 cevvitalplYHIFALTANGLVFMKIGgcnhliSNP--RDMPGFVKELKKTRFTAFTGVNTLFNGLLN--TPGFDQIDFS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 408 SLR-TLGSvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETG-GICIAPRPSEEgaeiLPGMAMRPFFGIVPVLMDEKGS 485
Cdd:PRK08751 330 SLKmTLGG-GMAVQRSVAERWKQVTG---LTLVEAYGLTETSpAACINPLTLKE----YNGSIGLPIPSTDACIKDDAGT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 486 VVEGSNVsGALCISQAwpgmaRTIYGDHQR------FVDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRL 559
Cdd:PRK08751 402 VLAIGEI-GELCIKGP-----QVMKGYWKRpeetakVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 560 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 639
Cdd:PRK08751 471 YPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA----LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNV 546
|
....*....
gi 1622839330 640 GKVMRRLLR 648
Cdd:PRK08751 547 GKILRRELR 555
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
526-648 |
9.06e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 90.50 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 605
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE 511
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622839330 606 vvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK08974 512 ----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
116-653 |
1.54e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 89.65 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 116 QHVQKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMP-VSPLAVAAMLACARIGavhtvI 194
Cdd:PLN02330 36 QDAELYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPnVAEYGIVALGIMAAGG-----V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRIND----AKCKVVITfnQGLRGGRVMELKkivdeavkhCPTVqhVLVAHRTDNKVHMGDLdipLEQEM 270
Cdd:PLN02330 107 FSGANPTALESEIKKqaeaAGAKLIVT--NDTNYGKVKGLG---------LPVI--VLGEEKIEGAVNWKEL---LEAAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 271 AKEDPVcAPESMGSEDVLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLvFDHRPgDIFGCVADIGWITG-HSYVVYGP 349
Cdd:PLN02330 171 RAGDTS-DNEEILQTDLCALPFSSGTTGISKGVMLTHRN--LVANLCSSL-FSVGP-EMIGQVVTLGLIPFfHIYGITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 350 LCngATsvlfestpvYPNAGRYwETVERLKINQFYGA------------PTAVRLLLKygDAWVKKYDRSSL--RTLGSV 415
Cdd:PLN02330 246 CC--AT---------LRNKGKV-VVMSRFELRTFLNAlitqevsfapivPPIILNLVK--NPIVEEFDLSKLklQAIMTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 416 GEPINCE---AWEWLHRVVgdsrcTLVDTWWQTETGGICIAPRPSEEGAeilpGMAMRPFFG-IVPVL----MDEKGSVV 487
Cdd:PLN02330 312 AAPLAPElltAFEAKFPGV-----QVQEAYGLTEHSCITLTHGDPEKGH----GIAKKNSVGfILPNLevkfIDPDTGRS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 488 EGSNVSGALCI-SQAwpgMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAE 563
Cdd:PLN02330 383 LPKNTPGELCVrSQC---VMQGYYNNKEetdRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 564 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM 643
Cdd:PLN02330 455 LEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE---EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIM 531
|
570
....*....|
gi 1622839330 644 RRLLRKIITS 653
Cdd:PLN02330 532 RRLLKEKMLS 541
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
140-648 |
1.80e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 89.44 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRH-GVCRGDCVAIYMP---VSPLAV-AAMlacaRIGAVHTVIFAGFSAASLAGRINDAKCKV 214
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPnvlQYPVAVfGAM----RAGLIVVNTNPLYTAREMEHQFNDSGAKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 215 VITF------------NQGLRGGRVMEL--------KKIVDEAVKHcptVQHVLVAHRTDNKVHMGDLdipleQEMAKED 274
Cdd:PRK05677 126 LVCLanmahlaekvlpKTGVKHVIVTEVadmlpplkRLLINAVVKH---VKKMVPAYHLPQAVKFNDA-----LAKGAGQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 PVcAPESMGSEDVLFMLYTSGSTGMPKGivhtqagyllyAALTHK-LVfdhrpGDIFGCVADIGWITGH-SYVVYGPL-- 350
Cdd:PRK05677 198 PV-TEANPQADDVAVLQYTGGTTGVAKG-----------AMLTHRnLV-----ANMLQCRALMGSNLNEgCEILIAPLpl 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 351 ---------CnGATSVLFESTPVYPNAGRYWETVERL---KINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEP 418
Cdd:PRK05677 261 yhiyaftfhC-MAMMLIGNHNILISNPRDLPAMVKELgkwKFSGFVGLNTLFVALCNNEA--FRKLDFSALKLTLSGGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 419 INCEAWEWLHRVVGdsrCTLVDTWWQTETGGI-CIAPRpseegAEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVsGALC 497
Cdd:PRK05677 338 LQLATAERWKEVTG---CAICEGYGMTETSPVvSVNPS-----QAIQVGTIGIPVPSTLCKVIDDDGNELPLGEV-GELC 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 498 IS--QAWPGmartiYGDHQRFVDAYFKAyPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 575
Cdd:PRK05677 409 VKgpQVMKG-----YWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVL 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839330 576 ESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 648
Cdd:PRK05677 483 QCAAIGVPDEKSGEAIKVFVVVKPGET---LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
115-647 |
4.20e-18 |
|
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: 87.61 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 115 DQHVQKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemaked 274
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 275 pvcapesmGSEDVLFMLYTSGSTGMPKGI-VHTQAgyLLYAALTHKLVFDHRPGDIFGCVADIGWiTGHSYVVYGPLCNG 353
Cdd:cd17645 102 --------NPDDLAYVIYTSGSTGLPKGVmIEHHN--LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ATsvlfesTPVYPNAGRYweTVERLkiNQFYGAPTAVRLLLKYGDA-WVKKYDRSSLRTLGSVGEPINceawewlhrVVG 432
Cdd:cd17645 171 AA------LHVVPSERRL--DLDAL--NDYFNQEGITISFLPTGAAeQFMQLDNQSLRVLLTGGDKLK---------KIE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 433 DSRCTLVDTWWQTETGGICIAPRPSEEGAEILPGMAMRPffgiVPVLMDEKGSVVEGSNVSGALCIsqAWPGMARTIYG- 511
Cdd:cd17645 232 RKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDN----TRVYILDEALQLQPIGVAGELCI--AGEGLARGYLNr 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 512 ---DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 588
Cdd:cd17645 306 pelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 589 EAAFAFIVVKdsagdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd17645 386 KYLVAYVTAP-----EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
137-650 |
1.74e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TFNqglrggrvmELKKIVDEAVKHCPTVQH-----VLVAHRTDNKVHMGDLDIPLEQEMAKEDPvcAPESMGS------- 284
Cdd:PLN03102 117 VDR---------SFEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 EDVLFMLYTSGSTGMPKGIVHTQAGYLLyAALThklvfdhrpgdifgcvADIGWITGHSYVVYGPL----CNG------- 353
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYL-STLS----------------AIIGWEMGTCPVYLWTLpmfhCNGwtftwgt 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 354 ----ATSVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLKyGDAWVKKYDRSSLRTLGSVGEP-------INCE 422
Cdd:PLN03102 249 aargGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPPpaalvkkVQRL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 423 AWEWLHrVVGDSRCT--LVDTWWQTETGGIciaprPSEEGAEILPGMAMRpFFGIVPVLMDEKG---SVVEGSNVSGALC 497
Cdd:PLN03102 324 GFQVMH-AYGLTEATgpVLFCEWQDEWNRL-----PENQQMELKARQGVS-ILGLADVDVKNKEtqeSVPRDGKTMGEIV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 498 ISqawpgmARTIYGDHQRFVDAYFKAYP-GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 576
Cdd:PLN03102 397 IK------GSSIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 577 SAVIGYPHDIKGEAAFAFIVVKDS----AGDSDVVVQELKSMVA---TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PLN03102 471 TAVVAMPHPTWGETPCAFVVLEKGettkEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
.
gi 1622839330 650 I 650
Cdd:PLN03102 551 I 551
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
138-659 |
2.04e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 86.05 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 138 VRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIT 217
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 218 ----FNQGLRGGRVMELKKivDEAVKhcPTVQHVLVAHRTDNKV---HMGDLDIPLEQEMAKEDPVCAPESMGSE-DVLF 289
Cdd:PLN02479 124 dqefFTLAEEALKILAEKK--KSSFK--PPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADEwQSIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 290 MLYTSGSTGMPKGIV-HTQAGYLLyaALTHKLVFDHRPGDI-------FGCVadiGWITGHSYVVygpLCngATSVLFES 361
Cdd:PLN02479 200 LGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVylwtlpmFHCN---GWCFTWTLAA---LC--GTNICLRQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 362 TpvypNAGRYWETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWL-HRVVgdsrctl 438
Cdd:PLN02479 270 V----TAKAIYSAIANYGVTHFCAAPVVLNTIVNApkSETILPLPRVVHVMTAGAAPPPSVLFAMSEKgFRVT------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 439 vDTWWQTETGG---ICI-APR----PSEEGAEI----------LPGMAMRPFFGIVPVLMDEK--GSVVEGSNVsgalci 498
Cdd:PLN02479 339 -HTYGLSETYGpstVCAwKPEwdslPPEEQARLnarqgvryigLEGLDVVDTKTMKPVPADGKtmGEIVMRGNM------ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 499 sqAWPGMARTIYGDHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 578
Cdd:PLN02479 412 --VMKGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 579 VIGYPHDIKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRkiitSEAQ 656
Cdd:PLN02479 483 VVARPDERWGESPCAFVTLKPGVDKSDeaALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR----AKAK 557
|
...
gi 1622839330 657 ELG 659
Cdd:PLN02479 558 EMG 560
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
129-649 |
1.32e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 83.19 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 129 WERDEPG---TEVRITYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLA 204
Cdd:PRK07867 15 AEDDDRGlyfEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 205 GRINDAKCKVVITFNqglrggrvmelkkivdeavKHCPTVQHVlvahrtDNKVHMGDLDIPL-EQEMAKEDPVCAPESMG 283
Cdd:PRK07867 95 RDIAHADCQLVLTES-------------------AHAELLDGL------DPGVRVINVDSPAwADELAAHRDAEPPFRVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 284 SEDVLFMLY-TSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIfgCVADIGWItgHSYVV---YGP-LCNGATSVL 358
Cdd:PRK07867 150 DPDDLFMLIfTSGTSGDPKAVRCTH-RKVASAGVMLAQRFGLGPDDV--CYVSMPLF--HSNAVmagWAVaLAAGASIAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 359 ---FestpvypNAGRYWETVERlkinqfYGAPTA--VRLLLKYGDAWVKKYD--RSSLRTL-GSVGEPINCEAWEwlhRV 430
Cdd:PRK07867 225 rrkF-------SASGFLPDVRR------YGATYAnyVGKPLSYVLATPERPDdaDNPLRIVyGNEGAPGDIARFA---RR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 431 VGdsrCTLVDTWWQTEtGGICIAPRPSEEgaeilPGMAMRPFFGI----------VPVLMDEKGSVVEGSNVSGALcISQ 500
Cdd:PRK07867 289 FG---CVVVDGFGSTE-GGVAITRTPDTP-----PGALGPLPPGVaivdpdtgteCPPAEDADGRLLNADEAIGEL-VNT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 501 AWPGMARTIY----GDHQRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPE 576
Cdd:PRK07867 359 AGPGGFEGYYndpeADAERMRG-------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839330 577 SAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:PRK07867 432 VAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
119-463 |
6.29e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.48 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 119 QKSPESVALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVI 194
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 195 FAGFSAASLAGRINDAKCKVVITFNQGLRGGRVMELKKivdEAVKHCPTVqhvlvahrtDNKVHMG--DLDiPLEQEMAK 272
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK---PSVRRLVTV---------GGRLLWGgtTLA-TLLRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 273 EDPVCAPesMGSEDVLFMLYTSGSTGMPKGIVHTQAGYLlyAALTH-KLVFDHRPGDIfgcvaDIgwitgHSY---VVYG 348
Cdd:PRK09274 164 APFPMAD--LAPDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEAlREDYGIEPGEI-----DL-----PTFplfALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 349 PLCnGATSVLFESTPVYP---NAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWE 425
Cdd:PRK09274 230 PAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 426 WLHRVVGD--------------------SRCTLVDTWWQTETG-GICIApRPSeEGAEI 463
Cdd:PRK09274 307 RFRAMLPPdaeiltpygatealpissieSREILFATRAATDNGaGICVG-RPV-DGVEV 363
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
122-647 |
9.21e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 80.81 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAA 201
Cdd:PRK13383 49 PGRTAII---DDDGA---LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 202 SLAGRINDAKCKVVITFNQglrggrvmelkkIVDEAVKhcptvqhvlvahrTDNKVHMGDLDIPLEQEMAKEDPVCAPES 281
Cdd:PRK13383 123 ALAAALRAHHISTVVADNE------------FAERIAG-------------ADDAVAVIDPATAGAEESGGRPAVAAPGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 282 MgsedvlfMLYTSGSTGMPKGIVHT---QAGYLLYAALTHKLVFdhRPGDIFGCVADIGWITGHSYVVYGPLCNGA--TS 356
Cdd:PRK13383 178 I-------VLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRL--RTGSRISVAMPMFHGLGLGMLMLTIALGGTvlTH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 357 VLFESTPVYPNAGRYwetverlKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrc 436
Cdd:PRK13383 249 RHFDAEAALAQASLH-------RADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 437 TLVDTWWQTETGgICIAPRPSEegAEILPGMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGmartiygdhQRF 516
Cdd:PRK13383 319 ILYNGYGSTEVG-IGALATPAD--LRDAPETVGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAG---------TRY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 517 VDAYFKAY-PGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 595
Cdd:PRK13383 386 TDGGGKAVvDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 596 VVKDSagdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK13383 466 VLHPG---SGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
132-650 |
1.06e-15 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 80.40 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 132 DEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAK 211
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 212 cKVVITFNQGL---RGGRVMELKKIVDEAVkhcptvqhvlvahrtdnkvHMGDLDIPLEQEMAKEDPVCAPESmGSEDVL 288
Cdd:cd05906 112 -HIWQLLGSPVvltDAELVAEFAGLETLSG-------------------LPGIRVLSIEELLDTAADHDLPQS-RPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 289 FMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFgcvadIGW-----ITGHSYVVYGPLCNGATSVLFESTP 363
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 364 VYPNAGRYWETVERLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLV 439
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLL--EPYGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 440 DT-----WWQTETGGICI------APRPSEE------GAEIlPGMAMRpffgivpvLMDEKGSVVEGSNVsGALCISqaw 502
Cdd:cd05906 320 PDairpaFGMTETCSGVIysrsfpTYDHSQAlefvslGRPI-PGVSMR--------IVDDEGQLLPEGEV-GRLQVR--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 503 pGMARTiygdhqrfvdayfkayPGYY---------FTGDGAHRT------EGGYYQITGRMDDVINISGHRLGTAEIEDA 567
Cdd:cd05906 387 -GPVVT----------------KGYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIVNGVNYYSHEIEAA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 568 IADHPAVPESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAkyAVPDEILVVKR--LPKTRSGK 641
Cdd:cd05906 450 VEEVPGVEPSFTAAFAVRDPGaeteELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLPKeeIPKTSLGK 527
|
....*....
gi 1622839330 642 VMRRLLRKI 650
Cdd:cd05906 528 IQRSKLKAA 536
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
261-648 |
1.63e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.07 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 261 DLDIPLEQEMAKEDPVCAPES-MGSEDVLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKlvFDHRPGDIFGCVADIGw 338
Cdd:PRK13388 125 DVDTPAYAELVAAAGALTPHReVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPLF- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 339 itgHSYVVY---GP-LCNGATSVLfestPVYPNAGRYWETVerlkinQFYGAP--TAVRLLLKYGDAWVKKYDRS--SLR 410
Cdd:PRK13388 202 ---HSNAVMagwAPaVASGAAVAL----PAKFSASGFLDDV------RRYGATyfNYVGKPLAYILATPERPDDAdnPLR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 411 T-LGSVGEPINCEawEWLHRVvgdsRCTLVDTWWQTETGGICIAPRPSEEGAeilpgmAMRPFFGIV-----------PV 478
Cdd:PRK13388 269 VaFGNEASPRDIA--EFSRRF----GCQVEDGYGSSEGAVIVVREPGTPPGS------IGRGAPGVAiynpetltecaVA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 479 LMDEKGSVVEGSNVSGALcISQAWPGMARTIYGDH----QRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINI 554
Cdd:PRK13388 337 RFDAHGALLNADEAIGEL-VNTAGAGFFEGYYNNPeataERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 555 SGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATK--IAKYAVPDEILVVK 632
Cdd:PRK13388 409 DGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD---GATFDPDAFAAFLAAQpdLGTKAWPRYVRIAA 485
|
410
....*....|....*.
gi 1622839330 633 RLPKTRSGKVMRRLLR 648
Cdd:PRK13388 486 DLPSTATNKVLKRELI 501
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
57-113 |
1.98e-15 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 70.58 E-value: 1.98e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 57 YPALSAQAAREPAAFWGPLARDtLLWDTPYHTVWDCDFStGKIGWFLGGQLNVSVNC 113
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
140-652 |
2.94e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.12 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRH-GVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDakCKVVITF 218
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVD--CSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 nqglrggrvmelkkIVDEAVKHCPTVQhVLVAHRTDNKVH-MGDLDIPLEQEMAKEDPVCAPES-MGSEDVLFMLYTSGS 296
Cdd:PLN02574 145 --------------TSPENVEKLSPLG-VPVIGVPENYDFdSKRIEFPKFYELIKEDFDFVPKPvIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 297 TGMPKGIVHTQAGYL----LYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYW 372
Cdd:PLN02574 210 TGASKGVVLTHRNLIamveLFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 373 ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVgepiNCEAWEWLHRVVGD-----SRCTLVDTWWQTET 447
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKK----AKGVCGEVLKSLKQV----SCGAAPLSGKFIQDfvqtlPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 448 GGICIAPRPSEEGAE------ILPGMAMRpffgivpVLMDEKGSVVEGSNvSGALCISQawPGMARTIYGDHQRFVDAYF 521
Cdd:PLN02574 358 TAVGTRGFNTEKLSKyssvglLAPNMQAK-------VVDWSTGCLLPPGN-CGELWIQG--PGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 522 KayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSA 601
Cdd:PLN02574 428 K--DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622839330 602 GDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 652
Cdd:PLN02574 506 TLSQ---EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
521-652 |
5.71e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 77.73 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 521 FKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDS 600
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 601 AGDsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 652
Cdd:PRK07445 399 SIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
137-647 |
7.10e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 77.48 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TfnqglrggrvmelkkivdeavkhcptvqhvlvahrTDNkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGS 296
Cdd:cd05914 85 V-----------------------------------SDE-----------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 297 TGMPKGIVHTQAG----------YLLYAALTHKLVFdhRP-GDIFGCVADIgwitghsyvVYgPLCNGATSVLFESTP-- 363
Cdd:cd05914 101 TGNSKGVMLTYRNivsnvdgvkeVVLLGKGDKILSI--LPlHHIYPLTFTL---------LL-PLLNGAHVVFLDKIPsa 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 364 ---------VYPNAG--RYWETVERLK---INQFYGAPTAVRLLLKYGDAWVKKYDRSSL--------RTLGSVGEPINC 421
Cdd:cd05914 169 kiialafaqVTPTLGvpVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 422 EAWEWLHRVvgdsRCTLVDTWWQTETGGICIAPRPSEE----GAEILPGMAMRPFfgiVPVLMDEKGS-VVEGSNVsgal 496
Cdd:cd05914 249 DVEEFLRTI----GFPYTIGYGMTETAPIISYSPPNRIrlgsAGKVIDGVEVRID---SPDPATGEGEiIVRGPNV---- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 497 cisqawpgMaRTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINI-SGHRLGTAEIEDAIADHPAVP 575
Cdd:cd05914 318 --------M-KGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVL 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 576 ESAVIGYPHDIKG----EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYA-VPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:cd05914 387 ESLVVVQEKKLVAlayiDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
114-647 |
1.11e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 78.16 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTV 193
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAASLAGRINDAKCKVVITfnqglrggrvmelkkiVDEavkhcptvqhvlVAHRTDNkvhmGDLDIPLEQEMAKE 273
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLIT----------------TAD------------QLPRFAD----VPDLTSLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 274 DPVCAPESMGS-EDVLFMLYTSGSTGMPKGIVHTQagyllyAALTHKLVFDHrpgDIFGCVAD--IGWITGHSYVV---- 346
Cdd:PRK10252 586 PQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQ------TAIVNRLLWMQ---NHYPLTADdvVLQKTPCSFDVsvwe 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 -YGPLCNGATSVLFEstpvyPNAGRYWETVERL----KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGE--PI 419
Cdd:PRK10252 657 fFWPFIAGAKLVMAE-----PEAHRDPLAMQQFfaeyGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEalPA 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 420 N-CEAWEW-----LHRVVGDSRCTlVD-TWW--------QTETGGICIAPRPSEEGAEILPGMaMRPffgiVPVlmdekg 484
Cdd:PRK10252 732 DlCREWQQltgapLHNLYGPTEAA-VDvSWYpafgeelaAVRGSSVPIGYPVWNTGLRILDAR-MRP----VPP------ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 485 svvegsNVSGALCIS--QawpgMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHR 558
Cdd:PRK10252 800 ------GVAGDLYLTgiQ----LAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQR 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 559 LGTAEIEDAIADHP----AVPESAVIGYPHDIKGEAA--FAFIVVKDSAG-DSDVvvqeLKSMVATKIAKYAVPDEILVV 631
Cdd:PRK10252 870 IELGEIDRAMQALPdveqAVTHACVINQAAATGGDARqlVGYLVSQSGLPlDTSA----LQAQLRERLPPHMVPVVLLQL 945
|
570
....*....|....*.
gi 1622839330 632 KRLPKTRSGKVMRRLL 647
Cdd:PRK10252 946 DQLPLSANGKLDRKAL 961
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
529-647 |
2.17e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 75.84 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 529 FTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfIVVKDSAGDSDvvv 608
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA-KVISHEEIDPV--- 369
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622839330 609 qELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK08308 370 -QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
523-654 |
3.18e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 74.70 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 523 AYPGYYFTGDGAHRTEGgYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsAG 602
Cdd:PRK07824 231 AEPGWFRTDDLGALDDG-VLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG---DG 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 603 DSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSE 654
Cdd:PRK07824 307 GPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
289-647 |
9.95e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 289 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHRPGDifgCVADIGWIT--GHSYVVYGPLCNGATSVLfestpvyp 366
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFYSINfdAASERLLVPLLCGARVVL-------- 2404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 367 NAGRYWETVE--------RLKINQF---YGAPTAVRLllkygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSr 435
Cdd:PRK05691 2405 RAQGQWGAEEicqlireqQVSILGFtpsYGSQLAQWL--------AGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ- 2475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 436 cTLVDTWWQTETGGI---CIAPRPSEEGAEILPgmAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARtiyGD 512
Cdd:PRK05691 2476 -LFFNAYGPTETVVMplaCLAPEQLEEGAASVP--IGRVVGARVAYILDADLALVP-QGATGELYVGGA--GLAQ---GY 2546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 513 HQR-------FVDAYFKAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGypH 584
Cdd:PRK05691 2547 HDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA--L 2624
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 585 DIKGEAAFAFIVVKDSAGDSDVVVQEL----KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK05691 2625 DTPSGKQLAGYLVSAVAGQDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
122-646 |
3.08e-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: 72.43 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 122 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGD-CVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 200
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 201 ASLAGRINDAKCKVVITfnqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcape 280
Cdd:cd17648 75 ERIQFILEDTGARVVIT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 281 smGSEDVLFMLYTSGSTGMPKGIVHTQAGYL-LYAALThKLVFDHRPGD-----IFGCVAD-------IGWITGHSYVVY 347
Cdd:cd17648 92 --NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnLRTSLS-ERYFGRDNGDeavlfFSNYVFDffveqmtLALLNGQKLVVP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 348 GPlcngatSVLFEStpvypnaGRYWETVERLKINQFYGAPTAVRLllkygdawvkkYD---RSSLRTLGSVGEPINCEAW 424
Cdd:cd17648 169 PD------EMRFDP-------DRFYAYINREKVTYLSGTPSVLQQ-----------YDlarLPHLKRVDAAGEEFTAPVF 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 425 EWLHrvvGDSRCTLVDTWWQTETGgICIAPRPSEEGA-------EILPGM-------AMRPffgiVPVlmdekGSVveGS 490
Cdd:cd17648 225 EKLR---SRFAGLIINAYGPTETT-VTNHKRFFPGDQrfdkslgRPVRNTkcyvlndAMKR----VPV-----GAV--GE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 491 NVSGALCISQAW---PGMARtiygdhQRFVDAYFKA--------YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRL 559
Cdd:cd17648 290 LYLGGDGVARGYlnrPELTA------ERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 560 GTAEIEDAIADHPAVPESAVI-GYPHDIKGEAAFAFIV---VKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLP 635
Cdd:cd17648 364 EPGEVEAALASYPGVRECAVVaKEDASQAQSRIQKYLVgyyLPEPGHVPE---SDLLSFLRAKLPRYMVPARLVRLEGIP 440
|
570
....*....|..
gi 1622839330 636 KTRSGKV-MRRL 646
Cdd:cd17648 441 VTINGKLdVRAL 452
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
139-649 |
7.63e-13 |
|
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: 71.23 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIfagfsaaslagrindakckvvitf 218
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 NQGLRGgrvmelkkivdEAVKHCPTV---QHVLVahrtdnkvhmgdldipleqemakedpvcapesmgseDVLFMLYTSG 295
Cdd:cd05940 59 NYNLRG-----------ESLAHCLNVssaKHLVV------------------------------------DAALYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 296 STGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIFGCVAdIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 375
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLP-LYHSTALIVGWSACLASGATLVIRKKF----SASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 376 --ERLKINQFYGapTAVRLLLKygdAWVKKYDRS-SLRTLgsVGEPINCEAWEWLHRVVGDSRCTlvDTWWQTEtGGICI 452
Cdd:cd05940 167 rkYQATIFQYIG--ELCRYLLN---QPPKPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPRIA--EFYAATE-GNSGF 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 453 APRPSEEGAEILPGMAMRPFFGIVPVLMD-EKGSVVEGSNvsgALCI--SQAWPGMARTIYGDHQRFvDAY--------- 520
Cdd:cd05940 237 INFFGKPGAIGRNPSLLRKVAPLALVKYDlESGEPIRDAE---GRCIkvPRGEPGLLISRINPLEPF-DGYtdpaatekk 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 521 -----FKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAF 592
Cdd:cd05940 313 ilrdvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAGM 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 593 AFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 649
Cdd:cd05940 391 AAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
286-644 |
2.50e-12 |
|
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: 68.45 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLFESTpvy 365
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 366 pNAGRYWETVERLKINqFYG--APTAVRLLlkygDAWVKK-YDRSSLRTLGSVGEPINCEAWEwlhrVVGDSrctlvdTW 442
Cdd:cd17637 76 -DPAEALELIEEEKVT-LMGsfPPILSNLL----DAAEKSgVDLSSLRHVLGLDAPETIQRFE----ETTGA------TF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 443 W----QTETGG-ICIAPRPSEEGAEILPGMAMRpfFGIV-----PVLMDEKGSVVegsnVSGALCISQAWPGMARTIYGd 512
Cdd:cd17637 140 WslygQTETSGlVTLSPYRERPGSAGRPGPLVR--VRIVddndrPVPAGETGEIV----VRGPLVFQGYWNLPELTAYT- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 513 hqrfvdayFKAypGYYFTGDGAHRTEGGYYQITGRM--DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIK-GE 589
Cdd:cd17637 213 --------FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPKwGE 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839330 590 AAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 644
Cdd:cd17637 282 GIKAVCVLKPGAT---LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
479-657 |
2.88e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 479 LMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQR----FVDAYFKAyPG--YYFTGDGAHRTEGGYYQITGRMDDVI 552
Cdd:PRK05691 4053 LLDEALELVPLGAV-GELCV--AGTGVGRGYVGDPLRtalaFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQV 4128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 553 NISGHRLGTAEIEDAIADHPAVPESAViGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVK 632
Cdd:PRK05691 4129 KIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLD 4207
|
170 180
....*....|....*....|....*
gi 1622839330 633 RLPKTRSGKVMRRLLRKIITSEAQE 657
Cdd:PRK05691 4208 RLPLNANGKLDRKALPALDIGQLQS 4232
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
141-649 |
7.32e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 68.23 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVItfn 219
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglrggrvmelkkiVDEavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmgsEDVLFMLYTSGSTGM 299
Cdd:cd05937 84 --------------VDP------------------------------------------------DDPAILIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 300 PKG-IVHTQAGYLLYAALTHKLVFD------------HRPGDIFGCVADIG----------------W----ITGHSYVV 346
Cdd:cd05937 102 PKAaAISWRRTLVTSNLLSHDLNLKngdrtytcmplyHGTAAFLGACNCLMsggtlalsrkfsasqfWkdvrDSGATIIQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 347 Y-GPLCNgatsvLFESTP------------VYPNAGR--YWETV-ERL---KINQFYGAPTAVRLLLKYG-DAWvkkydr 406
Cdd:cd05937 182 YvGELCR-----YLLSTPpspydrdhkvrvAWGNGLRpdIWERFrERFnvpEIGEFYAATEGVFALTNHNvGDF------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 407 sslrTLGSVGE--PInceaWEWLHRvvGDSRCTLVDT-----WWQTETGGICIAPRpsEEGAEILpgmaMRPFFgivpvl 479
Cdd:cd05937 251 ----GAGAIGHhgLI----RRWKFE--NQVVLVKMDPetddpIRDPKTGFCVRAPV--GEPGEML----GRVPF------ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 480 mdekgsvvegSNVSgalcisqAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRL 559
Cdd:cd05937 309 ----------KNRE-------AFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENV 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 560 GTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAFIVVKDSAGD-SDVVVQELKSMVATKIAKYAVPDEILVVKRLP 635
Cdd:cd05937 372 STTEVADVLGAHPDIAEANVYGVKvpgHD--GRAGCAAITLEESSAVpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVA 449
|
570
....*....|....
gi 1622839330 636 KTRSGKVMRRLLRK 649
Cdd:cd05937 450 TTDNHKQQKGVLRD 463
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
131-642 |
7.78e-12 |
|
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: 67.88 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 131 RDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtviFAGFSAASLAGRInda 210
Cdd:cd17654 8 IDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQRS--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 211 kckvvitfnqglrggrvmeLKKIVDEAVKHCPTVQHVLVA--HRTDNKVHMgdlDIPLEQEMAkedpvcapesmgsedvl 288
Cdd:cd17654 81 -------------------LTVMKKCHVSYLLQNKELDNAplSFTPEHRHF---NIRTDECLA----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 289 FMLYTSGSTGMPKG-----------IVHTQAGYLLYAA----LTHKLVFDHRPGDIFGCVADIG-WITGHSYVVYGPLCn 352
Cdd:cd17654 122 YVIHTSGTTGTPKIvavphkcilpnIQHFRSLFNITSEdilfLTSPLTFDPSVVEIFLSLSSGAtLLIVPTSVKVLPSK- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 353 gATSVLFESTPVypnagryweTVERLkinqfygAPTavrLLLKYGDAWVKKYDRS---SLRTLGSVGE--PINCEAWEWL 427
Cdd:cd17654 201 -LADILFKRHRI---------TVLQA-------TPT---LFRRFGSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 428 HRVVGDSRCTLVDTwwqTETGGICIAPRPSEEGAEILPGMamrPFFGIVPVLMDEKGSVVEGSNVSGAL---CISQAWPG 504
Cdd:cd17654 261 GKGNRTRIFNIYGI---TEVSCWALAYKVPEEDSPVQLGS---PLLGTVIEVRDQNGSEGTGQVFLGGLnrvCILDDEVT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 505 MARTIYgdhqrfvdayfkaypgyYFTGDGAHRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYph 584
Cdd:cd17654 335 VPKGTM-----------------RATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS-- 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 585 diKGEAAFAFIVVKDSagdSDVVVQELksmVATKIAKYAVPDEILVVKRLPKTRSGKV 642
Cdd:cd17654 395 --DQQRLIAFIVGESS---SSRIHKEL---QLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
124-630 |
1.18e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 67.87 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 124 SVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAAS 202
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 203 LAGRINDAKCKVVITfnqglrggrVMELKKIVDEAVKHCPTVQHVLV-AHRTDNKVHMGDLDIPLEQEMAKEDPV----- 276
Cdd:cd17632 132 LAPILAETEPRLLAV---------SAEHLDLAVEAVLEGGTPPRLVVfDHRPEVDAHRAALESARERLAAVGIPVttltl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 277 -------------CAPESmgSEDVLFML-YTSGSTGMPKGIVHT--------------QAGYLLYAALTHKLVFDHRPGD 328
Cdd:cd17632 203 iavrgrdlppaplFRPEP--DDDPLALLiYTSGSTGTPKGAMYTerlvatfwlkvssiQDIRPPASITLNFMPMSHIAGR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 329 IfgcvadigwitghsyVVYGPLCNGAT---------SVLFES-TPVYPNA----GRYWETVerlkiNQFYGAPTAVRLLL 394
Cdd:cd17632 281 I---------------SLYGTLARGGTayfaaasdmSTLFDDlALVRPTElflvPRVCDML-----FQRYQAELDRRSVA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 395 KYGDAWVKKYDRSSLR--TLG-------SVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETGGIciaprpseegaeILP 465
Cdd:cd17632 341 GADAETLAERVKAELRerVLGgrllaavCGSAPLSAEMKAFMESLLDLD---LHDGYGSTEAGAV------------ILD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 466 GMAMRPffgivPV----LMD--EKGSVVEGS-NVSGALCI--SQAWPGMARTIYGDHQRFvDAyfkayPGYYFTGDGAHR 536
Cdd:cd17632 406 GVIVRP-----PVldykLVDvpELGYFRTDRpHPRGELLVktDTLFPGYYKRPEVTAEVF-DE-----DGFYRTGDVMAE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 537 TEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAVIGyphdiKGEAAF--AFIVVKDSAGDsDVVVQELKS 613
Cdd:cd17632 475 LGPDRLVYVDRRNNVLKLSqGEFVTVARLEAVFAASPLVRQIFVYG-----NSERAYllAVVVPTQDALA-GEDTARLRA 548
|
570 580
....*....|....*....|....*.
gi 1622839330 614 MVAT---KIAK------YAVPDEILV 630
Cdd:cd17632 549 ALAEslqRIAReaglqsYEIPRDFLI 574
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
285-653 |
2.91e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 66.36 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 EDVLFMLYTSGSTGMPKGIVHTQagyllyaaltHKLVFDhrpgdIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV 364
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVHN-----MFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 365 YPNAGRY-------------W-ETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPIN---CEAWEW 426
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDyelCHEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 427 LHRVVGDSRCTLVDTWWQTE-TGGICIAPrpseegaeilpgmAMRPFFGIV----PVLMDEKGSVVEGSNVSGALCISQA 501
Cdd:cd05908 251 HMSKYGLKRNAILPVYGLAEaSVGASLPK-------------AQSPFKTITlgrrHVTHGEPEPEVDKKDSECLTFVEVG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 502 WP---GMARTIYGDHQRFVDAYF--------KAYPGYY---------FTGDGAHRT------EGGYYQITGRMDDVINIS 555
Cdd:cd05908 318 KPideTDIRICDEDNKILPDGYIghiqirgkNVTPGYYnnpeatakvFTDDGWLKTgdlgfiRNGRLVITGREKDIIFVN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 556 GHRLGTAEIEDAIADHPAVP--ESAVIG-YPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVaTKIAKYAVpDEILVVK 632
Cdd:cd05908 398 GQNVYPHDIERIAEELEGVElgRVVACGvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHL-NKRGGWQI-NEVLPIR 475
|
410 420
....*....|....*....|.
gi 1622839330 633 RLPKTRSGKVMRRLLRKIITS 653
Cdd:cd05908 476 RIPKTTSGKVKRYELAQRYQS 496
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
139-373 |
3.50e-10 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 63.08 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRH-GVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVIT 217
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 218 fnqglrggrVMELKKIVDEAvkhCPTVQ----HVLVAHRTDNKVHMGDLDIPLEQemAKEDPVcaPESMGSEdVLFM--- 290
Cdd:cd05938 85 ---------APELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVISLLDKVDA--ASDEPV--PASLRAH-VTIKspa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 291 --LYTSGSTGMPKGIVHTQAGYLLYAALTHklvfdhrpgdIFGCVA-DIGWITGHSYVVYGPL-----C--NGATSVL-- 358
Cdd:cd05938 148 lyIYTSGTTGLPKAARISHLRVLQCSGFLS----------LCGVTAdDVIYITLPLYHSSGFLlgiggCieLGATCVLkp 217
|
250
....*....|....*.
gi 1622839330 359 -FestpvypNAGRYWE 373
Cdd:cd05938 218 kF-------SASQFWD 226
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
135-581 |
4.42e-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: 62.49 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMP------VSPLAVaaMLAcariGAVHTVIFAGFSAASLAGRIN 208
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 209 DAKCKVVITfnqglrgGRV---MELKKIVDEAVKHCPTVQH-VLVAHRT-DNKVHMGDldiPLEqemakEDPVCAPESMG 283
Cdd:cd05932 76 HSESKALFV-------GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 284 SedvlfMLYTSGSTGMPKGIVHTQA--GYLLYAALTHklvFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFES 361
Cdd:cd05932 141 T-----LIYTSGTTGQPKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 362 TPVYPnagrywETVERLKINQFYGAPtavRLLLK-----YGDAWVKKYDR-------SSL--------------RTLGSV 415
Cdd:cd05932 213 LDTFV------EDVQRARPTLFFSVP---RLWTKfqqgvQDKIPQQKLNLllkipvvNSLvkrkvlkglgldqcRLAGCG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 416 GEPINCEAWEWLHRVVGDsrctLVDTWWQTETGGICIAPRP--SEEG--AEILPGMAMRpffgivpvlMDEKGSVVEGSn 491
Cdd:cd05932 284 SAPVPPALLEWYRSLGLN----ILEAYGMTENFAYSHLNYPgrDKIGtvGNAGPGVEVR---------ISEDGEILVRS- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 492 vsgalcisqawPGMARTIYGDHQRFVDAyFKAyPGYYFTGDGAHRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIAD 570
Cdd:cd05932 350 -----------PALMMGYYKDPEATAEA-FTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAE 416
|
490
....*....|.
gi 1622839330 571 HPAVPESAVIG 581
Cdd:cd05932 417 HDRVEMVCVIG 427
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
528-642 |
6.81e-10 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 62.15 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 528 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDIKGEAAFA 593
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSYivPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 594 FIVVKDSAGDSDVVV----------QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 642
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
137-681 |
1.12e-09 |
|
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: 61.22 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 137 EVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVI 216
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TFNqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdldipleqemakedpvcapesmGSEDVLFMLYTSGS 296
Cdd:cd17640 83 VEN---------------------------------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 297 TGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIgWitgHSY---VVYGPLCNGAtSVLFESTPVYPN------ 367
Cdd:cd17640 100 TGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAYTSIRTLKDdlkrvk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 368 ------AGRYWETVERLKINQFYGAPTAVRLLLKYgdawvkkydrssLRTLGSVGEPINCeawewlhrvvGDSRCTLVDT 441
Cdd:cd17640 174 phyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGISG----------GGALPPHVDT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 442 WWQ------------TETGGICIAPRPSeegaEILPGMAMRPFFGIVPVLMDEKGSVVEGSNVSGALcisqawpgMARti 509
Cdd:cd17640 232 FFEaigievlngyglTETSPVVSARRLK----CNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIV--------WVR-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 510 yGDHqrFVDAYFK---------AYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAV 579
Cdd:cd17640 298 -GPQ--VMKGYYKnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMV 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 580 IGypHDIKgeAAFAFIVvkdsaGDSDVVVQELKSmVATKIAKyaVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG 659
Cdd:cd17640 375 VG--QDQK--RLGALIV-----PNFEELEKWAKE-SGVKLAN--DRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIA 442
|
570 580
....*....|....*....|..
gi 1622839330 660 DTTTLEDPSIITEILSAYQKCK 681
Cdd:cd17640 443 PFALLEEPFIENGEMTQTMKIK 464
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
140-359 |
1.42e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 61.15 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglRGGRVMELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDIPLEQE----MAKEDPVCAPESMGS----------E 285
Cdd:PTZ00216 200 ---NGKNVPNLLRLMKSGGMPNTTI------------IYLDSLPASVDTEgcrlVAWTDVVAKGHSAGShhplnipennD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQaGYLLYAALThklvFDHRPGDIFGCVADigwitGHSYVVYGPLCN----GATSVLF 359
Cdd:PTZ00216 265 DLALIMYTSGTTGDPKGVMHTH-GSLTAGILA----LEDRLNDLIGPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
141-656 |
1.50e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 61.26 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 141 TYRELLETTCRLANTLKRHgVCRGDCVAIYMPVSPLAVAAMLACA---RIGAV--HTVIFAGFSAASLAGRIndakcKVV 215
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKY-SVEGERIGLMLPNATISAAVIFGASlrrRIPAMmnYTAGVKGLTSAITAAEI-----KTI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 216 ITFNQGLRGGRVMELKKIVDEAvkhcptvqhvlvahrtdNKVHMGDLdiplEQEMAKED----------PVCAPESMGSE 285
Cdd:PRK08043 307 FTSRQFLDKGKLWHLPEQLTQV-----------------RWVYLEDL----KDDVTTADklwifahllmPRLAQVKQQPE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfestpvY 365
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL------Y 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 366 PNAGRYwETVERLKINQ----FYGAPTavrLLLKYGdAWVKKYDRSSLRTLGSVGEPINceawewlhrvvgDSRCTLvdt 441
Cdd:PRK08043 439 PSPLHY-RIVPELVYDRnctvLFGTST---FLGNYA-RFANPYDFARLRYVVAGAEKLQ------------ESTKQL--- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 442 wWQTETG-------GI--C---------IAPRPSEEGaEILPGMAMRpffgIVPVLMDEKGSVVE--GSNV-SGALCISQ 500
Cdd:PRK08043 499 -WQDKFGlrilegyGVteCapvvsinvpMAAKPGTVG-RILPGMDAR----LLSVPGIEQGGRLQlkGPNImNGYLRVEK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 501 awPGMARTIYGDhqrfvDAYFKAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAV 579
Cdd:PRK08043 573 --PGVLEVPTAE-----NARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATA 645
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 580 IgYPHDIKGEAAFAFivVKDSAGDSDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 656
Cdd:PRK08043 646 I-KSDASKGEALVLF--TTDSELTREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
140-330 |
1.76e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.90 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFN 219
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 QglrggrvmELKKIVDEAvKHCPTVQHVLVAHRTDNKVHMGDLD--------IPLEQEMAKEDPVcAPESMGSEDVLFML 291
Cdd:PLN02387 187 K--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGssnwtvssFSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622839330 292 YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHRPGDIF 330
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
133-653 |
3.15e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.01 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 133 EPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIY--MPV--SPLAVAAMLACARIGAVHT----VIFAGFSAASLA 204
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVWAEDTLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 205 gRINDAKCKVVITfnqglrGGRVMELKKIVDEAvkhcpTVQHVLVAhrtdnkvhmgdldipleqEMAKEDPVcAPESMGS 284
Cdd:PRK07768 103 -VIGMIGAKAVVV------GEPFLAAAPVLEEK-----GIRVLTVA------------------DLLAADPI-DPVETGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 EDVLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVFDHRPGDIFG---CVADIGWItGHSYVvygPLCNGATSVL 358
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGN--LYAnaeAMFVAAEFDVETDVMVSwlpLFHDMGMV-GFLTV---PMYFGAELVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 359 feSTPV-YPNAGRYWETVerlkINQFYGAPTA---------VRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:PRK07768 226 --VTPMdFLRDPLLWAEL----ISKYRGTMTAapnfayallARRLRRQAKP--GAFDLSSLRFALNGAEPIDPADVEDLL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 429 RV---VGDSRCTLVDTWWQTETG-GICIAPR---------------------PSEEGA--------EILPGMAMRpffgi 475
Cdd:PRK07768 298 DAgarFGLRPEAILPAYGMAEATlAVSFSPCgaglvvdevdadllaalrravPATKGNtrrlatlgPPLPGLEVR----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 476 vpvLMDEKGSV----------VEGSNVSgalcisqawPGMaRTIYGdHQRFVDAYfkaypGYYFTGDGAHRTEGGYYQIT 545
Cdd:PRK07768 373 ---VVDEDGQVlpprgvgvieLRGESVT---------PGY-LTMDG-FIPAQDAD-----GWLDTGDLGYLTEEGEVVVC 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 546 GRMDDVINISGHRLGTAEIEDAIADHPAV-PESAV-IGYPHDIKGEaAFAfIVVKDSAGDSDVVVQELKSMVATKIAKyA 623
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE-GFA-VAVESNAFEDPAEVRRIRHQVAHEVVA-E 510
|
570 580 590
....*....|....*....|....*....|....*
gi 1622839330 624 V---PDEILVVK--RLPKTRSGKVMRRLLRKIITS 653
Cdd:PRK07768 511 VgvrPRNVVVLGpgSIPKTPSGKLRRANAAELVTP 545
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
140-581 |
1.19e-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: 58.20 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITFN 219
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 QglrgGRVMELKKIVDEAvkhcPTVQHVLVA-------HRTDNKVHMGDLdIPLEQEMAKEDPVCAPESMGS---EDVLF 289
Cdd:cd17641 92 E----EQVDKLLEIADRI----PSVRYVIYCdprgmrkYDDPRLISFEDV-VALGRALDRRDPGLYEREVAAgkgEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 290 MLYTSGSTGMPKGIVhTQAGYLLYAALTHKLVFDHRPGDIFGCVADIGWITGHSYVVYGPLCNG--------ATSVLFES 361
Cdd:cd17641 163 LCTTSGTTGKPKLAM-LSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeePETMMEDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 362 TPVYPN----AGRYWETV---------ERLKINQFY-----------------GAPTAVRLLLKYG--DAWVKK--YDR- 406
Cdd:cd17641 242 REIGPTfvllPPRVWEGIaadvrarmmDATPFKRFMfelgmklglraldrgkrGRPVSLWLRLASWlaDALLFRplRDRl 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 407 --SSLRTLGSVGEPINCEAWEWLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPGMAMRPFFGiVPVLMDEKG 484
Cdd:cd17641 322 gfSRLRSAATGGAALGPDTFRFFHAIGVP----LKQLYGQTELAGAYTVHR----DGDVDPDTVGVPFPG-TEVRIDEVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 485 SVVEGSnvsgalcisqawPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAHRTEGGYYQITGRMDDVINIS-GHRLGTAE 563
Cdd:cd17641 393 EILVRS------------PGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQF 458
|
490
....*....|....*...
gi 1622839330 564 IEDAIADHPAVPESAVIG 581
Cdd:cd17641 459 IENKLKFSPYIAEAVVLG 476
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
528-642 |
2.33e-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: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 528 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDiKGEAAFA 593
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENvtlvrrdkdeepTLVSYivPQD-KSDELEE 758
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 594 FIVVKDSAGDSDVVVQ----------ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 642
Cdd:TIGR03443 759 FKSEVDDEESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
113-307 |
4.18e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.43 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 113 CLDQHVQKSPESVALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSP----LAVAAMLACARIG 188
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 189 AVHtvifagfSAASLAGRiNDAKCKVVItfnQGLRGGRVmelkkIVDEAVKHCPTVQHVLVAHR---TDNKVHMGDLDIP 265
Cdd:PRK08180 123 PVS-------PAYSLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAATP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622839330 266 LEQEMAKEDPVCAPESM---GSEDVLFMLYTSGSTGMPKGIVHTQ 307
Cdd:PRK08180 187 FAALLATPPTAAVDAAHaavGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
114-647 |
5.03e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 56.06 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGavHTV 193
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYL------GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 194 IFAGFSAAslAGRIND----AKCKVVITfnqglrggrVMELkkivDEAVKHCPTVQhvlvahrTDNkvhmgdldipLEQE 269
Cdd:PRK04813 80 IPVDVSSP--AERIEMiievAKPSLIIA---------TEEL----PLEILGIPVIT-------LDE----------LKDI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 270 MAKEDPVCAPESMGSEDVLFMLYTSGSTGMPKGiVHTQAGYLLyaALTHKLVFDhrpgdiFGCVADIGWITGHSY----- 344
Cdd:PRK04813 128 FATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKG-VQISHDNLV--SFTNWMLED------FALPEGPQFLNQAPYsfdls 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 345 --VVYGPLCNGATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVR--LLLKYGDAwvKKYdrSSLRTLGSVGEPIN 420
Cdd:PRK04813 199 vmDLYPTLASGGTLVALPKD-MTANFKQLFETLPQLPINVWVSTPSFADmcLLDPSFNE--EHL--PNLTHFLFCGEELP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 421 CEAWEWLHRVVGDSRctLVDTWWQTETggiCIAPRPSEEGAEI------LP-GMAmRPFFGIVpvLMDEKGSVVEGSNvS 493
Cdd:PRK04813 274 HKTAKKLLERFPSAT--IYNTYGPTEA---TVAVTSIEITDEMldqykrLPiGYA-KPDSPLL--IIDEEGTKLPDGE-Q 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 494 GALCISQawPGMARTIYGDHQRfVDAYFKAYPGY--YFTGDgAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 571
Cdd:PRK04813 345 GEIVISG--PSVSKGYLNNPEK-TAEAFFTFDGQpaYHTGD-AGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839330 572 PAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDV-VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 647
Cdd:PRK04813 421 SYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
286-642 |
3.88e-07 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 52.69 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 286 DVLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHklvfdhrpgdifgcvADIGWITGHS-YVVYGPLCNGATsvLFESTPV 364
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA-LLAQALVL---------------AVLQAIDEGTvFLNSGPLFHIGT--LMFTLAT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 365 YPNAGR-----------YWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSvgepinceAWEWLHRVVGD 433
Cdd:cd17636 63 FHAGGTnvfvrrvdaeeVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSSPA--------APEWNDMATVD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 srctlvDTWW--------QTETGG-----------ICIAPRPSeegaeilPGMAMRpffgivpvLMDEKGSVVEGSNVsG 494
Cdd:cd17636 133 ------TSPWgrkpggygQTEVMGlatfaalgggaIGGAGRPS-------PLVQVR--------ILDEDGREVPDGEV-G 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 495 ALCIsQAWPGMARtiYGDH-----QRFVDayfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 569
Cdd:cd17636 191 EIVA-RGPTVMAG--YWNRpevnaRRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLR 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839330 570 DHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 642
Cdd:cd17636 261 QHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS---VTEAELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
530-658 |
9.21e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 52.11 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 530 TGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD---------- 599
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiwsdneke 497
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839330 600 SAGDSDVVVQE-LKSMVATK-IAKYAVPDEILV-VKRLPKTRSGKVMRRLLRKIITSEAQEL 658
Cdd:PLN02860 498 NAKKNLTLSSEtLRHHCREKnLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRREVLSHLQSL 559
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
119-311 |
1.13e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 51.41 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 119 QKSPESVALIwERDEpgtevRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVhtVIFagf 198
Cdd:PRK09029 14 QVRPQAIALR-LNDE-----VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR--VLP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 199 saaslagrINDAKCkvvitfnqglrggrVMELKKIVDEAvkhcpTVQHVLVAHRTDNkvhMGDLDIPLEQEMAKEDPVC- 277
Cdd:PRK09029 83 --------LNPQLP--------------QPLLEELLPSL-----TLDFALVLEGENT---FSALTSLHLQLVEGAHAVAw 132
|
170 180 190
....*....|....*....|....*....|....
gi 1622839330 278 APESMGSedvlfMLYTSGSTGMPKGIVHTQAGYL 311
Cdd:PRK09029 133 QPQRLAT-----MTLTSGSTGLPKAAVHTAQAHL 161
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
140-306 |
1.84e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 51.06 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 140 ITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVITfn 219
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 220 qglrggrvmelkkivdeavkhcptvqhvlvahrtDNKvhmgdldipleqemakedpvcapesmgSEDVLFMLYTSGSTGM 299
Cdd:cd17639 84 ----------------------------------DGK---------------------------PDDLACIMYTSGSTGN 102
|
....*..
gi 1622839330 300 PKGIVHT 306
Cdd:cd17639 103 PKGVMLT 109
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-581 |
2.08e-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: 50.92 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKCKVVItf 218
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 219 nqglrggrvmelkkivdeavkhcptvqhvlvahrtdnkvhmgdlDIPLeqemakedpvcapesmgSEDVLFMLYTSGSTG 298
Cdd:cd05910 80 --------------------------------------------GIPK-----------------ADEPAAILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 299 MPKGIVHTQAgylLYAALTHKL--VFDHRPGDI----FGCVAdigwitghsyvVYGPLCnGATSVLFESTPVYP---NAG 369
Cdd:cd05910 99 TPKGVVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 370 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD---------------- 433
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSDeaeiltpygatealpv 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 434 ----SRCTLVDTWWQTETG-GICIAPRPSEEGAEILPGMA--MRPFFGIVPVLMDEKGSV-VEGSNVSGALCISQAWPGM 505
Cdd:cd05910 242 ssigSRELLATTTAATSGGaGTCVGRPIPGVRVRIIEIDDepIAEWDDTLELPRGEIGEItVTGPTVTPTYVNRPVATAL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 506 ARTIYGDHQ---RFVD-AYFKAYPGYYFTGDGAHRTEGgyyqitgrmddviniSGHRLGTAEIEDAIADHPAVPESAVIG 581
Cdd:cd05910 322 AKIDDNSEGfwhRMGDlGYLDDEGRLWFCGRKAHRVIT---------------TGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
526-658 |
3.02e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 50.69 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 526 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIadHPAVPES----AVIGYPHDIKGEAafafIVV--KD 599
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEK----LVVlhTC 1092
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839330 600 SAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitseAQEL 658
Cdd:PRK08633 1093 GAEDVEELKRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL----ALAL 1144
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
135-387 |
3.08e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 50.61 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 135 GTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAkcKV 214
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA--EV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 215 VITFNQglrGGRVMELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDIPLEQEMAKEDPVCAP----ESMGS------ 284
Cdd:PLN02861 151 SIAFVQ---ESKISSILSCLPKCSSNLKTI------------VSFGDVSSEQKEEAEELGVSCFSweefSLMGSldcelp 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 285 ----EDVLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFdhrpgdifgcVADIGWITGHSYVVYGPLCNGATSVLfE 360
Cdd:PLN02861 216 pkqkTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLAHVYDQVI-E 284
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622839330 361 STPVYPNAG-RYW--------ETVERLKINQFYGAP 387
Cdd:PLN02861 285 TYCISKGASiGFWqgdirylmEDVQALKPTIFCGVP 320
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
133-304 |
1.44e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 48.48 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 133 EPGTEVRITYRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAASLAGRINDAKC 212
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 213 KVVITFNQglrggRVMELKKIVDEAVKHCPTVQHV---------------LVAHRTDNKVHMGD---LDIPLEQEmaked 274
Cdd:PLN02614 153 SIVFVEEK-----KISELFKTCPNSTEYMKTVVSFggvsreqkeeaetfgLVIYAWDEFLKLGEgkqYDLPIKKK----- 222
|
170 180 190
....*....|....*....|....*....|
gi 1622839330 275 pvcapesmgsEDVLFMLYTSGSTGMPKGIV 304
Cdd:PLN02614 223 ----------SDICTIMYTSGTTGDPKGVM 242
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
139-657 |
6.20e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 139 RITYRELLETTCRLANTLKrHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHTVIfaGFSA--ASLAGRINDAKCKVVI 216
Cdd:PRK06814 658 PLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSAgiANILSACKAAQVKTVL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 217 TFNQGLRGGRvmeLKKIVDEavkhcpTVQHVLVAHRTDNKVHMGDLDiPLEQEMAKEDPVCAPESMGSEDVLFMLYTSGS 296
Cdd:PRK06814 735 TSRAFIEKAR---LGPLIEA------LEFGIRIIYLEDVRAQIGLAD-KIKGLLAGRFPLVYFCNRDPDDPAVILFTSGS 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 297 TGMPKGIVHTQAGYLLYAALTHKLVfDHRPGDIFGCVADIGwitgHSYVVYG----PLCNGATSVLfestpvYPNAGRYW 372
Cdd:PRK06814 805 EGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPVF----HSFGLTGglvlPLLSGVKVFL------YPSPLHYR 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 373 ---ETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINCEAWE-WLHRVvgdsRCTLVDTWWQTETG 448
Cdd:PRK06814 874 iipELIYDTNATILFGTDTFLNGYARYAHP----YDFRSLRYVFAGAEKVKEETRQtWMEKF----GIRILEGYGVTETA 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 449 GI--CIAP---RPSEEGaEILPGMAMR--PFFGIvpvlmDEKGSV-VEGSNV-SGALCISQawPGMARTIYGdhqrfvda 519
Cdd:PRK06814 946 PViaLNTPmhnKAGTVG-RLLPGIEYRlePVPGI-----DEGGRLfVRGPNVmLGYLRAEN--PGVLEPPAD-------- 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 520 yfkaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAafaFIVVKD 599
Cdd:PRK06814 1010 ------GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER---IILLTT 1080
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839330 600 SAgdsDVVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKV----MRRLLRKIITSEAQE 657
Cdd:PRK06814 1081 AS---DATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEAA 1140
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
564-683 |
1.04e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 45.14 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 564 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIvvkdsAGDSDVVVQELKSMVATKIAKYAvPDEILVVKRLPKTRSGKVM 643
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622839330 644 RRLLRKIITSEAQELGD-TTTLEDPSIITEILSAYQKCKDK 683
Cdd:PRK09188 319 DDILRLIAMNQIDELDDlLREPEIRGLVEAIAAHRLNLTDR 359
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
142-328 |
2.59e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 44.23 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 142 YRELLETTCRLANTLKRHGVCRGDCVAIYMPVSPLAVAAMLACARIGAVHT-----VIFAGFSA--ASLAGRINDAKCKV 214
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 215 VITfnqglrggrVMELKKIVDEAVKHCPTVqhvlvahrtdnkvhmgdLDIPLEQEMAKEDPVCAPESMGSEDVLFMLYTS 294
Cdd:PRK09192 132 IIT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSS 185
|
170 180 190
....*....|....*....|....*....|....*
gi 1622839330 295 GSTGMPKGIVHTQ-AGYLLYAALTHKLVfDHRPGD 328
Cdd:PRK09192 186 GSTRFPRGVIITHrALMANLRAISHDGL-KVRPGD 219
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
525-646 |
4.62e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 43.22 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 525 PGYYF-TGDGAHRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAG- 602
Cdd:PRK05851 394 PDDWFpTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG-EGSARPGLVIAAEFRGp 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622839330 603 DSDVVVQELKSMVATKIAkyAVPDEILVVK--RLPKTRSGKvMRRL 646
Cdd:PRK05851 472 DEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
114-309 |
1.76e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 41.65 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 114 LDQHVQKSPESVA---LIWERDEPGTEVRITYRELLETTCRLANTLKRHgVCRGDCVAIYMPVSPLAVAAMLACARIGAV 190
Cdd:PRK12476 40 IERNIANVGDTVAyryLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 191 HTVIFA----GfSAASLAGRINDAKCKVVITfnqglrggrvmelkkivDEAVKhcPTVQHVLVAHRTDNKVHMGDLD-IP 265
Cdd:PRK12476 119 AVPLFApelpG-HAERLDTALRDAEPTVVLT-----------------TTAAA--EAVEGFLRNLPRLRRPRVIAIDaIP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622839330 266 leqEMAKEDPVCAPesMGSEDVLFMLYTSGSTGMPKG--IVHTQAG 309
Cdd:PRK12476 179 ---DSAGESFVPVE--LDTDDVSHLQYTSGSTRPPVGveITHRAVG 219
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
278-534 |
3.03e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 40.80 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 278 APESMGSEDVLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHRPGDIFGCVAD-IGW--ITGHSYVVYGPLCNGA 354
Cdd:PRK12582 213 AIAAITPDTVAKYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPDPPPPVSLDwMPWnhTMGGNANFNGLLWGGG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 355 TSVLFESTPVypnAGRYWETVERLK-INQ--FYGAPTAVRLL---LKYGDAWVKKYdRSSLRTLGSVGEPINCEAWEWLH 428
Cdd:PRK12582 292 TLYIDDGKPL---PGMFEETIRNLReISPtvYGNVPAGYAMLaeaMEKDDALRRSF-FKNLRLMAYGGATLSDDLYERMQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839330 429 ----RVVGdSRCTLVDTWWQTETGGI-CIAPRPSEEGAEI---LPGMAMRpffgIVPVlmDEKGSV-VEGSNVSgalcis 499
Cdd:PRK12582 368 alavRTTG-HRIPFYTGYGATETAPTtTGTHWDTERVGLIglpLPGVELK----LAPV--GDKYEVrVKGPNVT------ 434
|
250 260 270
....*....|....*....|....*....|....*
gi 1622839330 500 qawPGMartiYGDHQRFVDAYFKAypGYYFTGDGA 534
Cdd:PRK12582 435 ---PGY----HKDPELTAAAFDEE--GFYRLGDAA 460
|
|
| |
