|
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 ... |
45-670 |
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: 1089.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 45 AAQPGSYPALSAQAAQEPAAFWGPLARDTLVWDTPYHTVWDCDFrTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIWE 124
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSF-PPFYKWFVGGELNVSYNCVDRHLEARPDKVAIIWE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 125 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDA 204
Cdd:TIGR02188 80 GDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 205 KCKAVITFNQGLRGGRVVELKKIVDEAVKSCP-TVQHVLVAHRTDTKV-PMG-SLDIPLEQEMAKEAPVCTPESMSSEDM 281
Cdd:TIGR02188 160 GAKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVeGRDVWWHDLMAKASAYCEPEPMDSEDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 282 LFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPD 361
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 362 AGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTET 441
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 442 GGICIAPRPSedGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISQAWPGMARTIYGDHQRFVDAYFRAYPGY 521
Cdd:TIGR02188 400 GGIMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMV 601
Cdd:TIGR02188 478 YFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDEL 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 602 VNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQDLGDTTTLEDPSVITEILSA 670
Cdd:TIGR02188 558 RKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
50-660 |
0e+00 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 1085.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 50 SYPALSAQAAQEPAAFWGPLARDtLVWDTPYHTVWDCDFRTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIWERDEPG 129
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 130 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAV 209
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 210 ITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPM-GSLDIPLEQEMAKEAPVCTPESMSSEDMLFMLYTS 288
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 289 GSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDAGRYWET 368
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 369 VQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTETGGICIAP 448
Cdd:cd05966 321 VEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 449 RPSEdgAEILPGMAMRPFFGIVPVLMDEKGNVlEGGDVSGALCISQAWPGMARTIYGDHQRFVDAYFRAYPGYYFTGDGA 528
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNE-VEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 529 HRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLS 608
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 18034773 609 VATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRgQDLGDTTTLED 660
Cdd:cd05966 558 VRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGE-EELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
44-672 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 987.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 44 AAAQPGSYPALSAQAAQEPAAFWGPLARDtLVWDTPYHTVWDCDfrTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIW 123
Cdd:PRK00174 12 ALIDMEQYKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 124 ERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRIND 203
Cdd:PRK00174 89 EGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIID 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 204 AKCKAVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPM-GSLDIPLEQEMAKEAPVCTPESMSSEDML 282
Cdd:PRK00174 169 AGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWvEGRDLWWHELVAGASDECEPEPMDAEDPL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 283 FMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDA 362
Cdd:PRK00174 249 FILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 363 GRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTETG 442
Cdd:PRK00174 329 GRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 443 GICIAPRPsedGA-EILPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQAWPGMARTIYGDHQRFVDAYFRAYPGY 521
Cdd:PRK00174 409 GIMITPLP---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEGG-EGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGM 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMV 601
Cdd:PRK00174 485 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDEL 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 602 VNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQdLGDTTTLEDPSVITEILSAFQ 672
Cdd:PRK00174 565 RKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEI-LGDTSTLADPSVVEKLIEARQ 634
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
95-667 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 833.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 95 WFLGGQLNVSVNCLDQHVQKSPETIALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAA 174
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 175 MLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMG 254
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 255 SlDIPLEQEMAKEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWIT 334
Cdd:COG0365 161 G-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 335 GHSYVVYGPLCNGATTVLFESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN 414
Cdd:COG0365 240 GHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 415 HEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPRPsedGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQ 494
Cdd:COG0365 320 PEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEE-GELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 495 AWPGMARTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVI 574
Cdd:COG0365 393 PWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 575 GYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIItsRGQDLGD 654
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA--EGRPLGD 550
|
570
....*....|...
gi 18034773 655 TTTLEDPSVITEI 667
Cdd:COG0365 551 TSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
46-669 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 677.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 46 AQPGSYPALSAQAAQEPAAFWGPLArDTLVWDTPYHTVWDC----DFRTG--KIGWFLGGQLNVSVNCLDQHVQK-SPET 118
Cdd:PLN02654 27 SSPQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCLDRNVEAgNGDK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 119 IALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLA 198
Cdd:PLN02654 106 IAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 199 GRINDAKCKAVITFNQGLRGGRVVELKKIVDEA----------VKSCPTVQHVLVAHRTDTKVPMGSlDIPLEQEMAKEA 268
Cdd:PLN02654 186 QRIVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-DVWWQDVVPNYP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 PVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGA 348
Cdd:PLN02654 265 TKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TTVLFESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDG 428
Cdd:PLN02654 345 TVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 429 RCTLVDTWWQTETGGICIAPRPsedGAEIL-PGMAMRPFFGIVPVLMDEKGNVLEgGDVSGALCISQAWPGMARTIYGDH 507
Cdd:PLN02654 425 RCPISDTWWQTETGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIE-GECSGYLCVKKSWPGAFRTLYGDH 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 508 QRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFA 587
Cdd:PLN02654 501 ERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYA 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 588 FIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQDLGDTTTLEDPSVITEI 667
Cdd:PLN02654 581 FVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQL 660
|
..
gi 18034773 668 LS 669
Cdd:PLN02654 661 IA 662
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
57-637 |
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: 650.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 57 QAAQEPAAFWGPLARDtLVWDTPYHTVWDCDFRTGK--IGWFLGGQLNVSVNCLDQHVQKSPETIALIWERDEpGTEVR- 133
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFN 213
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 QGLRGGRVVELKKIVDEAVK-SCPTVQHVLVAHRTDTKVP-MGSLDIPLEQEMAKEAPVCTPESMSSEDMLFMLYTSGST 291
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 292 GTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDAGRYWETVQR 371
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 372 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTETGGICIAPRPs 451
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLP- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 452 edGAEIL-PGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAWPGMARTIYGDHQRFVDAYFRAYPGYYFTGDGAHR 530
Cdd:cd17634 404 --GAIELkAGSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 531 TEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVA 610
Cdd:cd17634 481 DEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
570 580
....*....|....*....|....*..
gi 18034773 611 TKIAKYAVPDQILVVKRLPKTRSGKVM 637
Cdd:cd17634 561 KEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
51-667 |
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: 584.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 51 YPALSAQAAQEPAAFWGPLARdTLVWDTPYHTVWDCDfRTGKIGWFLGGQLNVSVNCLDQHVQKS-PETIALIWERDEPG 129
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 130 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAV 209
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 210 ITFNQGLRGGRVVELKKIVDEAVK-SCPTVQHVLVAHR----TDTKVPMGSLDipLEQEMAKEAPV-CTPesMSSEDMLF 283
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALElSGHKPHHVLVLNRpqvpADLTKPGRDLD--WSELLAKAEPVdCVP--VAATDPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 284 MLYTSGSTGTPKGLVHTQAGYL--LYAAMTHklVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPV-YP 360
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAvaLNWSMRN--IYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 361 DAGRYWETVQRLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQ 438
Cdd:cd05967 313 DPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 439 TETGGICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLeGGDVSGALCISQAW-PGMARTIYGDHQRFVDAYFRA 517
Cdd:cd05967 390 TETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 518 YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS- 596
Cdd:cd05967 469 FPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKi 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 597 DENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIItsRGQDLGDTTTLEDPSVITEI 667
Cdd:cd05967 549 TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
50-670 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 531.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 50 SYPALSAQAAQEPAAFWGPLARdtLV-WDTPYHTVwdCDF-RTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIWERDE 127
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR--RIdWQTPFTQV--LDYsNPPFARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 128 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCK 207
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 208 AVITFNQGLRGGRVVELKKIVDEAVKSCP-TVQHVLVAHR---TDTKVPMGSLDIPLEQEMAKEAPVcTPESMSSEDMLF 283
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIALAQhKPRHVLLVDRglaPMARVAGRDVDYATLRAQHLGARV-PVEWLESNEPSY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 284 MLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDAG 363
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 364 RYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGG 443
Cdd:PRK10524 318 IWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VPVIDNYWQTETGW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 444 ICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISQAW-PGMARTIYGDHQRFVDAYFRAY-PGY 521
Cdd:PRK10524 395 PILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDEN-- 599
Cdd:PRK10524 475 YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADre 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034773 600 ---MVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIitSRGQDLGDTTTLEDPSVITEILSA 670
Cdd:PRK10524 555 arlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI--AEGRDPGDLTTIEDPAALQQIRQA 626
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
49-661 |
2.37e-176 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 516.27 E-value: 2.37e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 49 GSYPALSAQAAQEPAAFWGPLARDTLV-WDTPYHTVWDCDFRTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIWErDE 127
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIeWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE-GE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 128 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCK 207
Cdd:cd05968 86 DGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 208 AVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDiPLEQEMAKEAPVCTPESMSSEDMLFMLYT 287
Cdd:cd05968 166 ALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGR-DLSYDEEKETAGDGAERTESEDPLMIIYT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 288 SGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGhSYVVYGPLCNGATTVLFESTPVYPDAGRYWE 367
Cdd:cd05968 245 SGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 368 TVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTE-TGGI-- 444
Cdd:cd05968 324 MVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiSGGIlg 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 445 CIAPRP----SEDGAeiLPGMAmrpffgivPVLMDEKGNVLEggDVSGALCISQAWPGMARTIYGDHQRFVDAYFRAYPG 520
Cdd:cd05968 404 NVLIKPikpsSFNGP--VPGMK--------ADVLDESGKPAR--PEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 521 YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENM 600
Cdd:cd05968 472 VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEA 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 601 VVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITsrGQDLGDTTTLEDP 661
Cdd:cd05968 552 LAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYL--GKELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
95-660 |
7.38e-150 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 446.65 E-value: 7.38e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 95 WFLGGQLNVSVNCLDQHVqKSP--ETIALIWERdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAV 172
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 173 AAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQGLRggrvvelKKIVDEAvkscPTVQHVLVAHRTDTKVP 252
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDL----PSLKHVLLVGEDVEEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 253 mGSLDipLEQEMAKEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQaGYLLYAAMTHKLVFDYQPGDVFGCVADIGW 332
Cdd:PRK04319 182 -GTLD--FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-NAMLQHYQTGKYVLDLHEDDVYWCTADPGW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 333 ITGHSYVVYGPLCNGATTVLFESTPvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP 412
Cdd:PRK04319 258 VTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 INHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPRPSEDgaeILPGMAMRPFFGIVPVLMDEKGNVLEGgDVSGALCI 492
Cdd:PRK04319 335 LNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAMD---IKPGSMGKPLPGIEAAIVDDQGNELPP-NRMGNLAI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 SQAWPGMARTIYGDHQRFvDAYFRayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETA 572
Cdd:PRK04319 408 KKGWPSMMRGIWNNPEKY-ESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 573 VIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRkiitSR--GQ 650
Cdd:PRK04319 485 VIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK----AWelGL 560
|
570
....*....|
gi 18034773 651 DLGDTTTLED 660
Cdd:PRK04319 561 PEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
135-644 |
3.06e-130 |
|
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: 391.87 E-value: 3.06e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfnq 214
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 215 glrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldiplEQEMAkeapvctpESMSSEDMLFMLYTSGSTGTP 294
Cdd:cd05969 79 ----------------------------------------------TEELY--------ERTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 295 KGLVHTQAGYLLYAaMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPvypDAGRYWETVQRLKI 374
Cdd:cd05969 105 KGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 375 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPRPSEDg 454
Cdd:cd05969 181 TVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPCMP- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 455 aeILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAWPGMARTIYGDHQRFvDAYFRAypGYYFTGDGAHRTEGG 534
Cdd:cd05969 257 --IKPGSMGKPLPGVKAAVVDENGNELPPGTK-GILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 535 YYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIA 614
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLG 410
|
490 500 510
....*....|....*....|....*....|
gi 18034773 615 KYAVPDQILVVKRLPKTRSGKVMRRLLRKI 644
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
135-643 |
6.69e-112 |
|
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: 343.94 E-value: 6.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfnq 214
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 215 glrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmSSEDMLFMLYTSGSTGTP 294
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 295 KGLVHTqAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVypDAGRYWETVQRLKI 374
Cdd:cd05972 97 KGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 375 NQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGgICIAPRPsedG 454
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP---D 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 455 AEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAWPGMARTiYGDHQRFVDAYFRAypGYYFTGDGAHRTEGG 534
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE-GDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 535 YYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIA 614
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
gi 18034773 615 KYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-549 |
5.75e-105 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 325.81 E-value: 5.75e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFnqglrggrVVELKKIVDEAVKSCPTVQHVLVAHRTdtkvPMGSLDIPLEQEMAKE 267
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITD--------DALKLEELLEALGKLEVVKLVLVLDRD----PVLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQaGYLLYAAMTHKLV----FDYQPGDVFGCVADIGWITGHSYVVYGP 343
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLFESTPVyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLHK 423
Cdd:pfam00501 223 LLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 VVGdgrCTLVDTWWQTETGGICIAPRPsEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISQawPGMARTI 503
Cdd:pfam00501 300 LFG---GALVNGYGLTETTGVVTTPLP-LDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 18034773 504 YGDHQRFVDAYFRayPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 549
Cdd:pfam00501 374 LNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
108-651 |
1.88e-99 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 312.51 E-value: 1.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemake 267
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 apvctpesmssedmlFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNG 347
Cdd:COG0318 104 ---------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 ATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGd 427
Cdd:COG0318 168 ATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 428 grCTLVDTWWQTETGGICIAPRpsEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawPGMARTIYGDH 507
Cdd:COG0318 241 --VRIVEGYGLTETSPVVTVNP--EDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEV-GEIVVRG--PNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 508 QRFVDAyFRayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFA 587
Cdd:COG0318 314 EATAEA-FR--DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVA 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034773 588 FIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQD 651
Cdd:COG0318 391 FVVLRP---GAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
49-661 |
4.57e-85 |
|
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: 280.31 E-value: 4.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 49 GSYPALSAQAAQEPAAFWgplardTLVWD---TPYHTVWDCDFRTGKI----GWFLGGQLNVSVNCLDQHVQksPETIAL 121
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLLRHADA--DDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 122 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRI 201
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 202 NDAKCKAVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIP----LEQEMAKE-APVCTPESM 276
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 277 SSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVvyGPLCNGATTVLFEST 356
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 357 PVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDgrctlvDTW 436
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 437 WQTETGG--IC--------IAP-RPSEDGAEILpGMAMRPFfgivpvlmDEKGNVLEGgdVSGALCISQAWPGMARTIYG 505
Cdd:cd05943 399 LASISGGtdIIscfvggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 506 DH--QRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGE 583
Cdd:cd05943 468 DPdgSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDE 547
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 584 AAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIItsRGQDLGDTTTLEDP 661
Cdd:cd05943 548 RVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII--AGRPVKNAGALANP 623
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
280-637 |
2.28e-80 |
|
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: 258.75 E-value: 2.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 280 DMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMThKLVFDYQPGDVFGCVADIGWItGHSYVVYGPLCNGATTVLFEStpvy 359
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 360 PDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQT 439
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 440 ETGGICIAPRPseDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAWPGMARTIYGDHQRFVDayfraYP 519
Cdd:cd04433 150 ETGGTVATGPP--DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEI-GELVVRGPSVMKGYWNNPEATAAVD-----ED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 520 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDEN 599
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP---GAD 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 18034773 600 MVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVM 637
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
49-680 |
1.49e-79 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 266.28 E-value: 1.49e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 49 GSYPALSAQAAQEPAAFWgplardTLVWD-------TPYHTVWDcdfRTGKIG--WFLGGQLNVSVNCLDQHvqkSPETI 119
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 120 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAG 199
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 200 RINDAKCKAVITFNqGLR-GGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLD--IPLEQEMAK-EAPVCTPES 275
Cdd:PRK03584 181 RFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVF----GCvadiGWITgHSYVVYGPLCnGATTV 351
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 352 LFESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDgrct 431
Cdd:PRK03584 334 LYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA---- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 432 lvDTWWQTETGG--IC---IAprpsedGAEILP-----------GMAMRPFfgivpvlmDEKGNVLEGGdvSGALCISQA 495
Cdd:PRK03584 410 --DVWLASISGGtdICscfVG------GNPLLPvyrgeiqcrglGMAVEAW--------DEDGRPVVGE--VGELVCTKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 WPGMArtIY----GDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPET 571
Cdd:PRK03584 472 FPSMP--LGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 572 AVIGYPHDIKGEAAFAFIVLKDNIS-DEnmvvnELKLSVATKIAKYA----VPDQILVVKRLPKTRSGKVMRRLLRKIIT 646
Cdd:PRK03584 550 LVIGQEWPDGDVRMPLFVVLAEGVTlDD-----ALRARIRTTIRTNLsprhVPDKIIAVPDIPRTLSGKKVELPVKKLLH 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 18034773 647 srGQDLGD---TTTLEDPsvitEILSAFQKYEEQRAA 680
Cdd:PRK03584 625 --GRPVKKavnRDALANP----EALDWFADLAELRAA 655
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
46-673 |
3.08e-77 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 259.67 E-value: 3.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 46 AQPGSYPALSAQAAQEPAAFWGPLARDTLVWDTPYHTVWDCDfrtgKI--GWFLGGQLNVSVNCLDQHVqKSPET---IA 120
Cdd:PTZ00237 5 SDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGD----EIypDWFKGGELNTCYNVLDIHV-KNPLKrdqDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 121 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGR 200
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 201 INDAKCKAVITFNQGLRGGRVVELKKIVDEAVK-SCPTVQHVLVAHRTD-------------TKVPmGSLDIPLEQEMAK 266
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIElSTFKPSNVITLFRNDitsesdlkkietiPTIP-NTLSWYDEIKKIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 E---APVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYvVYGP 343
Cdd:PTZ00237 239 EnnqSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF-LYGS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLFESTPVYPDAGR--YWETVQRLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPINHEAW 418
Cdd:PTZ00237 318 LSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 EWLHKVVGdGRCTLVdtWWQTETGG---ICIAPRPSEDGAEILPGmamrPFfgIVPVLMDEKGNVL---EGGDVSGALCI 492
Cdd:PTZ00237 398 EYIENKLK-IKSSRG--YGQTEIGItylYCYGHINIPYNATGVPS----IF--IKPSILSEDGKELnvnEIGEVAFKLPM 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 SqawPGMARTIYGDHQRFvDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETA 572
Cdd:PTZ00237 469 P---PSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 573 VIGYPHDIKGEAAFAFIVLKDNISDENMVVNELK----LSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:PTZ00237 545 SIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKneinNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDS 624
|
650 660
....*....|....*....|....*
gi 18034773 649 GQDLGDTTtlEDPSVITEILSAFQK 673
Cdd:PTZ00237 625 NYQLPDNV--NDSEIFYKIKELYMK 647
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-643 |
1.44e-71 |
|
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: 241.60 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 102 NVSVNCLDQHVQKS-----PETIALIWERDEpGTEVRITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAM 175
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGK-GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 176 LACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNqglrggrvvELKKIVDEAVKSCPTVQHVLV--AHRTDtkvpm 253
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKTKLLvsEKSRD----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 254 GSLDIpleQEMAKEAP---VCTpeSMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADI 330
Cdd:cd05928 151 GWLNF---KELLNEAStehHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 331 GWITGHSYVVYGPLCNGATtVLFESTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVG 410
Cdd:cd05928 226 GWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 411 EPINHEAWE-WLHKVVGDgrctLVDTWWQTETGGICIAPRpsedGAEILPGMAMRPFFGIVPVLMDEKGNVL---EGGDV 486
Cdd:cd05928 301 EPLNPEVLEkWKAQTGLD----IYEGYGQTETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVLppgTEGDI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 487 sgALCISQAWPGMARTIYGDHQRFVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHP 566
Cdd:cd05928 373 --GIRVKPIRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHP 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 567 AVPETAVIGYPHDIKGEAAFAFIVLKD--NISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05928 449 AVVESAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-642 |
1.07e-70 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 239.32 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 102 NVSVNCLDQHVQKSPETIALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 181
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWC-DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 182 GAIHTVVFAGFSAESLAGRINDAKCKAVITFNQGlrggrvvELKKIVDEAVKSCPTVQHVLVAHrtdTKVPMGSLDipLE 261
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECPSKPKLVWVG---DPVPEGWID--FR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 262 QEMAKEAPVCTP----ESMSSEDMLFMLYTSGSTGTPKGLVHTQAgYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHS 337
Cdd:cd05970 164 KLIKNASPDFERptanSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 338 YVVYGPLCNGATTVLFESTPVYPDAgrYWETVQRLKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINHEA 417
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 418 WEWLHKVVGdgrCTLVDTWWQTETGgICIAPRPsedGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDvSGALCI--SQA 495
Cdd:cd05970 318 FNTFKEKTG---IKLMEGFGQTETT-LTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtSKG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 WP-GMARTIYGDHQRFVDAYFrayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVI 574
Cdd:cd05970 390 KPvGLFGGYYKDAEKTAEVWH---DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 575 GYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05970 467 GVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
100-642 |
3.72e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 237.39 E-value: 3.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 100 QLNVSvNCLDQHVQKSPETIALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACA 179
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 180 RIGAI-HTV-VFagFSAESLAGRINDAKCKAVItFNQglrggrvvELKKIVDEAVKSCPTVQHVLVAHRTDTKvPMGSLD 257
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS--------EFVPLLAAILPQLPTVRTVIVEGDGPAA-PLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 258 IPLEqEMAKEAPVCTPESMSSEDMLF-MLYTSGSTGTPKGLVHTQAGYLLYAAMTHKlVFDYQPGDV-------FGCVAd 329
Cdd:PRK06187 146 GEYE-ELLAAASDTFDFPDIDENDAAaMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA-WLKLSRDDVylvivpmFHVHA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 330 IGWItghsyvvYGPLCNGATTVL---FESTPVypdagryWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL 406
Cdd:PRK06187 223 WGLP-------YLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFSSLRLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 407 GSVGEPINH---EAWEWLHKvvgdgrCTLVDTWWQTETGG-ICIAPRPSEDGAEI-LPGMAMRPFFGIVPVLMDEKGNVL 481
Cdd:PRK06187 287 IYGGAALPPallREFKEKFG------IDLVQGYGMTETSPvVSVLPPEDQLPGQWtKRRSAGRPLPGVEARIVDDDGDEL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 482 E--GGDVsGALCISQAWpgMARTIYGDHQRFVDAYfraYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIE 559
Cdd:PRK06187 361 PpdGGEV-GEIIVRGPW--LMQGYWNRPEATAETI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 560 DAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRR 639
Cdd:PRK06187 435 DALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP---GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKR 511
|
...
gi 18034773 640 LLR 642
Cdd:PRK06187 512 VLR 514
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
134-643 |
1.32e-68 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 230.87 E-value: 1.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfn 213
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggRVVELKKIvdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmsSEDMLFMLYTSGSTGT 293
Cdd:cd05973 79 ------DAANRHKL--------------------------------------------------DSDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTQAGYLLYAAMTHKLVfDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFEStPVYPDAgrYWETVQRLK 373
Cdd:cd05973 103 PKGVPVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEG-GFSVES--TWRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 374 INQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGgiCIAPRPSED 453
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELG--MVLANHHAL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 454 GAEILPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQA-WPGMArtiYGDHQRFVDAYFRAypGYYFTGDGAHRTE 532
Cdd:cd05973 253 EHPVHAGSAGRAMPGWRVAVLDDDGDELGPG-EPGRLAIDIAnSPLMW---FRGYQLPDTPAIDG--GYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 533 GGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATK 612
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKR 406
|
490 500 510
....*....|....*....|....*....|.
gi 18034773 613 IAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
133-642 |
2.15e-64 |
|
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: 221.47 E-value: 2.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVitf 212
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrVVE---LKKIVDEAVKSCPTVQHVLVA--HRTDTKVPMgsldipLEQEMAKEAPVCTPESMSSEDMLFMLYT 287
Cdd:cd05959 106 --------VVSgelAPVLAAALTKSEHTLVVLIVSggAGPEAGALL------LAELVAAEAEQLKPAATHADDPAFWLYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 288 SGSTGTPKGLVHTQAGyLLYAAMTH-KLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFestPVYPDAGRYW 366
Cdd:cd05959 172 SGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 367 ETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICI 446
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 447 APRPSEdgaeILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawPGMArTIYGdHQRfvDAYFRAYPGYYF-TG 525
Cdd:cd05959 323 SNRPGR----VRYGTTGKPVPGYEVELRDEDGGDVADGEP-GELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTrTG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 526 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNEL 605
Cdd:cd05959 392 DKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEEL 471
|
490 500 510
....*....|....*....|....*....|....*..
gi 18034773 606 KLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05959 472 KEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
130-637 |
2.62e-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: 220.93 E-value: 2.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 130 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAV 209
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 210 ITFNQGLrggrvvelkKIVDEAVKSCPTVQHV-LVAHRTDTKVPMGSLDIPLEQEMAKEAPVCTPEsmSSEDMLFMLYTS 288
Cdd:cd05911 87 FTDPDGL---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 289 GSTGTPKGLVHTQAGYLLYAAMTHKLVFD-YQPGDVFGCVADIGWITGHSYVVYGPLCnGATTVLFEStpvyPDAGRYWE 367
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK----FDSELFLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 368 TVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVgdGRCTLVDTWWQTETGGICIA 447
Cdd:cd05911 231 LIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGYGMTETGGILTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 448 PRPSEDGAE----ILPGMAMRpffgivpvLMDEKGNVLEGGDVSGALCIS--QAWPG-------MARTIYGDhqrfvday 514
Cdd:cd05911 307 NPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyynnpeaTKETFDED-------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 515 fraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDN 594
Cdd:cd05911 371 -----GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 18034773 595 isdENMVVNELKLSVATKIAKY-AVPDQILVVKRLPKTRSGKVM 637
Cdd:cd05911 446 ---EKLTEKEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
129-642 |
5.08e-64 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 218.84 E-value: 5.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 129 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKA 208
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 VITfnqglrggrvvelkkivDEavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmsSEDMLFMLYTS 288
Cdd:cd05971 82 LVT-----------------DG-----------------------------------------------SDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 289 GSTGTPKGLVHTQA---GYLLYAAMTHKLVfdYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVypDAGRY 365
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF--DPKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 366 WETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDgrcTLVDTWWQTETG--- 442
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTECNlvi 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 443 GICIAPRPSEDGAeilpgMAmRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAWPGMARTiYGDHQRFVDAYFRAypGYY 522
Cdd:cd05971 249 GNCSALFPIKPGS-----MG-KPIPGHRVAIVDDNGTPLPPGEV-GEIAVELPDPVAFLG-YWNNPSATEKKMAG--DWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 523 FTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVV 602
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 18034773 603 NELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05971 399 REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
108-638 |
1.48e-62 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 214.78 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVItfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemake 267
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 apvctpesmssEDMLFMLYTSGSTGTPKGLVHTQaGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNG 347
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 ATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinheAWEWLHKVVGD 427
Cdd:cd17631 166 GTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 428 GRCTLVDTWWQTETG-GICIAPRpseDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawPGMARTIYGD 506
Cdd:cd17631 236 RGVKFVQGYGMTETSpGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEV-GEIVVRG--PHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 HQR----FVDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKG 582
Cdd:cd17631 310 PEAtaaaFRDGWFH-------TGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWG 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 583 EAAFAFIVLKDNIS-DENMVVNELKlsvaTKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:cd17631 383 EAVVAVVVPRPGAElDEDELIAHCR----ERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
49-678 |
1.23e-61 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 217.44 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 49 GSYPALSAQAAQEPAAFWGPLARDT-LVWDTPYHTVWDCDFRTGKIgWFLGGQLNVSVNCLdQHVQKSPetiALIWeRDE 127
Cdd:TIGR01217 35 GGYDALHRWSVDELDTFWKAVWEWFdVRFSTPCARVVDDRTMPGAQ-WFPGARLNYAENLL-RAAGTEP---ALLY-VDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 128 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCK 207
Cdd:TIGR01217 109 THEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 208 AVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVahrtdtkvpmgsldIPLEQEMAKEAPVcTPESMSSEDM------ 281
Cdd:TIGR01217 189 LLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVH--------------IPYLGPRETEAPK-IDGALDLEDFtaaaqa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 282 -------------LFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITgHSYVVYGpLCNGA 348
Cdd:TIGR01217 254 aelvfeqlpfdhpLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM-WNWLVSG-LATGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TTVLFESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHkvvgdg 428
Cdd:TIGR01217 332 TLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY------ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 429 RCTLVDTWWQTETGG--ICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGdvSGALCISQAWPGMARTIYGD 506
Cdd:TIGR01217 406 DEIKADVWLASISGGtdICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGE--VGELVCTNPMPSMPIRFWND 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 HQ--RFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEA 584
Cdd:TIGR01217 484 PDgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYR 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 585 AFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRgqdlgdttTLEDPSVI 664
Cdd:TIGR01217 564 VVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGT--------PVDNPGAI 635
|
650
....*....|....*.
gi 18034773 665 T--EILSAFQKYEEQR 678
Cdd:TIGR01217 636 DnpELLDLYEELAELR 651
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
134-642 |
5.83e-60 |
|
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: 207.70 E-value: 5.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfn 213
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmSSEDMLFMLYTSGSTGT 293
Cdd:cd05919 89 ---------------------------------------------------------------SADDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADI--GWITGHSyvVYGPLCNGATTVLFestPVYPDAGRYWETVQR 371
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 372 LKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPRPS 451
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 452 EdgaeILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCI--SQAWPGMARTIYGDHQRFVDayfraypGYYFTGDGAH 529
Cdd:cd05919 256 A----WRLGSTGRPVPGYEIRLVDEEGHTIPPGEE-GDLLVrgPSAAVGYWNNPEKSRATFNG-------GWYRTGDKFC 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 530 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSV 609
Cdd:cd05919 324 RDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHL 403
|
490 500 510
....*....|....*....|....*....|...
gi 18034773 610 ATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05919 404 LERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
116-641 |
8.22e-60 |
|
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: 207.38 E-value: 8.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpes 275
Cdd:cd05930 75 RLAYILEDSGAKLVLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 mSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAmTHKLVFDYQPGDVFGCVADIGWItGHSYVVYGPLCNGATTVLFES 355
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL-WMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 356 TPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINHEAWEWLHKVVGdgRCTLVDT 435
Cdd:cd05930 168 EVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELLP--GARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 436 WWQTETGGICIA---PRPSEDGAEILPGmamRPFFGIVPVLMDEKGNVLEGGdVSGALCISQAwpGMARTIYGDH----Q 508
Cdd:cd05930 241 YGPTEATVDATYyrvPPDDEEDGRVPIG---RPIPNTRVYVLDENLRPVPPG-VPGELYIGGA--GLARGYLNRPeltaE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 509 RFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAF 588
Cdd:cd05930 315 RFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAY 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 18034773 589 IVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05930 395 VVPDE---GGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
108-642 |
9.97e-56 |
|
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: 197.02 E-value: 9.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIhtV 187
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAG--FSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgslDIPLEQEMA 265
Cdd:cd05936 77 VPLNplYTPRELEHILNDSGAKALIV---------------------------------------------AVSFTDLLA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 266 KEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGylLYAAMT---HKLVFDYQPGDVFGCVADIGWITGHSYVVYG 342
Cdd:cd05936 112 AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN--LVANALqikAWLEDLLEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEAWEWLH 422
Cdd:cd05936 190 PLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 423 KVVGdgrCTLVDTWWQTETGGIcIAPRPSEDgaEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCIS--QAWPGma 500
Cdd:cd05936 264 ELTG---VPIVEGYGLTETSPV-VAVNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEV-GELWVRgpQVMKG-- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 501 rtiYGDH-----QRFVDayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIG 575
Cdd:cd05936 335 ---YWNRpeetaEAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 576 YPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05936 405 VPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
50-650 |
4.42e-54 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 197.99 E-value: 4.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 50 SYPALSAQAAQEPAAFWgplardTLVWDT---PYHT----VWDCDFRTGKIG-WFLGGQLNVSVNCLDQHVQKSPETIAL 121
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW------SIVLDElslVFSVpprcILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 122 IWeRDEPGTEV---RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLA 198
Cdd:PLN03052 195 IW-RDEGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 199 GRINDAKCKAVITFNQGLRGGRVVELKKIVDEAvkSCPTVQhVLVAHRTDTKVPMGSLDIPLEQEMAKEAPVCTPES--- 275
Cdd:PLN03052 274 TRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEyka 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 --MSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMT--HklvFDYQPGDVFGCVADIGWITGHsYVVYGPLCNGATTV 351
Cdd:PLN03052 351 veQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLA 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 352 LFESTPVYPDAGRYwetVQRLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINHEAWEWL----- 421
Cdd:PLN03052 427 LYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWLmsrag 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 422 HKVVgdgrctlVDTWWQTETGGICIAP---RPSEDGAEILPGMAMRPFfgivpvLMDEKGNVLEgGDVSG----ALCisq 494
Cdd:PLN03052 497 YKPI-------IEYCGGTELGGGFVTGsllQPQAFAAFSTPAMGCKLF------ILDDSGNPYP-DDAPCtgelALF--- 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 495 awPGM----ARTIYGDHQrfvDAYFRAYPGYYFT-----GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAM-AD 564
Cdd:PLN03052 560 --PLMfgasSTLLNADHY---KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAA 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 565 HPAVPETAVIGYPHDIKG-EAAFAFIVLKDNiSDENMVVNELKLSVATKIAKYAVP----DQILVVKRLPKTRSGKVMRR 639
Cdd:PLN03052 635 DESVLETAAIGVPPPGGGpEQLVIAAVLKDP-PGSNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRR 713
|
650
....*....|.
gi 18034773 640 LLRKIITSRGQ 650
Cdd:PLN03052 714 VLRQQLAQELS 724
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
122-643 |
5.59e-54 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 193.62 E-value: 5.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 122 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAI-HTVVFAgFSAESLAGR 200
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTINPR-LFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 201 INDAKCKAVITFNqglrggrvvELKKIVDEAVKSCPTVQHVLV-AHRTDTKVPMGSLDIPLEQEMAKEAPVCTPESMSSE 279
Cdd:cd12119 93 INHAEDRVVFVDR---------DFLPLLEAIAPRLPTVEHVVVmTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 280 DMLFMLYTSGSTGTPKGLVHTQAGYLLYA-AMTHKLVFDYQPGDVFGCVADI----GWITGHSyvvyGPLCnGATTVLfe 354
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWGLPYA----AAMV-GAKLVL-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 355 sTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINHEAWEWLHkvvgdgrct 431
Cdd:cd12119 237 -PGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 432 lVDT---WWQTETG--GICIAPRPSEDGAEILPGMAMR-----PFFGIVPVLMDEKGNVLE-GGDVSGALCISQAWpgMA 500
Cdd:cd12119 305 -VRVihaWGMTETSplGTVARPPSEHSNLSEDEQLALRakqgrPVPGVELRIVDDDGRELPwDGKAVGELQVRGPW--VT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 501 RTIYGDHQR----FVDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGY 576
Cdd:cd12119 382 KSYYKNDEEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGV 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 577 PHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd12119 455 PHPKWGERPLAVVVLKE---GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
108-646 |
3.43e-52 |
|
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: 188.82 E-value: 3.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIhtV 187
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFS---AEsLAGRINDAKCKAVITfnqgLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDtkvPMGSLDIPLEQEM 264
Cdd:COG1021 103 VFALPAhrrAE-ISHFAEQSEAVAYII----PDRHRGFDYRALARELQAEVPSLRHVLVVGDAG---EFTSLDALLAAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 265 AKEAPVCTPesmssEDMLFMLYTSGSTGTPKGLVHTQAGYlLYAAMTHKLVFDYQPGDVFGCVADIgwitGHSY-----V 339
Cdd:COG1021 175 DLSEPRPDP-----DDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPA----AHNFplsspG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 340 VYGPLCNGATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWE 419
Cdd:COG1021 245 VLGVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 420 WLHKVVGdgrCTLV-----------------DTWWQTETGGiciapRPSEDGAEILpgmamrpffgIVpvlmDEKGNVLE 482
Cdd:COG1021 319 RVRPALG---CTLQqvfgmaeglvnytrlddPEEVILTTQG-----RPISPDDEVR----------IV----DEDGNPVP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 483 GGDVsGALcisqawpgMAR---TIYGdhqrfvdaYFRAyP----------GYYFTGDGAHRTEGGYYQITGRMDDVINIS 549
Cdd:COG1021 377 PGEV-GEL--------LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 550 GHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKdnisDENMVVNELKLSVATK-IAKYAVPDQILVVKRL 628
Cdd:COG1021 439 GEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR----GEPLTLAELRRFLRERgLAAFKLPDRLEFVDAL 514
|
570
....*....|....*...
gi 18034773 629 PKTRSGKVMRRLLRKIIT 646
Cdd:COG1021 515 PLTAVGKIDKKALRAALA 532
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
108-643 |
6.13e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 182.03 E-value: 6.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK07656 11 LARAARRFGDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFNQGLrggrvvelkKIVDEAVKSCPTVQHVlVAHRTDTKVPMGSLDIPLEQEMAKE 267
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFL---------GVDYSATTRLPALEHV-VICETEEDDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPESMSSEDMLFMLYTSGSTGTPKG--LVHTQAgYLLYAAMTHKLvfDYQPGD----------VFGCVAdiGWITg 335
Cdd:PRK07656 155 DPAERAPEVDPDDVADILFTSGTTGRPKGamLTHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 336 hsyvvygPLCNGATTVLfesTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINH 415
Cdd:PRK07656 229 -------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASMPV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 416 EAWEWLHKVVGdgrCTLVDTWWQ-TETGGI-CIAPRpsEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCIS 493
Cdd:PRK07656 296 ALLERFESELG---VDIVLTGYGlSEASGVtTFNRL--DDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEV-GELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 494 -----QAWPGM----ARTIYGDhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMAD 564
Cdd:PRK07656 370 gpnvmKGYYDDpeatAAAIDAD-------------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 565 HPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS-DENMVVNELKlsvaTKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:PRK07656 437 HPAVAEAAVIGVPDERLGEVGKAYVVLKPGAElTEEELIAYCR----EHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
131-642 |
6.40e-50 |
|
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: 180.37 E-value: 6.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHR-GDRVAIYMPVSPLAVAAMLACARIGAIhtvvfagfsaeslagrindakCKAV 209
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 210 ITFnqgLRGGrvvELKKIVDEAVKScptvqHVLVAHRTDTkvpmgsldipleqemakeapvctpesmsSEDMLFMLYTSG 289
Cdd:cd05958 67 MPL---LRPK---ELAYILDKARIT-----VALCAHALTA----------------------------SDDICILAFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 290 STGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTpvypDAGRYWETV 369
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 370 QRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPR 449
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 450 PSEdgaeILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawPGMARTIYGDHQRfvdAYFRAypGYYFTGDGAH 529
Cdd:cd05958 259 PGD----ARPGATGKPVPGYEAKVVDDEGNPVPDGTI-GRLAVRG--PTGCRYLADKRQR---TYVQG--GWNITGDTYS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 530 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSV 609
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHA 406
|
490 500 510
....*....|....*....|....*....|...
gi 18034773 610 ATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05958 407 KAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
112-651 |
7.01e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 179.36 E-value: 7.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:PRK08316 21 ARRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVITfNQGLRGgrvvelkkIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIpleQEMAKEAPVC 271
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLV-DPALAP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 TPE-SMSSEDMLFMLYTSGSTGTPKGlvhtqagyllyAAMTHK-LVFDYQpgdvfGCVADIGWITG----------HS-- 337
Cdd:PRK08316 163 EPDvELADDDLAQILYTSGTESLPKG-----------AMLTHRaLIAEYV-----SCIVAGDMSADdiplhalplyHCaq 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 338 -YVVYGP-LCNGATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTlGSVG----- 410
Cdd:PRK08316 227 lDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRK-GYYGasimp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 411 EPINHEAWEWLHKVvgdgrcTLVDTWWQTEtggicIAP-----RPSEdgAEILPGMAMRPFFGIVPVLMDEKGNVLEGGD 485
Cdd:PRK08316 300 VEVLKELRERLPGL------RFYNCYGQTE-----IAPlatvlGPEE--HLRRPGSAGRPVLNVETRVVDDDGNDVAPGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 486 V------SGALCISqawpgmartIYGDHQRFVDAyFRAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIE 559
Cdd:PRK08316 367 VgeivhrSPQLMLG---------YWDDPEKTAEA-FRG--GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 560 DAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRR 639
Cdd:PRK08316 435 EALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA---GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKR 511
|
570
....*....|..
gi 18034773 640 LLRKIITSRGQD 651
Cdd:PRK08316 512 ELRERYAGAFTD 523
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
128-643 |
4.19e-47 |
|
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: 173.65 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 128 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCK 207
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 208 AVITFNQGLRggrvvelkkivdEAVKSCPTVQ--HVLVAHRTDTKVPMGSLDiPLEQEMAKEAPVCTPESMSSEDMLFML 285
Cdd:cd05926 89 LVLTPKGELG------------PASRAASKLGlaILELALDVGVLIRAPSAE-SLSNLLADKKNAKSEGVPLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 286 YTSGSTGTPKGLVHTQAGYLL---YAAMTHKLvfdyQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfestPVYPDA 362
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAAsatNITNTYKL----TPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL----PPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 363 GRYWETVQRLKINQFYGAPTAVRLLLK-YGDAWVKKYdrSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTET 441
Cdd:cd05926 228 STFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFG---APVLEAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 442 GG------ICIAPRPsedgaeilPGMAMRPFfGIVPVLMDEKGNVLEGGDVsGALCISQawPGMARTIYGDHQ-----RF 510
Cdd:cd05926 303 AHqmtsnpLPPGPRK--------PGSVGKPV-GVEVRILDEDGEILPPGVV-GEICLRG--PNVTRGYLNNPEanaeaAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 511 VDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIV 590
Cdd:cd05926 371 KDGWFR-------TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 18034773 591 LKDNISdenMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05926 444 LREGAS---VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
112-641 |
7.59e-47 |
|
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: 172.05 E-value: 7.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVITFNqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvc 271
Cdd:cd05945 75 SPAERIREILDAAKPALLIADG---------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 tpesmssEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLvFDYQPGDVFGCVADIgwitghS-----YVVYGPLCN 346
Cdd:cd05945 97 -------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 347 GATTVLFESTpVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINHEAWEWLHKVVG 426
Cdd:cd05945 163 GATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 427 DgrCTLVDTWWQTETGGICIA---PRPSEDGAEILP-GmamRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawPGMART 502
Cdd:cd05945 240 D--ARIYNTYGPTEATVAVTYievTPEVLDGYDRLPiG---YAKPGAKLVILDEDGRPVPPGEK-GELVISG--PSVSKG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 503 iYGDHQRFVDAYFRAYPGY--YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDI 580
Cdd:cd05945 312 -YLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 581 KGEAAFAFIVLKDNISDENmvVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05945 391 KVTELIAFVVPKPGAEAGL--TKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
110-642 |
3.79e-46 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 170.99 E-value: 3.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVF 189
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 190 AGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqHVLVAHRTDTKVPMGSLDIPLEQEMAKEAP 269
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLT----------------------------HPALAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 270 vcTPESMSSEDMLFMLYTSGSTGTPKGLV--HTQAGYLLYAamtHKLVFDYQPGDVFGCVADIGWITGHSYVvYGPLCNG 347
Cdd:cd17651 129 --PDPALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 ATTVLfESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEP--INHEAWEWLhkvV 425
Cdd:cd17651 203 ATLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQlvLTEDLREFC---A 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 GDGRCTLVDTWWQTETGGICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCIsqAWPGMARTIYG 505
Cdd:cd17651 277 GLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPG-VPGELYI--GGAGLARGYLN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 506 D----HQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIK 581
Cdd:cd17651 354 RpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 582 GEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd17651 434 EKRLVAYVVGDP---EAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
133-643 |
1.50e-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: 169.63 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITF 212
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 NqglrggrvvELKKIVDEAVKSCPTVQHVLVAHRTdtkvPMGSLDipLEQEMAKEAPVCTPESMSSEDMLFMLYTSGSTG 292
Cdd:TIGR02262 110 G---------ALLPVIKAALGKSPHLEHRVVVGRP----EAGEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFestPVYPDAGRYWETVQRL 372
Cdd:TIGR02262 175 MPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 373 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINHE-AWEWLHKVVGDgrctLVDTWWQTETGGICIAPRPS 451
Cdd:TIGR02262 252 QPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTEMLHIFLSNLPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 452 EdgaeILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawpGMARTIYGDHQRFVDAYFRAypGYYFTGDGAHRT 531
Cdd:TIGR02262 326 D----VRYGTSGKPVPGYRLRLVGDGGQDVADGEP-GELLISG---PSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 532 EGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYP---HDIKGEaafAFIVLKdniSDENMVVNELKLS 608
Cdd:TIGR02262 396 DDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVAdedGLIKPK---AFVVLR---PGQTALETELKEH 469
|
490 500 510
....*....|....*....|....*....|....*
gi 18034773 609 VATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:TIGR02262 470 VKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-642 |
3.35e-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: 166.70 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITf 212
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeAPVCtpesmssedmlfMLYTSGSTG 292
Cdd:cd05934 82 -------------------------------------------------------DPAS------------ILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTQAgYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTpvypDAGRYWETVQRL 372
Cdd:cd05934 95 PPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 373 KINQFYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPRPS 451
Cdd:cd05934 170 GATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 452 EDGaeilPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAWP-GMARTIYGDHqrfvDAYFRAYP-GYYFTGDGAH 529
Cdd:cd05934 242 PRR----PGSIGRPAPGYEVRIVDDDGQELPAGEP-GELVIRGLRGwGFFKGYYNMP----EATAEAMRnGWFHTGDLGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 530 RTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELKLSV 609
Cdd:cd05934 313 RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRP---GETLDPEELFAFC 389
|
490 500 510
....*....|....*....|....*....|...
gi 18034773 610 ATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05934 390 EGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
109-641 |
1.13e-44 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 166.61 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITfnQGLRGGRVVELKKIVDeavkscptvqhvlvahrtdtkvpmgsLDIPLEQEMAKEA 268
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAVV--------------------------IDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 PVCtpesMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLlyaamthKLVFD-----YQPGDVFGCVADIGWiTGHSYVVYGP 343
Cdd:cd12117 130 AVP----VSPDDLAYVMYTSGSTGRPKGVAVTHRGVV-------RLVKNtnyvtLGPDDRVLQTSPLAF-DASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLFESTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVkkydrSSLRTLGSVGEPINHEAWEWLHK 423
Cdd:cd12117 198 LLNGARLVLAPKGTLL-DPDALGALIAEEGVTVLWLTAALFNQLADEDPECF-----AGLRELLTGGEVVSPPHVRRVLA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 VVGDGR---------CTLVDTWWQTetggiciaPRPSEDGAEILPGmamRPFFGIVPVLMDEKGNVLEGGdVSGALCISQ 494
Cdd:cd12117 272 ACPGLRlvngygpteNTTFTTSHVV--------TELDEVAGSIPIG---RPIANTRVYVLDEDGRPVPPG-VPGELYVGG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 495 AwpGMARTIYGD----HQRFVDAYFRayPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAV 568
Cdd:cd12117 340 D--GLALGYLNRpaltAERFVADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034773 569 PETAVIGYPHDIKGEAAFAFIVLKDNISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd12117 416 REAVVVVREDAGGDKRLVAYVVAEGALDAA-----ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
135-573 |
9.43e-44 |
|
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: 162.43 E-value: 9.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfn 213
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggrvvelkkivdeavksCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEAPvctPESMSSEDMLFMLYTSGSTGT 293
Cdd:TIGR01733 79 ---------------------DSALASRLAGLVLPVILLDPLELAALDDAPAPPPP---DAPSGPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTQAGyLLYAAMTHKLVFDYQPGDVfgcvadigWITGHSYV-------VYGPLCNGATTVLFESTPVYPDAGRYW 366
Cdd:TIGR01733 135 PKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 367 ETVQRLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRctLVDTWWQTETGGICI 446
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTVWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 447 A---PRPSEDGAEILP-GmamRPFFGIVPVLMDEKGNVLEGGdVSGALCISQawPGMARTIYGD----HQRFVDAYFRAY 518
Cdd:TIGR01733 279 AtlvDPDDAPRESPVPiG---RPLANTRLYVLDDDLRPVPVG-VVGELYIGG--PGVARGYLNRpeltAERFVPDPFAGG 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 519 PGY--YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAV 573
Cdd:TIGR01733 353 DGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
108-645 |
2.95e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 164.07 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVI---TFnqglrggRVVELKKIVDEAVKSCPTVQHVLVAHrTDTKVPMGSLDIPLEQEM 264
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVvpkTF-------RGFDHAAMARRLRPELPALRHVVVVG-GDGADSFEALLITPAWEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 265 AKEAP-VCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQ----AGYLLYAAMthklvFDYQPGDVFGCVADIGWITGHSYV 339
Cdd:PRK13295 182 EPDAPaILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 340 VYGPLCNGATTVLFEStpvypdagryWETVQRLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEP 412
Cdd:PRK13295 257 LMMPVMLGATAVLQDI----------WDPARAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 INHEAWEWLHKVVGdgrCTLVDTWWQTETGGIC-IAPRPSEDGAEI-----LPGMAMRpffgivpvLMDEKGNVLEGGDV 486
Cdd:PRK13295 324 IPGALVERARAALG---AKIVSAWGMTENGAVTlTKLDDPDERASTtdgcpLPGVEVR--------VVDADGAPLPAGQI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 487 sGALCISqawpgmARTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHP 566
Cdd:PRK13295 393 -GRLQVR------GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 567 AVPETAVIGYPHDIKGEAAFAFIVLK--DNISDENMvVNELKlsvATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKI 644
Cdd:PRK13295 466 AIAQVAIVAYPDERLGERACAFVVPRpgQSLDFEEM-VEFLK---AQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
|
.
gi 18034773 645 I 645
Cdd:PRK13295 542 L 542
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
133-643 |
8.38e-42 |
|
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: 157.54 E-value: 8.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITf 212
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivdeavkscPTVqhvlvaHRTDTKVPMGsldipleqemakeapvctpesmssEDMLFMLYTSGSTG 292
Cdd:cd05903 80 -----------------------PER------FRQFDPAAMP------------------------DAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTqAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTpvypDAGRYWETVQRL 372
Cdd:cd05903 107 EPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 373 KINQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPI----NHEAWEWLHKVVgdgrctlVDTWWQTETGGICI 446
Cdd:cd05903 182 GVTFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVprslARRAAELLGAKV-------CSAYGSTECPGAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 447 APRPSEDGAEIlpGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQawPGMartIYGDHQRfVDAYFRAYP-GYYFTG 525
Cdd:cd05903 251 SITPAPEDRRL--YTDGRPLPGVEIKVVDDTGATLAPG-VEGELLSRG--PSV---FLGYLDR-PDLTADAAPeGWFRTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 526 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS-DENMVVNE 604
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALlTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 18034773 605 LKlsvATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05903 402 LD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
113-636 |
2.61e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 158.67 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 113 QKSPETIALIWErdepGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGF 192
Cdd:PRK06178 44 RERPQRPAIIFY----GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 193 SAESLAGRINDAKCKAVITFNQglrggrvveLKKIVdEAVKSCPTVQHVLVAHRTD------TKVPMGSLDIP------- 259
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQ---------LAPVV-EQVRAETSLRHVIVTSLADvlpaepTLPLPDSLRAPrlaaaga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 260 ---LEQEMAKEAPVCTPeSMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGH 336
Cdd:PRK06178 188 idlLPALRACTAPVPLP-PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 337 SYVVYGPLCNGATTVLFESTpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVG-----E 411
Cdd:PRK06178 267 NFGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVVSfvkklN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 412 PINHEAWewlHKVVGdgrCTLVDT-WWQTETGGICIAPRPSEDGAEILPGmamRPFFGIVPV------LMD-EKGNVLEG 483
Cdd:PRK06178 341 PDYRQRW---RALTG---SVLAEAaWGMTETHTCDTFTAGFQDDDFDLLS---QPVFVGLPVpgtefkICDfETGELLPL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 484 GdVSGALCISQawPGMARTIYG----DHQRFVDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIE 559
Cdd:PRK06178 412 G-AEGEIVVRT--PSLLKGYWNkpeaTAEALRDGWLH-------TGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 560 DAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPdQILVVKRLPKTRSGKV 636
Cdd:PRK06178 482 ALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP---GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV 554
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
133-641 |
3.81e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 157.81 E-value: 3.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVIT 211
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 212 fnqglrggrVVELKKIVDEAVKSCPtVQHVLVAHRTDTKVPMGSLDIP--LEQEMAKEAPVCT----------------P 273
Cdd:PRK08314 115 ---------GSELAPKVAPAVGNLR-LRHVIVAQYSDYLPAEPEIAVPawLRAEPPLQALAPGgvvawkealaaglappP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 274 ESMSSEDMLFMLYTSGSTGTPKGLVHTQaGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLF 353
Cdd:PRK08314 185 HTAGPDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 354 -----EStpvypdAGRyweTVQRLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdg 428
Cdd:PRK08314 264 prwdrEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTG-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 429 rCTLVDTWWQTETggicIAP-------RPSEDGAEIlpgmamrPFFGIVPVLMD-EKGNVLEGGD-----VSGALCISQA 495
Cdd:PRK08314 331 -LDYVEGYGLTET----MAQthsnppdRPKLQCLGI-------PTFGVDARVIDpETLEELPPGEvgeivVHGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 WPGMART----IYGDHQRFvdayFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPET 571
Cdd:PRK08314 399 WNRPEATaeafIEIDGKRF----FR-------TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 572 AVIGYPHDIKGEAAFAFIVLK---------DNISD---ENMvvnelklsvatkiAKYAVPDQILVVKRLPKTRSGKVMRR 639
Cdd:PRK08314 468 CVIATPDPRRGETVKAVVVLRpeargktteEEIIAwarEHM-------------AAYKYPRIVEFVDSLPKSGSGKILWR 534
|
..
gi 18034773 640 LL 641
Cdd:PRK08314 535 QL 536
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
132-651 |
6.64e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.58 E-value: 6.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 132 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLAcariGAIHTVVFA---GFSAESLAGRINDAKCKA 208
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 VITfnqgLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQ------------EMAKE---APVCtP 273
Cdd:PRK07529 133 LVT----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRrkaharildfdaELARQpgdRLFS-G 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 274 ESMSSEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGD----------VFGCVAdigwitghsyVVYGP 343
Cdd:PRK07529 208 RPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV----------TGLAP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLfeSTPV-YPDAG---RYWETVQRLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRTLGSVGEPINHEAWE 419
Cdd:PRK07529 277 LARGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 420 WLHKVVGdgrCTLVDTWWQTE-TGGICIAPR--PSEDGA--EILPGMAMRpffgIVPVlmDEKGNVLE--GGDVSGALCI 492
Cdd:PRK07529 352 RFEAATG---VRIVEGYGLTEaTCVSSVNPPdgERRIGSvgLRLPYQRVR----VVIL--DDAGRYLRdcAVDEVGVLCI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 SQA--WPGMARtiyGDHQRFvdayFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPE 570
Cdd:PRK07529 423 AGPnvFSGYLE---AAHNKG----LWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVAL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 571 TAVIGYPHDIKGEAAFAFIVLKDNISDEnmvVNELKLSVATKIA-KYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRG 649
Cdd:PRK07529 496 AAAVGRPDAHAGELPVAYVQLKPGASAT---EAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDAIRRV 572
|
..
gi 18034773 650 QD 651
Cdd:PRK07529 573 LR 574
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
108-668 |
8.10e-40 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 157.71 E-value: 8.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvQHVLVAHRTDTKVPMgsldIPLEQEMAKE 267
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLT---------------------------QSALAARLPELGVPV----LALDALALAA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPESM-SSEDMLFMLYTSGSTGTPKGLVHTQAGYL-LYAAMTHklVFDYQPGDVFGCVADIG-----WitghsyVV 340
Cdd:COG1020 605 EPATNPPVPvTPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQR--RYGLGPGDRVLQFASLSfdasvW------EI 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 341 YGPLCNGATTVLFESTPVyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINHEAWEW 420
Cdd:COG1020 677 FGALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRR 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 421 LHKVVGDGR---------CTLVDTWWQTETGGICIAP----RPsedgaeiLPGMAMRpffgivpVLmDEKGN-VLEGgdV 486
Cdd:COG1020 751 WRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSvpigRP-------IANTRVY-------VL-DAHLQpVPVG--V 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 487 SGALCIsqAWPGMARTIYGDH----QRFVDAYFrAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIED 560
Cdd:COG1020 814 PGELYI--GGAGLARGYLNRPeltaERFVADPF-GFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 561 AMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDEnmvVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRL 640
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAA---AALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
|
570 580
....*....|....*....|....*...
gi 18034773 641 LRKIITSRGQDLGDTTTLEDPSVITEIL 668
Cdd:COG1020 968 LPAPAAAAAAAAAAPPAEEEEEEAALAL 995
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
109-642 |
3.72e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 151.38 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITFNQGLrggrvvelkKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAkea 268
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPA--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 pvcTPESMSSEDMLfMLYTSGSTGTPKGL--------VHTQAGYLlyaAMTHKLvFDYQPGDVFGCVADIgwitGHSyvv 340
Cdd:PRK13391 148 ---TPIADESLGTD-MLYSSGTTGRPKGIkrplpeqpPDTPLPLT---AFLQRL-WGFRSDMVYLSPAPL----YHS--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 341 yGPL--CN-----GATTVLFESTpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP- 412
Cdd:PRK13391 213 -APQraVMlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPc 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 ---INHEAWEWLHKVVGdgrctlvDTWWQTETGGICIAprpseDGAEIL--PGMAMRPFFGIVPVLmdekgnvleggDVS 487
Cdd:PRK13391 288 ppqVKEQMIDWWGPIIH-------EYYAATEGLGFTAC-----DSEEWLahPGTVGRAMFGDLHIL-----------DDD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 488 GALCIsqawPGMARTIYGDHQR-FVdaYFR----------AYPGYYFTGDGAHRTEGGYYQITGRMDDVInISGhrlGT- 555
Cdd:PRK13391 345 GAELP----PGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISG---GVn 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 556 ---AEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTR 632
Cdd:PRK13391 415 iypQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLP 494
|
570
....*....|
gi 18034773 633 SGKVMRRLLR 642
Cdd:PRK13391 495 TGKLYKRLLR 504
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
112-641 |
6.29e-39 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 150.74 E-value: 6.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:cd05923 11 ASRAPDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRI-NDAKCKAVITFN----QGLRGGRVVELKkivdeavkscptvqhvlVAHRTDTKVPMGSLDIPleqemak 266
Cdd:cd05923 87 LKAAELAELIeRGEMTAAVIAVDaqvmDAIFQSGVRVLA-----------------LSDLVGLGEPESAGPLI------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EAPVCTPEsmsseDMLFMLYTSGSTGTPKGLVHTQ-AGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLC 345
Cdd:cd05923 143 EDPPREPE-----QPAFVFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 346 NGATTVLfestPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVV 425
Cdd:cd05923 218 LDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 gDGRctLVDTWWQTETGGICIAPRPSedgaeilPGMAMRPFFG----IVPVL--MDEKGNVLEGGDVSGALCISQAWPGM 499
Cdd:cd05923 292 -PGE--KVNIYGTTEAMNSLYMRDAR-------TGTEMRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAADAAFTGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 500 ARTIYGDHQRFVDayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHD 579
Cdd:cd05923 362 LNQPEATAKKLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034773 580 IKGEAAFAFIVLkdniSDENMVVNEL-KLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05923 435 RWGQSVTACVVP----REGTLSADELdQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
133-643 |
8.79e-39 |
|
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: 148.98 E-value: 8.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVIt 211
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 212 fnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmsseDMLFMLYTSGST 291
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 292 GTPKGLVHTQAGYllyAAMTHKLV--FDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfesTPvYPDAGRYWETV 369
Cdd:cd05941 102 GRPKGVVLTHANL---AANVRALVdaWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEF---LP-KFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 370 QRLKINQFYGAPTAVRLLLKYGDAWVKKYD---RSSLRTL-----GSVGEPIN-HEAWEwlhKVVGDgrcTLVDTWWQTE 440
Cdd:cd05941 175 LMPSITVFMGVPTIYTRLLQYYEAHFTDPQfarAAAAERLrlmvsGSAALPVPtLEEWE---AITGH---TLLERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 441 TGgicIAPRPSEDGAEIlPGMAMRPFFGI-VPVLMDEKGNVLEGGDVsGALCIsqAWPGMARTIYGDHQRFVDAyFRAyP 519
Cdd:cd05941 249 IG---MALSNPLDGERR-PGTVGMPLPGVqARIVDEETGEPLPRGEV-GEIQV--RGPSVFKEYWNKPEATKEE-FTD-D 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 520 GYYFTGDGAHRTEGGYYQITGRM-DDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIsdE 598
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGA--A 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 18034773 599 NMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05941 398 ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
116-641 |
1.48e-38 |
|
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: 148.61 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvcTPEs 275
Cdd:cd17643 75 RIAFILADSGPSLLLT------------------------------------------------------------DPD- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 msseDMLFMLYTSGSTGTPKGLVHTQAGYL-LYAAMTHklVFDYQPGDVfgcvadigWITGHSYV-------VYGPLCNG 347
Cdd:cd17643 94 ----DLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQR--WFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 ATTVLfestpVYPDAGR----YWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINHEAWEWL 421
Cdd:cd17643 160 GRLVV-----VPYEVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRPW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 422 HKVVGDGRCTLVDTWWQTETggiCIAPRPSEDGAEILPGMAM----RPFFGIVPVLMDEKGNVLEGGdVSGALCISQawP 497
Cdd:cd17643 231 AGRFGLDRPQLVNMYGITET---TVHVTFRPLDAADLPAAAAspigRPLPGLRVYVLDADGRPVPPG-VVGELYVSG--A 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 498 GMARTIYG----DHQRFVDAYFRAyPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPET 571
Cdd:cd17643 305 GVARGYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDA 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 572 AVIGYPHDIKGEAAFAFIVLKDNISDenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17643 384 AVIVREDEPGDTRLVAYVVADDGAAA---DIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
165-642 |
2.37e-38 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 149.20 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 165 MPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQGLRGGRVVELkkiVDEAVKSCPTVQHVLVA 244
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPL---YSKVVEAAPAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 245 HRTDTKVPMGS--------LDIPLEQEMAKEAPVcTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVF 316
Cdd:PLN03051 78 AGEPVAVPLREqdlswcdfLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 317 DYQPGDVFGCVADIGWITGhSYVVYGPLCNGATTVLFESTPVYPDAGRYwetVQRLKINQFYGAPTAVRLLLKYGDAWVK 396
Cdd:PLN03051 156 DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAME 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 397 KYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRcTLVDTWWQTETGGICIAPRPSEDGAeilPGMAMRPFFGIVPVLMDE 476
Cdd:PLN03051 232 GLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQA---PGAFSTASLGTRFVLLND 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 477 KGnVLEGGDVSgalCISQAwpGMARTIYGDHQRFVDA-----YFRAYPGYYFT-------GDGAHRTEGGYYQITGRMDD 544
Cdd:PLN03051 308 NG-VPYPDDQP---CVGEV--ALAPPMLGASDRLLNAdhdkvYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 545 VINISGHRLGTAEIEDAM-ADHPAVPETAVIGYPhDIKGEAAFAFIVLKDNISDENMV---VNELKLSVATKIAKYAVP- 619
Cdd:PLN03051 382 TMNLGGIKTSSVEIERACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEEKKGFDqarPEALQKKFQEAIQTNLNPl 460
|
490 500
....*....|....*....|....*.
gi 18034773 620 ---DQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PLN03051 461 fkvSRVKIVPELPRNASNKLLRRVLR 486
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
134-643 |
2.82e-38 |
|
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: 147.33 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINdakckavitfn 213
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglRGGRVVelkKIVDEAVKScptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmssEDMLFMLYTSGSTGT 293
Cdd:cd05974 70 ---RGGAVY---AAVDENTHA--------------------------------------------DDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTQAGYLLYAAMTHKLVfDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVypDAGRYWETVQRLK 373
Cdd:cd05974 100 PKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 374 INQFYGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGIcIAPRPsed 453
Cdd:cd05974 177 VTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP--- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 454 GAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsgALCISQAWP-GMARTIYGDHQRFVDAYfraYPGYYFTGDGAHRTE 532
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGAPATEGEV--ALDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 533 GGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATK 612
Cdd:cd05974 321 DGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRER 400
|
490 500 510
....*....|....*....|....*....|.
gi 18034773 613 IAKYAVPDQiLVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05974 401 LAPYKRIRR-LEFAELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
116-641 |
3.80e-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: 3.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALiweRDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd12116 1 PDATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelkkivDEAvkscptvqhvlvahrTDTKVPMGSLDIPLEQEMAKEAPVCTPES 275
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MSSEDMLFMLYTSGSTGTPKGLVHTQAGYL-LYAAMTHKLvfDYQPGDVFGCVADIGW-ITGHSyvVYGPLCNGATTVLF 353
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERL--GLGPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 354 ESTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGdaWvkkYDRSSLRTL-GsvGEPinheawewLHKVVGDGRCTL 432
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAG--W---QGRAGLTALcG--GEA--------LPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 433 VDTWWQ----TETGGICIAPRPSEDGAEILPGmamRPFFGIVPVLMDEKGN-VLEGgdVSGALCIsqAWPGMARTIYGD- 506
Cdd:cd12116 263 VGSLWNlygpTETTIWSTAARVTAAAGPIPIG---RPLANTQVYVLDAALRpVPPG--VPGELYI--GGDGVAQGYLGRp 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 ---HQRFVDAYFrAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIK 581
Cdd:cd12116 336 altAERFVPDPF-AGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGD 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 582 GEAAfAFIVLKDNIS-DEnmvvNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd12116 415 RRLV-AYVVLKAGAApDA----AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
110-644 |
4.84e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 148.92 E-value: 4.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGA 183
Cdd:PRK07788 57 HAARRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 184 IHTVVFAGFSAESLAGRINDAKCKAVITFNqglrggrvvELKKIVDEAVKSCPTVqHVLVAHRTDTKvPMGSLDIPLEQE 263
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAAREGVKALVYDD---------EFTDLLSALPPDLGRL-RAWGGNPDDDE-PSGSTDETLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 264 MA--KEAPVCTPESMSSedmlFMLYTSGSTGTPKGLVHTQAGYLLYAAMthklVFDYQP---GDVFGCVADIGWITGHSY 338
Cdd:PRK07788 194 IAgsSTAPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLAG----LLSRVPfraGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 339 VVYGpLCNGATTVL---FestpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINH 415
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 416 EAWEWLHKVVGDGRCTLvdtWWQTETGGICIApRPSEdgAEILPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQA 495
Cdd:PRK07788 338 ELATRALEAFGPVLYNL---YGSTEVAFATIA-TPED--LAEAPGTVGRPPKGVTVKILDENGNEVPRG-VVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 WPgMARTIYGDHQRFVDayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIG 575
Cdd:PRK07788 411 FP-FEGYTDGRDKQIID-------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 576 YPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKI 644
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 ... |
108-641 |
5.54e-38 |
|
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: 147.81 E-value: 5.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERdepgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITfNQGLRGGRVVELKKivdeavkscPTVQHVLVAHRTDTkvpmgsldiPLEQEMAKE 267
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLT-TADLAARLPAGGDV---------ALLGDEALAAPPAT---------PPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCtpesmssedmlfMLYTSGSTGTPKGLVHTQAG---YLLYaaMTHKlvFDYQPGDVFGCVADIGWITGhSYVVYGPL 344
Cdd:cd17646 139 NLAY------------VIYTSGSTGRPKGVMVTHAGivnRLLW--MQDE--YPLGPGDRVLQKTPLSFDVS-VWELFWPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 345 CNGATTVLFEstpvyP----DAGRYWETVQRLKINQFYGAPTAVRLLLkygdAWVKKYDRSSLRTLGSVGEPINHEAWEW 420
Cdd:cd17646 202 VAGARLVVAR-----PgghrDPAYLAALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 421 LHKVVGdgrCTLVDTWWQTETGgICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCIsqAWPGMA 500
Cdd:cd17646 273 FLALPG---AELHNLYGPTEAA-IDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVG-VPGELYL--GGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 501 RTIYG----DHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGY 576
Cdd:cd17646 346 RGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 577 PHDIKGEAAFAFIVLKDNISDENmvVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17646 426 AAPAGAARLVGYVVPAAGAAGPD--TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
106-656 |
4.82e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 145.57 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 106 NCLDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIH 185
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 186 TVVFAGFSAESLAGRINDAKCKAVI---TFNQGLRGGRVVELK---KIVDEAVKSCPTVQHVLVAHRtDTKVPMGSLDip 259
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchaDFPEHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 260 leqemakeapvctpesmsSEDMLFMLYTSGSTGTPKG--LVHTQAGYLLyaamTHKLVfDYQPG----DVFGCVADIGwi 333
Cdd:PRK07470 162 ------------------HDDPCWFFFTSGTTGRPKAavLTHGQMAFVI----TNHLA-DLMPGtteqDASLVVAPLS-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 334 tgHSYVVYGpLCN---GATTVLFESTPVYPDAgrYWETVQRLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVG 410
Cdd:PRK07470 217 --HGAGIHQ-LCQvarGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 411 EPINHE----AWEWLHKVvgdgrctLVDTWWQTE-TGGICIAPRP---SEDGAEILPGMAMRPFFGIVPVLMDEKGNVLE 482
Cdd:PRK07470 290 APMYRAdqkrALAKLGKV-------LVQYFGLGEvTGNITVLPPAlhdAEDGPDARIGTCGFERTGMEVQIQDDEGRELP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 483 GGDVSGALCISQA-WPGMARTIYGDHQRFVDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 561
Cdd:PRK07470 363 PGETGEICVIGPAvFAGYYNNPEANAKAFRDGWFR-------TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 562 MADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS-DEnmvvNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRL 640
Cdd:PRK07470 436 LLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPvDE----AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKM 511
|
570
....*....|....*..
gi 18034773 641 LRKIITSRGQ-DLGDTT 656
Cdd:PRK07470 512 VREELEERGLlDLERAP 528
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
110-660 |
5.71e-37 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 145.66 E-value: 5.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALIwerDEPGTevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVF 189
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 190 AGFSAESLAGRINDAKCKAVIT---FNQGLRGGRVVELKKIVdeavkscPTVQHVLVahrTDTKVPMGSlDIPLEQEMAK 266
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlFKQTRPVDLILPLQNQL-------PQLQQIVG---VDKLAPATS-SLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLL----YAAMTHkLVFDyqpgDVFGCVADIGWITGHSYVVYG 342
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFEStpVYPDAGryWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPI----NHEAW 418
Cdd:PRK06087 250 PFLIGARSVLLDI--FTPDAC--LALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIpkkvARECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 EwlHKVVgdgrctLVDTWWQTETggiciAPR---PSEDGAEILPGMAMRPFFGIVPVLMDEKGNVL----EGGDVSgalc 491
Cdd:PRK06087 324 Q--RGIK------LLSVYGSTES-----SPHavvNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLppgcEGEEAS---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 492 isqawpgmartiYGDHQrFVdAYF-------RAY--PGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAM 562
Cdd:PRK06087 387 ------------RGPNV-FM-GYLdepeltaRALdeEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDIL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 563 ADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNisDENMVVNELKLSVATK-IAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK06087 453 LQHPKIHDACVVAMPDERLGERSCAYVVLKAP--HHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
570
....*....|....*....
gi 18034773 642 RKIITSRgqdLGDTTTLED 660
Cdd:PRK06087 531 RKDIMRR---LTQDVCEEI 546
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
116-642 |
1.48e-36 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 142.89 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWErDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd17649 1 PDAVALVFG-DQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvQHvlvahrtdtkvpmgsldipleqemakeapvctPES 275
Cdd:cd17649 75 RLRYMLEDSGAGLLLT---------------------------HH--------------------------------PRQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MSsedmlFMLYTSGSTGTPKGLVHTQAGYLLYAAMThKLVFDYQPGDVFGCVADIGWITGHSYVvYGPLCNGATTVLfES 355
Cdd:cd17649 96 LA-----YVIYTSGSTGTPKGVAVSHGPLAAHCQAT-AERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL-RP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 356 TPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINHE-AWEWLhkvvgDGRCTLVD 434
Cdd:cd17649 168 DELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRWL-----KAPVRLFN 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 435 TWWQTE---TGGICIAPRPSEDGAEILP-GmamRPFFGIVPVLMDEKGNVLEGGdVSGALCIsqAWPGMARTIYG----D 506
Cdd:cd17649 242 AYGPTEatvTPLVWKCEAGAARAGASMPiG---RPLGGRSAYILDADLNPVPVG-VTGELYI--GGEGLARGYLGrpelT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 HQRFV-DAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIkGEAA 585
Cdd:cd17649 316 AERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 586 FAFIVLKDNISDENMVVnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd17649 395 VAYVVLRAAAAQPELRA-QLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
116-641 |
1.58e-36 |
|
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: 143.91 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITFNQglrggrvvELKKIVDEAVKscptvqhvLVAHRTDtkvPMGSLDIPLEQEMAKEAPVCTPEs 275
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAE--------LAEKLASLALP--------VVLLDSA---EFDSLSFSDLLFEADEAEPPVVV- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLV-FDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVlfe 354
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVV--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 355 stpVYP--DAGRYWETVQRLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDgrCTL 432
Cdd:cd05904 232 ---VMPrfDLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN--VDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 433 VDTWWQTETGGICIAPRPSEDGAE-------ILPGMAMRpffgIVPVlmdEKGNVLEGGDvSGALCISQawPGM------ 499
Cdd:cd05904 305 GQGYGMTESTGVVAMCFAPEKDRAkygsvgrLVPNVEAK----IVDP---ETGESLPPNQ-TGELWIRG--PSImkgyln 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 500 -----ARTIYGDhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVI 574
Cdd:cd05904 375 npeatAATIDKE-------------GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 575 GYPHDIKGEAAFAFIVLK--DNISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05904 442 PYPDEEAGEVPMAFVVRKpgSSLTED-----EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
129-642 |
5.48e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 141.96 E-value: 5.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 129 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKA 208
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 VITfnqglrGGRVVELkkiVDEAVKSCPtvqhvlvAHRTDTKVPMGSLD--IPLEQEMAKEAPVCTPESMSSEDmlfMLY 286
Cdd:PRK08276 87 LIV------SAALADT---AAELAAELP-------AGVPLLLVVAGPVPgfRSYEEALAAQPDTPIADETAGAD---MLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 287 TSGSTGTPKGLVhtqagyllyAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGA-------------TTVLF 353
Cdd:PRK08276 148 SSGTTGRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVVVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 354 ESTpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEA----WEWLHKVVgdgr 429
Cdd:PRK08276 219 EKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVkramIDWWGPII---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 430 ctlVDTWWQTETGGICIAprPSEDGAEiLPGMAMRPFFGIVPVLmDEKGNVLEGGDVSgalCISQAWPGMARTIYGDHQR 509
Cdd:PRK08276 291 ---HEYYASSEGGGVTVI--TSEDWLA-HPGSVGKAVLGEVRIL-DEDGNELPPGEIG---TVYFEMDGYPFEYHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 510 FVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAMADHPAVPETAVIGYPHDIKGEAA 585
Cdd:PRK08276 361 TAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVAVFGVPDEEMGERV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 586 FAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK08276 435 KAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
108-642 |
1.06e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 141.80 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCkAVITFNQGLRGgrvVELKKIVDEAVKSC-PTVQHVLVAHRT--DTKVPMGSLDIPLEQEM 264
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRA-RWLVVWPGFKG---IDFAAILAAVPPDAlPPLRAIAVVDDAadATPAPAPGARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 265 AKEAPVCTPESMSSEDMLFMLY-TSGSTGTPKGLVHTQAGYLLYAAMTHKlVFDYQPGDVFGCVADIGWITGHSYVVyGP 343
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-GA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLFestPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVG-EPINHEAWEWL- 421
Cdd:PRK06164 244 LAGGAPLVCE---PVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFGFASfAPALGELAALAr 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 422 -HKVVGDG-----------RCTLVDTWWQT--ETGGiciapRPSEDGAEilpgmamrpffgiVPVLMDEKGNVLEGGdVS 487
Cdd:PRK06164 317 aRGVPLTGlygssevqalvALQPATDPVSVriEGGG-----RPASPEAR-------------VRARDPQDGALLPDG-ES 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 488 GALCISQawPGMARTIYGDHQRFVDAYFRayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPA 567
Cdd:PRK06164 378 GEIEIRA--PSLMRGYLDNPDATARALTD--DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 568 VPETAVIGYPHDIKGEAAfAFIVLKDNIS-DENMVVNELKLSVatkiAKYAVPDQILVVKRLPKTRSG---KVMRRLLR 642
Cdd:PRK06164 454 VAAAQVVGATRDGKTVPV-AFVIPTDGASpDEAGLMAACREAL----AGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
133-641 |
1.51e-34 |
|
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: 136.45 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITf 212
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmGSldipleqemakeapvctpesmSSEDMLFMLYTSGSTG 292
Cdd:cd05935 80 -----------------------------------------GS---------------------ELDDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTQaGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTpvypDAGRYWETVQRL 372
Cdd:cd05935 98 LPKGCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARW----DRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 373 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIAPRPSE 452
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTETMSQTHTNPPLR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 453 DGAEILpGMamrPFFGIVPVLMD-EKGNVLEGGdVSGALCIS--QAWPGMARTIYGDHQRFVD----AYFRaypgyyfTG 525
Cdd:cd05935 248 PKLQCL-GI---P*FGVDARVIDiETGRELPPN-EVGEIVVRgpQIFKGYWNRPEETEESFIEikgrRFFR-------TG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 526 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKD----NISDENMV 601
Cdd:cd05935 316 DLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyrgKVTEEDII 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 18034773 602 VnelklSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05935 396 E-----WAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
112-641 |
1.58e-34 |
|
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: 137.06 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:cd12115 9 AARTPDAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvc 271
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 tpesmSSEDMLFMLYTSGSTGTPKGLV--HTQAGYLLYAAMTHklvfdYQPGDVFGCVA------DIGwitghSYVVYGP 343
Cdd:cd12115 103 -----DPDDLAYVIYTSGSTGRPKGVAieHRNAAAFLQWAAAA-----FSAEELAGVLAstsicfDLS-----VFELFGP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLFESTPVYPDAGRYWETVQrlkINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINHEAWEWLHK 423
Cdd:cd12115 168 LATGGKVVLADNVLALPDLPAAAEVTL---INT---VPSAAAELLRHDAL------PASVRVVNLAGEPLPRDLVQRLYA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 VVGDGRctLVDTWWQTE-TGGICIAPRPSEDGAEILPGmamRPFFGIVPVLMDEKGNVLEGGdVSGALCISQAwpGMART 502
Cdd:cd12115 236 RLQVER--VVNLYGPSEdTTYSTVAPVPPGASGEVSIG---RPLANTQAYVLDRALQPVPLG-VPGELYIGGA--GVARG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 503 IYGD----HQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPEtAVIGYPH 578
Cdd:cd12115 308 YLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVVAIG 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034773 579 DIKGEAAF-AFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd12115 387 DAAGERRLvAYIVAEP---GAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
108-641 |
1.77e-34 |
|
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: 137.46 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVItfnqglrggrvvelkkiVDEavkscptvQHVLVAHRtdtkvpmgsldiPLEQEMAKE 267
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYI-----------------VPD--------RHAGFDHR------------ALARELAES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APvctpesmsseDMLFMLYTSGSTGTPKGLVHTQAGYLlYAAMTHKLVFDYQPGDVFGCVADIGwitgHSYV-----VYG 342
Cdd:cd05920 138 IP----------EVALFLLSGGTTGTPKLIPRTHNDYA-YNVRASAEVCGLDQDTVYLAVLPAA----HNFPlacpgVLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWLH 422
Cdd:cd05920 203 TLLAGGRVVLAPD----PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALARRVP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 423 KVVGdgrCTLVDTWWQTEtGGICIApRPsEDGAEILPGMAMRPffgIVP----VLMDEKGNVLEGGDVsGALcisqawpg 498
Cdd:cd05920 277 PVLG---CTLQQVFGMAE-GLLNYT-RL-DDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGEE-GEL-------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 499 MAR---TIYGdhqrfvdaYFRAyP----------GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADH 565
Cdd:cd05920 339 LTRgpyTIRG--------YYRA-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRH 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 566 PAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKlsvATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05920 410 PAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
109-642 |
3.06e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 137.12 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:PRK08008 14 DDLADVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITFNQGLRGGRVVELKKIVdeavkscpTVQHVLVAHRTDTKVPmGSLDipLEQEMAKEA 268
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAT--------PLRHICLTRVALPADD-GVSS--FTQLKAQQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 P-VCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQ-----AGYllYAAMTHKLVFDyqpgDVFGCVADIGWITGHSYVVYG 342
Cdd:PRK08008 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLTVMPAFHIDCQCTAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFEStpvYpDAGRYWETVQRLKINQFYGAPTAVR-LLLKYGDAWvkkyDRS-SLRTLG-----SVGEpinH 415
Cdd:PRK08008 236 AFSAGATFVLLEK---Y-SARAFWGQVCKYRATITECIPMMIRtLMVQPPSAN----DRQhCLREVMfylnlSDQE---K 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 416 EAWEWLHKVvgdgrcTLVDTWWQTETGGICIAPRPSEdgAEILPGMAmRPFFGIVPVLMDEKGNVLEGGDVsGALCIsQA 495
Cdd:PRK08008 305 DAFEERFGV------RLLTSYGMTETIVGIIGDRPGD--KRRWPSIG-RPGFCYEAEIRDDHNRPLPAGEI-GEICI-KG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 WPGmaRTIYGDHQRFVDAYFRAYP--GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAV 573
Cdd:PRK08008 374 VPG--KTIFKEYYLDPKATAKVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 574 IGYPHDIKGEAAFAFIVLKDNisdENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK08008 452 VGIKDSIRDEAIKAFVVLNEG---ETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
106-646 |
3.26e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 136.63 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 106 NCLDQHVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAih 185
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFEEKK------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 186 TVVFAG--FSAESLAGRINDAKCKAVITfNQGLRGGRVVELKKIVDEavkscptvqhvlvahrtdtkvpmgsldipLEQE 263
Cdd:PRK03640 78 VAVLLNtrLSREELLWQLDDAEVKCLIT-DDDFEAKLIPGISVKFAE-----------------------------LMNG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 264 MAKEApvcTPESMSSEDMLF-MLYTSGSTGTPKGLVHTQAGYLlYAAMTHKLVFDYQPGDVFGCVADIGWITGHSY---- 338
Cdd:PRK03640 128 PKEEA---EIQEEFDLDEVAtIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSIlmrs 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 339 VVYGplcngATTVLFESTpvypDAGRYWETVQRLKINQFYGAPTAV-RLLLKYGDAwvkKYDrSSLRT--LGsvGEPIN- 414
Cdd:PRK03640 204 VIYG-----MRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLqRLLERLGEG---TYP-SSFRCmlLG--GGPAPk 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 415 ---HEAWEWlhkvvgdgRCTLVDTWWQTETggiC--IAPRPSEDGAEILpGMAMRPFFGI--------VPVLMDEKGN-V 480
Cdd:PRK03640 269 pllEQCKEK--------GIPVYQSYGMTET---AsqIVTLSPEDALTKL-GSAGKPLFPCelkiekdgVVVPPFEEGEiV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 481 LEGGDV-SGALCISQAwpgmartiygDHQRFVDayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIE 559
Cdd:PRK03640 337 VKGPNVtKGYLNREDA----------TRETFQD-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 560 DAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRR 639
Cdd:PRK03640 400 EVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEE-----ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
....*..
gi 18034773 640 LLRKIIT 646
Cdd:PRK03640 475 ELKQLVE 481
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
108-644 |
8.00e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 136.44 E-value: 8.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFNqGLRGGRVVElkkIVDEAVKSCPTVQHVLVAH----RTDTKVPMGSLDIP---L 260
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTSDYHA---MLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 261 EQEMAKEAPVCTPE-------SMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMT---------HKLVFDYQPGDVF 324
Cdd:PRK12583 176 WHELQARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVaeslgltehDRLCVPVPLYHCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 325 GCV-ADIGWITghsyvvygplcNGAtTVLFESTPVYPDAgrYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSL 403
Cdd:PRK12583 256 GMVlANLGCMT-----------VGA-CLVYPNEAFDPLA--TLQAVEEERCTALYGVPTMFIAELDHPQ--RGNFDLSSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 404 RTLGSVGEPINHEAwewLHKVVGDGRCTLVD-TWWQTETGGICIA-------PRPSEDGAEILPGMAMRpffgivpvLMD 475
Cdd:PRK12583 320 RTGIMAGAPCPIEV---MRRVMDEMHMAEVQiAYGMTETSPVSLQttaaddlERRVETVGRTQPHLEVK--------VVD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 476 EKGNVLEGGDVsGALC-----ISQAWPGM----ARTIYGDhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVI 546
Cdd:PRK12583 389 PDGATVPRGEI-GELCtrgysVMKGYWNNpeatAESIDED-------------GWMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 547 NISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKdniSDENMVVNELKLSVATKIAKYAVPDQILVVK 626
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLH---PGHAASEEELREFCKARIAHFKVPRYFRFVD 531
|
570
....*....|....*...
gi 18034773 627 RLPKTRSGKVMRRLLRKI 644
Cdd:PRK12583 532 EFPMTVTGKVQKFRMREI 549
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
116-635 |
1.43e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 135.40 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVItFNQGLrGGRVVELKkivdeavKSCPTVQHVL-VAHRTDTKVPMGSldIPLEQEMAKEAPVCTPE 274
Cdd:PRK07798 91 ELRYLLDDSDAVALV-YEREF-APRVAEVL-------PRLPKLRTLVvVEDGSGNDLLPGA--VDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 275 SMSSEDmLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGAT----- 349
Cdd:PRK07798 160 ERSPDD-LYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaaf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 350 -------TVLFESTPVYpDAGRYWETVQRLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEP 412
Cdd:PRK07798 239 aalfsgqTVVLLPDVRF-DADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIASGGAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 INHEAWEWLHKVVGDgrCTLVDTWWQTETG--GICI-APRPSEDGaeilpgmamRPFFGIVP--VLMDEKGNVLEGGDVS 487
Cdd:PRK07798 308 FSPSVKEALLELLPN--VVLTDSIGSSETGfgGSGTvAKGAVHTG---------GPRFTIGPrtVVLDEDGNPVEPGSGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 488 galcisqawPGM-ART------IYGDHQRfVDAYFRAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEI 558
Cdd:PRK07798 377 ---------IGWiARRghiplgYYKDPEK-TAETFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 559 EDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDN--ISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGK 635
Cdd:PRK07798 447 EEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGarPDLA-----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
116-641 |
2.51e-33 |
|
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: 133.36 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd17650 1 PDAIAVSDA------TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpes 275
Cdd:cd17650 75 RLQYMLEDSGAKLLLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 mSSEDMLFMLYTSGSTGTPKGLVHTQAGYL-LYAAMTHKLVFDYQPGDVFGcvadigwITGHSYVVYG-----PLCNGAT 349
Cdd:cd17650 91 -QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFDVFAgdfarSLLNGGT 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 350 TVLFESTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPInhEAWEWLHKVVGd 427
Cdd:cd17650 163 LVICPDEVKL-DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QDFKTLAARFG- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 428 GRCTLVDTWWQTETggiCIAPRPSEDGAEILPGMAM----RPFFGIVPVLMDEKGNVLEGGdVSGALCISQAwpGMARTI 503
Cdd:cd17650 237 QGMRIINSYGVTEA---TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQPVG-VAGELYIGGA--GVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 504 YGD----HQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIgYPHD 579
Cdd:cd17650 311 LNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VRED 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034773 580 IKGEAAF-AFIVlkdniSDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17650 390 KGGEARLcAYVV-----AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
143-642 |
4.32e-33 |
|
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: 132.95 E-value: 4.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 143 TCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAgfsaeslagRINDAKCKAVITFNQGLRGGRVV 222
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV---------PLNPTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 223 elkkIVDEAVKScpTVQHVLVAHRTDTKVpmgsldIPLEQEMAKEAPVCTPESmSSEDMLFMLYTSGSTGTPKG--LVHT 300
Cdd:cd05922 74 ----LADAGAAD--RLRDALPASPDPGTV------LDADGIRAARASAPAHEV-SHEDLALLLYTSGSTGSPKLvrLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 301 QagyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSyVVYGPLCNGATTVLfESTPVYPDAgrYWETVQRLKINQFYGA 380
Cdd:cd05922 141 N---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATGLAGV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 381 PTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRctLVDTWWQTE-TGGICIAPRPSEDGAeilP 459
Cdd:cd05922 214 PSTYAMLTRLG---FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEaTRRMTYLPPERILEK---P 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 460 GMAMRPFFGIVPVLMDEKGNVLEGGDV-----SGALCISQAWPGMARTiyGDHQRFVDAYFraypgyyfTGDGAHRTEGG 534
Cdd:cd05922 286 GSIGLAIPGGEFEILDDDGTPTPPGEPgeivhRGPNVMKGYWNDPPYR--RKEGRGGGVLH--------TGDLARRDEDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 535 YYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPhDIKGEAAFAFIVLKDNISDEnmvvnELKLSVATKIA 614
Cdd:cd05922 356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPK-----DVLRSLAERLP 429
|
490 500
....*....|....*....|....*...
gi 18034773 615 KYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05922 430 PYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
108-641 |
3.32e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 131.69 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFNqglrggrvVELKKIVDeaVKSCPTVQHVLVAHRTD------------------- 248
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLD--------LVFPRVTN--VQSATKIEHVIVTRIADflpfpknllypfvqkkqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 249 --TKVPMGSL-----DIPLEQEMAKEAPvCTPESmsseDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPG 321
Cdd:PRK06710 174 lvVKVSESETihlwnSVEKEVNTGVEVP-CDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 322 D--VFGcVADIGWITGHSYVVYGPLCNGATTVLFestPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKygDAWVKKYD 399
Cdd:PRK06710 249 EevVLG-VLPFFHVYGMTAVMNLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 400 RSSLRTLGSVGEPINHEAWEWLHKVVGDgrcTLVDTWWQTETGGICIAPRPSEdgaEILPGMAMRPFFGIVPVLMD-EKG 478
Cdd:PRK06710 322 ISSIRACISGSAPLPVEVQEKFETVTGG---KLVEGYGLTESSPVTHSNFLWE---KRVPGSIGVPWPDTEAMIMSlETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 479 NVLEGGD-----VSGALCISQAW--PGMARTIYGDhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGH 551
Cdd:PRK06710 396 EALPPGEigeivVKGPQIMKGYWnkPEETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 552 RLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKT 631
Cdd:PRK06710 463 NVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE---GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKT 539
|
570
....*....|
gi 18034773 632 RSGKVMRRLL 641
Cdd:PRK06710 540 TVGKILRRVL 549
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
131-644 |
1.10e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 129.88 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 TFNQGLrggrvvELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIPleqemAKEAPVCtPESMSSEDMLFMLYTSGS 290
Cdd:PRK06155 124 VEAALL------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLP-----PLDAPAP-AAAVQPGDTAAILYTSGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 291 TGTPKGLVHTQAGYLLYAAMTHKLVfDYQPGDVFGCVADIGWITGHSyVVYGPLCNGATTVLfesTPVYpDAGRYWETVQ 370
Cdd:PRK06155 192 TGPSKGVCCPHAQFYWWGRNSAEDL-EIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVL---EPRF-SASGFWPAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 371 RLKINQFYGAPTAVRLLLKYGDawvKKYDR-SSLRT-LGSVGEPINHEAWEwlhkvvgdGRC--TLVDTWWQTETGGICI 446
Cdd:PRK06155 266 RHGATVTYLLGAMVSILLSQPA---RESDRaHRVRVaLGPGVPAALHAAFR--------ERFgvDLLDGYGSTETNFVIA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 447 APRPSEDgaeilPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQAWPG-MARTIYGDHQRFVDAYFRAYpgyYFTG 525
Cdd:PRK06155 335 VTHGSQR-----PGSMGRLAPGFEARVVDEHDQELPDG-EPGELLLRADEPFaFATGYFGMPEKTVEAWRNLW---FHTG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 526 DGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNEL 605
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRH 485
|
490 500 510
....*....|....*....|....*....|....*....
gi 18034773 606 KLSvatKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKI 644
Cdd:PRK06155 486 CEP---RLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
125-643 |
2.79e-31 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 128.72 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 125 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAI-HTVVFAGFsAESLAGRIND 203
Cdd:PRK06018 31 RSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 204 AKCKAVI---TFnqglrggrVVELKKIVDEavksCPTVQHVLV----AHRTDTKVPMG-SLDIPLEQEMAKEAPVCTPES 275
Cdd:PRK06018 110 AEDRVVItdlTF--------VPILEKIADK----LPSVERYVVltdaAHMPQTTLKNAvAYEEWIAEADGDFAWKTFDEN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MSSEdmlfMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKlvfdyqpGDVFGCVADIGWITghsyVVygPLCNGATTVLFES 355
Cdd:PRK06018 178 TAAG----MCYTSGTTGDPKGVLYSHRSNVLHALMANN-------GDALGTSAADTMLP----VV--PLFHANSWGIAFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 356 TP------VYP----DAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinheawEWLHKVV 425
Cdd:PRK06018 241 APsmgtklVMPgaklDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP------RSMIKAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 GDGRCTLVDTWWQTET---GGICIAPRPSEDgaeiLPG--------MAMRPFFGIVPVLMDEKGNVLE-GGDVSGALCIS 493
Cdd:PRK06018 315 EDMGVEVRHAWGMTEMsplGTLAALKPPFSK----LPGdarldvlqKQGYPPFGVEMKITDDAGKELPwDGKTFGRLKVR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 494 QawPGMARTIYGDHQRFVDAyfrayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAV 573
Cdd:PRK06018 391 G--PAVAAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 574 IGYPHDIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:PRK06018 464 IGVYHPKWDERPLLIVQLKP---GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
116-641 |
3.47e-31 |
|
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: 127.39 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd12114 1 PDATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelKKIVDEAVKSCPTVQHVLVahrtdtkVPMGSLDIPLEQEMAkeapvctpes 275
Cdd:cd12114 75 RREAILADAGARLVLT-------------DGPDAQLDVAVFDVLILDL-------DALAAPAPPPPVDVA---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 msSEDMLFMLYTSGSTGTPKGLVHTQAGYL-LYAAMTHKLVFDyqPGDVFGCVA----DIGwitghSYVVYGPLCNGATT 350
Cdd:cd12114 125 --PDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 351 VLfestpvyPDAGR-----YW-ETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINHEAWEWLHKV 424
Cdd:cd12114 196 VL-------PDEARrrdpaHWaELIERHGVTLWNSVPALLEMLLDVLEAAQALL--PSLRLVLLSGDWIPLDLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 425 VGDgrCTLVDTWWQTETGGICIA---PRPSEDGAEI-----LPGMAMRpffgivpvLMDEKGNVLEGGdVSGALCISQAw 496
Cdd:cd12114 267 APD--ARLISLGGATEASIWSIYhpiDEVPPDWRSIpygrpLANQRYR--------VLDPRGRDCPDW-VPGELWIGGR- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 497 pGMARTIYGDHQRFVDAYFRAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVI 574
Cdd:cd12114 335 -GVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 575 GYPhDIKGEAAFAFIVLKDNisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd12114 414 VLG-DPGGKRLAAFVVPDND--GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
116-642 |
5.06e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 127.79 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:PRK06188 26 PDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVItFNQGLRGGRVVELkkivdeaVKSCPTVQHVLvahrTDTKVPMGSlDIPLEQEMAKEAPVcTPES 275
Cdd:PRK06188 100 DHAYVLEDAGISTLI-VDPAPFVERALAL-------LARVPSLKHVL----TLGPVPDGV-DLLAAAAKFGPAPL-VAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MSSeDMLFMLYTSGSTGTPKGLVHTQAGYllyAAMTHKLVFDYQ-PGDV-FGCVADIGWITGhsYVVYGPLCNGATTVLF 353
Cdd:PRK06188 166 LPP-DIAGLAYTGGTTGKPKGVMGTHRSI---ATMAQIQLAEWEwPADPrFLMCTPLSHAGG--AFFLPTLLRGGTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 354 ESTpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN----HEAWEWLHKVvgdgr 429
Cdd:PRK06188 240 AKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSpvrlAEAIERFGPI----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 430 ctLVDTWWQTETGgICIAPRPSEDGAEILPGM---AMRPFFGIVPVLMDEKGNVLEGGDVsGALCISQawPGMARTIYGD 506
Cdd:PRK06188 309 --FAQYYGQTEAP-MVITYLRKRDHDPDDPKRltsCGRPTPGLRVALLDEDGREVAQGEV-GEICVRG--PLVMDGYWNR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 HQRFVDAyFRAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAF 586
Cdd:PRK06188 383 PEETAEA-FRD--GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVT 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 587 AFIVLKdniSDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK06188 460 AVVVLR---PGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
113-642 |
5.24e-31 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 127.95 E-value: 5.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 113 QKSPETIALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGF 192
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 193 SAESLAGRINDAKCKAVItFNQglrggrvvELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSL-DIPLEQEmakeaPVC 271
Cdd:PRK13382 128 AGPALAEVVTREGVDTVI-YDE--------EFSATVDRALADCPQATRIVAWTDEDHDLTVEVLiAAHAGQR-----PEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 TPESMSSedmlfMLYTSGSTGTPKGLVHTQAGyllyAAMTHKLVFDYQP---GDVFGCVADIGWITGHSYVVYGPL--CN 346
Cdd:PRK13382 194 TGRKGRV-----ILLTSGTTGTPKGARRSGPG----GIGTLKAILDRTPwraEEPTVIVAPMFHAWGFSQLVLAASlaCT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 347 GATTVLFEstpvyPDAgryweTVQRLKINQFYG---APTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHK 423
Cdd:PRK13382 265 IVTRRRFD-----PEA-----TLDLIDRHRATGlavVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 VVGDgrcTLVDTWWQTETGGICIApRPSEDGAEilPGMAMRPFFGIVPVLMDEKGNVLEGGDVSgalcisqawpgmarTI 503
Cdd:PRK13382 335 QFGD---VIYNNYNATEAGMIATA-TPADLRAA--PDTAGRPAEGTEIRILDQDFREVPTGEVG--------------TI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 504 YGDHQRFVDAYFRA-----YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPH 578
Cdd:PRK13382 395 FVRNDTQFDGYTSGstkdfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034773 579 DIKGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK13382 475 EQYGQRLAAFVVLKP---GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
105-643 |
6.81e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 127.59 E-value: 6.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 105 VNCLDQHVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAI 184
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 185 HTVVFAGFSAESLAGRINDAKCKAVITfnqglrGGRVVELKKIVDEAVkscPTVQHVLVA-HRTDTKVPmgSLDIPLEQE 263
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT------EAALAPVATAVRDIV---PLLSTVVVAgGSSDDSVL--GYEDLLAEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 264 MAKEAPVCTPESMSSedmlFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVAD-IGWITGHSYVVYG 342
Cdd:PRK07786 163 GPAHAPVDIPNDSPA----LIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGADINSDVGFVGVpLFHIAGIGSMLPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 pLCNGATTVLfestpvYP----DAGRYWETVQRLKINQFYGAPTAVRLLLkyGDAWVKKYDRsSLRTLGSVGEPINHEAW 418
Cdd:PRK07786 238 -LLLGAPTVI------YPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDL-ALRVLSWGAAPASDTLL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 EWLHKVVGDGRctLVDTWWQTETGGI-CI-----APRPSEDGAEILPGMAMRpffgivpvLMDEKGNVLEGGDVSGalcI 492
Cdd:PRK07786 308 RQMAATFPEAQ--ILAAFGQTEMSPVtCMllgedAIRKLGSVGKVIPTVAAR--------VVDENMNDVPVGEVGE---I 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 SQAWPGMARTIYGDHQRFVDAYfraYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETA 572
Cdd:PRK07786 375 VYRAPTLMSGYWNNPEATAEAF---AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 573 VIGYPHDIKGEAAFAFIVLKDniSDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:PRK07786 452 VIGRADEKWGEVPVAVAAVRN--DDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
109-650 |
1.76e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.31 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:PRK12316 518 EEQVERTPEAPALAF------GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptVQHVLVAHRTDTKVPMGSLDIP-LEQE-MAK 266
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLS--------------------------QSHLGRKLPLAAGVQVLDLDRPaAWLEgYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EAPVctpESMSSEDMLFMLYTSGSTGTPKGLV--HTQAGYLLYAAMThklVFDYQPGDVFGCVADIGWITGHsYVVYGPL 344
Cdd:PRK12316 646 ENPG---TELNPENLAYVIYTSGSTGKPKGAGnrHRALSNRLCWMQQ---AYGLGVGDTVLQKTPFSFDVSV-WEFFWPL 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 345 CNGATTVLfESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINHEAWEWLHKV 424
Cdd:PRK12316 719 MSGARLVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEALPADAQEQVFAK 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 425 VGDGRctLVDTWWQTE-TGGICIAPRPSEDGAEILPGmamRPFFGIVPVLMDEKGNVLEGGdVSGALCISQAwpGMARTI 503
Cdd:PRK12316 794 LPQAG--LYNLYGPTEaAIDVTHWTCVEEGGDSVPIG---RPIANLACYILDANLEPVPVG-VLGELYLAGR--GLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 504 YG----DHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGyphd 579
Cdd:PRK12316 866 HGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---- 941
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 580 IKGEAAFAFIVLKDNISDenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQ 650
Cdd:PRK12316 942 VDGKQLVGYVVLESEGGD---WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQ 1009
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
108-639 |
2.18e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 126.15 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFNQGlrggrvvelkkivdEAVKSCPTVQH--VLVAHRTDTKVPMGSLDIPLEQEMA 265
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADG--------------PHDRAEPTTRWwpLTVNVGGDSGPSGGTLSVHLDAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 266 KEAPVCTPESMSSEDMLFMlYTSGSTGTPKGLVHTQAGYllyAAMTHKLVFDYQPGDVFGCVADIGWITGHSYV--VYGP 343
Cdd:PRK05852 164 PTPATSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LCNGATTVLfestpvyPDAGRY-----WETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAW 418
Cdd:PRK05852 240 LASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 EWLHKVVG--------------DGRCTLVDTWWQTETGGICIAPRPSEDGAEIlpgMAMRPFFGIVPVlmDEKGNVLEGG 484
Cdd:PRK05852 313 QALQTEFAapvvcafgmteathQVTTTQIEGIGQTENPVVSTGLVGRSTGAQI---RIVGSDGLPLPA--GAVGEVWLRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 485 dvsgalcisqawPGMARTIYGD----HQRFVDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIED 560
Cdd:PRK05852 388 ------------TTVVRGYLGDptitAANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEG 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 561 AMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISdenMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRR 639
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP---PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
134-643 |
2.83e-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: 125.28 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFN 213
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 QGLRggrvvelkkIVDEAVKSCPTVQHVLvahRTDTKVPMgSLDIPLE-----QEMAKEAPVCTPESMSSEDMLFMLYTS 288
Cdd:TIGR03098 106 ERLD---------LLHPALPGCHDLRTLI---IVGDPAHA-SEGHPGEepaswPKLLALGDADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 289 GSTGTPKGLVHTQAGYLLYA-AMTHKLvfDYQPGDVFGCVADIGWITGHSYVVYGPLCnGATTVLFEstpvYPDAGRYWE 367
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAqSVATYL--ENRPDDRLLAVLPLSFDYGFNQLTTAFYV-GATVVLHD----YLLPRDVLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 368 TVQRLKINQFYGAPTAVRLLLKygDAWvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVdtWWQTETGGICIA 447
Cdd:TIGR03098 246 ALEKHGITGLAAVPPLWAQLAQ--LDW-PESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLM--YGLTEAFRSTYL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 448 P------RPSEDGAEIlpgmamrPFFGIvpVLMDEKGNVLEGGDvSGALCisQAWPGMARTIYGDHQRfVDAYFRAYPGY 521
Cdd:TIGR03098 321 PpeevdrRPDSIGKAI-------PNAEV--LVLREDGSECAPGE-EGELV--HRGALVAMGYWNDPEK-TAERFRPLPPF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 Y----------FTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVL 591
Cdd:TIGR03098 388 PgelhlpelavWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTP 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 18034773 592 KDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:TIGR03098 468 PG---GEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
133-642 |
5.82e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.15 E-value: 5.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKcKAVITF 212
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE-PRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 NQGLRGGR--VVELKKIVDEAvkscptvqhvlvahrtdtkvpmgsldiplEQEMAKEAPVCTPESMSsedmlFMLYTSGS 290
Cdd:PRK09088 101 DDAVAAGRtdVEDLAAFIASA-----------------------------DALEPADTPSIPPERVS-----LILFTSGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 291 TGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfeSTPVYPDAGRYWETVQ 370
Cdd:PRK09088 147 SGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILV--SNGFEPKRTLGRLGDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 371 RLKINQFYGAPTAVRLLLKYGDawvkkYDRSSLRTLGSV---GEPinHEAWE---WLhkvvgDGRCTLVDTWWQTETGGI 444
Cdd:PRK09088 224 ALGITHYFCVPQMAQAFRAQPG-----FDAAALRHLTALftgGAP--HAAEDilgWL-----DDGIPMVDGFGMSEAGTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 445 CIAPRPSEDGAEILpGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQawPGMARTIYGDHQRFVDAYFRAypGYYFT 524
Cdd:PRK09088 292 FGMSVDCDVIRAKA-GAAGIPTPTVQTRVVDDQGNDCPAG-VPGELLLRG--PNLSPGYWRRPQATARAFTGD--GWFRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 525 GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDEnmvVNE 604
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLD---LER 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 18034773 605 LKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
109-643 |
1.16e-29 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 122.42 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALiwerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHtvv 188
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 fagfsaeslagrindakckavitfnqglrggrvvelkkivdeavksCPTvqhvlvahrtDTKVPMGSLDIPLEQEMAKEA 268
Cdd:cd17653 75 ----------------------------------------------VPL----------DAKLPSARIQAILRTSGATLL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 pVCTPesmSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLvFDYQPGDVFGCVADIGW--ITGhsyVVYGPLCN 346
Cdd:cd17653 99 -LTTD---SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 347 GATTVLfeSTPVYPdagryWETVQRlKINQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPINHeawewlhkvvg 426
Cdd:cd17653 171 GGTLVL--ADPSDP-----FAHVAR-TVDALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEAVPP----------- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 427 dgrcTLVDTWWQ----------TETGgICIAPRPSEDGAEILPGMAMRpffGIVPVLMDEKGN-VLEGgdVSGALCISQa 495
Cdd:cd17653 224 ----SLLDRWSPgrrlynaygpTECT-ISSTMTELLPGQPVTIGKPIP---NSTCYILDADLQpVPEG--VVGEICISG- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 wPGMARTIYGDHQ----RFVDAYFraYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAM-ADHPAV 568
Cdd:cd17653 293 -VQVARGYLGNPAltasKFVPDPF--WPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEV 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 569 PETAVIgyphdIKGEAAFAFIVlkdnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd17653 370 TQAAAI-----VVNGRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
134-642 |
2.40e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.21 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMP---VSPLAVAAMLacaRIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 tfnqglrggrVVELKKIVDEAVKSCPTVQHVLVA-----------------HRTDTKVPMGSLD--IPLEQEMAKEAPVC 271
Cdd:PRK07059 126 ----------VLENFATTVQQVLAKTAVKHVVVAsmgdllgfkghivnfvvRRVKKMVPAWSLPghVRFNDALAEGARQT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 -TPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYL---LYAAMTHKLVFDYQPGD---VFGCVADIgwitghsYVVYGPL 344
Cdd:PRK07059 196 fKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPL-------YHIFALT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 345 CN-------GATTVLFestPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR-TLG---SVGEPI 413
Cdd:PRK07059 269 VCgllgmrtGGRNILI---PNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIvANGggmAVQRPV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 414 nheAWEWLHKVvgdgRCTLVDTWWQTETGGICIAPRPSEDGAEILPGMAMrPFFGIVpvLMDEKGNVLEGGDVsGALCIS 493
Cdd:PRK07059 344 ---AERWLEMT----GCPITEGYGLSETSPVATCNPVDATEFSGTIGLPL-PSTEVS--IRDDDGNDLPLGEP-GEICIR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 494 --QAWPG-------MARTIYGDhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMAD 564
Cdd:PRK07059 413 gpQVMAGywnrpdeTAKVMTAD-------------GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 565 HPAVPETAVIGYPHDIKGEAAFAFIVLKD-NISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFVVKKDpALTEE-----DVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
108-575 |
3.03e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 123.29 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFNQGLrggrvveLKKiVDEAVKSCPTVQHVLV----AHRTDTKVpmgsldIPLEQE 263
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVldprGLRDDPRL------LSLDEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 264 MAKEAPVCTPE-------SMSSEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGH 336
Cdd:COG1022 161 LALGREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTLSFLPLAHVFER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 337 SYVVYGpLCNGATTVLFESTP-VYPDAG-----------RYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLR 404
Cdd:COG1022 240 TVSYYA-LAAGATVAFAESPDtLAEDLRevkptfmlavpRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 405 TLG-SVGEPINHEAWEWL--HKV---VGdGRC-----------------------TLVDTWWQTETGGICIAPRPSedga 455
Cdd:COG1022 319 GKSpSLLLRLKHALADKLvfSKLreaLG-GRLrfavsggaalgpelarffralgiPVLEGYGLTETSPVITVNRPG---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 456 EILPGMAMRPFFGiVPVLMDEKGNVLeggdVSGalcisqawPGM-----------ARTIYGDhqrfvdayfraypGYYFT 524
Cdd:COG1022 394 DNRIGTVGPPLPG-VEVKIAEDGEIL----VRG--------PNVmkgyyknpeatAEAFDAD-------------GWLHT 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 525 GDGAHRTEGGYYQITGRMDDVINISGhrlGT----AEIEDAMADHPAVPETAVIG 575
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
133-642 |
4.92e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 121.73 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYM----PVSPLAVAAMlacaRIGAIHTVVFAGFSAESLAGRINDAKCKA 208
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMrndfAFFEAAYAAM----RLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 VITFNQGLRGgrvveLKKIVDEAVK--SCPTVQHVLVAHRTD---TKVPMGSLDIP--LEQEMAKEAPVcTPESMSsedm 281
Cdd:PRK12406 87 LIAHADLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISpalLTPPAGAIDWEgwLAQQEPYDGPP-VPQPQS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 282 lfMLYTSGSTGTPKGlVHTQAGYLLYAAMTHKLVfdyqpgdvfgcVADIGWITGHSYVVYGPLCN-------------GA 348
Cdd:PRK12406 157 --MIYTSGTTGHPKG-VRRAAPTPEQAAAAEQMR-----------ALIYGLKPGIRALLTGPLYHsapnayglragrlGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TTVLfesTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP----INHEAWEWLHKV 424
Cdd:PRK12406 223 VLVL---QPRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPcpadVKRAMIEWWGPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 425 VgdgrctlVDTWWQTETGGICIAPrpSEDgAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISqawPGMARTIY 504
Cdd:PRK12406 299 I-------YEYYGSTESGAVTFAT--SED-ALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI---AGNPDFTY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 505 GDHQRFVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAMADHPAVPETAVIGYPHDI 580
Cdd:PRK12406 366 HNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMV-ISG---GVniypAEIEAVLHAVPGVHDCAVFGIPDAE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034773 581 KGEAAFAFIVLKDNIS-DENMVVNELKLSVAtkiaKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK12406 440 FGEALMAVVEPQPGATlDEADIRAQLKARLA----GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-648 |
6.29e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 118.74 E-value: 6.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 278 SEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfeSTP 357
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVL--AGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 358 V-YPDAGRY---WETVQRLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTL 432
Cdd:cd05944 78 AgYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVELRARFEDATG---LPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 433 VDTWWQTETggICIAPRPSEDGAEILPGMAMR-PFFGIVPVLMDEKGNVLE--GGDVSGALCIsqAWPGMAR-TIYGDHQ 508
Cdd:cd05944 150 VEGYGLTEA--TCLVAVNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRdcAPDEVGEICV--AGPGVFGgYLYTEGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 509 RFVDAYfrayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAF 588
Cdd:cd05944 226 KNAFVA----DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAY 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 589 IVLKDNISDENmvvNELKLSVATKIA-KYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:cd05944 302 VQLKPGAVVEE---EELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
283-643 |
8.42e-29 |
|
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: 117.43 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 283 FMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLV-FDyqPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPD 361
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 362 AGRYWETVQRLkinqfygAPTAVRLLLKYG--DAWVKkydrsSLRTLGSVGEPINHEawewLHKVVGDGRCTLVDTWWQT 439
Cdd:cd17630 82 LAPPGVTHVSL-------VPTQLQRLLDSGqgPAALK-----SLRAVLLGGAPIPPE----LLERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 440 ETGGICIAPRPSEDGA----EILPGMAMRpffgivpvlmdekgnVLEGGDVsgalcisqaWPGMARTIYGDHQRFVDAYF 515
Cdd:cd17630 146 ETASQVATKRPDGFGRggvgVLLPGRELR---------------IVEDGEI---------WVGGASLAMGYLRGQLVPEF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 516 RAyPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNI 595
Cdd:cd17630 202 NE-DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18034773 596 SDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd17630 281 DPA-----ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
279-642 |
2.53e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 116.61 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 279 EDMLFMLYTSGSTGTPKG--LVH---TQAGYLLYAAMthklvfDYQPGDV----------FGCVADIGWITGHsyvvygp 343
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGatLTHhniVNNGYFIGERL------GLTEQDRlcipvplfhcFGSVLGVLACLTH------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 lcnGATTVLFEstPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEAWEWLHK 423
Cdd:cd05917 69 ---GATMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELMKRVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 VVGDGRCTLVdtWWQTETGGICIAPRPsEDGAE--------ILPGMAMRpffgivpvLMDEKGNVLEGGDVSGALCISQA 495
Cdd:cd05917 141 VMNMKDVTIA--YGMTETSPVSTQTRT-DDSIEkrvntvgrIMPHTEAK--------IVDPEGGIVPPVGVPGELCIRGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 496 wpGMARTIYGDHQRFVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIG 575
Cdd:cd05917 210 --SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 576 YPHDIKGEAAFAFIVLKDNisdENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05917 286 VPDERYGEEVCAWIRLKEG---AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
116-644 |
5.63e-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: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd17642 31 PGTIAFT----DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITFNQGLRggRVVELKKIVdeavkscPTVQHVLV-AHRTDTKVPMgSLDIPLEQEMA---KEAPVC 271
Cdd:cd17642 107 ELDHSLNISKPTIVFCSKKGLQ--KVLNVQKKL-------KIIKTIIIlDSKEDYKGYQ-CLYTFITQNLPpgfNEYDFK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 TPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHS-YVVYGPLCNGATT 350
Cdd:cd17642 177 PPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGmFTTLGYLICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 351 VL---FESTpvypdagRYWETVQRLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVV-- 425
Cdd:cd17642 257 VLmykFEEE-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFkl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 -----GDGrctLVDTwwqteTGGICIAP----RPSEDGAeilpgmaMRPFFGiVPVLMDEKGNVLeGGDVSGALCISQaw 496
Cdd:cd17642 328 pgirqGYG---LTET-----TSAILITPegddKPGAVGK-------VVPFFY-AKVVDLDTGKTL-GPNERGELCVKG-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 497 PGMARTIYGDHQRFVDAYFRayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGY 576
Cdd:cd17642 389 PMIMKGYVNNPEATKALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 577 PHDIKGEAAFAFIVLKDNIS-DENMVVNELKLSVATkiAKYaVPDQILVVKRLPKTRSGKVMRRLLRKI 644
Cdd:cd17642 467 PDEDAGELPAAVVVLEAGKTmTEKEVMDYVASQVST--AKR-LRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
111-642 |
8.58e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 117.80 E-value: 8.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 111 HVQKSPETIALIWErdEPGTEVriTYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFA 190
Cdd:PRK13390 6 HAQIAPDRPAVIVA--ETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 191 GFSAESLAGRINDAKCKAVITfnqglrggrVVELKKIVDEAVKSCPTvqHVLVAHRTDTkvpMGSLdiplEQEMAKEAPV 270
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVA---------SAALDGLAAKVGADLPL--RLSFGGEIDG---FGSF----EAALAGAGPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 271 CTPESMSSedmlFMLYTSGSTGTPKGLVHTQAGYLLYaamthklvfdyQPGDVFGCVADIGWITGHSYVVY--------G 342
Cdd:PRK13390 144 LTEQPCGA----VMLYSSGTTGFPKGIQPDLPGRDVD-----------APGDPIVAIARAFYDISESDIYYssapiyhaA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PL--CN-----GATTVLFESTpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP--- 412
Cdd:PRK13390 209 PLrwCSmvhalGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpv 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 -INHEAWEWLHKVVgdgrctlVDTWWQTETGGICIAprpseDGAEIL--PGMAMRPFFGIVPVLmDEKGNVLEGGDVSGA 489
Cdd:PRK13390 285 dVKHAMIDWLGPIV-------YEYYSSTEAHGMTFI-----DSPDWLahPGSVGRSVLGDLHIC-DDDGNELPAGRIGTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 490 LCISQAWPgmaRTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVP 569
Cdd:PRK13390 352 YFERDRLP---FRYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVH 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034773 570 ETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK13390 429 DVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
110-647 |
2.18e-27 |
|
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: 116.10 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAihtvV 188
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRindakckavitfnqglrggrvveLKKIVDEaVKScptvqHVLVAHrtdtkvpmgsldipleqemakea 268
Cdd:cd05918 76 FVPLDPSHPLQR-----------------------LQEILQD-TGA-----KVVLTS----------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 pvctpesmSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLyAAMTHKLVFDYQPG-----------DVfgCVADIgwitghs 337
Cdd:cd05918 104 --------SPSDAAYVIFTSGSTGKPKGVVIEHRALST-SALAHGRALGLTSEsrvlqfasytfDV--SILEI------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 338 yvvYGPLCNGATTVlfestpVYPDAGRyW----ETVQRLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVG 410
Cdd:cd05918 166 ---FTTLAAGGCLC------IPSEEDR-LndlaGFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 411 EPINHEAWE-WLHKVvgdgrcTLVDTWWQTET--GGICIAPRPSEDGAEILPGMAMRPFfgIVpvlmdEKGN----VLEG 483
Cdd:cd05918 225 EALTQSDVDtWADRV------RLINAYGPAECtiAATVSPVVPSTDPRNIGRPLGATCW--VV-----DPDNhdrlVPIG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 484 GdvSGALCISQawPGMARTIYGDHQR----FV-DAYFRAYPGY------YFTGDGAHRTEGGYYQITGRMDDVINISGHR 552
Cdd:cd05918 292 A--VGELLIEG--PILARGYLNDPEKtaaaFIeDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQR 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 553 LGTAEIEDAMADHPAVPETAVIGY--PHDIKGEAAF-AFIVLKDNISDENM--------------VVNELKLSVATKIAK 615
Cdd:cd05918 368 VELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLvAFVVLDGSSSGSGDgdslflepsdefraLVAELRSKLRQRLPS 447
|
570 580 590
....*....|....*....|....*....|..
gi 18034773 616 YAVPDQILVVKRLPKTRSGKVMRRLLRKIITS 647
Cdd:cd05918 448 YMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
112-641 |
2.92e-27 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 115.89 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:cd17655 7 AEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVIT---FNQGLRGGRVVELkkIVDEAVKscptvqhvlvaHRTDTKVPmgsldipleqemakea 268
Cdd:cd17655 81 YPEERIQYILEDSGADILLTqshLQPPIAFIGLIDL--LDEDTIY-----------HEESENLE---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 PVCtpesmSSEDMLFMLYTSGSTGTPKG-------LVH-----TQAGYL---LYAAMTHKLVFDYQPGDVFGCVadigwI 333
Cdd:cd17655 132 PVS-----KSDDLAYVIYTSGSTGKPKGvmiehrgVVNlvewaNKVIYQgehLRVALFASISFDASVTEIFASL-----L 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 334 TGHSYVVYG--PLCNGATTVlfestpvypdagrywETVQRLKINQFYGAPTAVRLLlkygdAWVKKYDRSSLRTLGSVGE 411
Cdd:cd17655 202 SGNTLYIVRkeTVLDGQALT---------------QYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 412 PINHE-AWEWLHKVvgDGRCTLVDTWWQTETggiCIaprpsedGAEILPGMAMRPFFGIVPV----------LMDEKGNV 480
Cdd:cd17655 262 ALSTElAKKIIELF--GTNPTITNAYGPTET---TV-------DASIYQYEPETDQQVSVPIgkplgntriyILDQYGRP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 481 LEGGdVSGALCISQAwpGMARTiYGDH-----QRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGT 555
Cdd:cd17655 330 QPVG-VAGELYIGGE--GVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIEL 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 556 AEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVlkdniSDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGK 635
Cdd:cd17655 406 GEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGK 480
|
....*.
gi 18034773 636 VMRRLL 641
Cdd:cd17655 481 VDRKAL 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
116-648 |
2.92e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.11 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSA 194
Cdd:PRK06839 16 PDRIAIITEEEE------MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 195 ESLAGRINDAkckavitfnqglrGGRVVELKKIVDEAVKSCPTVQHVlvahrtdtkVPMGSLDIPLEQEMAKEAPVCTPe 274
Cdd:PRK06839 90 NELIFQLKDS-------------GTTVLFVEKTFQNMALSMQKVSYV---------QRVISITSLKEIEDRKIDNFVEK- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 275 smSSEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfe 354
Cdd:PRK06839 147 --NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 355 stPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEawewLHKVVGDGRCTLVD 434
Cdd:PRK06839 222 --PRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEE----LMREFIDRGFLFGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 435 TWWQTETggiciAPRP---SEDGAEILPGMAMRP-FFGIVPVLMDEKGNVLEGG----DVSGALCISQAW---PGMARTI 503
Cdd:PRK06839 294 GFGMTET-----SPTVfmlSEEDARRKVGSIGKPvLFCDYELIDENKNKVEVGEvgelLIRGPNVMKEYWnrpDATEETI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 504 YGdhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGE 583
Cdd:PRK06839 369 QD--------------GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 584 AAFAFIVLKdniSDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:PRK06839 435 IPIAFIVKK---SSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
116-641 |
5.06e-27 |
|
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: 114.66 E-value: 5.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:cd17652 1 PDAPAVVFG------DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpes 275
Cdd:cd17652 75 RIAYMLADARPALLLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 mSSEDMLFMLYTSGSTGTPKGLV--HTQAGYLLYAAMTHklvFDYQPGDVFGCVADIGWiTGHSYVVYGPLCNGATTVLF 353
Cdd:cd17652 91 -TPDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSF-DASVWELLMALLAGATLVLA 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 354 ESTPVYPDAGrYWETVQRLKINQFYGAPTAVrlllkygdAWVKKYDRSSLRTLGSVGEPINHE-AWEWlhkvvGDGRCtL 432
Cdd:cd17652 166 PAEELLPGEP-LADLLREHRITHVTLPPAAL--------AALPPDDLPDLRTLVVAGEACPAElVDRW-----APGRR-M 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 433 VDTWWQTETGGICIAPRPSEDGAEILPGmamRPFFGIVPVLMDEKGNVLEGGdVSGALCIsqAWPGMARTiYGDH----- 507
Cdd:cd17652 231 INAYGPTETTVCATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPG-VPGELYI--AGAGLARG-YLNRpglta 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 508 QRFVDAYFRAyPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAA 585
Cdd:cd17652 304 ERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRL 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 586 FAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17652 383 VAYVVPAP---GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
112-651 |
6.81e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.57 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:PRK12467 522 ARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVITFNQGLRGGRVVelkkivdeavkscptvqhvlvahrtdTKVPMGSLDIPLEQeMAKEAPVC 271
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPVP--------------------------AGLRSLCLDEPADL-LCGYSGHN 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 TPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLvFDYQPGDVFGCVADIGWITGHsYVVYGPLCNGATTV 351
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALASGATLH 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 352 LFESTPVYpDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInheAWEWLHKVV--GDGr 429
Cdd:PRK12467 727 LLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEAL---QVDLLARVRalGPG- 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 430 CTLVDTWWQTETGGICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQAwpGMARtiyGDHQR 509
Cdd:PRK12467 798 ARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGA--GLAR---GYHRR 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 510 -------FVDAYFRAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDiK 581
Cdd:PRK12467 872 paltaerFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-A 950
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034773 582 GEAAFAFIVLKDNISD--ENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQD 651
Cdd:PRK12467 951 GLQLVAYLVPAAVADGaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQA 1022
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-643 |
7.00e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.75 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:PRK12316 4561 ARMTPDAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVITFNQGLRGGRVvelkkivdeavkscPTVQHVLVAHRTDTKVPMGSLDiPLEQEMAkeapvc 271
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRLPI--------------PDGLASLALDRDEDWEGFPAHD-PAVRLHP------ 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 tpesmssEDMLFMLYTSGSTGTPKG-----------LVHTQAGYLLYAA--MTHKLVFDYqpgDVFGcvadIGWitghsy 338
Cdd:PRK12316 4694 -------DNLAYVIYTSGSTGRPKGvavshgslvnhLHATGERYELTPDdrVLQFMSFSF---DGSH----EGL------ 4753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 339 vvYGPLCNGATTVLFESTPVYPDAGRYWETVQRLKINQFygAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPIN---- 414
Cdd:PRK12316 4754 --YHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVF--PPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAqasy 4826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 415 HEAWE-----WLHKVVGDGRCTLVDTWWQTETGGICiaprpsedGAEILPgmAMRPFFGIVPVLMDEKGNVLEGGdVSGA 489
Cdd:PRK12316 4827 DLAWRalkpvYLFNGYGPTETTVTVLLWKARDGDAC--------GAAYMP--IGTPLGNRSGYVLDGQLNPLPVG-VAGE 4895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 490 LCISQAwpGMARtiyGDH-------QRFVDAYFRAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 561
Cdd:PRK12316 4896 LYLGGE--GVAR---GYLerpaltaERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEAR 4970
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 562 MADHPAVPETAVIGYPHDIkGEAAFAFIV-----LKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKV 636
Cdd:PRK12316 4971 LREHPAVREAVVIAQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
....*..
gi 18034773 637 MRRLLRK 643
Cdd:PRK12316 5050 DRKALPQ 5056
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
108-638 |
9.73e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 114.91 E-value: 9.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITFNqGLRGGRVV--------ELKKIVDEAVKSC--PTVQHVLvahRTDTKVPMGSLD 257
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVamlyelapELATCEPGQLQSArlPELRRVI---FLGDEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 258 IPLEQEMAKEAPVCT----PESMSSEDMLFMLYTSGSTGTPKG--LVH---TQAGYLLYAAMthklvfDYQPGD------ 322
Cdd:PRK08315 174 FDELLALGRAVDDAElaarQATLDPDDPINIQYTSGTTGFPKGatLTHrniLNNGYFIGEAM------KLTEEDrlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 323 ----VFGCVadIGwitghsyvVYGPLCNGATTVlfestpvYP----DAGRYWETVQRLKINQFYGAPTAVRLLLKYGDaw 394
Cdd:PRK08315 248 plyhCFGMV--LG--------NLACVTHGATMV-------YPgegfDPLATLAAVEEERCTALYGVPTMFIAELDHPD-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 395 VKKYDRSSLRT---LGSVGePInheawEWLHKVVGDGRCTLVdT--WWQTETGGICIAPRPsEDGAE--------ILPGM 461
Cdd:PRK08315 309 FARFDLSSLRTgimAGSPC-PI-----EVMKRVIDKMHMSEV-TiaYGMTETSPVSTQTRT-DDPLEkrvttvgrALPHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 462 AmrpffgiVPVLMDEKGNVLEGGdVSGALC-----ISQAWPGM----ARTIYGDhqrfvdayfraypGYYFTGDGAHRTE 532
Cdd:PRK08315 381 E-------VKIVDPETGETVPRG-EQGELCtrgysVMKGYWNDpektAEAIDAD-------------GWMHTGDLAVMDE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 533 GGYYQITGRMDDVI-----NISGhRlgtaEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELKL 607
Cdd:PRK08315 440 EGYVNIVGRIKDMIirggeNIYP-R----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP---GATLTEEDVRD 511
|
570 580 590
....*....|....*....|....*....|....*
gi 18034773 608 SVATKIAKYAVPDQILVVKRLPKTRSGKV----MR 638
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKIqkfkMR 546
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
114-642 |
1.52e-26 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 113.82 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 114 KSPETIALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFS 193
Cdd:PRK07514 14 ADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 194 AESLAGRINDAKCKAVItfnqgLRGGRVVELKKIVDEAvkscpTVQHV--LVAHRTdtkvpmGSLdiplEQEMAKEAPVC 271
Cdd:PRK07514 89 LAELDYFIGDAEPALVV-----CDPANFAWLSKIAAAA-----GAPHVetLDADGT------GSL----LEAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 272 TPESMSSEDMLFMLYTSGSTGTPKGLVHTQaGYLLYAAMTHKLVFDYQPGDV-------------FgcVAdigwitghSY 338
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSH-GNLLSNALTLVDYWRFTPDDVlihalpifhthglF--VA--------TN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 339 VVygpLCNGATTVL---FESTPV---YPDAgryweTVqrlkinqFYGAPT-AVRLLlkyGDAWVKKYDRSSLRTLGSVGE 411
Cdd:PRK07514 218 VA---LLAGASMIFlpkFDPDAVlalMPRA-----TV-------MMGVPTfYTRLL---QEPRLTREAAAHMRLFISGSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 412 PI---NHEAWEwlhKVVGDgrcTLVDTWWQTETGGICIAPRpseDGAEI-------LPGMAMRpffgivpVLMDEKGNVL 481
Cdd:PRK07514 280 PLlaeTHREFQ---ERTGH---AILERYGMTETNMNTSNPY---DGERRagtvgfpLPGVSLR-------VTDPETGAEL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 482 EGGD-----VSGALCISQAW--PGMARtiygdhqrfvdAYFRAyPGYYFTGDGAHRTEGGYYQITGRMDDVInISG-HRL 553
Cdd:PRK07514 344 PPGEigmieVKGPNVFKGYWrmPEKTA-----------EEFRA-DGFFITGDLGKIDERGYVHIVGRGKDLI-ISGgYNV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 554 GTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS-DENMVVNELKlsvaTKIAKYAVPDQILVVKRLPKTR 632
Cdd:PRK07514 411 YPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAlDEAAILAALK----GRLARFKQPKRVFFVDELPRNT 486
|
570
....*....|
gi 18034773 633 SGKVMRRLLR 642
Cdd:PRK07514 487 MGKVQKNLLR 496
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
115-641 |
2.96e-26 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 112.95 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 115 SPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSA 194
Cdd:cd17656 1 TPDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 195 ESLAGRINDAKCKAVITFNQglrggrvvelkkivdEAVKSCPTVQHVLVAHRTDTKVPMGSLDIpleqemakeapvctpe 274
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQRH---------------LKSKLSFNKSTILLEDPSISQEDTSNIDY---------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 275 SMSSEDMLFMLYTSGSTGTPKGLVhtqagyLLYAAMTHKLVFDY-QPGDVFGcvADIGWITGHSYVV-----YGPLCNGA 348
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQ------LEHKNMVNLLHFEReKTNINFS--DKVLQFATCSFDVcyqeiFSTLLSGG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TTVLFeSTPVYPDAGRYWETVQRLKINQFYgAPTAVRLLLkygdAWVKKYDRS---SLRTLGSVGEP--INHEAWEWLHK 423
Cdd:cd17656 196 TLYII-REETKRDVEQLFDLVKRHNIEVVF-LPVAFLKFI----FSEREFINRfptCVKHIITAGEQlvITNEFKEMLHE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 vvgdGRCTLVDTWWQTETGGICIAPRPSEDGAEILPGMAmRPFFGIVPVLMDEKGNVLEGGDVsGALCISQAwpGMARTI 503
Cdd:cd17656 270 ----HNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIG-KPISNTWIYILDQEQQLQPQGIV-GELYISGA--SVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 504 YGD----HQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHD 579
Cdd:cd17656 342 LNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034773 580 IKGEAAFAFIVLKDNISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17656 422 KGEKYLCAYFVMEQELNIS-----QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
111-642 |
3.33e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.06 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 111 HVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFA 190
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 191 GFSAESLAGRINDAKCKAVItfnqglrggrvvelkkiVDEAVKSCPTVQHVLV-----AHRTDTKVPMGSLDIPleqEMA 265
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETPKIvidaaAQADSRRLAQGGLEIP---PQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 266 KEAPvctpesmssEDMLFMLYTSGSTGTPKGLVHTQaGYLLYAAMTHklvfdyqpgdvfgcVADIGWITGHSYVVYGPLC 345
Cdd:PRK06145 145 AVAP---------TDLVRLMYTSGTTDRPKGVMHSY-GNLHWKSIDH--------------VIALGLTASERLLVVGPLY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 346 N-GA-----TTVLFESTPVYP----DAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWvkKYDRSSLRTLGSVGEPINH 415
Cdd:PRK06145 201 HvGAfdlpgIAVLWVGGTLRIhrefDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEKTPE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 416 EAWEWLHKVVGDGRctLVDTWWQTETggiCIAPRPSEDGAEILP-GMAMRPFFGIVPVLMDEKGNVLEGGdVSGALCISQ 494
Cdd:PRK06145 279 SRIRDFTRVFTRAR--YIDAYGLTET---CSGDTLMEAGREIEKiGSTGRALAHVEIRIADGAGRWLPPN-MKGEICMRG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 495 awPGMARTIYGDHQRFVDAYfraYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVI 574
Cdd:PRK06145 353 --PKVTKGYWKDPEKTAEAF---YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 575 GYPHDIKGEAAFAFIVLKDNISdenMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGAT---LTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
135-638 |
1.18e-25 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 110.23 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfnq 214
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 215 glrggrvvelkkivdeavKSCPTVQHVLvahrtdtkvpmgSLDIPlEQEMAKEAPVCTPESMSSEDMLFMLYTSGSTGTP 294
Cdd:TIGR01923 78 ------------------DSLLEEKDFQ------------ADSLD-RIEAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 295 KGLVHTQaGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSyVVYGPLCNGATTVLfestpVYPDAgRYWETVQRLKI 374
Cdd:TIGR01923 127 KAVPHTF-RNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLS-ILFRWLIEGATLRI-----VDKFN-QLLEMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 375 NQFYGAPTAVRLLLKygdawvKKYDRSSLRTLGSVGEPINHEawewLHKVVGDGRCTLVDTWWQTETGGICIAPRPSEDG 454
Cdd:TIGR01923 199 THISLVPTQLNRLLD------EGGHNENLRKILLGGSAIPAP----LIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 455 AEILPGmamRPFFGI-VPVLMDEKGNVLEggdvsgalcISQAWPGMARTiYGDHQRFVDAYFRAypGYYFTGDGAHRTEG 533
Cdd:TIGR01923 269 ARPDVG---RPLAGReIKIKVDNKEGHGE---------IMVKGANLMKG-YLYQGELTPAFEQQ--GWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 534 GYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDEnmvvnELKLSVATKI 613
Cdd:TIGR01923 334 GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQA-----KLIAYLTEKL 408
|
490 500
....*....|....*....|....*
gi 18034773 614 AKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:TIGR01923 409 AKYKVPIAFEKLDELPYNASGKILR 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
109-650 |
1.22e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.90 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:PRK12316 3064 EEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdEAVKSCPTVQHVLVahrtdtkvpmgsLDIPLEQEMAKEA 268
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLS------------------QSHLRLPLAQGVQV------------LDLDRGDENYAEA 3187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 PvcTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLvFDYQPGDVFGCVADIGWiTGHSYVVYGPLCNGA 348
Cdd:PRK12316 3188 N--PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TTVLfESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINHEAwewLHKVVGDG 428
Cdd:PRK12316 3264 RVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA----HRCTSLKRIVCGGEALPADL---QQQVFAGL 3335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 429 rcTLVDTWWQTETGGICIAPRPSEDGAEILPgmAMRPFFGIVPVLMDEKGNVLEGGDVsGALCIsqAWPGMARtiyGDHQ 508
Cdd:PRK12316 3336 --PLYNLYGPTEATITVTHWQCVEEGKDAVP--IGRPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR---GYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 509 R-------FVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIgyphDIK 581
Cdd:PRK12316 3406 RpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVD 3481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 582 GEAAFAFIVLKDNISDenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQ 650
Cdd:PRK12316 3482 GRQLVAYVVPEDEAGD---LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ 3547
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
108-644 |
1.29e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.72 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAkckavitfnqglrggrvvelkkivdeAVKSCPTVQHVLvahrTDTKVPMGSLDIPLEQ-EMAK 266
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDS--------------------------GVKLLLTQAHLL----EQLPAPAGDTALTLDRlDLNG 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EAPVCTPESMSSEDMLFMLYTSGSTGTPKGL--------VHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADigwitghsy 338
Cdd:PRK12467 3225 YSENNPSTRVMGENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSFDGAQER--------- 3295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 339 vVYGPLCNGATTVLFESTPVYPDagRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINHEAW 418
Cdd:PRK12467 3296 -FLWTLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAGG----ADCASLDIYVFGGEAVPPAAF 3368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 E---------WLHKVVGDGRCTLVDTWWQTETGGICIAPRpsedgaeiLPgmAMRPFFGIVPVLMDEKGNVLEGGdVSGA 489
Cdd:PRK12467 3369 EqvkrklkprGLTNGYGPTEAVVTVTLWKCGGDAVCEAPY--------AP--IGRPVAGRSIYVLDGQLNPVPVG-VAGE 3437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 490 LCIsqAWPGMARtiyGDHQ-------RFVDAYFRAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 561
Cdd:PRK12467 3438 LYI--GGVGLAR---GYHQrpsltaeRFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEAR 3512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 562 MADHPAVPETAVIGYPHDiKGEAAFAFIVLKDNISDenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK12467 3513 LLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
...
gi 18034773 642 RKI 644
Cdd:PRK12467 3589 PDP 3591
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
131-643 |
1.86e-25 |
|
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: 110.47 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 tfnqglrggrvvelkkiVDEAvkscptvqhvlvaHRTDTKVPMGSLDIPLEQemakeapvctPESmsSEDMLFMLYTSGS 290
Cdd:cd12118 107 -----------------VDRE-------------FEYEDLLAEGDPDFEWIP----------PAD--EWDPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 291 TGTPKGLVHTQAG-YLlyAAMTHKLVFDYQPGDVFGCVADI----GWItghsyVVYGPLCNGATTVLFESTpvypDAGRY 365
Cdd:cd12118 145 TGRPKGVVYHHRGaYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC-----FPWTVAAVGGTNVCLRKV----DAKAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 366 WETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYD-RSSLRTLGSVGEPINHEAWEWLHKVVgdgrctlVDTWWQTETGG- 443
Cdd:cd12118 214 YDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDV-------THVYGLTETYGp 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 444 --ICiAPRPSEDGaeiLPG---MAMRPFFGIVPVLMDEkgnvLEGGDVSGAlcisQAWPGMARTI-------------YG 505
Cdd:cd12118 287 atVC-AWKPEWDE---LPTeerARLKARQGVRYVGLEE----VDVLDPETM----KPVPRDGKTIgeivfrgnivmkgYL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 506 DHQRFVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAA 585
Cdd:cd12118 355 KNPEATAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 586 FAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQIlVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd12118 433 CAFVELKE---GAKVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
108-648 |
2.73e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 110.46 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQksPETIALIW-ERdepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAaMLACARIGAIh 185
Cdd:PRK10946 31 LTRHAA--SDAIAVICgER-------QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYIT-FFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 186 tVVFAGFSAESL-----AGRINDAkckAVItfnqGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTdtkvpmgsLDIPL 260
Cdd:PRK10946 100 -PVNALFSHQRSelnayASQIEPA---LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDD--------GEHSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 261 EQEMAKEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLlYAAMTHKLVFDYQPGDVFGCVADigwiTGHSYVV 340
Cdd:PRK10946 164 DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSVRRSVEICGFTPQTRYLCALP----AAHNYPM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 341 YGPlcnGATTVLFESTPVY----PDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTL--------GS 408
Cdd:PRK10946 239 SSP---GALGVFLAGGTVVlapdPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLqvggarlsET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 409 VGEPINHEAWEWLHKVVG--DGrctLV------DTWWQT-ETGGiciapRPSEDGAEIlpgmamrpffGIVpvlmDEKGN 479
Cdd:PRK10946 316 LARRIPAELGCQLQQVFGmaEG---LVnytrldDSDERIfTTQG-----RPMSPDDEV----------WVA----DADGN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 480 VLEGGDVsGALcisqawpgMARTIYGdhqrfvdayFRAY---P----------GYYFTGDGAHRTEGGYYQITGRMDDVI 546
Cdd:PRK10946 374 PLPQGEV-GRL--------MTRGPYT---------FRGYyksPqhnasafdanGFYCSGDLVSIDPDGYITVVGREKDQI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 547 NISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisdenmvvnELKLSVATK------IAKYAVPD 620
Cdd:PRK10946 436 NRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE----------PLKAVQLRRflreqgIAEFKLPD 505
|
570 580
....*....|....*....|....*...
gi 18034773 621 QILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:PRK10946 506 RVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
133-650 |
7.76e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 109.32 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIhtVVFAG--FSAESLAGRINDAKCKAVI 210
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV--VVEHNplYTAHELEHPFEDHGARVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 TFN------QGLRGGrvVELKKIVD-EAVKSCPTVQhvlvahRTDTKVPMGSLD-------------IPLEQEMAKEAP- 269
Cdd:PRK05605 135 VWDkvaptvERLRRT--TPLETIVSvNMIAAMPLLQ------RLALRLPIPALRkaraaltgpapgtVPWETLVDAAIGg 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 270 ---VCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGD--------VFgcvadigwitgHSY 338
Cdd:PRK05605 207 dgsDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPervlaalpMF-----------HAY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 339 -----VVYGPLCnGATTVLFEStpvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTL--GSVGE 411
Cdd:PRK05605 276 gltlcLTLAVSI-GGELVLLPA----PDIDLILDAMKKHPPTWLPGVPPLYEKIAE--AAEERGVDLSGVRNAfsGAMAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 412 PINH-EAWEwlhKVVGdGRctLVDTWWQTETGGICIA--------------PRPS--------EDGAEILPGmamrpffg 468
Cdd:PRK05605 349 PVSTvELWE---KLTG-GL--LVEGYGLTETSPIIVGnpmsddrrpgyvgvPFPDtevrivdpEDPDETMPD-------- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 469 ivpvlmDEKGNVL-EGGDV-SGALCISQAwpgmartiygDHQRFVDAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVI 546
Cdd:PRK05605 415 ------GEEGELLvRGPQVfKGYWNRPEE----------TAKSFLDGWFR-------TGDVVVMEEDGFIRIVDRIKELI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 547 NISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLkdnisDENMVVNE--LKLSVATKIAKYAVPDQILV 624
Cdd:PRK05605 472 ITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVL-----EPGAALDPegLRAYCREHLTRYKVPRRFYH 546
|
570 580
....*....|....*....|....*.
gi 18034773 625 VKRLPKTRSGKVMRRLLRKIITSRGQ 650
Cdd:PRK05605 547 VDELPRDQLGKVRRREVREELLEKLG 572
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
110-643 |
1.09e-24 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 108.87 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVF 189
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 190 A---GFSAESLAGRINDAKCKAVITfnqglrggrVVELKKIVDEAVKSCPTVQHVLVAHrTDTKvpmgsldipleqeMAK 266
Cdd:cd05931 80 PptpGRHAERLAAILADAGPRVVLT---------TAAALAAVRAFAASRPAAGTPRLLV-VDLL-------------PDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFG----CVADIGWITGhsyvVYG 342
Cdd:cd05931 137 SAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFesTPVY----PdaGRYWETVQRLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPIN-- 414
Cdd:cd05931 212 PLYSGGPSVLM--SPAAflrrP--LRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVRpa 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 415 -----HEA-------WEWLH--------------KVVGDGRCTLVDTWWQTEtGGICIAPRPSEDGAEI------LPGMA 462
Cdd:cd05931 287 tlrrfAEAfapfgfrPEAFRpsyglaeatlfvsgGPPGTGPVVLRVDRDALA-GRAVAVAADDPAARELvscgrpLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 463 MRpffgIVPvlmDEKGNVLEGGDVsGALCISQawPGMARTIYGDhQRFVDAYFRAYP-----GYYFTGDGAHRTEGGYYq 537
Cdd:cd05931 366 VR----IVD---PETGRELPDGEV-GEIWVRG--PSVASGYWGR-PEATAETFGALAatdegGWLRTGDLGFLHDGELY- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 538 ITGRMDDVINISGHRLGTAEIEDAMAD-HPAVPETAVigyphdikgeAAFA---------FIVLKDNISDENMVVNELKL 607
Cdd:cd05931 434 ITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPGCV----------AAFSvpddgeerlVVVAEVERGADPADLAAIAA 503
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 18034773 608 SVATKIAK-YAV-PDQILVVKR--LPKTRSGKVMRRLLRK 643
Cdd:cd05931 504 AIRAAVAReHGVaPADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
132-644 |
1.44e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 108.37 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 132 VRITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAVAAMLacaRIGAIHTVVFAGFSAESLAGRINDAKCK 207
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPnvlQYPIAVFGAL---RAGLIVVNTNPLYTAREMRHQFKDSGAR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 208 AVITFNqgLRGGRVVELkkIVDEAVKSC---------PTVQHVLVAHRTDT---KVPMGSLD--IPLEQEMAKEAPV-CT 272
Cdd:PRK12492 125 ALVYLN--MFGKLVQEV--LPDTGIEYLieakmgdllPAAKGWLVNTVVDKvkkMVPAYHLPqaVPFKQALRQGRGLsLK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 273 PESMSSEDMLFMLYTSGSTGTPKGlvhtqagyllyAAMTH-KLVFDYQpgDVFGCVADIGwITGHsyvvygPLCNGATTV 351
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKG-----------AMLTHgNLVANML--QVRACLSQLG-PDGQ------PLMKEGQEV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 352 LFESTPVY------------------------P-DAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTL 406
Cdd:PRK12492 261 MIAPLPLYhiyaftancmcmmvsgnhnvlitnPrDIPGFIKELGKWRFSALLGLNTLFVALMDHPG--FKDLDFSALKLT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 407 GSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETGGICIApRPSEDGAEI------LPGMAMRpffgivpvLMDEKGNV 480
Cdd:PRK12492 339 NSGGTALVKATAERWEQLTG---CTIVEGYGLTETSPVAST-NPYGELARLgtvgipVPGTALK--------VIDDDGNE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 481 LEGGDvSGALCIS--QAWPGMARTIYGDHQrFVDAyfrayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEI 558
Cdd:PRK12492 407 LPLGE-RGELCIKgpQVMKGYWQQPEATAE-ALDA-----EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 559 EDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKdnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:PRK12492 480 EDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR----DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILR 555
|
....*.
gi 18034773 639 RLLRKI 644
Cdd:PRK12492 556 RELRDI 561
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
134-575 |
1.82e-24 |
|
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: 106.91 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfn 213
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakEAPvctpesmssEDMLFMLYTSGSTGT 293
Cdd:cd05907 84 -----------------------------------------------------EDP---------DDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDAgrywetVQRLK 373
Cdd:cd05907 102 PKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDD------LSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 374 INQFYGAPtavRLLLK-YGDAWVKK--------YDR---SSLRTLGSVGEPINHEAWEWLHKvVGdgrCTLVDTWWQTET 441
Cdd:cd05907 175 PTVFLAVP---RVWEKvYAAIKVKAvpglkrklFDLavgGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 442 GGICIAPRPsEDGAEILPGMAMRPffgiVPVLMDEKGNVLeggdVSGalcisqawPGMARTIYGDHQRFVDAYFRayPGY 521
Cdd:cd05907 248 SAVVTLNPP-GDNRIGTVGKPLPG----VEVRIADDGEIL----VRG--------PNVMLGYYKNPEATAEALDA--DGW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 522 YFTGDGAHRTEGGYYQITGRMDDVI-NISGHRLGTAEIEDAMADHPAVPETAVIG 575
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
134-642 |
2.13e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 107.93 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAV-AAMlacaRIGAIHTVVFAGFSAESLAGRINDAKCKA 208
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPnvlQYPVAVfGAM----RAGLIVVNTNPLYTAREMEHQFNDSGAKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 VITfnqglrggrvveLKKIVDEAVKSCPT--VQHVLVAHRTD------------------TKVPMGSLD--IPLEQEMAK 266
Cdd:PRK05677 126 LVC------------LANMAHLAEKVLPKtgVKHVIVTEVADmlpplkrllinavvkhvkKMVPAYHLPqaVKFNDALAK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EA--PVcTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGylLYAAMTH-KLVFDYQPGDvfGC--------VADIGWITG 335
Cdd:PRK05677 194 GAgqPV-TEANPQADDVAVLQYTGGTTGVAKGAMLTHRN--LVANMLQcRALMGSNLNE--GCeiliaplpLYHIYAFTF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 336 HSYVVygpLCNGATTVLFeSTPvyPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINH 415
Cdd:PRK05677 269 HCMAM---MLIGNHNILI-SNP--RDLPAMVKELGKWKFSGFVGLNTLFVALCNNEA--FRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 416 EAWEWLHKVVGdgrCTLVDTWWQTETGGI-CIAPRpsedgAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCIS- 493
Cdd:PRK05677 341 ATAERWKEVTG---CAICEGYGMTETSPVvSVNPS-----QAIQVGTIGIPVPSTLCKVIDDDGNELPLGEV-GELCVKg 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 494 -QAWPGmartiYGDHQRFVDAYFRAyPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETA 572
Cdd:PRK05677 412 pQVMKG-----YWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 573 VIGYPHDIKGEAAFAFIVLKDNisdENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK05677 486 AIGVPDEKSGEAIKVFVVVKPG---ETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
557-635 |
2.34e-24 |
|
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: 96.84 E-value: 2.34e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 557 EIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGK 635
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL---LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
134-643 |
5.00e-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: 105.12 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAvitfn 213
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmssEDMLFMLYTSGSTGT 293
Cdd:cd05912 77 -----------------------------------------------------------------DDIATIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTqAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGpLCNGATTVLFESTpvypDAGRYWETVQRLK 373
Cdd:cd05912 92 PKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLINSGK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 374 INQFYGAPTAV-RLLLKYGDAWvkkydRSSLRT--LGsvGEPINHEAWEwlhkvvgdgRCT-----LVDTWWQTETGGIC 445
Cdd:cd05912 166 VTIISVVPTMLqRLLEILGEGY-----PNNLRCilLG--GGPAPKPLLE---------QCKekgipVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 446 IAPRPsEDgAEILPGMAMRPFFGIVpvLMDEKGNVLEGGDvsGALCISQawPGMARTIYGDHQR----FVDAYFRaypgy 521
Cdd:cd05912 230 VTLSP-ED-ALNKIGSAGKPLFPVE--LKIEDDGQPPYEV--GEILLKG--PNVTKGYLNRPDAteesFENGWFK----- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 yfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDEnmv 601
Cdd:cd05912 297 --TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEE--- 371
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 18034773 602 vnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05912 372 --ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
108-641 |
2.79e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 106.02 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDakCKAVITFNQGLRGGRVvelkkivdeavkscPTVQHVLVahrtdtkvpmgsldIPLEQEMAKE 267
Cdd:PRK05691 1211 LDPDYPAERLAYMLAD--SGVELLLTQSHLLERL--------------PQAEGVSA--------------IALDSLHLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPE-SMSSEDMLFMLYTSGSTGTPKGLVHTqagyllYAAMTHKL-----VFDYQPGDVFGCVADIGWITGhSYVVY 341
Cdd:PRK05691 1261 WPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNT------HAALAERLqwmqaTYALDDSDVLMQKAPISFDVS-VWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 342 GPLCNGATTVLfESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINHEAWE-- 419
Cdd:PRK05691 1334 WPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA----AACTSLRRLFSGGEALPAELRNrv 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 420 -------WLHKVVGDGRCTLVDTWWQtetggiCIAprpsEDGAEILPGmamRPFFGIVPVLMDEKGNVLEGGdVSGALCI 492
Cdd:PRK05691 1409 lqrlpqvQLHNRYGPTETAINVTHWQ------CQA----EDGERSPIG---RPLGNVLCRVLDAELNLLPPG-VAGELCI 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 SQAwpGMARTIYG----DHQRFV-DAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPA 567
Cdd:PRK05691 1475 GGA--GLARGYLGrpalTAERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034773 568 VPETAVIGYpHDIKGEAAFAFIVLKDNISDENmvvNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK05691 1553 VAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
109-641 |
3.62e-23 |
|
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: 103.28 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITfnQGlrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakea 268
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT--QP----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 pvctpesmssEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPgDVFGCVADIGWITGhSYVVYGPLCNGA 348
Cdd:cd17644 106 ----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TTVLfESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINHEAWEWLHKVVGDg 428
Cdd:cd17644 174 TLVL-RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 429 RCTLVDTWWQTETGGICIAPRPSEDGAEILPGMAM-RPFFGIVPVLMDEKGNVLEGGdVSGALCISQAwpGMARTIYG-- 505
Cdd:cd17644 251 FIQLINVYGPTEATIAATVCRLTQLTERNITSVPIgRPIANTQVYILDENLQPVPVG-VPGELHIGGV--GLARGYLNrp 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 506 --DHQRFVDAYFRAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIK 581
Cdd:cd17644 328 elTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPG 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 582 GEAAFAFIVLKDNISdenMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17644 408 NKRLVAYIVPHYEES---PSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
108-643 |
3.82e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 104.19 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITfnqglrGGRVVELKkivdEAVKSCPTVQHVLVAHRTDTKV-PMGSLDipLEQeMAK 266
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIV------GEELVEAF----EEARADLARPPRLWVAGGDTLDdPEGYED--LAA-AAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 267 EAPVCTPES---MSSEDMLFMLYTSGSTGTPKGLVHTQAGYLL-YAAMTHKLvfDYQPGDVFGCVADIGWITGHSYVVYG 342
Cdd:PRK08279 184 GAPTTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKaMGGFGGLL--RLTPDDVLYCCLPLYHNTGGTVAWSS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFESTpvypDAGRYWETVQRlkinqfYGApTAV-------RLLLkygDAWVKKYDRS-SLRTLgsVGEPIN 414
Cdd:PRK08279 262 VLAAGATLALRRKF----SASRFWDDVRR------YRA-TAFqyigelcRYLL---NQPPKPTDRDhRLRLM--IGNGLR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 415 HEAWEWLHKVVGDGRctLVDTWWQTE--TGGICIAPRPSEDGaeILPGMAMRPfFGIV--------PVlMDEKGNVLEGG 484
Cdd:PRK08279 326 PDIWDEFQQRFGIPR--ILEFYAASEgnVGFINVFNFDGTVG--RVPLWLAHP-YAIVkydvdtgePV-RDADGRCIKVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 485 DVSGALCISQAwpgmartiyGDHQRFV--------------------DAYFRaypgyyfTGDGAHRTEGGYYQITGRMDD 544
Cdd:PRK08279 400 PGEVGLLIGRI---------TDRGPFDgytdpeasekkilrdvfkkgDAWFN-------TGDLMRDDGFGHAQFVDRLGD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 545 VINISGHRLGTAEIEDAMADHPAVPETAVIGYP---HDikGEAAFAFIVLKDnisDENMVVNELKLSVATKIAKYAVPDQ 621
Cdd:PRK08279 464 TFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgTD--GRAGMAAIVLAD---GAEFDLAALAAHLYERLPAYAVPLF 538
|
570 580
....*....|....*....|..
gi 18034773 622 ILVVKRLPKTRSGKVMRRLLRK 643
Cdd:PRK08279 539 VRLVPELETTGTFKYRKVDLRK 560
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
126-636 |
6.16e-23 |
|
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: 102.79 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 126 DEPGTEVriTYRELLETTCRLANTLKRhGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAK 205
Cdd:cd05909 2 DTLGTSL--TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 206 CKAVITFNQGLRGGRVVELKKIVDEAVkscptvqhvlVAHRTDTKVPMGSLD---------IPLEQEMAKEAPVCTpesm 276
Cdd:cd05909 79 IKTVLTSKQFIEKLKLHHLFDVEYDAR----------IVYLEDLRAKISKADkckaflagkFPPKWLLRIFGVAPV---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 277 SSEDMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfest 356
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKN-LLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 357 pvYPDAGRYW---ETVQRLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLV 433
Cdd:cd05909 220 --HPNPLDYKkipELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG---IRIL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 434 DTWWQTETGGICIAPRPSEDGAE-----ILPGMAMRpffgIVPVLMDEKGNVLEGG--DVSGalcisqawPGMARTIYGD 506
Cdd:cd05909 291 EGYGTTECSPVISVNTPQSPNKEgtvgrPLPGMEVK----IVSVETHEEVPIGEGGllLVRG--------PNVMLGYLNE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 HQRFVDAYFRaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADH-PAVPETAVIGYPHDIKGEAA 585
Cdd:cd05909 359 PELTSFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKI 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 18034773 586 FAFIVLKDNISDEnmVVNELKlsvATKIAKYAVPDQILVVKRLPKTRSGKV 636
Cdd:cd05909 436 VLLTTTTDTDPSS--LNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
134-642 |
7.19e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 103.03 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLAN-TLKRHGVHRGDRVAIYMPVS---PLAVAAMLaCARIGAI------------HTVVFAGFSA--- 194
Cdd:PRK08751 51 ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNClqyPIATFGVL-RAGLTVVnvnplytprelkHQLIDSGASVlvv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 195 -----ESLAGRINDAKCKAVITFNQG-LRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSldiplEQEMAkea 268
Cdd:PRK08751 130 idnfgTTVQQVIADTPVKQVITTGLGdMLGFPKAALVNFVVKYVKKLVPEYRINGAIRFREALALGR-----KHSMP--- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 pvctPESMSSEDMLFMLYTSGSTGTPKGlvhtqagyllyAAMTHK-LVFDYQPGDvfgcvadiGWITGHsyvvyGPLCNG 347
Cdd:PRK08751 202 ----TLQIEPDDIAFLQYTGGTTGVAKG-----------AMLTHRnLVANMQQAH--------QWLAGT-----GKLEEG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 ATTVLfESTPVY-------------------------PDAGRYWETVQRLKINQFYGAPTAVRLLLKygDAWVKKYDRSS 402
Cdd:PRK08751 254 CEVVI-TALPLYhifaltanglvfmkiggcnhlisnpRDMPGFVKELKKTRFTAFTGVNTLFNGLLN--TPGFDQIDFSS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 403 LR-TLGSvGEPINHEAWEWLHKVVGdgrCTLVDTWWQTETG-GICIAPR--PSEDGAEILPgmamrpffgiVP----VLM 474
Cdd:PRK08751 331 LKmTLGG-GMAVQRSVAERWKQVTG---LTLVEAYGLTETSpAACINPLtlKEYNGSIGLP----------IPstdaCIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 475 DEKGNVLEGGDVsGALCISQAwpgmaRTIYGDHQR------FVDAyfrayPGYYFTGDGAHRTEGGYYQITGRMDDVINI 548
Cdd:PRK08751 397 DDAGTVLAIGEI-GELCIKGP-----QVMKGYWKRpeetakVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 549 SGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKdnisDENMVVNELKLSVATKIAKYAVPDQILVVKRL 628
Cdd:PRK08751 466 SGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK----DPALTAEDVKAHARANLTGYKQPRIIEFRKEL 541
|
570
....*....|....
gi 18034773 629 PKTRSGKVMRRLLR 642
Cdd:PRK08751 542 PKTNVGKILRRELR 555
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
116-649 |
1.08e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 102.33 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITFNqglrggrvvELKKIVDEAVKSCPtVQHVLVAHRTDTKVPMGSL--DIPLEQEMAKEAPVCTP 273
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDT---------EFAEVAREALALLP-GPKPLVIDVDDPEYPGGRFigALDYEAFLASGDPDFAW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 274 ESMSSE-DMLFMLYTSGSTGTPKGLV-HTQAGYLlyAAMTHKLVFDYQPGDV-------FGCVadiGWitGHSYVVygpL 344
Cdd:PRK08162 176 TLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL--NALSNILAWGMPKHPVylwtlpmFHCN---GW--CFPWTV---A 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 345 CNGATTVLFESTpvypDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRS-SLRTLG-----SVGEPINHEAW 418
Cdd:PRK08162 246 ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPvHAMVAGaappaAVIAKMEEIGF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 EWLHkVVGdgrctLVDTW-------WQTETGGICIAPR-----------PSEDGAEILPGMAMRPffgiVPV---LMDE- 476
Cdd:PRK08162 322 DLTH-VYG-----LTETYgpatvcaWQPEWDALPLDERaqlkarqgvryPLQEGVTVLDPDTMQP----VPAdgeTIGEi 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 477 --KGNVLEGGdvsgalcisqawpgmartiYGDHQRFVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVInISG-HRL 553
Cdd:PRK08162 392 mfRGNIVMKG-------------------YLKNPKATEEAFAG--GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 554 GTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS-DENMVVNELKlsvaTKIAKYAVPDQIlVVKRLPKTR 632
Cdd:PRK08162 450 SSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASaTEEEIIAHCR----EHLAGFKVPKAV-VFGELPKTS 524
|
570
....*....|....*..
gi 18034773 633 SGKVMRRLLRKIITSRG 649
Cdd:PRK08162 525 TGKIQKFVLREQAKSLK 541
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-676 |
1.18e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.27 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 112 VQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAG 191
Cdd:PRK12316 2013 AARAPEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptVQHVLvahrTDTKVPMGSLDIPLEQEMA-KEAPV 270
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT--------------------------QRHLL----ERLPLPAGVARLPLDRDAEwADYPD 2136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 271 CTPE-SMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKlVFDYQPGDvfgCVADIGWIT--GHSYVVYGPLCNG 347
Cdd:PRK12316 2137 TAPAvQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNG 2212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 ATTVLFESTpvYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawvKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGD 427
Cdd:PRK12316 2213 ARVLIRDDE--LWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALRP 2287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 428 GRctLVDTWWQTETggiCIAPRPSEDGAEILPGMAMRPffgIVPVLMDEKGNVLEGG------DVSGALCISQAwpGMAR 501
Cdd:PRK12316 2288 VY--LFNGYGPTEA---VVTPLLWKCRPQDPCGAAYVP---IGRALGNRRAYILDADlnllapGMAGELYLGGE--GLAR 2357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 502 TIYG----DHQRFVDAYFRAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGY 576
Cdd:PRK12316 2358 GYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ 2437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 577 pHDIKGEAAFAFIVLKDNISDenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQDLGDTT 656
Cdd:PRK12316 2438 -DGASGKQLVAYVVPDDAAED---LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAP 2513
|
570 580
....*....|....*....|
gi 18034773 657 TLEDPSVITEILSAFQKYEE 676
Cdd:PRK12316 2514 QEGLEQRLAAIWQAVLKVEQ 2533
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
133-642 |
3.65e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 100.94 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGAI-HTVVFAGFSaESLAGRINDAK 205
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTINPRLFP-EQIAYIVNHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 206 CKAV---ITFnqglrggrvvelKKIVDEAVKSCPTVQHVLV----AHRTDTKVPMGSLDIPLE-QEMAKEAPVCTPESMS 277
Cdd:PRK07008 112 DRYVlfdLTF------------LPLVDALAPQCPNVKGWVAmtdaAHLPAGSTPLLCYETLVGaQDGDYDWPRFDENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 278 SedmlfMLYTSGSTGTPKGLVHTQAGYLL--YAAMThklvfdyqPgDVFGCVA-DI-----------GW-------ITGH 336
Cdd:PRK07008 180 S-----LCYTSGTTGNPKGALYSHRSTVLhaYGAAL--------P-DAMGLSArDAvlpvvpmfhvnAWglpysapLTGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 337 SYVVYGPLCNGATTV-LFESTPVYPDAGrywetvqrlkinqfygAPTAVRLLLKYGDAWVKKYdrSSL-RTL--GSVGEP 412
Cdd:PRK07008 246 KLVLPGPDLDGKSLYeLIEAERVTFSAG----------------VPTVWLGLLNHMREAGLRF--STLrRTVigGSACPP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 INHEAWEWLHKVvgdgrcTLVDTWWQTET---GGICI-----APRPSEDGAEILPGMAmRPFFGIVPVLMDEKGNVLegg 484
Cdd:PRK07008 308 AMIRTFEDEYGV------EVIHAWGMTEMsplGTLCKlkwkhSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGREL--- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 485 dvsgalcisqAWPGMArtiYGD-HQR---FVDAYFR--AYP---GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGT 555
Cdd:PRK07008 378 ----------PWDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 556 AEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIsdeNMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGK 635
Cdd:PRK07008 445 IDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGK 521
|
....*..
gi 18034773 636 VMRRLLR 642
Cdd:PRK07008 522 LQKLKLR 528
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
144-642 |
1.33e-21 |
|
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: 98.60 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 144 CRLANTLKRHGVHRG----DRVAIYMPVSPLAvaamlacaRIGAIHTVVFAGFSAESLAGRINDakCKAVITFNQGLRGG 219
Cdd:cd05929 12 FHQRRLLLLDVYSIAlnrnARAAAAEGVWIAD--------GVYIYLINSILTVFAAAAAWKCGA--CPAYKSSRAPRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 220 R-VVELKKIVdeAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEApvctpesmssedmlfMLYTSGSTGTPKGLV 298
Cdd:cd05929 82 CaIIEIKAAA--LVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGWK---------------MLYSGGTTGRPKGIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 299 HTQAGYLLYAA--MTHKLVFDYQPGDVFGCVADIGWITGHSyVVYGPLCNGATTVLFESTpvypDAGRYWETVQRLKINQ 376
Cdd:cd05929 145 RGLPGGPPDNDtlMAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----DPEEFLRLIERYRVTF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 377 FYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN---HEAW-EWLHKVVgdgrctlvdtwWQ----TETGGICIAp 448
Cdd:cd05929 220 AQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPpwvKEQWiDWGGPII-----------WEyyggTEGQGLTII- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 449 rpseDGAEIL--PGMAMRPFFGIVPVLmDEKGNVLEggdvsgalcisqawPGMARTIYgdhqrfvdayFRAYPGYYFT-- 524
Cdd:cd05929 288 ----NGEEWLthPGSVGRAVLGKVHIL-DEDGNEVP--------------PGEIGEVY----------FANGPGFEYTnd 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 525 ----------------GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAF 588
Cdd:cd05929 339 pektaaarneggwstlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 18034773 589 IVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05929 419 VQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
134-642 |
1.54e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 98.97 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMP---VSPLAVAAMLacaRIGAIHTVVFAGFSAESLAGRINDAKCKAV 209
Cdd:PRK08974 49 MTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPnllQYPIALFGIL---RAGMIVVNVNPLYTPRELEHQLNDSGAKAI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 210 ItfnqglrggrVVE-----LKKIVDEAvkscpTVQHVLVAHRTDT-KVPMGSL---------------DIPLEQEM---- 264
Cdd:PRK08974 126 V----------IVSnfahtLEKVVFKT-----PVKHVILTRMGDQlSTAKGTLvnfvvkyikrlvpkyHLPDAISFrsal 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 265 --AKEAPVCTPEsMSSEDMLFMLYTSGSTGTPKGlvhtqagyllyAAMTHklvfdyqpGDVFGCVADIGWItghsyvvYG 342
Cdd:PRK08974 191 hkGRRMQYVKPE-LVPEDLAFLQYTGGTTGVAKG-----------AMLTH--------RNMLANLEQAKAA-------YG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVLFESTPVYP------------DAGrywetVQRLKINQFYGAPTAVRLLLKYG-----------DAWV---- 395
Cdd:PRK08974 244 PLLHPGKELVVTALPLYHifaltvncllfiELG-----GQNLLITNPRDIPGFVKELKKYPftaitgvntlfNALLnnee 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 396 -KKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgrCTLVDTWWQTE---------------TGGICIaPRPSEDgaeilp 459
Cdd:PRK08974 319 fQELDFSSLKLSVGGGMAVQQAVAERWVKLTG---QYLLEGYGLTEcsplvsvnpydldyySGSIGL-PVPSTE------ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 460 gmaMRpffgivpvLMDEKGNVLEGGDvSGALCISQAwpgmaRTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQIT 539
Cdd:PRK08974 389 ---IK--------LVDDDGNEVPPGE-PGELWVKGP-----QVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 540 GRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKdnisDENMVVNELKLSVATKIAKYAVP 619
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK----DPSLTEEELITHCRRHLTGYKVP 527
|
570 580
....*....|....*....|...
gi 18034773 620 DQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK08974 528 KLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
134-642 |
1.96e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 99.34 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfN 213
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 QGLR----GGRVVELKKIVDEAVKSCPTvqhvlvahrtdtkvpmgsldipleqemakeapvcTPESMSSEDMLFMLYTSG 289
Cdd:PRK06060 110 DALRdrfqPSRVAEAAELMSEAARVAPG----------------------------------GYEPMGGDALAYATYTSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 290 STGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfESTPVYPDAGRYWETv 369
Cdd:PRK06060 156 TTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 370 qRLKINQFYGAPTavrLLLKYGDAWVKKYDRSsLRTLGSVGEPINHEAWEWLHKVVGDgrCTLVDTWWQTETGGICIAP- 448
Cdd:PRK06060 234 -RFGPSVLYGVPN---FFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSNr 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 449 ----RPSEDGaEILPGMAMRpffgivpVLMDEKGNVLEGGDvsGALCISQawPGMARTIYGDHQRFVDAyfrayPGYYFT 524
Cdd:PRK06060 307 vdewRLGTLG-RVLPPYEIR-------VVAPDGTTAGPGVE--GDLWVRG--PAIAKGYWNRPDSPVAN-----EGWLDT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 525 GDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNE 604
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 18034773 605 LKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK06060 450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
117-643 |
2.65e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 98.32 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 117 ETIALIWERDEPGTevrITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:PRK05620 25 DTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKaVITFNQglrggrvvELKKIVDEAVKSCPTVQHVLV-----AHRTDTKVPMGSLDIPLEQEMAKEAPV 270
Cdd:PRK05620 102 QIVHIINHAEDE-VIVADP--------RLAEQLGEILKECPCVRAVVFigpsdADSAAAHMPEGIKVYSYEALLDGRSTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 271 CTPESMSSEDMLFMLYTSGSTGTPKGLVHT-QAGYLLYAAMTHKLVFDYQPGDVFGCVADIgwitghsyvvYGPLCNGAT 349
Cdd:PRK05620 173 YDWPELDETTAAAICYSTGTTGAPKGVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPI----------YHVLSWGVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 350 TVLFES-TP-VYPDAGRYWETVQRLKIN----QFYGAPTA-VRLLLKYGDawvKKYDRSSLRTL---GSVGEPINHEAWE 419
Cdd:PRK05620 243 LAAFMSgTPlVFPGPDLSAPTLAKIIATamprVAHGVPTLwIQLMVHYLK---NPPERMSLQEIyvgGSAVPPILIKAWE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 420 WLHKVvgdgrcTLVDTWWQTETGGICIAPRPSEdGAEILPGMAMRPFFGIVPVLMDEK----GNVLEGGD-------VSG 488
Cdd:PRK05620 320 ERYGV------DVVHVWGMTETSPVGTVARPPS-GVSGEARWAYRVSQGRFPASLEYRivndGQVMESTDrnegeiqVRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 489 ALCI-------SQAWPGMARTIYGDHQRFVDAYFRAyPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 561
Cdd:PRK05620 393 NWVTasyyhspTEEGGGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 562 MADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK05620 472 IMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
..
gi 18034773 642 RK 643
Cdd:PRK05620 552 RQ 553
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
284-638 |
3.09e-21 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 95.26 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 284 MLYTSGSTGTPKGLVhtqagyllyaaMTHKlvfdyQPGDVFGCVADIGWIT-GHSYVVYGPLCN------GATTVLFEST 356
Cdd:cd17638 5 IMFTSGTTGRSKGVM-----------CAHR-----QTLRAAAAWADCADLTeDDRYLIINPFFHtfgykaGIVACLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 357 PVYP----DAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGrcTL 432
Cdd:cd17638 69 TVVPvavfDVDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE--TV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 433 VDTWWQTETGGICIApRPsEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDV-SGALCISQAwpgMARTIYGDhqrfv 511
Cdd:cd17638 145 LTAYGLTEAGVATMC-RP-GDDAETVATTCGRACPGFEVRIADDGEVLVRGYNVmQGYLDDPEA---TAEAIDAD----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 512 dayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVL 591
Cdd:cd17638 215 --------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18034773 592 KDNIS-DENMVVNELKlsvaTKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:cd17638 287 RPGVTlTEEDVIAWCR----ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
108-681 |
5.52e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.69 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK12467 1580 IEDQAAATPEAVALVF------GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqHVLVAHRTDTKVPMGSLDIPLEQEMAKE 267
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT----------------------------QSHLQARLPLPDGLRSLVLDQEDDWLEG 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPESMSSEDML-FMLYTSGSTGTPKGLVHTQAGYL-LYAAMTHKlvfdyqpgdvFGCVADIGWITGHSYV------ 339
Cdd:PRK12467 1706 YSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCATQEA----------YQLSAADVVLQFTSFAfdvsvw 1775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 340 -VYGPLCNGATTVLFESTpVYPDAGRYWETVQRLKI----------NQF------YGAPTAVRLLLKYGDAWVKKYDRSS 402
Cdd:PRK12467 1776 eLFWPLINGARLVIAPPG-AHRDPEQLIQLIERQQVttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRPW 1854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 403 LRTLGSVGepinheawewLHKVVGDGRCTLVDTWWQtetggiciAPRPSEDGAEILP-GMamrPFFGIVPVLMDEKGNVL 481
Cdd:PRK12467 1855 LERLPDTG----------LFNLYGPTETAVDVTHWT--------CRRKDLEGRDSVPiGQ---PIANLSTYILDASLNPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 482 EGGdVSGALCISQAwpGMARtiyGDH-------QRFVDAYFrAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHR 552
Cdd:PRK12467 1914 PIG-VAGELYLGGV--GLAR---GYLnrpaltaERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFR 1986
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 553 LGTAEIEDAMADHPAVPETAVIgyPHD-IKGEAAFAFIV-----LKDNISDENMVVNELKLSVATKIAKYAVPDQILVVK 626
Cdd:PRK12467 1987 IELGEIEARLREQGGVREAVVI--AQDgANGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLA 2064
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 627 RLPKTRSGKVMRRLLRKIitsrgqdlgdtttleDPSVITEILSAFQKYEEQRAAT 681
Cdd:PRK12467 2065 RMPLTPNGKLDRKALPAP---------------DASELQQAYVAPQSELEQRLAA 2104
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
110-641 |
7.98e-21 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 96.62 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVF 189
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 190 AGFSAESLAgRINDAKCKAVITFNqglRGGRVvelkkivdeAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEAP 269
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPAAALVA---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 270 vctpeSMSSEDMLFMLYTSGSTGTPKGLvhtqagyLLyaamthklvfdyqPGDVFGCVADIGWITGHSYVVYgplCNGAT 349
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAV-------LL-------------ANRTFFAVPDILQKEGLNWVTW---VVGET 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 350 TvlFESTPVYPDAGRYW----------------------ETVQRLKINQFYGAPTAVRLL---LKYGDAwvkkyDRSSLR 404
Cdd:PRK05857 217 T--YSPLPATHIGGLWWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLvseLKSANA-----TVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 405 TLGSVGEpinheawewlHKVVGDGR---CTLVDT---WWQTETG--GICIaPRPSEDGAEILPGMAMRPFFGIVPVLMDE 476
Cdd:PRK05857 290 LVGYGGS----------RAIAADVRfieATGVRTaqvYGLSETGctALCL-PTDDGSIVKIEAGAVGRPYPGVDVYLAAT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 477 KG---NVLEGGDVS--GALCISQawPGMARTIYGDHQRFVDAYFRaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGH 551
Cdd:PRK05857 359 DGigpTAPGAGPSAsfGTLWIKS--PANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 552 RLGTAEIEDAMADHPAVPETAVIGYPhDIKGEAAFAFIVLKDNISDENMVVnELKLSVATKIAK----YAVPDQILVVKR 627
Cdd:PRK05857 434 NIAPDEVDRIAEGVSGVREAACYEIP-DEEFGALVGLAVVASAELDESAAR-ALKHTIAARFRResepMARPSTIVIVTD 511
|
570
....*....|....
gi 18034773 628 LPKTRSGKVMRRLL 641
Cdd:PRK05857 512 IPRTQSGKVMRASL 525
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
135-643 |
1.34e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.82 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQ 214
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 215 glrggRVVELKKIVDEavkscPTVQHVLVAHRTDTKVPMGSLDIPLEQEmakeapvCTPESMSSEDMLFMLYTSGSTGTP 294
Cdd:PLN02246 132 -----YVDKLKGLAED-----DGVTVVTIDDPPEGCLHFSELTQADENE-------LPEVEISPDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 295 KGLVhtqagyllyaaMTHK-LV-------------FDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVL---FEstp 357
Cdd:PLN02246 195 KGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpkFE--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 358 vypdAGRYWETVQRLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINHEAWEWLHK-----VVGDGrctl 432
Cdd:PLN02246 261 ----IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKELEDAFRAklpnaVLGQG---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 433 vdtWWQTETG---GICIA----PRPSEDGAeilPGMAMRPffGIVPVLMDEKGNVLeGGDVSGALCI--SQAWPG----- 498
Cdd:PLN02246 331 ---YGMTEAGpvlAMCLAfakePFPVKSGS---CGTVVRN--AELKIVDPETGASL-PRNQPGEICIrgPQIMKGylndp 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 499 --MARTIYGDhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGY 576
Cdd:PLN02246 402 eaTANTIDKD-------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPM 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 577 PHDIKGEAAFAFIVLKD--NISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:PLN02246 469 KDEVAGEVPVAFVVRSNgsEITED-----EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
279-638 |
6.09e-20 |
|
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: 91.55 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 279 EDMLFMLYTSGSTGTPKGLVhtQAGYLLYAAMTH--KLVFDYQPGDVFGCVADIGWITGHSYVvygplcngATTVLFEST 356
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVL--LANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWI--------LTCLIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 357 PVYPDAGRYWETVqrLKINQFYGA------PTA---VRLLLKYGDAWVKKydrssLRTLGSVGE-PINHEA--WEWlhkv 424
Cdd:cd17635 71 CVTGGENTTYKSL--FKILTTNAVtttclvPTLlskLVSELKSANATVPS-----LRLIGYGGSrAIAADVrfIEA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 425 vgDGRCTLVDTWWQTETGGICIAPRpSEDGAEIlpGMAMRPFFGIVPVLMDEKG-NVLEGGDvsGALCISQAWpgMARTI 503
Cdd:cd17635 140 --TGLTNTAQVYGLSETGTALCLPT-DDDSIEI--NAVGRPYPGVDVYLAATDGiAGPSASF--GTIWIKSPA--NMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 504 YGDHQRFVDAYFRaypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGE 583
Cdd:cd17635 211 WNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 584 AAFAFIVlKDNISDENMVVNeLKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:cd17635 288 LVGLAVV-ASAELDENAIRA-LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-635 |
2.76e-19 |
|
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: 90.13 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 278 SEDMLFMLYTSGSTGTPKGLVHTQA---GYLLYAAMTHKLVF--DYQPGDVFGCVADIGW------ITGHSYVVYGPLCN 346
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFtpSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 347 GATTVLFESTPVYPDAgrYWETVQRLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPINHE 416
Cdd:cd05924 82 GGQTVVLPDDRFDPEE--VWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLSPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 417 AWEWLHKVVGDgrCTLVDTWWQTETGGICIA-PRPSEDGAeilpgmamRPFFGIVP--VLMDEKGNVLE-GGDVSGALci 492
Cdd:cd05924 150 VKQGLLELVPN--ITLVDAFGSSETGFTGSGhSAGSGPET--------GPFTRANPdtVVLDDDGRVVPpGSGGVGWI-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 sqAWPG-MARTIYGDHQRfVDAYFRAYPG--YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVP 569
Cdd:cd05924 218 --ARRGhIPLGYYGDEAK-TAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVY 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 570 ETAVIGYPHDIKGEAAFAFIVLKDN--ISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGK 635
Cdd:cd05924 295 DVLVVGRPDERWGQEVVAVVQLREGagVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
280-638 |
2.95e-19 |
|
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: 89.39 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 280 DMLFMLYTSGSTGTPKGLVHTQAGYLlyaamthklvfdyqpgDVFGCVADIGWITGHSYV-VYGPLC-----NGATTVLF 353
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI----------------ESFVCNEDLFNISGEDAIlAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 354 ESTPVYPDAG----RYWETVQRLKINQFYGAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPINHEAWEWLHKVVGDGR 429
Cdd:cd17633 65 LGGTFIGQRKfnpkSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKNIFPKAN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 430 ctLVDTWWQTETGGICIaprpSEDGAEILPGMAMRPFFGIVPVLMDEkgnvleGGDVSGALCISQAwpgMARTIYgdhqr 509
Cdd:cd17633 139 --LIEFYGTSELSFITY----NFNQESRPPNSVGRPFPNVEIEIRNA------DGGEIGKIFVKSE---MVFSGY----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 510 fVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAfI 589
Cdd:cd17633 199 -VRGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-L 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18034773 590 VLKDNISDENmvvneLKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:cd17633 277 YSGDKLTYKQ-----LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
133-643 |
4.70e-19 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 90.56 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITf 212
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgSLDIPLEQEMAKEAPVCTPESMssEDMLFMLYTSGSTG 292
Cdd:cd05939 82 ------------------------------------------NLLDPLLTQSSTEPPSQDDVNF--RDKLFYIYTSGTTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTQAGYLLYAAMTHKlVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVL---FESTPVYPDAGRYwetv 369
Cdd:cd05939 118 LPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIrkkFSASNFWDDCVKY---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 370 qRLKINQFYGapTAVRLLLkygDAWVKKYD-RSSLRTLgsVGEPINHEAWEWLHKVVG-----------DGRCTLVDTWW 437
Cdd:cd05939 193 -NCTIVQYIG--EICRYLL---AQPPSEEEqKHNVRLA--VGNGLRPQIWEQFVRRFGipqigefygatEGNSSLVNIDN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 438 QT-----------------------ETG-------GICIAPRPSEDGA---EILPGMAMRPFFGIVpvlmDEKGNvlegg 484
Cdd:cd05939 265 HVgacgfnsrilpsvypirlikvdeDTGelirdsdGLCIPCQPGEPGLlvgKIIQNDPLRRFDGYV----NEGAT----- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 485 dvsgalcisqawpgmartiygdHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMAD 564
Cdd:cd05939 336 ----------------------NKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSN 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 565 HPAVPETAVIGY--PHdIKGEAAFAFIVLKDNISDenmvVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:cd05939 394 VLGLEDVVVYGVevPG-VEGRAGMAAIVDPERKVD----LDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
.
gi 18034773 643 K 643
Cdd:cd05939 469 K 469
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
131-643 |
5.07e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 90.95 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 TFNqglrggrvvELKKIVDEAVKscptvqhvLVAHRTDTKVPMGSLDiPLEQEMAKEAPVCTPESMSSE-DMLFMLYTSG 289
Cdd:cd05915 102 FDP---------NLLPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 290 STGTPKGLVHTQAG-YLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFEstpvYPDAGRYWET 368
Cdd:cd05915 164 TTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 369 VQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinheawEWLHKVVGDGRCTLVDTWWQTETGGICIA- 447
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAP------RSLIARFERMGVEVRQGYGLTETSPVVVQn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 448 ---PR----PSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISQAwpGMARTIYGDHQRFVDAYFRAypG 520
Cdd:cd05915 314 fvkSHleslSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGP--WITGGYYGNEEATRSALTPD--G 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 521 YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENM 600
Cdd:cd05915 390 FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 18034773 601 VVNELKLSVATkiaKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05915 470 LNEHLLKAGFA---KWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
111-648 |
8.44e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 89.84 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 111 HVQKSPETIALIwERDEpgtevRITYRELLETTCRLANTLkRHGVHRGDRVAIYMPVSP-----LAVAAMLACARIgAIH 185
Cdd:PRK07638 10 HASLQPNKIAIK-ENDR-----VLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIeflqlFAGAAMAGWTCV-PLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 186 TvvfaGFSAESLAGRINDAKCKAVITFNQglrggrvvELKKIVDEavkSCPTVQhvlvahrTDTKVPMgsldipLEQEMA 265
Cdd:PRK07638 82 I----KWKQDELKERLAISNADMIVTERY--------KLNDLPDE---EGRVIE-------IDEWKRM------IEKYLP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 266 KEAPVCTPEsmssEDMLFMLYTSGSTGTPKGLVHTQAGYLlYAAMTHKLVFDYQPGD---VFGCVAdigwitgHSYVVYG 342
Cdd:PRK07638 134 TYAPIENVQ----NAPFYMGFTSGSTGKPKAFLRAQQSWL-HSFDCNVHDFHMKREDsvlIAGTLV-------HSLFLYG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 P---LCNGATTVLFES-TPVypdagRYWETVQRLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSvGEPINHEAW 418
Cdd:PRK07638 202 AistLYVGQTVHLMRKfIPN-----QVLDKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISS-GAKWEAEAK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 419 E-----WLHkvvgdgrCTLVDTWWQTETGGICiAPRPSEdgAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVsGALCIS 493
Cdd:PRK07638 271 EkikniFPY-------AKLYEFYGASELSFVT-ALVDEE--SERRPNSVGRPFHNVQVRICNEAGEEVQKGEI-GTVYVK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 494 QAWPGMARTIYGDHQRFVDAyfrayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAV 573
Cdd:PRK07638 340 SPQFFMGYIIGGVLARELNA-----DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVV 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 574 IGYPHDIKGEAAFAFIvlkdnisDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:PRK07638 415 IGVPDSYWGEKPVAII-------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
520-642 |
8.70e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 89.66 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 520 GYYFTGDGAHRTEGGYYQITGRMD-DVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDE 598
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAAD 429
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18034773 599 nmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLR 642
Cdd:PRK07787 430 -----ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
109-641 |
1.15e-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: 89.15 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 109 DQHVQKSPETIALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakea 268
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 pvctpesmSSEDMLFMLYTSGSTGTPKGlVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWiTGHSYVVYGPLCNGA 348
Cdd:cd17645 102 --------NPDDLAYVIYTSGSTGLPKG-VMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 349 TT-VLFESTPVYPDA-GRYWETvQRLKINqFYGAPTAVRLLlkygdawvkKYDRSSLRTLGSVGEPINhEAWEWLHKVV- 425
Cdd:cd17645 172 ALhVVPSERRLDLDAlNDYFNQ-EGITIS-FLPTGAAEQFM---------QLDNQSLRVLLTGGDKLK-KIERKGYKLVn 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 --GDGRCTLVDTWWQT--ETGGICIApRPSEDgaeilpgmamrpffgiVPVLMDEKGNVLEGGDVSGALCIsqAWPGMAR 501
Cdd:cd17645 240 nyGPTENTVVATSFEIdkPYANIPIG-KPIDN----------------TRVYILDEALQLQPIGVAGELCI--AGEGLAR 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 502 TIYG----DHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYP 577
Cdd:cd17645 301 GYLNrpelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKE 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034773 578 HDIKGEAAFAFIVLKDNISDEnmvvnELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd17645 381 DADGRKYLVAYVTAPEEIPHE-----ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
113-457 |
2.59e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.80 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 113 QKSPETIALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVV 188
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRINDAKCKAVITFNQGLRGGRVVELKKivdeavkscPTVQH-VLVAHRTDTkvPMGSLDIPLEQEMAKE 267
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK---------PSVRRlVTVGGRLLW--GGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APvctPESMSSEDMLFMLYTSGSTGTPKGLVHTQAgylLYAAMTHKL--VFDYQPGDVfgcvaDIgwitgHSY---VVYG 342
Cdd:PRK09274 166 FP---MADLAPDDMAAILFTSGSTGTPKGVVYTHG---MFEAQIEALreDYGIEPGEI-----DL-----PTFplfALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCnGATTVLFESTPVYP---DAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINHEAWE 419
Cdd:PRK09274 230 PAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 420 WLHKVVGDG--------------------RCTLVDTWWQTETG-GICIApRPSeDGAEI 457
Cdd:PRK09274 307 RFRAMLPPDaeiltpygatealpissiesREILFATRAATDNGaGICVG-RPV-DGVEV 363
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
262-643 |
1.94e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 85.89 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 262 QEMAKEAPVCTPESMSSEDMLFMLY-TSGSTGTPKGLVHTQaGYLLYAAMTHKLVFDYQPGDVfgCVADIGWItgHSYVV 340
Cdd:PRK07867 134 DELAAHRDAEPPFRVADPDDLFMLIfTSGTSGDPKAVRCTH-RKVASAGVMLAQRFGLGPDDV--CYVSMPLF--HSNAV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 341 ---YGP-LCNGATTVL---FESTPVYPDAGRYWETVQrlkinQFYGAPTAVRLLL--KYGDAwvkkydRSSLRTL-GSVG 410
Cdd:PRK07867 209 magWAVaLAAGASIALrrkFSASGFLPDVRRYGATYA-----NYVGKPLSYVLATpeRPDDA------DNPLRIVyGNEG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 411 EPINHEAWEwlhkvvgdGR--CTLVDTWWQTEtGGICIAPRPSEDgaeilPGMAMRPFFGI----------VPVLMDEKG 478
Cdd:PRK07867 278 APGDIARFA--------RRfgCVVVDGFGSTE-GGVAITRTPDTP-----PGALGPLPPGVaivdpdtgteCPPAEDADG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 479 NVLEGGDVSGALcISQAWPGMARTIYGDHQrfVDAYfRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEI 558
Cdd:PRK07867 344 RLLNADEAIGEL-VNTAGPGGFEGYYNDPE--ADAE-RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 559 EDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELkLSVATKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:PRK07867 420 ERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEF-LAAQPDLGPKQWPSYVRVCAELPRTATFKVLK 498
|
....*
gi 18034773 639 RLLRK 643
Cdd:PRK07867 499 RQLSA 503
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
131-644 |
2.08e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 TFNqglrggrvvELKKIVDEAVKSCPTVQH-----VLVAHRTDTKVPMGSLDIPLEQEMAKEAPvcTPESMSS------- 278
Cdd:PLN03102 117 VDR---------SFEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 279 EDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMthklvfdyqpgdvfgcvADIGWITGHSYVVYGPL----CNGAT----T 350
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYLSTLS-----------------AIIGWEMGTCPVYLWTLpmfhCNGWTftwgT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 351 VLFESTPV---YPDAGRYWETVQRLKINQFYGAPTAVRLLLKyGDAWVKKYDRSSLRTLGSVGEP-------INHEAWEW 420
Cdd:PLN03102 249 AARGGTSVcmrHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPPpaalvkkVQRLGFQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 421 LHKV-VGDGRCTLVDTWWQTETGGIciaprPSEDGAEILPGMAMRpFFGIVPVLMDEKG---NVLEGGDVSGALCISqaw 496
Cdd:PLN03102 328 MHAYgLTEATGPVLFCEWQDEWNRL-----PENQQMELKARQGVS-ILGLADVDVKNKEtqeSVPRDGKTMGEIVIK--- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 497 pgmARTIYGDHQRFVDAYFRAYP-GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIG 575
Cdd:PLN03102 399 ---GSSIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 576 YPHDIKGEAAFAFIVLKDniSDENMVVNELKLSVATK---------IAKYAVPDQILVVKRLPKTRSGKVMRRLLRKI 644
Cdd:PLN03102 476 MPHPTWGETPCAFVVLEK--GETTKEDRVDKLVTRERdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
257-642 |
4.32e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 81.61 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 257 DIPLEQEMAKEAPVCTPESMSSEDMLFMLY-TSGSTGTPKGLVHTQAGYLLYA-AMTHKlvFDYQPGDVFGCVADIGwit 334
Cdd:PRK13388 127 DTPAYAELVAAAGALTPHREVDAMDPFMLIfTSGTTGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPLF--- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 335 gHSYVVY---GP-LCNGATTVLfestPVYPDAGRYWETVQRlkinqfYGAP--TAVRLLLKYGDAWVKKYDRS--SLRT- 405
Cdd:PRK13388 202 -HSNAVMagwAPaVASGAAVAL----PAKFSASGFLDDVRR------YGATyfNYVGKPLAYILATPERPDDAdnPLRVa 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 406 LGSVGEPINHEAWEwlhkvvgdgR---CTLVDTWWQTETGGICIAprpsEDGAEilPGMAMRPFFGIV-----------P 471
Cdd:PRK13388 271 FGNEASPRDIAEFS---------RrfgCQVEDGYGSSEGAVIVVR----EPGTP--PGSIGRGAPGVAiynpetltecaV 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 472 VLMDEKGNVLEGGDVSGALcISQAWPGMARTIYGDHQRFVDayfRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGH 551
Cdd:PRK13388 336 ARFDAHGALLNADEAIGEL-VNTAGAGFFEGYYNNPEATAE---RMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 552 RLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDnisDENMVVNELK--LSVATKIAKYAVPDQILVVKRLP 629
Cdd:PRK13388 412 NLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD---GATFDPDAFAafLAAQPDLGTKAWPRYVRIAADLP 488
|
410
....*....|...
gi 18034773 630 KTRSGKVMRRLLR 642
Cdd:PRK13388 489 STATNKVLKRELI 501
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
132-653 |
5.25e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 81.43 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 132 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVIT 211
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 212 FNQGLRggRVVELKKIVDEAVKSC--PTVQHVLVAHRTDTKV---PMGSLDIPLEQEMAKEAPVCTPESMSSE-DMLFML 285
Cdd:PLN02479 124 DQEFFT--LAEEALKILAEKKKSSfkPPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADEwQSIALG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 286 YTSGSTGTPKGLV-HTQAGYLLyaAMTHKLVFDYQPGDV-------FGCVadiGWITGHSYVVygpLCnGATTVLFESTp 357
Cdd:PLN02479 202 YTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVylwtlpmFHCN---GWCFTWTLAA---LC-GTNICLRQVT- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 358 vypdAGRYWETVQRLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPInheaweWLHKVVGDG-RCTlvD 434
Cdd:PLN02479 272 ----AKAIYSAIANYGVTHFCAAPVVLNTIVNApkSETILPLPRVVHVMTAGAAPPPS------VLFAMSEKGfRVT--H 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 435 TWWQTETGG---ICI-APR----PSEDGAEI----------LPGMAMRPFFGIVPVLMDEK--------GNVLEGGDVSG 488
Cdd:PLN02479 340 TYGLSETYGpstVCAwKPEwdslPPEEQARLnarqgvryigLEGLDVVDTKTMKPVPADGKtmgeivmrGNMVMKGYLKN 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 489 ALCISQAWPGmartiygdhqrfvdayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAV 568
Cdd:PLN02479 420 PKANEEAFAN---------------------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 569 PETAVIGYPHDIKGEAAFAFIVLKDNI--SDENMVVNELKLSVATKIAKYAVPDQIlVVKRLPKTRSGKVMRRLLRkiit 646
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKPGVdkSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR---- 553
|
....*..
gi 18034773 647 SRGQDLG 653
Cdd:PLN02479 554 AKAKEMG 560
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
51-107 |
8.99e-16 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 71.73 E-value: 8.99e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 51 YPALSAQAAQEPAAFWGPLARDtLVWDTPYHTVWDCDFRtGKIGWFLGGQLNVSVNC 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
108-641 |
3.18e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 79.70 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkiVDEavkscptvqhvlVAHRtdtkVPMGSLDIPLEQEMAKE 267
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLIT----------------TAD------------QLPR----FADVPDLTSLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPESMSS-EDMLFMLYTSGSTGTPKGLVHTQagyllyAAMTHKLV-----FDYQPGDVfgcvadIGWITGHSYVV- 340
Cdd:PRK10252 586 PQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQ------TAIVNRLLwmqnhYPLTADDV------VLQKTPCSFDVs 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 341 ----YGPLCNGATTVLFEstpvyPDAGRYWETVQRL----KINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEP 412
Cdd:PRK10252 654 vwefFWPFIAGAKLVMAE-----PEAHRDPLAMQQFfaeyGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEA 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 413 INHE---AWEW-----LHKVVGDGRCTlVD-TWW--------QTETGGICIAPRPSEDGAEILPGMaMRPffgiVPVlmd 475
Cdd:PRK10252 729 LPADlcrEWQQltgapLHNLYGPTEAA-VDvSWYpafgeelaAVRGSSVPIGYPVWNTGLRILDAR-MRP----VPP--- 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 476 ekgnvleggDVSGALCIS--QawpgMARTIYG----DHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS 549
Cdd:PRK10252 800 ---------GVAGDLYLTgiQ----LAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIR 866
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 550 GHRLGTAEIEDAMADHPAVpETAVI-------GYPHDIKGEAAFAFIVLKdniSDENMVVNELKLSVATKIAKYAVPDQI 622
Cdd:PRK10252 867 GQRIELGEIDRAMQALPDV-EQAVThacvinqAAATGGDARQLVGYLVSQ---SGLPLDTSALQAQLRERLPPHMVPVVL 942
|
570
....*....|....*....
gi 18034773 623 LVVKRLPKTRSGKVMRRLL 641
Cdd:PRK10252 943 LQLDQLPLSANGKLDRKAL 961
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
131-641 |
7.06e-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: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 TFNQglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmssEDMLFMLYTSGS 290
Cdd:cd05914 85 VSDE----------------------------------------------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 291 TGTPKGLVHTqaGYLLYAAMTHKLVFD-YQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTP-----------V 358
Cdd:cd05914 101 TGNSKGVMLT--YRNIVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPsakiialafaqV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 359 YPDAG--RYWETVQRLK---INQFYGAPTAVRLLLKYGDAWVKKYDRSSL--------RTLGSVGEPINHEAWEWLHKVv 425
Cdd:cd05914 179 TPTLGvpVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINPDVEEFLRTI- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 gdgRCTLVDTWWQTETGGICIAPRPSE----DGAEILPGMAMRPFfgiVPVLMDEKGNVLeggdVSGalcisqawPGMAR 501
Cdd:cd05914 258 ---GFPYTIGYGMTETAPIISYSPPNRirlgSAGKVIDGVEVRID---SPDPATGEGEII----VRG--------PNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 502 TIYGDHQRFVDAYFRAypGYYFTGDGAHRTEGGYYQITGRMDDVINI-SGHRLGTAEIEDAMADHPAVPETAVIGYPHDI 580
Cdd:cd05914 320 GYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 581 KG----EAAFAFIVLKDNISDENMVVNELKLSVATKIAKYA-VPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:cd05914 398 VAlayiDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
515-648 |
8.46e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 77.34 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 515 FRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDN 594
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 18034773 595 ISDenmvVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:PRK07445 399 SIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQR 448
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
126-644 |
2.97e-14 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 75.78 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 126 DEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAK 205
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 206 cKAVITFNQGL---RGGRVVELKKIVdeavkscpTVQHVLVahrtdtkVPMGSLDIPLEQEMAKEAPVCTPEsmsseDML 282
Cdd:cd05906 112 -HIWQLLGSPVvltDAELVAEFAGLE--------TLSGLPG-------IRVLSIEELLDTAADHDLPQSRPD-----DLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 283 FMLYTSGSTGTPKGLVHTQAGYL--LYAAMTHklvFDYQPGDVFgcvadIGW-----ITGHSYVVYGPLCNGATTVLFES 355
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILarSAGKIQH---NGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVHVPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 356 TPVYPDAGRYWETVQRLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINHEAWEWL------HKVV 425
Cdd:cd05906 243 EEILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLlrllepYGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 426 GDgrcTLVDTWWQTETGGICI-------APRPSED-----GAEIlPGMAMRpffgivpvLMDEKGNVLEGGDVsGALCIS 493
Cdd:cd05906 320 PD---AIRPAFGMTETCSGVIysrsfptYDHSQALefvslGRPI-PGVSMR--------IVDDEGQLLPEGEV-GRLQVR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 494 qawpGMARTiygdhqrfvdayfrayPGYY---------FTGDGAHRT------EGGYYQITGRMDDVINISGHRLGTAEI 558
Cdd:cd05906 387 ----GPVVT----------------KGYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIVNGVNYYSHEI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 559 EDAM--ADHPAVPETAVIGY--PHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAkyAVPDQILVVKR--LPKTR 632
Cdd:cd05906 447 EAAVeeVPGVEPSFTAAFAVrdPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLPKeeIPKTS 524
|
570
....*....|..
gi 18034773 633 SGKVMRRLLRKI 644
Cdd:cd05906 525 LGKIQRSKLKAA 536
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
129-575 |
5.40e-14 |
|
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: 74.81 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 129 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP------VSPLAVaaMLAcariGAIHTVVFAGFSAESLAGRIN 202
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 203 DAKCKAVITfnqglrgGRV---VELKKIVDEAVKSCPTVQH-VLVAHRT-DTKVPMGSldiPLEqemakEAPVCTPESMS 277
Cdd:cd05932 76 HSESKALFV-------GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 278 SedmlfMLYTSGSTGTPKGLVHTQAGYlLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTP 357
Cdd:cd05932 141 T-----LIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 358 VYPdagrywETVQRLKINQFYGAPtavRLLLK-----YGDAWVKKYDR-------SSL--------------RTLGSVGE 411
Cdd:cd05932 215 TFV------EDVQRARPTLFFSVP---RLWTKfqqgvQDKIPQQKLNLllkipvvNSLvkrkvlkglgldqcRLAGCGSA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 412 PINHEAWEWLHKVVGDgrctLVDTWWQTETGGICIAPRPSEDG----AEILPGMAMRpffgivpvlMDEKGNVLEGGdvs 487
Cdd:cd05932 286 PVPPALLEWYRSLGLN----ILEAYGMTENFAYSHLNYPGRDKigtvGNAGPGVEVR---------ISEDGEILVRS--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 488 galcisqawPGMARTIYGDHQRFVDAyFRAyPGYYFTGDGAHRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAMADHP 566
Cdd:cd05932 350 ---------PALMMGYYKDPEATAEA-FTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHD 418
|
....*....
gi 18034773 567 AVPETAVIG 575
Cdd:cd05932 419 RVEMVCVIG 427
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
134-646 |
6.29e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 74.88 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDakCKAVITF 212
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVD--CSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEAPVCTPES-MSSEDMLFMLYTSGST 291
Cdd:PLN02574 145 --------------TSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPvIKQDDVAAIMYSSGTT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 292 GTPKGLVHTQAGYLlyaAMTHKLV------FDYQPGD-VFGCVADIGWITGHSYVVYGPLCNGATTVLFESTpvypDAGR 364
Cdd:PLN02574 211 GASKGVVLTHRNLI---AMVELFVrfeasqYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 365 YWETVQRLKINQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGdgRCTLVDTWWQTETGGI 444
Cdd:PLN02574 284 MVKVIDRFKVTHFPVVPPILMALTKKAKG-VCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLP--HVDFIQGYGMTESTAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 445 CIAPRPSEDGAE------ILPGMAMRpffgivpVLMDEKGNVLEGGDvSGALCISQawPGMARTIYGDHQRFVDAYFRay 518
Cdd:PLN02574 361 GTRGFNTEKLSKyssvglLAPNMQAK-------VVDWSTGCLLPPGN-CGELWIQG--PGVMKGYLNNPKATQSTIDK-- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 519 PGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKdnisDE 598
Cdd:PLN02574 429 DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRR----QG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18034773 599 NMVVNELKLS-VATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIIT 646
Cdd:PLN02574 505 STLSQEAVINyVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
523-641 |
9.17e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.92 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 523 FTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEaafafIVLKDNISDENMVV 602
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGE-----RVKAKVISHEEIDP 368
|
90 100 110
....*....|....*....|....*....|....*....
gi 18034773 603 NELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
116-641 |
9.80e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 74.26 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAE 195
Cdd:PRK13383 49 PGRTAII---DDDGA---LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 196 SLAGRINDAKCKAVITFNQglrggrVVELKKIVDEAVkscptvqhVLVAHRTDTKvpmgsldipleQEMAKEAPVCTPES 275
Cdd:PRK13383 123 ALAAALRAHHISTVVADNE------FAERIAGADDAV--------AVIDPATAGA-----------EESGGRPAVAAPGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 276 MssedmlfMLYTSGSTGTPKGLVHT---QAGYLLYAAMTHKLVFDyqpgdvfgcvadigwiTGHSYVVYGPLCNG----- 347
Cdd:PRK13383 178 I-------VLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRLR----------------TGSRISVAMPMFHGlglgm 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 348 -------ATTVLfesTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEW 420
Cdd:PRK13383 235 lmltialGGTVL---THRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 421 LHKVVGDgrcTLVDTWWQTETG-GICIAPRPSEDGAEILPgmamRPFFGiVPVLMDEKGNVLEGGDVSGALCISQAWPGm 499
Cdd:PRK13383 312 FMDTYGD---ILYNGYGSTEVGiGALATPADLRDAPETVG----KPVAG-CPVRILDRNNRPVGPRVTGRIFVGGELAG- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 500 ARTIYGDHQRFVDayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHD 579
Cdd:PRK13383 383 TRYTDGGGKAVVD-------GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDE 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034773 580 IKGEAAFAFIVLKDNIS-DENMVVNELKlsvaTKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK13383 456 RFGHRLAAFVVLHPGSGvDAAQLRDYLK----DRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
280-638 |
1.33e-13 |
|
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: 72.30 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 280 DMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSyVVYGPLCNGATTVLFESTpvy 359
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 360 pDAGRYWETVQRLKINqFYG--APTAVRLLlkygDAWVKK-YDRSSLRTLGSVGEPINHEAWEwlhKVVGDgrctlvdTW 436
Cdd:cd17637 76 -DPAEALELIEEEKVT-LMGsfPPILSNLL----DAAEKSgVDLSSLRHVLGLDAPETIQRFE---ETTGA-------TF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 437 W----QTETGG-ICIAPrpsedgAEILPGMAMRPFFGIVPVLMDEKGNVLEGGD-----VSGALCISQAWPGMARTIYGd 506
Cdd:cd17637 140 WslygQTETSGlVTLSP------YRERPGSAGRPGPLVRVRIVDDNDRPVPAGEtgeivVRGPLVFQGYWNLPELTAYT- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 hqrfvdayFRAypGYYFTGDGAHRTEGGYYQITGRM--DDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPhDIK-GE 583
Cdd:cd17637 213 --------FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPKwGE 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 18034773 584 AAFAFIVLKdniSDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:cd17637 282 GIKAVCVLK---PGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
116-640 |
5.93e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 71.28 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGD-RVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSA 194
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 195 ESLAGRINDAKCKAVITfnqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpe 274
Cdd:cd17648 75 ERIQFILEDTGARVVIT--------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 275 smSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGD----VFgcvadigwitghSYVVYGP------- 343
Cdd:cd17648 92 --NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDeavlFF------------SNYVFDFfveqmtl 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 -LCNGATTVLFESTpVYPDAGRYWETVQRLKINQFYGAPTAVRLllkygdawvkkYD---RSSLRTLGSVGEPINHEAWE 419
Cdd:cd17648 158 aLLNGQKLVVPPDE-MRFDPDRFYAYINREKVTYLSGTPSVLQQ-----------YDlarLPHLKRVDAAGEEFTAPVFE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 420 wlhKVVGDGRCTLVDTWWQTETGGICIAPRPSEDGA------EILPGM-------AMRPffgiVPVlmdekGNVLE---G 483
Cdd:cd17648 226 ---KLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRfdkslgRPVRNTkcyvlndAMKR----VPV-----GAVGElylG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 484 GDvsgalCISQAW---PGMARtiygdhQRFVDAYFRA--------YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHR 552
Cdd:cd17648 294 GD-----GVARGYlnrPELTA------ERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQR 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 553 LGTAEIEDAMADHPAVPETAVI-GYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKT 631
Cdd:cd17648 363 IEPGEVEAALASYPGVRECAVVaKEDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
570
....*....|
gi 18034773 632 RSGKV-MRRL 640
Cdd:cd17648 443 INGKLdVRAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
110-641 |
1.07e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVF 189
Cdd:PRK05691 2196 AQAARTPQAPALTFAGQT------LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 190 AGFSAESLAGRINDAKCKAVITFNQGLRGgrvveLKKIVDEAVKSCPTVQHVLVAHRTDTKVPmgSLDIPLEQEmakeap 269
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEA-----LGELPAGVARWCLEDDAAALAAYSDAPLP--FLSLPQHQA------ 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 270 vctpesmssedmlFMLYTSGSTGTPKGLVHTQAGYllyaAMTHKLV---FDYQPGDvfgCVADIGWIT--GHSYVVYGPL 344
Cdd:PRK05691 2337 -------------YLIYTSGSTGKPKGVVVSHGEI----AMHCQAVierFGMRADD---CELHFYSINfdAASERLLVPL 2396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 345 CNGATTVLfestpvypDAGRYWET--------VQRLKINQF---YGAPTAVRLllkygdawVKKYDRSSLRTLGSVGEPI 413
Cdd:PRK05691 2397 LCGARVVL--------RAQGQWGAeeicqlirEQQVSILGFtpsYGSQLAQWL--------AGQGEQLPVRMCITGGEAL 2460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 414 NHEAWEWLHKVVGDGrcTLVDTWWQTETGGI---CIAPRPSEDGAEILPgmAMRPFFGIVPVLMDEKGNVLEGGdVSGAL 490
Cdd:PRK05691 2461 TGEHLQRIRQAFAPQ--LFFNAYGPTETVVMplaCLAPEQLEEGAASVP--IGRVVGARVAYILDADLALVPQG-ATGEL 2535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 491 CISQAwpGMARtiyGDHQR-------FVDAYFRAYPG-YYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAM 562
Cdd:PRK05691 2536 YVGGA--GLAQ---GYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRL 2610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 563 ADHPAVPETAVIGypHDIKGEAAFAFIVLKDNISDENMVVNELKLSVA----TKIAKYAVPDQILVVKRLPKTRSGKVMR 638
Cdd:PRK05691 2611 LEHPAVREAVVLA--LDTPSGKQLAGYLVSAVAGQDDEAQAALREALKahlkQQLPDYMVPAHLILLDSLPLTANGKLDR 2688
|
...
gi 18034773 639 RLL 641
Cdd:PRK05691 2689 RAL 2691
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
108-641 |
1.19e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 70.69 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 108 LDQHVQKSPETIALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTV 187
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYL------GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 188 VFAGFSAESLAGRINDAKCKAVITfnqglrggrvvelkkIVDEAVkscptvqhvlvahrTDTKVPMGSLDIpLEQEMAKE 267
Cdd:PRK04813 82 VDVSSPAERIEMIIEVAKPSLIIA---------------TEELPL--------------EILGIPVITLDE-LKDIFATG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 268 APVCTPESMSSEDMLFMLYTSGSTGTPKGlVHTQAGYLLyaAMTHKLVFDYQPGDVFGC-----------VADIgwitgh 336
Cdd:PRK04813 132 NPYDFDHAVKGDDNYYIIFTSGTTGKPKG-VQISHDNLV--SFTNWMLEDFALPEGPQFlnqapysfdlsVMDL------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 337 syvvYGPLCNGATTVLFESTpVYPDAGRYWETVQRLKINQFYGAPTAVR--LLLKYGDAwvKKYdrSSLRTLGSVGEPIN 414
Cdd:PRK04813 203 ----YPTLASGGTLVALPKD-MTANFKQLFETLPQLPINVWVSTPSFADmcLLDPSFNE--EHL--PNLTHFLFCGEELP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 415 HEAWEWLHKVVGDGRctLVDTWWQTETggiCIAPRPSEDGAEI------LP-GMAmRPFFGIVpvLMDEKGNVLEGGDvS 487
Cdd:PRK04813 274 HKTAKKLLERFPSAT--IYNTYGPTEA---TVAVTSIEITDEMldqykrLPiGYA-KPDSPLL--IIDEEGTKLPDGE-Q 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 488 GALCISQawPGMARTIYGDHQRfVDAYFRAYPGY--YFTGDgAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADH 565
Cdd:PRK04813 345 GEIVISG--PSVSKGYLNNPEK-TAEAFFTFDGQpaYHTGD-AGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034773 566 PAVPETAVIGYPHDIKGEAAFAFIVLKDN-ISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLL 641
Cdd:PRK04813 421 SYVESAVVVPYNKDHKVQYLIAYVVPKEEdFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
110-647 |
1.57e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.39 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 110 QHVQKSPETIALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVAAMLACARIGaihtvV 188
Cdd:PLN02330 36 QDAELYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPnVAEYGIVALGIMAAGG-----V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 189 FAGFSAESLAGRIND----AKCKAVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDtkvpmgsldipleqem 264
Cdd:PLN02330 107 FSGANPTALESEIKKqaeaAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVNWKELLEAAD---------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 265 aKEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGylLYAAMTHKLvFDYQPgDVFGCVADIGWITG-HSYVVYGP 343
Cdd:PLN02330 171 -RAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRN--LVANLCSSL-FSVGP-EMIGQVVTLGLIPFfHIYGITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 344 LC----NGATTVLfestpvypdagrywetVQRLKINQFYGA------------PTAVRLLLKygDAWVKKYDRSSL--RT 405
Cdd:PLN02330 246 CCatlrNKGKVVV----------------MSRFELRTFLNAlitqevsfapivPPIILNLVK--NPIVEEFDLSKLklQA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 406 LGSVGEPINHE---AWEwlHKVVGdgrCTLVDTWWQTETGGICIAPRPSEDGAeilpGMAMRPFFG-IVPVL----MDEK 477
Cdd:PLN02330 308 IMTAAAPLAPElltAFE--AKFPG---VQVQEAYGLTEHSCITLTHGDPEKGH----GIAKKNSVGfILPNLevkfIDPD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 478 GNVLEGGDVSGALCI-SQAwpgMARTIYGDHQ---RFVDAyfrayPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRL 553
Cdd:PLN02330 379 TGRSLPKNTPGELCVrSQC---VMQGYYNNKEetdRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 554 GTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELklsVATKIAKYAVPDQILVVKRLPKTRS 633
Cdd:PLN02330 451 APAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNF---VAANVAHYKKVRVVQFVDSIPKSLS 527
|
570
....*....|....
gi 18034773 634 GKVMRRLLRKIITS 647
Cdd:PLN02330 528 GKIMRRLLKEKMLS 541
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
134-324 |
3.28e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 69.76 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFN 213
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 QglrggrvvELKKIVDEAvKSCPTVQHVLVAHRTDTKVPMGSLD--------IPLEQEMAKEAPVcTPESMSSEDMLFML 285
Cdd:PLN02387 187 K--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGssnwtvssFSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170 180 190
....*....|....*....|....*....|....*....
gi 18034773 286 YTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVF 324
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
133-643 |
4.70e-12 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 68.53 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITf 212
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmsseDMLFMLYTSGSTG 292
Cdd:cd05940 82 -------------------------------------------------------------------DAALYIYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTQAGYLLYAAMTHKLVFDYqPGDVFGCVADIGWITGHSYVVYGPLCNGATTVL---FESTPVYPDAGRYWETv 369
Cdd:cd05940 95 LPKAAIISHRRAWRGGAFFAGSGGAL-PSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASNFWDDIRKYQAT- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 370 qrlkINQFYGapTAVRLLLKygdAWVKKYDRS-SLRTLgsVGEPINHEAWEWLHKVVGDGRCTlvDTWWQTEtGGICIAP 448
Cdd:cd05940 173 ----IFQYIG--ELCRYLLN---QPPKPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPRIA--EFYAATE-GNSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 449 RPSEDGAEILPGMAMRPFFGIVPV---------LMDEKGNVLEGGDVSGALCISQAWPGMARTIYGDHQ-------RFV- 511
Cdd:cd05940 239 FFGKPGAIGRNPSLLRKVAPLALVkydlesgepIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAatekkilRDVf 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 512 ---DAYFRaypgyyfTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYP---HDikGEAA 585
Cdd:cd05940 319 kkgDAWFN-------TGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAG 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 18034773 586 FAFIVLKDNisdENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05940 390 MAAIVLQPN---EEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
517-648 |
6.87e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 67.38 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 517 AYPGYYFTGDGAHRTEGgYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNIS 596
Cdd:PRK07824 231 AEPGWFRTDDLGALDDG-VLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18034773 597 DenmVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSR 648
Cdd:PRK07824 310 P---TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
118-302 |
9.71e-12 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 67.87 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 118 TIALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAES 196
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 197 LAGrINDAKCKAVITFNqglrggrvVELKKIVDEAVKSCPTVQHVLV--------AHR----------TDTKVPMGSLD- 257
Cdd:cd17632 132 LAP-ILAETEPRLLAVS--------AEHLDLAVEAVLEGGTPPRLVVfdhrpevdAHRaalesarerlAAVGIPVTTLTl 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18034773 258 IPLEQEMAKEAPVCTPEsmSSEDMLFML-YTSGSTGTPKGLVHTQA 302
Cdd:cd17632 203 IAVRGRDLPPAPLFRPE--PDDDPLALLiYTSGSTGTPKGAMYTER 246
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
473-659 |
3.28e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 473 LMDEKGNVLEGGDVsGALCIsqAWPGMARTIYGDHQR----FVDAYFRAyPG--YYFTGDGAHRTEGGYYQITGRMDDVI 546
Cdd:PRK05691 4053 LLDEALELVPLGAV-GELCV--AGTGVGRGYVGDPLRtalaFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQV 4128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 547 NISGHRLGTAEIEDAMADHPAVPETAViGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVK 626
Cdd:PRK05691 4129 KIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLD 4207
|
170 180 190
....*....|....*....|....*....|....*.
gi 18034773 627 RLPKTRSGKVMRRLLR--KIITSRGQD-LGDTTTLE 659
Cdd:PRK05691 4208 RLPLNANGKLDRKALPalDIGQLQSQAyLAPRNELE 4243
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
135-643 |
3.37e-11 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 65.92 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVItfn 213
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggrvvelkkiVDEavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmssEDMLFMLYTSGSTGT 293
Cdd:cd05937 84 --------------VDP------------------------------------------------DDPAILIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 294 PKGLVHTQAGYLLYAAMTHKlVFDYQPGD-VFGCVAdIGWITGHSYVVYGPLCNGATTVL---FEstpvypdAGRYWETV 369
Cdd:cd05937 102 PKAAAISWRRTLVTSNLLSH-DLNLKNGDrTYTCMP-LYHGTAAFLGACNCLMSGGTLALsrkFS-------ASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 370 QRLKINQFYGAPTAVRLLLkygDAWVKKYDRSSlRTLGSVGEPINHEAWEWLHK-----VVG------DGrctlVDTWWQ 438
Cdd:cd05937 173 RDSGATIIQYVGELCRYLL---STPPSPYDRDH-KVRVAWGNGLRPDIWERFRErfnvpEIGefyaatEG----VFALTN 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 439 TETGGICIaprpsedGAEILPGMAMRPFFG--IVPVLMD-EKGNVL--------------EGGDVSGALCIS--QAWPGM 499
Cdd:cd05937 245 HNVGDFGA-------GAIGHHGLIRRWKFEnqVVLVKMDpETDDPIrdpktgfcvrapvgEPGEMLGRVPFKnrEAFQGY 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 500 ARTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYP-- 577
Cdd:cd05937 318 LHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvp 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 578 -HDikGEAAFAFIVLKDNISDEnmvVNELKLSVAT----KIAKYAVPDQILVVKRLPKTRSGKVMRRLLRK 643
Cdd:cd05937 398 gHD--GRAGCAAITLEESSAVP---TEFTKSLLASlarkNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
127-647 |
1.59e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.25 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 127 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIY--MPV--SPLAVAAMLACARIGAIHT----VVFAGFSAESLA 198
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVWAEDTLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 199 gRINDAKCKAVI----------TFNQglRGGRVVElkkiVDEAVKSCPTvqhvlvahrtdtkvpmgsldipleqemakeA 268
Cdd:PRK07768 103 -VIGMIGAKAVVvgepflaaapVLEE--KGIRVLT----VADLLAADPI------------------------------D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 PVCTPESmsseDMLFMLYTSGSTGTPKGLVHTQAGylLYA---AMTHKLVFDYQPGDVFG---CVADIGWItGHSYVvyg 342
Cdd:PRK07768 146 PVETGED----DLALMQLTSGSTGSPKAVQITHGN--LYAnaeAMFVAAEFDVETDVMVSwlpLFHDMGMV-GFLTV--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 343 PLCNGATTVL-----FESTPVYpdagryWETVqrlkINQFYGAPTA---------VRLLLKYGDAwvKKYDRSSLRTLGS 408
Cdd:PRK07768 216 PMYFGAELVKvtpmdFLRDPLL------WAEL----ISKYRGTMTAapnfayallARRLRRQAKP--GAFDLSSLRFALN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 409 VGEPINHEAWEWLHKV---VGDGRCTLVDTWWQTETG-GICIAPR---------------------PSEDGA-------- 455
Cdd:PRK07768 284 GAEPIDPADVEDLLDAgarFGLRPEAILPAYGMAEATlAVSFSPCgaglvvdevdadllaalrravPATKGNtrrlatlg 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 456 EILPGMAMRpffgivpvLMDEKGNVLEGGDVsGALCISqawpGMARTI-YGDHQRFVDAyfRAYPGYYFTGDGAHRTEGG 534
Cdd:PRK07768 364 PPLPGLEVR--------VVDEDGQVLPPRGV-GVIELR----GESVTPgYLTMDGFIPA--QDADGWLDTGDLGYLTEEG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 535 YYQITGRMDDVINISGHRLGTAEIEDAMADHPAV-PETAV-IGYPHDIKGEaAFAfIVLKDNISDENMVVNELKLSVATK 612
Cdd:PRK07768 429 EVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE-GFA-VAVESNAFEDPAEVRRIRHQVAHE 506
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 18034773 613 IAKyAV---PDQILVVK--RLPKTRSGKVMRRLLRKIITS 647
Cdd:PRK07768 507 VVA-EVgvrPRNVVVLGpgSIPKTPSGKLRRANAAELVTP 545
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
133-652 |
5.40e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 62.51 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITf 212
Cdd:PLN02860 32 RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivDEAVKS---------CPTVQ-HVLVAHRTDTKVPmGSLDIpLEQEMAKEAPVCTPE---SMSSE 279
Cdd:PLN02860 111 ----------------DETCSSwyeelqndrLPSLMwQVFLESPSSSVFI-FLNSF-LTTEMLKQRALGTTEldyAWAPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 280 DMLFMLYTSGSTGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVyGPLCNGATTVLFestPVY 359
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSA-LIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLL---PKF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 360 pDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGR---------- 429
Cdd:PLN02860 248 -DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKlfsaygmtea 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 430 C------TLVDTWWQTETGGICIAPRPSEDGAEILPGMAM-RPF----FGIVPVLMDEKGNVLEGGdvsgalcisqawP- 497
Cdd:PLN02860 327 CssltfmTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVgKPAphveLKIGLDESSRVGRILTRG------------Ph 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 498 GMARtiYGDhQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYP 577
Cdd:PLN02860 395 VMLG--YWG-QNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 578 HDIKGEAAFAFIVLKDN----ISDENMVVNELKLSVAT--------KIAKYAVPDQILV-VKRLPKTRSGKVMRRLLRKI 644
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGwiwsDNEKENAKKNLTLSSETlrhhcrekNLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRRE 551
|
....*...
gi 18034773 645 ITSRGQDL 652
Cdd:PLN02860 552 VLSHLQSL 559
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
131-581 |
9.08e-10 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 61.61 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 131 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVI 210
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 211 TFNqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpesmSSEDMLFMLYTSGS 290
Cdd:cd17640 83 VEN---------------------------------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 291 TGTPKGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIgWitgHSY---VVYGPLCNGAtTVLFESTPVYPD------ 361
Cdd:cd17640 100 TGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAYTSIRTLKDdlkrvk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 362 ------AGRYWETVQRLKINQFYGAPTAVRLLLKYgdawvkkydrssLRTLGSVGEPINheawewlhkvvGDGRCTL-VD 434
Cdd:cd17640 174 phyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGIS-----------GGGALPPhVD 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 435 TWWQ------------TETGGICIAPRPSedgaEILPGMAMRPFFGIVPVLMDEKGN-VLEGGDVSGALcisqawpgmar 501
Cdd:cd17640 231 TFFEaigievlngyglTETSPVVSARRLK----CNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVW----------- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 502 tIYGDHqrFVDAYFR---------AYPGYYFTGDGAHRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAMADHPAVPET 571
Cdd:cd17640 296 -VRGPQ--VMKGYYKnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQI 372
|
490
....*....|
gi 18034773 572 AVIGypHDIK 581
Cdd:cd17640 373 MVVG--QDQK 380
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
134-344 |
2.26e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 60.76 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfn 213
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglRGGRVVELKKIVDEAVKSCPTVQHVlvahrtDTkVPmGSLD------IPLEQEMAK------EAPVCTPESmsSEDM 281
Cdd:PTZ00216 200 ---NGKNVPNLLRLMKSGGMPNTTIIYL------DS-LP-ASVDtegcrlVAWTDVVAKghsagsHHPLNIPEN--NDDL 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 282 LFMLYTSGSTGTPKGLVHTQAGylLYA---AMTHKLVfdyqpgDVFGCVADigwitGHSYVVYGPL 344
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHGS--LTAgilALEDRLN------DLIGPPEE-----DETYCSYLPL 319
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
125-636 |
2.50e-09 |
|
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: 60.18 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 125 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAihtvVFAGFSAESLAGRInda 204
Cdd:cd17654 8 IDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGA----AYAPIDPASPEQRS--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 205 kckavitfnqglrggrvveLKKIVDEAVKSCPTVQHVLVAHRTDTkvpmgsldiPLEQEMAKEAPVCtpesmssedMLFM 284
Cdd:cd17654 81 -------------------LTVMKKCHVSYLLQNKELDNAPLSFT---------PEHRHFNIRTDEC---------LAYV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 285 LYTSGSTGTPKGlVHTQAGYLLyAAMTH-KLVFDYQPGDVFgcvadigwiTGHSYVVYGP--------LCNGATTVLFES 355
Cdd:cd17654 124 IHTSGTTGTPKI-VAVPHKCIL-PNIQHfRSLFNITSEDIL---------FLTSPLTFDPsvveiflsLSSGATLLIVPT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 356 TPVYPDAGRYWETVQRLKINQFYGAPTavrLLLKYGDAWVKKYDRS---SLRTLGSVGE--PINHEAWEWLHKVVGDGRC 430
Cdd:cd17654 193 SVKVLPSKLADILFKRHRITVLQATPT---LFRRFGSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWRGKGNRTRIF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 431 TLVDTwwqTETGGICIAPR-PSEDGAEILpGMamrPFFGIVPVLMDEKGNVLEGGDVSGAL---CISQAWPGMartiygd 506
Cdd:cd17654 270 NIYGI---TEVSCWALAYKvPEEDSPVQL-GS---PLLGTVIEVRDQNGSEGTGQVFLGGLnrvCILDDEVTV------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 507 hqrfVDAYFRAypgyyfTGDGAHRTEGGYYqITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYphdiKGEAAF 586
Cdd:cd17654 336 ----PKGTMRA------TGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS----DQQRLI 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18034773 587 AFIVLKDNISDENmvvNELKLsvaTKIAKYAVPDQILVVKRLPKTRSGKV 636
Cdd:cd17654 401 AFIVGESSSSRIH---KELQL---TLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
135-635 |
3.56e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.11 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 135 TYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQ 214
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKYSV-EGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 215 GLRGGRVVELKKIVDEavkscptVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEAPVctpeSMSSEDMLFMLYTSGSTGTP 294
Cdd:PRK08043 312 FLDKGKLWHLPEQLTQ-------VRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQV----KQQPEDAALILFTSGSEGHP 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 295 KGLVHTQAGyLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLfestpvYPDAGRYW---ETVQR 371
Cdd:PRK08043 381 KGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL------YPSPLHYRivpELVYD 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 372 LKINQFYGAPTavrLLLKYGdAWVKKYDRSSLRTLGSVGEPINHEAWE-WLHKVvgdgRCTLVDTWWQTETGGIC----- 445
Cdd:PRK08043 454 RNCTVLFGTST---FLGNYA-RFANPYDFARLRYVVAGAEKLQESTKQlWQDKF----GLRILEGYGVTECAPVVsinvp 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 446 IAPRPSEDGaEILPGMAMRpffgIVPVLMDEKGNVLE--GGDV-SGALCISQawPGM-----ARTIYGDHQrfvdayfra 517
Cdd:PRK08043 526 MAAKPGTVG-RILPGMDAR----LLSVPGIEQGGRLQlkGPNImNGYLRVEK--PGVlevptAENARGEME--------- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 518 yPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIED-AMADHPAVPETAVIgYPHDIKGEAAFAFIVlkDNIS 596
Cdd:PRK08043 590 -RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGEALVLFTT--DSEL 665
|
490 500 510
....*....|....*....|....*....|....*....
gi 18034773 597 DENMVvneLKLSVATKIAKYAVPDQILVVKRLPKTRSGK 635
Cdd:PRK08043 666 TREKL---QQYAREHGVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
133-594 |
5.68e-09 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 59.23 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAihTVVFAGFS--AESLAGRINDAKCKAV 209
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGC--PVAFLNTNirSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 210 ITfnqglrggrVVELKKIVDEAvksCPTVQ----HVLVAHRTDTKVPMGSldipLEQEMAKEAPVCTPESMSSE----DM 281
Cdd:cd05938 83 VV---------APELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVIS----LLDKVDAASDEPVPASLRAHvtikSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 282 LFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHklvfdyqpgdVFGCVA-DIGWITGHSYVVYGPL-----C--NGATTVL- 352
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVLQCSGFLS----------LCGVTAdDVIYITLPLYHSSGFLlgiggCieLGATCVLk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 353 --FESTPVYPDAGRY-----------------------------------------WETVQR----LKINQFYGAPTAVR 385
Cdd:cd05938 217 pkFSASQFWDDCRKHnvtviqyigellrylcnqpqspndrdhkvrlaignglradvWREFLRrfgpIRIREFYGSTEGNI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 386 LLLKYGDawvkkydrsslrTLGSVGEPinheawEWLHKVVgdgrCTLVDTWWQTETG-------GICIAPRPSEDGAEIL 458
Cdd:cd05938 297 GFFNYTG------------KIGAVGRV------SYLYKLL----FPFELIKFDVEKEepvrdaqGFCIPVAKGEPGLLVA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 459 PGMAMRPFFGIV--PVLMDEK--GNVLEGGDV---SGALcisqawpgmartIYGDHQRFVdaYFRaypgyyftgdgahrt 531
Cdd:cd05938 355 KITQQSPFLGYAgdKEQTEKKllRDVFKKGDVyfnTGDL------------LVQDQQNFL--YFH--------------- 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 532 eggyyqitGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYP---HDikGEAAFAFIVLKDN 594
Cdd:cd05938 406 --------DRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvpgHE--GRIGMAAVKLKPG 461
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
522-636 |
7.89e-09 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 58.68 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPET------------AVIGY--PHDIKGEAAFA 587
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSYivPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 588 FIVLKDNISDENMVV----------NELKLSVATKIAKYAVPDQILVVKRLPKTRSGKV 636
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
282-636 |
2.14e-08 |
|
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: 56.54 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 282 LFMLYTSGSTGTPKGLVHTQAGYLLYAAMthklvfdyqpgdvfgcVADIGWITGHS-YVVYGPLCN------GATTVLFE 354
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLAQALV----------------LAVLQAIDEGTvFLNSGPLFHigtlmfTLATFHAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 355 STPVY---PDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSvgepinheAWEWLHKVVGDgrct 431
Cdd:cd17636 67 GTNVFvrrVDAEEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSSPA--------APEWNDMATVD---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 432 lvDTWW--------QTETGG-----------ICIAPRPSedgaeilPGMAMRpffgivpvLMDEKGNVLEGGDVsGALCI 492
Cdd:cd17636 133 --TSPWgrkpggygQTEVMGlatfaalgggaIGGAGRPS-------PLVQVR--------ILDEDGREVPDGEV-GEIVA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 493 sQAWPGMARtiYGDH-----QRFVDayfraypGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPA 567
Cdd:cd17636 195 -RGPTVMAG--YWNRpevnaRRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPA 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 568 VPETAVIGYPHDIKGEAAFAFIVLKDNIS-DENMVVNELKlsvaTKIAKYAVPDQILVVKRLPKTRSGKV 636
Cdd:cd17636 265 VADAAVIGVPDPRWAQSVKAIVVLKPGASvTEAELIEHCR----ARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
279-647 |
4.65e-08 |
|
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: 55.96 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 279 EDMLFMLYTSGSTGTPKGLVHTQagyllyaamtHKLVFDyqpgdVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPV 358
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVHN-----MFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 359 YPDAGRY-------------W-ETVQRLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHK 423
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 424 ---VVGDGRCTLVDTWWQTE-TGGICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKgNVLEGGDVSGALCISQAwpgm 499
Cdd:cd05908 251 hmsKYGLKRNAILPVYGLAEaSVGASLPKAQSPFKTITLGRRHVTHGEPEPEVDKKDS-ECLTFVEVGKPIDETDI---- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 500 aRTIYGDHQRFVDAYF--------RAYPGYY---------FTGDGAHRT------EGGYYQITGRMDDVINISGHRLGTA 556
Cdd:cd05908 326 -RICDEDNKILPDGYIghiqirgkNVTPGYYnnpeatakvFTDDGWLKTgdlgfiRNGRLVITGREKDIIFVNGQNVYPH 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 557 EIEDAMADHPAVP--ETAVIG-YPHDIKGEAAFAFIVLKDNISDENMVVNELKlSVATKIAKYAVpDQILVVKRLPKTRS 633
Cdd:cd05908 405 DIERIAEELEGVElgRVVACGvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIK-KHLNKRGGWQI-NEVLPIRRIPKTTS 482
|
410
....*....|....
gi 18034773 634 GKVMRRLLRKIITS 647
Cdd:cd05908 483 GKVKRYELAQRYQS 496
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-575 |
5.52e-08 |
|
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: 55.93 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKckavitf 212
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 213 nqglrggrvvelkkivdeavkscptvqhvlvahrtdtkvPMGSLDIPLEQEMAKeapvctpesmssedmlfMLYTSGSTG 292
Cdd:cd05910 75 ---------------------------------------PDAFIGIPKADEPAA-----------------ILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 293 TPKGLVHTQAgylLYAAMTHKL--VFDYQPGDV----FGCVAdigwitghsyvVYGPLCnGATTVLFESTPVYP---DAG 363
Cdd:cd05910 99 TPKGVVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 364 RYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINHEAWEWLHKVVGDGrCTLVDTWWQTETGG 443
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSDE-AEILTPYGATEALP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 444 IC-IAPR--------PSEDGAEILPGmamRPFFGI-VPVLMDEKGNVLEGGD-------VSGALCISQawPGMARTIYG- 505
Cdd:cd05910 241 VSsIGSRellatttaATSGGAGTCVG---RPIPGVrVRIIEIDDEPIAEWDDtlelprgEIGEITVTG--PTVTPTYVNr 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 506 -----------DHQRFVD-----AYFRAYPGYYFTGDGAHRTEGgyyqitgrmddviniSGHRLGTAEIEDAMADHPAVP 569
Cdd:cd05910 316 pvatalakiddNSEGFWHrmgdlGYLDDEGRLWFCGRKAHRVIT---------------TGGTLYTEPVERVFNTHPGVR 380
|
....*.
gi 18034773 570 ETAVIG 575
Cdd:cd05910 381 RSALVG 386
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
105-297 |
5.86e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 105 VNCLDQHVQKSPETIALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHrGDRVAIYMPVSPLAVAAMLACARIGAI 184
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 185 HTVVFAGFSA-----ESLAGRINDAKCKAVITfNQGLRGGrvveLKKIVDEAVKSCPTVQHVlvahrtDTkvpmgsLDIP 259
Cdd:PRK05691 91 AVPAYPPESArrhhqERLLSIIADAEPRLLLT-VADLRDS----LLQMEELAAANAPELLCV------DT------LDPA 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 18034773 260 LEQEMAKEApvctpesMSSEDMLFMLYTSGSTGTPKGL 297
Cdd:PRK05691 154 LAEAWQEPA-------LQPDDIAFLQYTSGSTALPKGV 184
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
134-300 |
9.08e-08 |
|
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: 55.30 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 134 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITfn 213
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 214 qglrggrvvelkkivdeavkscptvqhvlvahrtdtkvpmgsldipleqemakeapvctpeSMSSEDMLFMLYTSGSTGT 293
Cdd:cd17639 84 -------------------------------------------------------------DGKPDDLACIMYTSGSTGN 102
|
....*..
gi 18034773 294 PKGLVHT 300
Cdd:cd17639 103 PKGVMLT 109
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
129-381 |
1.29e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 54.85 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 129 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDA---- 204
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAevsi 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 205 ----------------KC----KAVITFnqglrGGRVVELKKIVDEAVKSCPTVQHVLVahrtdtkvpMGSLDIPLEQEm 264
Cdd:PLN02861 153 afvqeskissilsclpKCssnlKTIVSF-----GDVSSEQKEEAEELGVSCFSWEEFSL---------MGSLDCELPPK- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 265 aKEAPVCTpesmssedmlfMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFdyqpgdvfgcVADIGWITGHSYVVYGPL 344
Cdd:PLN02861 218 -QKTDICT-----------IMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPL 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18034773 345 CNGATTVLfESTPVYPDAG-RYW--------ETVQRLKINQFYGAP 381
Cdd:PLN02861 276 AHVYDQVI-ETYCISKGASiGFWqgdirylmEDVQALKPTIFCGVP 320
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
522-636 |
1.62e-07 |
|
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: 55.07 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 522 YFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPE--TAV----------IGY--PHDiKGEAAFA 587
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvTLVrrdkdeeptlVSYivPQD-KSDELEE 758
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034773 588 FIVLKDNISDENMVVN----------ELKLSVATKIAKYAVPDQILVVKRLPKTRSGKV 636
Cdd:TIGR03443 759 FKSEVDDEESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
136-301 |
8.29e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 52.31 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 136 YRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHT-----VVFAGFSA--ESLAGRINDAKCKA 208
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 VITfnqglrggrVVELKKIVDEAVKSCPTVqhvlvahrtdtkvpmgsLDIPLEQEMAKEAPVCTPESMSSEDMLFMLYTS 288
Cdd:PRK09192 132 IIT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSS 185
|
170
....*....|...
gi 18034773 289 GSTGTPKGLVHTQ 301
Cdd:PRK09192 186 GSTRFPRGVIITH 198
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
127-298 |
1.01e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 51.95 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 127 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKC 206
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 207 KAVItfnqglrggrvVELKKIvDEAVKSCPTVQHV----------------------LVAHRTDTKVPMG---SLDIPLE 261
Cdd:PLN02614 153 SIVF-----------VEEKKI-SELFKTCPNSTEYmktvvsfggvsreqkeeaetfgLVIYAWDEFLKLGegkQYDLPIK 220
|
170 180 190
....*....|....*....|....*....|....*..
gi 18034773 262 qemaKEAPVCTpesmssedmlfMLYTSGSTGTPKGLV 298
Cdd:PLN02614 221 ----KKSDICT-----------IMYTSGTTGDPKGVM 242
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
107-301 |
1.56e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 51.42 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 107 CLDQHVQKSPETIALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSP----LAVAAMLAcarig 182
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYA----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 183 aihTVVFAGFS-AESLAGRiNDAKCKAVItfnQGLRGGRVvelkkIVDEAVKSCPTVQHVLVAHR---TDTKVPMGSLDI 258
Cdd:PRK08180 118 ---GVPYAPVSpAYSLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAAT 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18034773 259 PLEQEMAKEAPVCTPESMSS---EDMLFMLYTSGSTGTPKGLVHTQ 301
Cdd:PRK08180 186 PFAALLATPPTAAVDAAHAAvgpDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
125-324 |
2.10e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.87 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 125 RDEP--GTEVR----------ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGF 192
Cdd:PLN02736 58 RDYKylGTRIRvdgtvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 193 SAESLAGRINDAKCKAVITFNQGLrggrvvelkKIVDEAVKSCPTVQHVLVAHRTDTKVP---------MGSLDIPLEQE 263
Cdd:PLN02736 138 GPDAVKFIVNHAEVAAIFCVPQTL---------NTLLSCLSEIPSVRLIVVVGGADEPLPslpsgtgveIVTYSKLLAQG 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034773 264 MAKEAPVCTPESmssEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMThKLVFDYQPGDVF 324
Cdd:PLN02736 209 RSSPQPFRPPKP---EDVATICYTSGTTGTPKGVVLTHGNLIANVAGS-SLSTKFYPSDVH 265
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
133-650 |
2.04e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.04 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 133 RITYRELLETTCRLANTLKrHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVfaGFSAeSLAGRIndAKCKA---- 208
Cdd:PRK06814 658 PLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSA-GIANIL--SACKAaqvk 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 209 -VITFNQGLRGGRvveLKKIVDEAVKScptvqhVLVAHRTDTKVPMGSLDiPLEQEMAKEAPVCTPESMSSEDMLFMLYT 287
Cdd:PRK06814 732 tVLTSRAFIEKAR---LGPLIEALEFG------IRIIYLEDVRAQIGLAD-KIKGLLAGRFPLVYFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 288 SGSTGTPKGLVHTQAGYLLYAAMTHKLVfDYQPGD-VFGCVADIgwitgHSYVVYG----PLCNGATTVLfestpvYPDA 362
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDkVFNALPVF-----HSFGLTGglvlPLLSGVKVFL------YPSP 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 363 GRYW---ETVQRLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPINHEAWE-WLHKVvgdgRCTLVDTWWQ 438
Cdd:PRK06814 870 LHYRiipELIYDTNATILFGTDTFLNGYARYAHP----YDFRSLRYVFAGAEKVKEETRQtWMEKF----GIRILEGYGV 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 439 TETGGI--CIAP---RPSEDGaEILPGMAMRpffgIVPVlmdekgnvlEGGDVSGALCISqawpG---MArtiygdhqrf 510
Cdd:PRK06814 942 TETAPViaLNTPmhnKAGTVG-RLLPGIEYR----LEPV---------PGIDEGGRLFVR----GpnvML---------- 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 511 vdAYFRA---------YPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIK 581
Cdd:PRK06814 994 --GYLRAenpgvleppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARK 1071
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034773 582 GEAafafIVL---KDNISDENMvvneLKLSVATKIAKYAVPDQILVVKRLPKTRSGKV----MRRLLRKIITSRGQ 650
Cdd:PRK06814 1072 GER----IILlttASDATRAAF----LAHAKAAGASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEA 1139
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
101-300 |
2.99e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.12 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 101 LNVSVNCLDQHVQKSPETIALIWER--DEP-GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLA 177
Cdd:PLN02430 41 ITTAWDIFSKSVEKYPDNKMLGWRRivDGKvGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 178 CARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQglrggrvvELKKIVDEAVKSCPTVQHV-----LVAHRTDTKVP 252
Cdd:PLN02430 121 CAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK--------KIKELLEPDCKSAKRLKAIvsftsVTEEESDKASQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034773 253 MGSLDIPLEQ--EMAKEAP--VCTPESMsseDMLFMLYTSGSTGTPKGLVHT 300
Cdd:PLN02430 193 IGVKTYSWIDflHMGKENPseTNPPKPL---DICTIMYTSGTSGDPKGVVLT 241
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
116-445 |
1.56e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 44.73 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 116 PETIALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVS----PLAVAAMLAcarigaihTVVFAG 191
Cdd:cd05921 9 PDRTWLA-EREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSiehaLMALAAMYA--------GVPAAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 192 FS-AESLAGRiNDAKCKAVItfnqGLRGGRVV------ELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSL-DIPLEQE 263
Cdd:cd05921 80 VSpAYSLMSQ-DLAKLKHLF----ELLKPGLVfaqdaaPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELaATPPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 264 MAKEAPVCTPESMSSedmlfMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKlVFDYQPGDVFGCVADIGW--ITGHSYVVY 341
Cdd:cd05921 155 VDAAFAAVGPDTVAK-----FLFTSGSTGLPKAVINTQRMLCANQAMLEQ-TYPFFGEEPPVLVDWLPWnhTFGGNHNFN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 342 GPLCNGATTVLFESTPVypdAGRYWETVQRLK---INQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINHE 416
Cdd:cd05921 229 LVLYNGGTLYIDDGKPM---PGGFEETLRNLReisPTVYFNVPAGWEMLVAAleKDEALRRRFFKRLKLMFYAGAGLSQD 305
|
330 340 350
....*....|....*....|....*....|...
gi 18034773 417 AWEWLHKV----VGDgRCTLVDTWWQTETGGIC 445
Cdd:cd05921 306 VWDRLQALavatVGE-RIPMMAGLGATETAPTA 337
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
121-296 |
1.62e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.73 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 121 LIWERDEPGTEVRITYRELLETTCRLANTLKRHgVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFA----GfSAES 196
Cdd:PRK12476 56 LDHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApelpG-HAER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 197 LAGRINDAKCKAVITfnqglrggrvvelkkivDEAVKscPTVQHVLVAHRTDTKVPMGSLD-IPleqemAKEAPVCTPES 275
Cdd:PRK12476 134 LDTALRDAEPTVVLT-----------------TTAAA--EAVEGFLRNLPRLRRPRVIAIDaIP-----DSAGESFVPVE 189
|
170 180
....*....|....*....|.
gi 18034773 276 MSSEDMLFMLYTSGSTGTPKG 296
Cdd:PRK12476 190 LDTDDVSHLQYTSGSTRPPVG 210
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
520-644 |
3.21e-04 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 44.14 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 520 GYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMadHPAVPET----AVIGYPHDIKGEaafAFIVLkdnI 595
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGE---KLVVL---H 1090
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18034773 596 SDENMVVNELKLSVA-TKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKI 644
Cdd:PRK08633 1091 TCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
558-644 |
1.18e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 41.67 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 558 IEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVlkdniSDENMVVNELKLSVATKIAKYAvPDQILVVKRLPKTRSGKVM 637
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFVE-----AELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
....*..
gi 18034773 638 RRLLRKI 644
Cdd:PRK09188 319 DDILRLI 325
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
120-444 |
5.10e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 40.03 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 120 ALIWERDEPGTEVR-ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESla 198
Cdd:PRK12582 66 PWLAQREPGHGQWRkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMS-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 199 griND-AKCK--------AVITFNQGLRGGRVVELKKIVDeavkscPTVQHVLVAHRTDTKVPMGSL-DIPLEQEMAKEA 268
Cdd:PRK12582 144 ---HDhAKLKhlfdlvkpRVVFAQSGAPFARALAALDLLD------VTVVHVTGPGEGIASIAFADLaATPPTAAVAAAI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 269 PVCTPESMSSedmlfMLYTSGSTGTPKGLVHTQAGYLLYAAMThKLVFDYQPGDVFGCVAD-IGW--ITGHSYVVYGPLC 345
Cdd:PRK12582 215 AAITPDTVAK-----YLFTSGSTGMPKAVINTQRMMCANIAMQ-EQLRPREPDPPPPVSLDwMPWnhTMGGNANFNGLLW 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 346 NGATTVLFESTPVypdAGRYWETVQRLK-INQ--FYGAPTAVRLL---LKYGDAWVKKYdRSSLRTLGSVGEPINHEAWE 419
Cdd:PRK12582 289 GGGTLYIDDGKPL---PGMFEETIRNLReISPtvYGNVPAGYAMLaeaMEKDDALRRSF-FKNLRLMAYGGATLSDDLYE 364
|
330 340
....*....|....*....|....*...
gi 18034773 420 WL--HKVVGDGRCTLVDTWW-QTETGGI 444
Cdd:PRK12582 365 RMqaLAVRTTGHRIPFYTGYgATETAPT 392
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
519-640 |
5.45e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 39.75 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034773 519 PGYYF-TGDGAHRTEGGYYqITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISD 597
Cdd:PRK05851 394 PDDWFpTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGPD 472
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18034773 598 ENMVVNELKLSVATKIAkyAVPDQILVVK--RLPKTRSGKvMRRL 640
Cdd:PRK05851 473 EAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| |
