|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
24-654 |
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: 1180.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 24 EEYQKFYQESLDNPAEFWSRVAKQFHWETPADQDkflkynFNISKGPISIKWMEGASTNLCYNLLDRNVRNgLGDQIAYY 103
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKV------LDWSKGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 104 WEGNHPDDySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERM 183
Cdd:cd05966 74 WEGDEPDQ-SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 184 FDCKAKLLITADGAWRGEKPLYLKALCDTALEKveemGHSVEKCIVVSHLKRvtpcqpdhveeEIPWTDDRDYWWHEEME 263
Cdd:cd05966 153 NDAQCKLVITADGGYRGGKVIPLKEIVDEALEK----CPSVEKVLVVKRTGG-----------EVPMTEGRDLWWHDLMA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 264 DKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLA 343
Cdd:cd05966 218 KQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 344 NGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYI 423
Cdd:cd05966 298 NGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 424 GKEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNHE 503
Cdd:cd05966 378 GKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 504 RFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCF 583
Cdd:cd05966 458 RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAF 537
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667955 584 ITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDRNVGDTSTLAD 654
Cdd:cd05966 538 VTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
7-665 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1128.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 7 IYDPNPAISQNAYISsFEEYQKFYQESLDNPAEFWSRVAKQFHWETPadqdkflkYNFNISKGPISIKWMEGASTNLCYN 86
Cdd:PRK00174 1 VFPPPAEFAANALID-MEQYKALYQESVEDPEGFWAEQAKRLDWFKP--------FDTVLDWNAPFIKWFEDGELNVSYN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 87 LLDRNVRNGlGDQIAYYWEGNHPDDySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAV 166
Cdd:PRK00174 72 CLDRHLKTR-GDKVAIIWEGDDPGD-SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 167 HSIVFAGFSPDSLAERMFDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEemghSVEKCIVVSHLKrvtpcqpdhveE 246
Cdd:PRK00174 150 HSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG-----------G 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 247 EIPWTDDRDYWWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTG 326
Cdd:PRK00174 215 DVDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 327 DVGWITGHTYVVYGPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGS 406
Cdd:PRK00174 295 DVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 407 VGEPINPEAWLWYYKYIGKEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLV 486
Cdd:PRK00174 375 VGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 487 FSQPWPGMMRTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAES 566
Cdd:PRK00174 455 IKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 567 AVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDRNV 646
Cdd:PRK00174 535 AVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEIL 614
|
650
....*....|....*....
gi 24667955 647 GDTSTLADEQIVEQLFANR 665
Cdd:PRK00174 615 GDTSTLADPSVVEKLIEAR 633
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
20-661 |
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: 1058.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 20 ISSFEEYQKFYQESLDNPAEFWSRVAKQ-FHWETPADqdKFLKYNFniskgPISIKWMEGASTNLCYNLLDRNVRNgLGD 98
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARElLDWFKPFT--KVLDWSF-----PPFYKWFVGGELNVSYNCVDRHLEA-RPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 99 QIAYYWEGNHPDDySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDS 178
Cdd:TIGR02188 73 KVAIIWEGDEPGE-VRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 179 LAERMFDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEEmghSVEKCIVVSHLKrvtpcqpdhvEEEIPWTDDRDYWW 258
Cdd:TIGR02188 152 LADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPV---SVEHVLVVRRTG----------NPVVPWVEGRDVWW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 259 HEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVV 338
Cdd:TIGR02188 219 HDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 339 YGPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLW 418
Cdd:TIGR02188 299 YGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 YYKYIGKEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGE-GYLVFSQPWPGMMRT 497
Cdd:TIGR02188 379 YYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEgGYLVIKQPWPGMLRT 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 498 LYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKG 577
Cdd:TIGR02188 459 IYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 578 ECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDR-NVGDTSTLADEQ 656
Cdd:TIGR02188 539 QAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAeILGDTSTLEDPS 618
|
....*
gi 24667955 657 IVEQL 661
Cdd:TIGR02188 619 VVEEL 623
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
74-661 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 875.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 74 KWMEGASTNLCYNLLDRNVRnGLGDQIAYYWEGnhPDDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILEL 153
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEG--EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 154 PIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEemghSVEKCIVVshl 233
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELP----SLEHVIVV--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 234 krvtpcqpDHVEEEIPWtdDRDYWWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIV 313
Cdd:COG0365 151 --------GRTGADVPM--EGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 314 FDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPV 393
Cdd:COG0365 221 LDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 394 LKHNLSGLKVLGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQTETGGHVITPLPGaTPMKPGSASFPFFGVKPTLLDEC 473
Cdd:COG0365 301 KKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 474 GIEIKGEGEGYLVFSQPWPGMMRTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEV 553
Cdd:COG0365 377 GNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 554 ESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:COG0365 457 ESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMR 536
|
570 580
....*....|....*....|....*...
gi 24667955 634 RVLRKIAvNDRNVGDTSTLADEQIVEQL 661
Cdd:COG0365 537 RLLRKIA-EGRPLGDTSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4-663 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 874.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 4 EKSIYDPNPAISQNAYISSFEEYQKFYQESLDNPAEFWSRVAKQFHWETPADQDKFLKYNFNISKGPISIKWMEGASTNL 83
Cdd:PLN02654 10 ENDLVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEVCSENLDVRKGPISIEWFKGGKTNI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 84 CYNLLDRNVRNGLGDQIAYYWEGNHPDdYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARI 163
Cdd:PLN02654 90 CYNCLDRNVEAGNGDKIAIYWEGNEPG-FDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 164 GAVHSIVFAGFSPDSLAERMFDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEEMGHSVEKCIVVSHLKRVTpcqpdh 243
Cdd:PLN02654 169 GAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYENQLAMK------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 244 vEEEIPWTDDRDYWWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYW 323
Cdd:PLN02654 243 -REDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 324 CTGDVGWITGHTYVVYGPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKV 403
Cdd:PLN02654 322 CTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 404 LGSVGEPINPEAWLWYYKYIGKEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEG 483
Cdd:PLN02654 402 LGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 484 YLVFSQPWPGMMRTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRV 563
Cdd:PLN02654 482 YLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 564 AESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVND 643
Cdd:PLN02654 562 AEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQ 641
|
650 660
....*....|....*....|.
gi 24667955 644 RN-VGDTSTLADEQIVEQLFA 663
Cdd:PLN02654 642 LDeLGDTSTLADPGVVDQLIA 662
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
26-632 |
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: 722.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 26 YQKFYQESLDNPAEFWSRVAKQFHWETPADQDKflkyNFNISKGPISIKWMEGASTNLCYNLLDRNVRNGlGDQIAYYWE 105
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVK----NTSFAPGAPSIKWFEDATLNLAANALDRHLREN-GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 106 GNHPDDySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFD 185
Cdd:cd17634 76 GDDTSQ-SRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 186 CKAKLLITADGAWRGEKPLYLKALCDTALEKveeMGHSVEKCIVVshlkrvtpcqpDHVEEEIPWTDDRDYWWHEEMEDK 265
Cdd:cd17634 155 SSSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVL-----------KRTGSDIDWQEGRDLWWRDLIAKA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 266 EPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANG 345
Cdd:cd17634 221 SPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 346 ATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGK 425
Cdd:cd17634 301 ATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 426 EQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNHERF 505
Cdd:cd17634 381 EKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 506 EDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFIT 585
Cdd:cd17634 461 EQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 24667955 586 PNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIM 632
Cdd:cd17634 541 LNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
26-661 |
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: 607.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 26 YQKFYQESLDNPAEFWSRVAKQFHWETPADQdkflkyNFNISKGPISiKWMEGASTNLCYNLLDRNVRNGLGDQIAYYWE 105
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEK------ILDNSNPPFT-RWFVGGRLNTCYNALDRHVEAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 106 ----GNhpddySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAE 181
Cdd:cd05967 74 spvtGT-----ERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 182 RMFDCKAKLLITADGAWRGEKPLYLKALCDTALekvEEMGHSVEKCIVVSHLKrvTPCQPDHVeeeipwtdDRDYWWHEE 261
Cdd:cd05967 149 RIDDAKPKLIVTASCGIEPGKVVPYKPLLDKAL---ELSGHKPHHVLVLNRPQ--VPADLTKP--------GRDLDWSEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 262 MEDKEPAcYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGP 341
Cdd:cd05967 216 LAKAEPV-DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 LANGATSVIFEGTP-FFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKF--GEGPVLKHNLSGLKVLGSVGEPINPEAWLW 418
Cdd:cd05967 295 LLHGATTVLYEGKPvGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 YYKYIGKeqcSIVDTFWQTETGGHVITPLPG--ATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPW-PGMM 495
Cdd:cd05967 375 AENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 496 RTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPV 575
Cdd:cd05967 452 LTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEL 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 576 KGECLYCFITPNEN-EVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAvNDRNVGDTSTLAD 654
Cdd:cd05967 532 KGQVPLGLVVLKEGvKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA-DGEDYTIPSTIED 610
|
....*..
gi 24667955 655 EQIVEQL 661
Cdd:cd05967 611 PSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
24-661 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 551.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 24 EEYQKFYQESLDNPAEFWSRVAKQFHWETPADQdkFLKYnfniSKGPISiKWMEGASTNLCYNLLDRNVRnGLGDQIAYY 103
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQ--VLDY----SNPPFA-RWFVGGRTNLCHNAVDRHLA-KRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 104 WEGNHPDDySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERM 183
Cdd:PRK10524 74 AVSTETDE-ERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 184 FDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEemgHSVEKCIVVShlKRVTPCqpdhveeeiPWTDDRDYWWHEEME 263
Cdd:PRK10524 153 DDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQ---HKPRHVLLVD--RGLAPM---------ARVAGRDVDYATLRA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 264 DKEPACYP-EWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPL 342
Cdd:PRK10524 219 QHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 ANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKY 422
Cdd:PRK10524 299 LAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 423 IGKeqcSIVDTFWQTETGGHVITPLPG--ATPMKPGSASFPFFGVKPTLLDECGIEIKGEGE-GYLVFSQPW-PGMMRTL 498
Cdd:PRK10524 379 LGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEkGVLVIEGPLpPGCMQTV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 499 YNNHERFEDTYFSKF-PGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKG 577
Cdd:PRK10524 456 WGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 578 ECLYCFITPNENEVFD-----QKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAvNDRNVGDTSTL 652
Cdd:PRK10524 536 QVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIA-EGRDPGDLTTI 614
|
650
....*....|...
gi 24667955 653 AD----EQIVEQL 661
Cdd:PRK10524 615 EDpaalQQIRQAL 627
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
23-654 |
1.24e-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: 1.24e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 23 FEEYQKFYQESLDNPAEFWSRVAKQ--FHWETPADQdkflkyNFNISKGPISIKWMEGASTNLCYNLLDRNVRNGlGDQI 100
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDvgIEWYEPPYQ------TLDLSGGKPWAAWFVGGRMNIVEQLLDKWLADT-RTRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 101 AYYWEGNhpDDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLA 180
Cdd:cd05968 79 ALRWEGE--DGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 181 ERMFDCKAKLLITADGAWRGEKPLYLKALCDTALEKVEemghSVEKCIVVSHLKRvtpcqpdhveeEIPWTDDRDYWWHE 260
Cdd:cd05968 157 TRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCP----TVEKVVVVRHLGN-----------DFTPAKGRDLSYDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 261 EMEDKEPACypEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGD-IYWCTgDVGWITGhTYVVY 339
Cdd:cd05968 222 EKETAGDGA--ERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWY 419
Cdd:cd05968 298 GGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 420 YKYIGKEQCSIVDTFWQTETGGHVITPLPgATPMKPGSASFPFFGVKPTLLDECGIEIKGEgEGYLVFSQPWPGMMRTLY 499
Cdd:cd05968 378 FETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPWPGMTRGFW 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 500 NNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGEC 579
Cdd:cd05968 456 RDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEA 535
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667955 580 LYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKiAVNDRNVGDTSTLAD 654
Cdd:cd05968 536 IVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA-AYLGKELGDLSSLEN 609
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
75-654 |
4.28e-173 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 505.97 E-value: 4.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 75 WMEGASTNLCYNLLDRNVRNGLGDQIAYYWEGNHPDdysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELP 154
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGRKDKVALRYLDASRK---EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 155 IAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGawrgekpLYLKalcdtalEKVEEMGHsVEKCIVVshlk 234
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPA-------LLER-------KPADDLPS-LKHVLLV---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 235 rvtpcqpDHVEEEIPWTDDrdywWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTfKIVF 314
Cdd:PRK04319 174 -------GEDVEEGPGTLD----FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 315 DYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGTpFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVL 394
Cdd:PRK04319 242 DLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGR-FSP--ERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 395 KHNLSGLKVLGSVGEPINPEAWLWYYKYIGKEqcsIVDTFWQTETGGHVITPLPgATPMKPGSASFPFFGVKPTLLDECG 474
Cdd:PRK04319 319 KYDLSSLRHILSVGEPLNPEVVRWGMKVFGLP---IHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 475 IEIKGEGEGYLVFSQPWPGMMRTLYNNHERFEDtYFSkfPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVE 554
Cdd:PRK04319 395 NELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 555 SVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRR 634
Cdd:PRK04319 472 SKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRR 551
|
570 580
....*....|....*....|
gi 24667955 635 VLRKIAVNdRNVGDTSTLAD 654
Cdd:PRK04319 552 VLKAWELG-LPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
116-641 |
4.49e-139 |
|
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: 414.21 E-value: 4.49e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwHEEMEDKepacypewMD 275
Cdd:cd05969 79 ---------------------------------------------------------------TEELYER--------TD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTfKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGTp 355
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTG-KYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGR- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 356 FFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGKeqcSIVDTFW 435
Cdd:cd05969 166 FDA--ESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV---PIHDTWW 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 436 QTETGGHVITPLPGaTPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNHERFEDTYFSkfpG 515
Cdd:cd05969 241 QTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSFID---G 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 516 YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQK 595
Cdd:cd05969 317 WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24667955 596 LISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAV 641
Cdd:cd05969 397 LKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
116-638 |
2.54e-115 |
|
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: 352.41 E-value: 2.54e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewmD 275
Cdd:cd05972 79 -------------------------------------------------------------------------------D 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTtAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGTP 355
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 356 FFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGegpVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGKeqcSIVDTFW 435
Cdd:cd05972 159 FDA--ERILELLERYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGL---PIRDGYG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 436 QTETGgHVITPLPGaTPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNHERFEDTYFSkfpG 515
Cdd:cd05972 231 QTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRG---D 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 516 YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQK 595
Cdd:cd05972 306 YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEE 385
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24667955 596 LISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05972 386 LAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
88-544 |
9.91e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 345.45 E-value: 9.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 88 LDRNVRNgLGDQIAYYwegnhPDDYSRgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVH 167
Cdd:pfam00501 1 LERQAAR-TPDKTALE-----VGEGRR-LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 168 SIVFAGFSPDSLAERMFDCKAKLLITADgawrgekplylkALCDTALEKVEEMGHSVEKCIVVSHLkrvtpcqPDHVEEE 247
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDD------------ALKLEELLEALGKLEVVKLVLVLDRD-------PVLKEEP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 248 IPWTDDRDYWWHEEmedkepacyPEWMDAEDPLFMLYTSGSTGKPKGVLHTTaGYLLYAATTFKIV----FDYKPGDIYW 323
Cdd:pfam00501 135 LPEEAKPADVPPPP---------PPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 324 CTGDVGWITGHTYVVYGPLANGATSVIFEGTPFFPGnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKhnLSGLKV 403
Cdd:pfam00501 205 STLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALDP-AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL--LSSLRL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 404 LGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQTETGGHVITPLPGATPM-KPGSASFPFFGVKPTLLDECGIEIKGEGE 482
Cdd:pfam00501 282 VLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDETGEPVPPGE 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 483 -GYLVFSQpwPGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVS 544
Cdd:pfam00501 359 pGELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
87-644 |
2.52e-94 |
|
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: 298.65 E-value: 2.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 87 LLDRNVRNGlGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAV 166
Cdd:COG0318 4 LLRRAAARH-PDRPALVFGG-------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 167 HSIVFAGFSPDSLAERMFDCKAKLLITAdgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhvee 246
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVTA---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 247 eipwtddrdywwheemedkepacypewmdaedplFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTG 326
Cdd:COG0318 104 ----------------------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVAL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 327 DVGWITGHTYVVYGPLANGATSVIFEGtpFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGS 406
Cdd:COG0318 149 PLFHVFGLTVGLLAPLLAGATLVLLPR--FDP--ERVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 407 VGEPINPEAWLWYYKYIGkeqCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIK-GE-GEgy 484
Cdd:COG0318 223 GGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPpGEvGE-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 485 LVFSQPWpgMMRTLYNNHERFEDTYFskfPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVA 564
Cdd:COG0318 298 IVVRGPN--VMKGYWNDPEATAEAFR---DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVA 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 565 ESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDR 644
Cdd:COG0318 373 EAAVVGVPDEKWGERVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
22-659 |
1.13e-91 |
|
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: 297.26 E-value: 1.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 22 SFEEYQKFYQESLDNPAEFWSRVAK----QFHW-ETPADQDKflkynfNISKGPisiKWMEGASTNLCYNLLdRNVRNGl 96
Cdd:cd05943 15 SLADYAALHRWSVDDPGAFWAAVWDfsgvRGSKpYDVVVVSG------RIMPGA---RWFPGARLNYAENLL-RHADAD- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 97 gDQIAYYWEGNHPDDYsrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSP 176
Cdd:cd05943 84 -DPAAIYAAEDGERTE---VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 177 DSLAERMFDCKAKLLITADGAWRGEKPLYLKalcDTALEKVEEMGhSVEKCIVVSHLkrVTPCQPDhVEEEIPWTddrdy 256
Cdd:cd05943 160 PGVLDRFGQIEPKVLFAVDAYTYNGKRHDVR---EKVAELVKGLP-SLLAVVVVPYT--VAAGQPD-LSKIAKAL----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 257 WWHEEM-EDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHT 335
Cdd:cd05943 228 TLEDFLaTGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 YVvyGPLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEA 415
Cdd:cd05943 308 LV--SGLAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPES 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 416 WLWYYKYIGKeqcsivDTFWQTETGG-HVITPLPGATPMKP---GSASFPFFGVKPTLLDECGIEIKGE-GEgyLVFSQP 490
Cdd:cd05943 386 FDYVYDHIKP------DVLLASISGGtDIISCFVGGNPLLPvyrGEIQCRGLGMAVEAFDEEGKPVWGEkGE--LVCTKP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 491 WPGMMRTLYN--NHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAV 568
Cdd:cd05943 458 FPSMPVGFWNdpDGSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 569 VSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIaVNDRNVGD 648
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI-IAGRPVKN 616
|
650
....*....|.
gi 24667955 649 TSTLADEQIVE 659
Cdd:cd05943 617 AGALANPESLD 627
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
22-666 |
9.46e-90 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 292.85 E-value: 9.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 22 SFEEYQKFYQESLDNPAEFWSRVAKQFH--WETPA----DQDKFLKYnfniskgpisiKWMEGASTNLCYNLLdrnvRNG 95
Cdd:PRK03584 32 SFDDYAALWRWSVEDLEAFWQSVWDFFGviGSTPYtvvlAGRRMPGA-----------RWFPGARLNYAENLL----RHR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 96 LGDQIA--YYWEGNHPddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAG 173
Cdd:PRK03584 97 RDDRPAiiFRGEDGPR----RELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 174 FSPDSLAERMFDCKAKLLITADGAWRGEKPLylkalcDTaLEKVEEM-GH--SVEKCIVVSHLkrvtpcQPDHVEEEIPW 250
Cdd:PRK03584 173 FGVQGVLDRFGQIEPKVLIAVDGYRYGGKAF------DR-RAKVAELrAAlpSLEHVVVVPYL------GPAAAAAALPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 251 TDDrdywWHEEMEDKEPA-CYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGD-IYWCTgDV 328
Cdd:PRK03584 240 ALL----WEDFLAPAEAAeLEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYT-TC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 329 GWITGHtYVVYGpLANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVG 408
Cdd:PRK03584 315 GWMMWN-WLVSG-LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 409 EPINPEAWLWYYKYIGKeqcsivDTFWQTETGG-HVITPLPGATPMKP---GSASFPFFGVKPTLLDECGIEIKGE-GEg 483
Cdd:PRK03584 393 SPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRPVVGEvGE- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 484 yLVFSQPWPGMMRTLYN--NHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHP 561
Cdd:PRK03584 466 -LVCTKPFPSMPLGFWNdpDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 562 RVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIM----RRVLR 637
Cdd:PRK03584 545 EVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLH 624
|
650 660
....*....|....*....|....*....
gi 24667955 638 KIAVNDrnVGDTSTLADEQIVEqLFANRP 666
Cdd:PRK03584 625 GRPVKK--AVNRDALANPEALD-WFADLA 650
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
278-632 |
2.91e-89 |
|
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: 281.48 E-value: 2.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIvFDYKPGDIYWCTGDVGWItGHTYVVYGPLANGATSVIFEGtpFF 357
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK--FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 358 PGndRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQT 437
Cdd:cd04433 77 PE--AALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 438 ETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPgmMRTLYNNherFEDTYFSKFPGYY 517
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MKGYWNN---PEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 518 CTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKli 597
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 24667955 598 sDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIM 632
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
26-645 |
3.85e-82 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 272.77 E-value: 3.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 26 YQKFYQESLDNPAEFWSRVAKQF-HWetpadqDKFlkYNFNISKGPISIKWMEGASTNLCYNLLDRNVRNGLG-DQIAYY 103
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKKYvHW------DKM--YDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKrDQDALI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 104 WEGNHPDDYSRgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERM 183
Cdd:PTZ00237 82 YECPYLKKTIK-LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 184 FDCKAKLLITADgawrgekplyLKALCDTALEKVEEMGHSVEkcivVSHLKrvtpcqPDHV----------------EEE 247
Cdd:PTZ00237 161 ETITPKLIITTN----------YGILNDEIITFTPNLKEAIE----LSTFK------PSNVitlfrnditsesdlkkIET 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 248 IPWTDDRDYWWHEEMEDKEPACYPEW----MDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYW 323
Cdd:PTZ00237 221 IPTIPNTLSWYDEIKKIKENNQSPFYeyvpVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 324 CTGDVGWITGHTYVvYGPLANGATSVIFEGTPFFPGN--DRYWSVIDKYKVTQFYTAPTAIRALMKFG-EGPVL--KHNL 398
Cdd:PTZ00237 301 SHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpEATIIrsKYDL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 399 SGLKVLGSVGEPIN---PEawlwyykYI-GKEQCSIVDTFWQTETGghvITPLPG-ATPMKPGSAS-FPFFGVKPTLLDE 472
Cdd:PTZ00237 380 SNLKEIWCGGEVIEesiPE-------YIeNKLKIKSSRGYGQTEIG---ITYLYCyGHINIPYNATgVPSIFIKPSILSE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 473 CGIEIkGEGE-GYLVFSQPWP-GMMRTLYNNHERFEDTyFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMST 550
Cdd:PTZ00237 450 DGKEL-NVNEiGEVAFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 551 AEVESVLTEHPRVAESAVVSRPHPVKGECLYCFIT---PNENEVFD-QKLISDLKKMVRERIGPFAMPDVIQNAPGLPKT 626
Cdd:PTZ00237 528 NTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVlkqDQSNQSIDlNKLKNEINNIITQDIESLAVLRKIIIVNQLPKT 607
|
650
....*....|....*....
gi 24667955 627 RSGKIMRRVLRKIaVNDRN 645
Cdd:PTZ00237 608 KTGKIPRQIISKF-LNDSN 625
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
117-637 |
1.91e-78 |
|
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: 256.98 E-value: 1.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITaDG 196
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-DG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 197 Awrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewmda 276
Cdd:cd05971 87 S------------------------------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFMLYTSGSTGKPKGVLHTTAgYLLYAATTFKIVFDYKP--GDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGT 354
Cdd:cd05971 88 DDPALIIYTSGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 355 PFFPGndRYWSVIDKYKVTQFYTAPTAIRaLMKFgEGPVLKHNLSGLKVLGSVGEPINPEAWLWyykyiGKEQCSI-VDT 433
Cdd:cd05971 167 KFDPK--AALDLMSRYGVTTAFLPPTALK-MMRQ-QGEQLKHAQVKLRAIATGGESLGEELLGW-----AREQFGVeVNE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 434 FW-QTEtGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNHERFEDtyfsK 512
Cdd:cd05971 238 FYgQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEK----K 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 513 FPG-YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEV 591
Cdd:cd05971 313 MAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24667955 592 FDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05971 393 PSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
116-638 |
1.42e-77 |
|
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: 254.37 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITaD 195
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 GAWRgekplylkalcdtalekveemgHSVekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewmd 275
Cdd:cd05973 80 AANR----------------------HKL--------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTT------AGYLLYAattfkivFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSV 349
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVPVPLralaafGAYLRDA-------VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTI 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 350 IFEGtPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMkfGEGPVLKHNLSG-LKVLGSVGEPINPEAWLWYYKYIGkeqC 428
Cdd:cd05973 160 LLEG-GFSV--ESTWRVIERLGVTNLAGSPTAYRLLM--AAGAEVPARPKGrLRRVSSAGEPLTPEVIRWFDAALG---V 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 429 SIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIkGEGE-GYLVFSQPWPGMMrtLYNNHERFED 507
Cdd:cd05973 232 PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDEL-GPGEpGRLAIDIANSPLM--WFRGYQLPDT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 508 TYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPN 587
Cdd:cd05973 309 PAIDG--GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLR 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24667955 588 ENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05973 387 GGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
85-637 |
2.77e-75 |
|
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: 250.36 E-value: 2.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 85 YN---LLDRNVRNGLGDQIAYYwegnhpdDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACA 161
Cdd:cd05959 3 YNaatLVDLNLNEGRGDKTAFI-------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 162 RIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAdgawrgekplylKALCDTALEKVEEMGHSVEKCIVvshlkrvtpCQP 241
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS------------GELAPVLAAALTKSEHTLVVLIV---------SGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 242 dhvEEEIPWTDDRDYWWHEEMEDKEPAcyPEWmdAEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTF-KIVFDYKPGD 320
Cdd:cd05959 135 ---AGPEAGALLLAELVAAEAEQLKPA--ATH--ADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 321 IYWCTGDVGWITGHTYVVYGPLANGATSVIFegtPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSG 400
Cdd:cd05959 207 VCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLP--SRDLSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 401 LKVLGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQTETGGHVITPLPGAtpMKPGSASFPFFGVKPTLLDECGIEIKGE 480
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 481 GEGYLVFSQPWPGMMrtLYNNHERFEDTyfskFPGYYC-TGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTE 559
Cdd:cd05959 357 EPGELYVRGPSSATM--YWNNRDKTRDT----FQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQ 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 560 HPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05959 431 HPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
22-639 |
3.97e-69 |
|
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: 237.86 E-value: 3.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 22 SFEEYQKFYQESLDNPAEFWSRVAKQFHWETPADQDKFLkynfNISKGPiSIKWMEGASTNLCYNLLDRNvrnGLGDQIA 101
Cdd:TIGR01217 33 AEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVV----DDRTMP-GAQWFPGARLNYAENLLRAA---GTEPALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 102 YYWEgnhpDDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAE 181
Cdd:TIGR01217 105 YVDE----THEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 182 RMFDCKAKLLITADGAWRGEKPlylkalcDTALEKVEEMGHSVEKCIVVSHLKRVTPCqpdhvEEEIPWTDDRDYWWHEE 261
Cdd:TIGR01217 181 RFQQIEPKLLFTVDGYRYNGKE-------HDRRDKVAEVRKELPTLRAVVHIPYLGPR-----ETEAPKIDGALDLEDFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 262 MEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHtYVVYGp 341
Cdd:TIGR01217 249 AAAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMMWN-WLVSG- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 LANGATSVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYk 421
Cdd:TIGR01217 327 LATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 422 yigkeQCSIVDTFWQTETGG-HVITPLPGATPMKP---GSASFPFFGVKPTLLDECGIEIKGEgEGYLVFSQPWPGMMRT 497
Cdd:TIGR01217 406 -----DEIKADVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQSWDPEGKPVTGE-VGELVCTNPMPSMPIR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 498 LYN--NHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPV 575
Cdd:TIGR01217 480 FWNdpDGSKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPD 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 576 KGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKI 639
Cdd:TIGR01217 560 GGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRV 623
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-637 |
1.42e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 232.77 E-value: 1.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 85 YNLLDRNVRNgLGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYM---PMILElpiAMLACA 161
Cdd:PRK06187 9 GRILRHGARK-HPDKEAVYFDG-------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDwnsHEYLE---AYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 162 RIGAV-HSI-VFagFSPDSLAERMFDCKAKLLItADGAWRGEkplylkalcdtaLEKVEEMGHSVEKCIVVshlkrvtpc 239
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDSEFVPL------------LAAILPQLPTVRTVIVE--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 240 qpdhveEEIPWTDDRDYWWH-EEMEDKEPACYPEWM-DAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTfKIVFDYK 317
Cdd:PRK06187 134 ------GDGPAAPLAPEVGEyEELLAAASDTFDFPDiDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAV-CAWLKLS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 318 PGDIY-----------WctgdvGWItghtyvvYGPLANGATSVI---FEGTPFfpgndryWSVIDKYKVTQFYTAPTAIR 383
Cdd:PRK06187 207 RDDVYlvivpmfhvhaW-----GLP-------YLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 384 ALMKFGEGPvlKHNLSGLKVLGSVGEPINPEAwlwYYKYIGKEQCSIVDTFWQTETGGHV-ITPLPGATP---MKPGSAS 459
Cdd:PRK06187 268 MLLKAPRAY--FVDFSSLRLVIYGGAALPPAL---LREFKEKFGIDLVQGYGMTETSPVVsVLPPEDQLPgqwTKRRSAG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 460 FPFFGVKPTLLDECGIEIKGEGE--GYLVFSQPWpgMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRV 537
Cdd:PRK06187 343 RPLPGVEARIVDDDGDELPPDGGevGEIIVRGPW--LMQGYWNRPEATAETIDG---GWLHTGDVGYIDEDGYLYITDRI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 538 DDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVI 617
Cdd:PRK06187 418 KDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRI 494
|
570 580
....*....|....*....|
gi 24667955 618 QNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK06187 495 AFVDELPRTSVGKILKRVLR 514
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
111-637 |
7.36e-66 |
|
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: 223.49 E-value: 7.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 111 DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKL 190
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 191 LITadgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacy 270
Cdd:cd05919 86 VVT----------------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 271 pewmDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDV--GWITGHTyvVYGPLANGATS 348
Cdd:cd05919 89 ----SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 349 VIFEGtpfFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSVGEPINPEAWLWYYKYIGkeqC 428
Cdd:cd05919 163 VLNPG---WPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGEALPRGLGERWMEHFG---G 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 429 SIVDTFWQTETGGHVITPLPGAtpMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwpGMMRTLYNNHERFEDT 508
Cdd:cd05919 235 PILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP--SAAVGYWNNPEKSRAT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 509 YFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNE 588
Cdd:cd05919 311 FNG---GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24667955 589 NEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05919 388 PAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
82-637 |
3.94e-65 |
|
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: 224.30 E-value: 3.94e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 82 NLCYNLLDRNVRNGlGDQIAYYWegnhPDDY--SRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLA 159
Cdd:cd05970 17 NFAYDVVDAMAKEY-PDKLALVW----CDDAgeERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 160 CARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGawrgekplylkalcDTALEKVEEmghSVEKCIVVSHLKRVTPC 239
Cdd:cd05970 92 LHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE--------------DNIPEEIEK---AAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 240 QPDHveeeipWTDdrdywWHEEMEDK----EPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAgYLLYAATTFKIVFD 315
Cdd:cd05970 155 VPEG------WID-----FRKLIKNAspdfERPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 316 YKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGTPFFPGNdrYWSVIDKYKVTQFYTAPTAIRALMKfgeGPVLK 395
Cdd:cd05970 223 VREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 396 HNLSGLKVLGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQTETGGHVITpLPGATPmKPGSASFPFFGVKPTLLDECGI 475
Cdd:cd05970 298 YDLSSLRYCTTAGEALNPEVFNTFKEKTG---IKLMEGFGQTETTLTIAT-FPWMEP-KPGSMGKPAPGYEIDLIDREGR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 476 EIKG--EGEGYLVFSQPWP-GMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAE 552
Cdd:cd05970 373 SCEAgeEGEIVIRTSKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 553 VESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIM 632
Cdd:cd05970 450 VESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIR 529
|
....*
gi 24667955 633 RRVLR 637
Cdd:cd05970 530 RVEIR 534
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
88-633 |
1.54e-63 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 217.09 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 88 LDRNVRNGlGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVH 167
Cdd:cd17631 1 LRRRARRH-PDRTALVFGG-------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 168 SIVFAGFSPDSLAERMFDCKAKLLItadgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveee 247
Cdd:cd17631 73 VPLNFRLTPPEVAYILADSGAKVLF------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 248 ipwtddrdywwheemedkepacypewmdaEDPLFMLYTSGSTGKPKGVLHTTaGYLLYAATTFKIVFDYKPGDIYWCTGD 327
Cdd:cd17631 98 -----------------------------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 328 VGWITGHTYVVYGPLANGATSVIFEGtpFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSV 407
Cdd:cd17631 148 LFHIGGLGVFTLPTLLRGGTVVILRK--FDP--ETVLDLIERHRVTSFFLVPTMIQALLQHPRFA--TTDLSSLRAVIYG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 408 GEPInPEAWLWYYKYIGKEqcsIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVF 487
Cdd:cd17631 222 GAPM-PERLLRALQARGVK---FVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 488 SQPwpGMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESA 567
Cdd:cd17631 298 RGP--HVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 568 VVSRPHPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPGAELD---EDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
116-638 |
2.35e-63 |
|
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: 218.34 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITaD 195
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT-P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 GAWRGEKplyLKALCDTALEkVEEMGHSVEKCIVVSHLKRVTPCQPDHVEeeipwtddrdywwheemedkepACYPEWMD 275
Cdd:cd05926 94 KGELGPA---SRAASKLGLA-ILELALDVGVLIRAPSAESLSNLLADKKN----------------------AKSEGVPL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVI---FE 352
Cdd:cd05926 148 PDDLALILHTSGTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLpprFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 353 GTPFfpgndryWSVIDKYKVTqFYTA-PTAIRALMKFgEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGkeqCSIV 431
Cdd:cd05926 227 ASTF-------WPDVRDYNAT-WYTAvPTIHQILLNR-PEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG---APVL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 432 DTFWQTETGgHVIT--PLPgATPMKPGSASFPFfGVKPTLLDECGIEIKGEGEGYLVFSQPwpGMMRTLYNNHE-RFEdt 508
Cdd:cd05926 295 EAYGMTEAA-HQMTsnPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNNPEaNAE-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 509 YFSKFpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNE 588
Cdd:cd05926 368 AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24667955 589 NEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05926 447 GASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
85-637 |
5.73e-62 |
|
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: 213.58 E-value: 5.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 85 YNLLDRNVRNgLGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIG 164
Cdd:cd05936 2 ADLLEEAARR-FPDKTALIFMG-------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 165 AVHSIVFAGFSPDSLAERMFDCKAKLLITAdgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhv 244
Cdd:cd05936 74 AVVVPLNPLYTPRELEHILNDSGAKALIVA-------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 245 eeeIPWTDDrdywwheeMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTaGYLLYAATTFKIVF--DYKPGDIY 322
Cdd:cd05936 104 ---VSFTDL--------LAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIKAWLedLLEGDDVV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 323 WCTGDVGWITGHTYVVYGPLANGATSVIFegTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLK 402
Cdd:cd05936 172 LAALPLFHVFGLTVALLLPLALGATIVLI--PRFRP--IGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 403 VLGSVGEPINPEawlwyykyigkeqcsiVDTFWQTETGGHVI--------------TPLPGatPMKPGSASFPFFGVKPT 468
Cdd:cd05936 246 LCISGGAPLPVE----------------VAERFEELTGVPIVegygltetspvvavNPLDG--PRKPGSIGIPLPGTEVK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 469 LLDECGIEIK-GEgEGYLVFSQPwpGMMRTLYNNHE----RFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNV 543
Cdd:cd05936 308 IVDDDGEELPpGE-VGELWVRGP--QVMKGYWNRPEetaeAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIV 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 544 SGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGL 623
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDEL 454
|
570
....*....|....
gi 24667955 624 PKTRSGKIMRRVLR 637
Cdd:cd05936 455 PKSAVGKILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
108-638 |
4.70e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 201.70 E-value: 4.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAER 182
Cdd:PRK08316 24 YPDktalvFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDCKAKLLITADgawrgekplylkALCDTALEKVEEMGHSvekcivvshlKRVTPCQPDHVEEEIPWTDDRDywWHEEM 262
Cdd:PRK08316 104 LDHSGARAFLVDP------------ALAPTAEAALALLPVD----------TLILSLVLGGREAPGGWLDFAD--WAEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 EDKEPACYPewmDAEDPLFMLYTSGSTGKPKGVLHTTAGYLL-YAATTfkIVFDYKPGDI-------YWCTGdvgwitgh 334
Cdd:PRK08316 160 SVAEPDVEL---ADDDLAQILYTSGTESLPKGAMLTHRALIAeYVSCI--VAGDMSADDIplhalplYHCAQ-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 335 TYVVYGP-LANGATSVIFEGtpffPGNDRYWSVIDKYKVTQFYTAPTAIRALMKfgeGPVL-KHNLSGLK---------- 402
Cdd:PRK08316 227 LDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLR---HPDFdTRDLSSLRkgyygasimp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 403 --VLGSVGEPInPEAWLWYYkyigkeqcsivdtFWQTEtgghvITPL-----PGATPMKPGSASFPFFGVKPTLLDECGI 475
Cdd:PRK08316 300 veVLKELRERL-PGLRFYNC-------------YGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 476 EIKgEGE-GYLVFSQPwpGMMRTLYNNHER----FEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMST 550
Cdd:PRK08316 361 DVA-PGEvGEIVHRSP--QLMLGYWDDPEKtaeaFRG-------GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVAS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 551 AEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGK 630
Cdd:PRK08316 431 REVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507
|
....*...
gi 24667955 631 IMRRVLRK 638
Cdd:PRK08316 508 ILKRELRE 515
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
101-638 |
8.69e-57 |
|
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: 201.16 E-value: 8.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 101 AYYWEGNHPDDYSrgLTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSL 179
Cdd:cd05928 29 ALWWVNGKGDEVK--WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 180 AERMFDCKAKLLITADGawrgekplyLKALCDTALEKVEemghSVEKCIVVSHLKRVTpcqpdhveeeipWTDDRDYWWH 259
Cdd:cd05928 107 LYRLQASKAKCIVTSDE---------LAPEVDSVASECP----SLKTKLLVSEKSRDG------------WLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 260 EemeDKEPACYPEwmDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVY 339
Cdd:cd05928 162 A---STEHHCVET--GSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSVIFEGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALM-------KFgegPVLKHNLSGlkvlgsvGEPIN 412
Cdd:cd05928 237 EPWIQGACVFVHHLPRFDP--LVILKTLSSYPITTFCGAPTVYRMLVqqdlssyKF---PSLQHCVTG-------GEPLN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 413 P---EAWlwyykyigKEQCS--IVDTFWQTETGghVITPLPGATPMKPGSASFPFFGVKPTLLDECG-IEIKG-EGEGYL 485
Cdd:cd05928 305 PevlEKW--------KAQTGldIYEGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGnVLPPGtEGDIGI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 486 VFSQPWPGMMRTLY-NNHERFEDTYFSKFpgyYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVA 564
Cdd:cd05928 375 RVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVV 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 565 ESAVVSRPHPVKGECLYCFI--TPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05928 452 ESAVVSSPDPIRGEVVKAFVvlAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
116-640 |
1.03e-54 |
|
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: 193.17 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERmfdckakllitad 195
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekVEEMGHSVEKCIVVSHlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewmd 275
Cdd:cd05974 68 ---------------------VDRGGAVYAAVDENTH------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTTAGYLL-YAATTFKIvfDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGT 354
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVgHLSTMYWI--GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 355 PFFPgnDRYWSVIDKYKVTQFYTAPTAIRALmkfgegpvLKHNLSGLKV----LGSVGEPINPEAWLWYYKYIGKeqcSI 430
Cdd:cd05974 162 RFDA--KRVLAALVRYGVTTLCAPPTVWRML--------IQQDLASFDVklreVVGAGEPLNPEVIEQVRRAWGL---TI 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 431 VDTFWQTETGGHVITPlPGaTPMKPGSASFPFFGVKPTLLDECGIEIKgEGEGYLVFSQPWP-GMMRTLYNNHERfedTY 509
Cdd:cd05974 229 RDGYGQTETTALVGNS-PG-QPVKAGSMGRPLPGYRVALLDPDGAPAT-EGEVALDLGDTRPvGLMKGYAGDPDK---TA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 510 FSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNEN 589
Cdd:cd05974 303 HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24667955 590 EVFDQKLISDLKKMVRERIGPFAMPDVIQNAPgLPKTRSGKIMRRVLRKIA 640
Cdd:cd05974 383 YEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
110-632 |
3.23e-54 |
|
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: 193.20 E-value: 3.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 110 DDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAK 189
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 190 LLITAdgawrgekplylKALCDTALEKVEEMGhSVEKCIVVshlkRVTPCQPDHVEEEIPWTDDRDYWWhEEMEDKEPAc 269
Cdd:cd05911 85 VIFTD------------PDGLEKVKEAAKELG-PKDKIIVL----DDKPDGVLSIEDLLSPTLGEEDED-LPPPLKDGK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 270 ypewmdaEDPLFMLYTSGSTGKPKGVLHTTAGYLlyaaTTFKIVFDYKPGDIywCTGDVG-------WITGHTYVVYGPL 342
Cdd:cd05911 146 -------DDTAAILYSSGTTGLPKGVCLSHRNLI----ANLSQVQTFLYGND--GSNDVIlgflplyHIYGLFTTLASLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 aNGATSVIFEGtpFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLKVLGSVGEPINPEAwlwyYKY 422
Cdd:cd05911 213 -NGATVIIMPK--FDS--ELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKEL----QEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 423 IGK--EQCSIVDTFWQTETGGhVITPLPGaTPMKPGSASFPFFGVKPTLLDECGIEIKG---EGEGYLVFSQPWPGMmrt 497
Cdd:cd05911 282 LAKrfPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGpnePGEICVRGPQVMKGY--- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 498 lYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKG 577
Cdd:cd05911 357 -YNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 578 ECLYCFITPNENEVFDQKlisDLKKMVRERIGPF-AMPDVIQNAPGLPKTRSGKIM 632
Cdd:cd05911 434 ELPRAYVVRKPGEKLTEK---EVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
82-638 |
1.67e-52 |
|
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: 188.89 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 82 NLCYNLLDRNVRNGLGDQIAYywegnhpDDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACA 161
Cdd:TIGR02262 4 NAAEDLLDRNVVEGRGGKTAF-------IDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 162 RIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGawrgekplyLKALCDTALEKVEEMGHsvekcIVVSHLKrvtpcQP 241
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA---------LLPVIKAALGKSPHLEH-----RVVVGRP-----EA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 242 DHVEeeipwtddrdywWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDI 321
Cdd:TIGR02262 138 GEVQ------------LAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 322 YWCTGDVGWITGHTYVVYGPLANGATSVIFegtPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGL 401
Cdd:TIGR02262 206 CFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLP--SEDQVRL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 402 KVLGSVGEPINPEAWLWYYKYIGKEqcsIVDTFWQTETGGHVITPLPGAtpMKPGSASFPFFGVKPTLLDECGiEIKGEG 481
Cdd:TIGR02262 281 RLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGG-QDVADG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 482 E-GYLVFSQPWPGMMrtLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEH 560
Cdd:TIGR02262 355 EpGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQH 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 561 PRVAESAVV--SRPHPVKGECLYCFITPNENEVFDqklisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:TIGR02262 430 PAVLEAAVVgvADEDGLIKPKAFVVLRPGQTALET-----ELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
96-638 |
1.35e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 180.87 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 96 LGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFS 175
Cdd:PRK07656 18 FGDKEAYVFGD-------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 176 PDSLAERMFDCKAKLLITADGawrgekplylkalcdtALEKVEEMGHSVEkcivvsHLKRVTPCQPDHVEEEIPWTDDrd 255
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGL----------------FLGVDYSATTRLP------ALEHVVICETEEDDPHTEKMKT-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 256 ywWHEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHT 335
Cdd:PRK07656 147 --FTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 YVVYGPLANGATSVIfegTPFF-PgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSVGEPInPE 414
Cdd:PRK07656 224 AGVNAPLMRGATILP---LPVFdP--DEVFRLIETERITVLPGPPTMYNSLLQHPDRS--AEDLSSLRLAVTGAASM-PV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 415 AWLwyyKYIGKE-QCSIVDT-FWQTETGGHV-ITPLPGATPMKPGSASFPFFGVKPTLLDECGIEI-KGE-GE----GYL 485
Cdd:PRK07656 296 ALL---ERFESElGVDIVLTgYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVpVGEvGEllvrGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 486 VfsqpwpgmMRTLYNNHERFEDTYfsKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAE 565
Cdd:PRK07656 373 V--------MKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAE 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 566 SAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK07656 443 AAVIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-637 |
1.35e-49 |
|
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: 178.64 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITadg 196
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 197 awrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewmda 276
Cdd:cd05934 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 eDPLFMLYTSGSTGKPKGVLHTTAgYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEgtPF 356
Cdd:cd05934 82 -DPASILYTSGTTGPPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP--RF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 357 FPGndRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNlsglKVLGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQ 436
Cdd:cd05934 158 SAS--RFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAH----RLRAAYGAPNPPELHEEFEERFG---VRLLEGYGM 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 437 TETGGHVITPLPGATPmkPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVF-SQPWPGMMRTLYNN----HERFEDtyfs 511
Cdd:cd05934 229 TETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrGLRGWGFFKGYYNMpeatAEAMRN---- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 512 kfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEV 591
Cdd:cd05934 303 ---GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24667955 592 FDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05934 380 LDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
114-637 |
2.52e-49 |
|
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: 178.44 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLli 192
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 tadgawrgekplylkALCDTALEKVEEMghsvekCIVVshlkrvtpcqpdhveeeipwtddrdywwheemedkepacype 272
Cdd:cd05958 87 ---------------ALCAHALTASDDI------CILA------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 273 wmdaedplfmlYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFE 352
Cdd:cd05958 104 -----------FTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 353 G-TPffpgnDRYWSVIDKYKVTQFYTAPTAIRALMkfGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGKEqcsIV 431
Cdd:cd05958 173 EaTP-----DLLLSAIARYKPTVLFTAPTAYRAML--AHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP---II 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 432 DTFWQTETGGHVITPLPGAtpMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwpgmmrTLYN-NHERFEDTYF 510
Cdd:cd05958 243 DGIGSTEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCRyLADKRQRTYV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 511 SKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENE 590
Cdd:cd05958 315 QG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24667955 591 VFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05958 393 IPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
20-638 |
7.69e-48 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 179.89 E-value: 7.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 20 ISSFEEYQKFyqeSLDNPAEFWSRVAKQ----FHwETPAdqdKFLKYNFNISKGPisiKWMEGASTNLCYNLLdRNVRNG 95
Cdd:PLN03052 119 ISSFSEFQRF---SVENPEVYWSIVLDElslvFS-VPPR---CILDTSDESNPGG---QWLPGAVLNVAECCL-TPKPSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 96 LGDQIAYYW--EGNhpDDYS-RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLAcarigavhsIVFA 172
Cdd:PLN03052 188 TDDSIAIIWrdEGS--DDLPvNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLA---------IILA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 173 G---------FSPDSLAERMFDCKAKLLITADGAWRGEK--PLYLKAlcdtalekVEEMGHsveKCIVVshlkrvtPCQP 241
Cdd:PLN03052 257 GcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKsiPLYSRV--------VEAKAP---KAIVL-------PADG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 242 DHVEEEIpwtDDRDYWWHEEMEDKEPACYPE-----WMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVfDY 316
Cdd:PLN03052 319 KSVRVKL---REGDMSWDDFLARANGLRRPDeykavEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 317 KPGDIY-WCTgDVGWITGHtYVVYGPLANGATSVIFEGTPFFPGNDRYwsVIDKyKVTQFYTAPTAIRALMKFG--EGpv 393
Cdd:PLN03052 395 RKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF--VQDA-KVTMLGTVPSIVKTWKNTNcmAG-- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 394 lkHNLSGLKVLGSVGEPINPEAWLW-----YYKYIgKEQCSivdtfwQTETGGHVITplpgATPMKP---GSASFPFFGV 465
Cdd:PLN03052 468 --LDWSSIRCFGSTGEASSVDDYLWlmsraGYKPI-IEYCG------GTELGGGFVT----GSLLQPqafAAFSTPAMGC 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 466 KPTLLDECGIEIKGE--GEGYLVFSQPWPGMMRTLYN-NHErfeDTYFSKFPGYYCT-----GDGARRDADGYLWITGRV 537
Cdd:PLN03052 535 KLFILDDSGNPYPDDapCTGELALFPLMFGASSTLLNaDHY---KVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRA 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 538 DDMLNVSGHLMSTAEVESVL-TEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKM----VRERIGPFA 612
Cdd:PLN03052 612 DDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIfnsaIQKKLNPLF 691
|
650 660
....*....|....*....|....*.
gi 24667955 613 MPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PLN03052 692 KVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
109-643 |
9.00e-48 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 178.23 E-value: 9.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 109 PDDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLAcariGAVHSIVFA---GFSPDSLAERMFD 185
Cdd:PRK07529 52 PLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 186 CKAKLLITAdgawrgeKPlYLKALCDTALEKVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPWTDDRDYWWHEEMeDK 265
Cdd:PRK07529 128 AGAKVLVTL-------GP-FPGTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFDAEL-AR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 266 EPA---CYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCtgdvGWITGHTYVVYG-- 340
Cdd:PRK07529 199 QPGdrlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFC----GLPLFHVNALLVtg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 341 --PLANGATSVIfeGTP-------FFpgnDRYWSVIDKYKVTQFYTAPTAIRALMKFgegPVLKHNLSGLKVLGSVGEPI 411
Cdd:PRK07529 274 laPLARGAHVVL--ATPqgyrgpgVI---ANFWKIVERYRINFLSGVPTVYAALLQV---PVDGHDISSLRYALCGAAPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 412 NPEAWLWYYKYIGKEqcsIVDTFWQTE-TGGHVITPLPGatPMKPGSAS--FPFFGVKPTLLDECGIEIK--GEGE-GYL 485
Cdd:PRK07529 346 PVEVFRRFEAATGVR---IVEGYGLTEaTCVSSVNPPDG--ERRIGSVGlrLPYQRVRVVILDDAGRYLRdcAVDEvGVL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 486 VFSQP--WPGMMRTLYNNHERFEDTYFSkfpgyycTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRV 563
Cdd:PRK07529 421 CIAGPnvFSGYLEAAHNKGLWLEDGWLN-------TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAV 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 564 AESAVVSRPHPVKGE--CLYCFITPNEnEVFDQKLISDLKKMVRERIgpfAMPDVIQNAPGLPKTRSGKIMRRVLRKIAV 641
Cdd:PRK07529 494 ALAAAVGRPDAHAGElpVAYVQLKPGA-SATEAELLAFARDHIAERA---AVPKHVRILDALPKTAVGKIFKPALRRDAI 569
|
..
gi 24667955 642 ND 643
Cdd:PRK07529 570 RR 571
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
116-636 |
1.25e-47 |
|
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: 173.87 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAER---MF-DCKAKLL 191
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA----YVPLDPSYPAERlayILeDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITadgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacyp 271
Cdd:cd05930 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewmDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAAtTFKIVFDYKPGDIYWCTGDVGWItGHTYVVYGPLANGATSVIF 351
Cdd:cd05930 91 ---DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL-WMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 -EGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHnlsgLKVLGSVGEPINPEAWLWYYKYIGKEQ--- 427
Cdd:cd05930 166 pEEVRKDP--EALADLLAEEGITVLHLTPSLLRLLLQELELAALPS----LRLVLVGGEALPPDLVRRWRELLPGARlvn 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 ------CSIVDTFWQTETGGHVITPLPGATPMkPGSASFpffgvkptLLDE----CGIEIKGE--------GEGYLvfsq 489
Cdd:cd05930 240 lygpteATVDATYYRVPPDDEEDGRVPIGRPI-PNTRVY--------VLDEnlrpVPPGVPGElyiggaglARGYL---- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 490 pwpgmmrtlyNNHE----RFEDTYFskFPG--YYCTGDGARRDADG---YLwitGRVDDMLNVSGHLMSTAEVESVLTEH 560
Cdd:cd05930 307 ----------NRPEltaeRFVPNPF--GPGerMYRTGDLVRWLPDGnleFL---GRIDDQVKIRGYRIELGEIEAALLAH 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 561 PRVAESAVVSRPHPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd05930 372 PGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
147-637 |
3.33e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 165.76 E-value: 3.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 147 MPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGAWRGEK--PLYlkalcdtalEKVEEMGHSv 224
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRalPLY---------SKVVEAAPA- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 225 eKCIVVSHLKRvtPCQPDHVEEEIPWTD--DRDYWWHEEmedkEPACY-PEWMDAEDPLFMLYTSGSTGKPKGV--LHTT 299
Cdd:PLN03051 71 -KAIVLPAAGE--PVAVPLREQDLSWCDflGVAAAQGSV----GGNEYsPVYAPVESVTNILFSSGTTGEPKAIpwTHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 300 AgylLYAATTFKIVFDYKPGDIY-WCTgDVGWITGhTYVVYGPLANGATSVIFEGTPFFPGndrYWSVIDKYKVTQFYTA 378
Cdd:PLN03051 144 P---LRCASDGWAHMDIQPGDVVcWPT-NLGWMMG-PWLLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 379 PTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLW------YYKYIgKEQCSivdtfwQTETGGHVI--TPLpga 450
Cdd:PLN03051 216 PSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWlssvrgYYKPV-IEYCG------GTELASGYIssTLL--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 451 TPMKPGSASFPFFGVKPTLLDECGIEIKGEGE--GYLVFSQPWPGMMRTLYN-NHERfedTYFSKFPGYYCTGDGARRDA 527
Cdd:PLN03051 286 QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPcvGEVALAPPMLGASDRLLNaDHDK---VYYKGMPMYGSKGMPLRRHG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 528 D-------GYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPR-VAESAVVSRPHPVKG-ECLYCFITP-NENEVFDQKLI 597
Cdd:PLN03051 363 DimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGpELLVIFLVLgEEKKGFDQARP 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24667955 598 SDLKKM----VRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PLN03051 443 EALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
98-636 |
2.27e-41 |
|
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: 156.70 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGNHpddysrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLAcarigavhsIVFAGfspd 177
Cdd:cd17643 2 EAVAVVDEDRR-------LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLA---------ILKAG---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 178 slaermfdckakllitadGAwrgekplYLkalcdtalekveemghsvekcivvshlkrvtPCQPDHVEEEIPWTddrdyw 257
Cdd:cd17643 62 ------------------GA-------YV-------------------------------PIDPAYPVERIAFI------ 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 wheeMEDKEPACYpeWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYL-LYAATTFkiVFDYKPGDIywctgdvgWITGHTY 336
Cdd:cd17643 80 ----LADSGPSLL--LTDPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQR--WFGFNEDDV--------WTLFHSY 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 337 V-------VYGPLANGATSVIFEG----TPffpgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLK--V 403
Cdd:cd17643 144 AfdfsvweIWGALLHGGRLVVVPYevarSP-----EDFARLLRDEGVTVLNQTPSAFYQLVEAADRD--GRDPLALRyvI 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 404 LGsvGEPINPeAWL--WYYKYiGKEQCSIVDTFWQTETGGHV----ITP--LPGATpMKPGSASFPFFGVkpTLLDECGI 475
Cdd:cd17643 217 FG--GEALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRV--YVLDADGR 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 476 EIK--GEGEGYLVFSQPWPGMMRTLYNNHERF-EDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAE 552
Cdd:cd17643 290 PVPpgVVGELYVSGAGVARGYLGRPELTAERFvANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGE 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 553 VESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIM 632
Cdd:cd17643 370 IEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAAD---IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLD 446
|
....
gi 24667955 633 RRVL 636
Cdd:cd17643 447 RAAL 450
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-636 |
4.81e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 157.43 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 112 YSRGLTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKL 190
Cdd:PRK08314 32 YGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 191 LITADgawrgekPLY---LKALCDTALEKVeemghsvekciVVSHLKRVTPCQ-----PDHVEEEIP---WTDDRDYWWH 259
Cdd:PRK08314 112 AIVGS-------ELApkvAPAVGNLRLRHV-----------IVAQYSDYLPAEpeiavPAWLRAEPPlqaLAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 260 EEMEDKEPACyPEWMDAEDPLFMLYTSGSTGKPKGVLHTtAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVY 339
Cdd:PRK08314 174 EALAAGLAPP-PHTAGPDDLAVLPYTSGTTGVPKGCMHT-HRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSVIFegtpffPGNDRYWS--VIDKYKVTQFYTAPTAIRALMkfGEGPVLKHNLSGLKVLGSVGEPInPEAwl 417
Cdd:PRK08314 252 APIYAGATVVLM------PRWDREAAarLIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAM-PEA-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 418 wyykyIG---KEQCSI--VDTFWQTETGGHVITPLPGATpmKPGSASFPFFGVKPTLLD-ECGIEIKGEGEGYLVFSQPw 491
Cdd:PRK08314 321 -----VAerlKELTGLdyVEGYGLTETMAQTHSNPPDRP--KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGP- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 492 pGMMRTLYNNHERFEDTyFSKFPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVV 569
Cdd:PRK08314 393 -QVFKGYWNRPEATAEA-FIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVI 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667955 570 SRPHPVKGECLYCFI--------TPNENEVFDqklisdlkkMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK08314 471 ATPDPRRGETVKAVVvlrpeargKTTEEEIIA---------WAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
103-640 |
4.54e-40 |
|
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: 154.53 E-value: 4.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 103 YWEG------------NHPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGA 165
Cdd:COG1021 21 YWRGetlgdllrrraeRHPDriavvDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 166 VHsiVFAGFSP-----DSLAERMfdcKAKLLITADgAWRG--EKPLY--LKALCDTalekveemghsVEKCIVVshlkrv 236
Cdd:COG1021 101 IP--VFALPAHrraeiSHFAEQS---EAVAYIIPD-RHRGfdYRALAreLQAEVPS-----------LRHVLVV------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 237 tpcqpDHVEEEIPWTDdrdyWWHEEMEDKEPACypewmDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIV-FD 315
Cdd:COG1021 158 -----GDAGEFTSLDA----LLAAPADLSEPRP-----DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICgLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 316 ykPGDIYWCTGDVGwitgHTY-----VVYGPLANGATsVIFEGTP----FFPgndrywsVIDKYKVTqfYTA--PTAIRA 384
Cdd:COG1021 224 --ADTVYLAALPAA----HNFplsspGVLGVLYAGGT-VVLAPDPspdtAFP-------LIERERVT--VTAlvPPLALL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 385 LMKFGEGPvlKHNLSGLKVLGSVGEPINPEAwlwyYKYIGKE-QCSIVDTFWQTEtgGHV-ITPL--PGAT-------PM 453
Cdd:COG1021 288 WLDAAERS--RYDLSSLRVLQVGGAKLSPEL----ARRVRPAlGCTLQQVFGMAE--GLVnYTRLddPEEVilttqgrPI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 454 KPGSAsfpffgVKptLLDECGIEIkGEGE-GYLVFSQPWpgmmrTL---YNNHER----F-EDtyfskfpGYYCTGDGAR 524
Cdd:COG1021 360 SPDDE------VR--IVDEDGNPV-PPGEvGELLTRGPY-----TIrgyYRAPEHnaraFtPD-------GFYRTGDLVR 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 525 RDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGE--CLycFITPNENEVfdqKLIsDLKK 602
Cdd:COG1021 419 RTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVPRGEPL---TLA-ELRR 492
|
570 580 590
....*....|....*....|....*....|....*....
gi 24667955 603 MVRER-IGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIA 640
Cdd:COG1021 493 FLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
114-636 |
2.08e-37 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 146.23 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 AdgawrgekplylkalCDTAlEKVEEMGHSVekcIVVshlkrvtpcqPDHVEEEIPWTDDRDywwheemEDKEPACYPEW 273
Cdd:cd05904 111 T---------------AELA-EKLASLALPV---VLL----------DSAEFDSLSFSDLLF-------EADEAEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPLFMLYTSGSTGKPKGVLHT-------TAGYLLYAATTFKivfdykPGDIYWCTGDVGWITGHTYVVYGPLANGA 346
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLThrnliamVAQFVAGEGSNSD------SEDVFLCVLPMFHIYGLSSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 347 TSVI---FEGTPFFpgndrywSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLKVLGSVGEPInpeawlwyykyi 423
Cdd:cd05904 229 TVVVmprFDLEELL-------AAIERYKVTHLPVVPPIVLALVKSPI--VDKYDLSSLRQIMSGAAPL------------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 424 GKE----------QCSIVDTFWQTETGGHV-ITPLPGATPMKPGSASFpffgVKPtlldecGIEIK------GEGEGYlv 486
Cdd:cd05904 288 GKElieafrakfpNVDLGQGYGMTESTGVVaMCFAPEKDRAKYGSVGR----LVP------NVEAKivdpetGESLPP-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 487 fSQP---W---PGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEH 560
Cdd:cd05904 356 -NQTgelWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSH 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 561 PRVAESAVVSRPHPVKGECLYCFI------TPNENEV--FDQKLISDLKKmVRErigpFAMPDVIqnapglPKTRSGKIM 632
Cdd:cd05904 433 PEILDAAVIPYPDEEAGEVPMAFVvrkpgsSLTEDEImdFVAKQVAPYKK-VRK----VAFVDAI------PKSPSGKIL 501
|
....
gi 24667955 633 RRVL 636
Cdd:cd05904 502 RKEL 505
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
116-636 |
3.71e-37 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 144.16 E-value: 3.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwHEEMEDKepACYPewmd 275
Cdd:cd05935 80 ---------------------------------------------------------------GSELDDL--ALIP---- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aedplfmlYTSGSTGKPKGVLHTtAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFegTP 355
Cdd:cd05935 91 --------YTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM--AR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 356 FfpGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLKVLGSVGEPInPEAWLwyYKYIGKEQCSIVDTFW 435
Cdd:cd05935 160 W--DRETALELIEKYKVTFWTNIPTMLVDLLATPE--FKTRDLSSLKVLTGGGAPM-PPAVA--EKLLKLTGLRFVEGYG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 436 QTETGGHVITPLPGAtpMKPGSASFPFFGVKPTLLD-ECGIEIKGEGEGYLVFSQPwpGMMRTLYNNHERFEDTyFSKFP 514
Cdd:cd05935 233 LTETMSQTHTNPPLR--PKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGP--QIFKGYWNRPEETEES-FIEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 515 G--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNEnEVF 592
Cdd:cd05935 308 GrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYR 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24667955 593 DQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd05935 387 GKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
114-644 |
2.24e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 143.02 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADGAWRGekplylkalcdtalekveemghsveKCIVVShLKRVTpcqpdhveeeipwtddrdywwhEEMEDKEPACYPEw 273
Cdd:PRK09088 101 DDAVAAG-------------------------RTDVED-LAAFI----------------------ASADALEPADTPS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEG 353
Cdd:PRK09088 132 IPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 354 tpFFPGNDRYWSVIDKYKVTQFYTAP---TAIRALMKFgEGPVLKHnlsgLKVLGSVGEPiNPE----AWLwyykyigKE 426
Cdd:PRK09088 211 --FEPKRTLGRLGDPALGITHYFCVPqmaQAFRAQPGF-DAAALRH----LTALFTGGAP-HAAedilGWL-------DD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 427 QCSIVDTFWQTETGGHVITPL-PGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQP--WPGMMRTLYNNHE 503
Cdd:PRK09088 276 GIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnlSPGYWRRPQATAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 504 RFEDTyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCF 583
Cdd:PRK09088 356 AFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLA 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667955 584 ITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDR 644
Cdd:PRK09088 430 IVPADGAPLD---LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
116-637 |
2.75e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 142.74 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAD 195
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkALCDTALEKVEEMGHSVEKCIVVShlkrvtpcqpdhveEEIPWTDDrdywwheemedkepacYPEWMD 275
Cdd:PRK08276 92 ------------ALADTAAELAAELPAGVPLLLVVA--------------GPVPGFRS----------------YEEALA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 A--EDPL-------FMLYTSGSTGKPKGVL--------HTTAGyllyaATTFKIVFDYKPGDiywctgdvgwitGHTYVV 338
Cdd:PRK08276 130 AqpDTPIadetagaDMLYSSGTTGRPKGIKrplpgldpDEAPG-----MMLALLGFGMYGGP------------DSVYLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 339 YGPL-------------ANGATSVIFEGtpFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLG 405
Cdd:PRK08276 193 PAPLyhtaplrfgmsalALGGTVVVMEK--FDA--EEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 406 SVGEPINPEAwlwyykyigKEQC------SIVDTFWQTETGGH-VITPLPGATpmKPGSASFPFFGVKpTLLDECGIEIK 478
Cdd:PRK08276 269 HAAAPCPVEV---------KRAMidwwgpIIHEYYASSEGGGVtVITSEDWLA--HPGSVGKAVLGEV-RILDEDGNELP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 479 GEGEGYLVFSQPWPGMmrTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLnVSGHL-MSTAEVESVL 557
Cdd:PRK08276 337 PGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVnIYPQEIENLL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 558 TEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK08276 412 VTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
116-638 |
4.29e-36 |
|
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: 140.98 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAD 195
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gAWRGEKplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwHEEMEDkepacypewmd 275
Cdd:cd05903 82 -RFRQFD--------------------------------------------------------PAAMPD----------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aeDPLFMLYTSGSTGKPKGVLHTtAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEG-T 354
Cdd:cd05903 94 --AVALLLFTSGTTGEPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 355 PffpgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGE--GPVLKHnlsgLKVLGSVGEPINPEAwlwyykyigKEQCS--- 429
Cdd:cd05903 171 P-----DKALALMREHGVTFMMGATPFLTDLLNAVEeaGEPLSR----LRTFVCGGATVPRSL---------ARRAAell 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 430 ---IVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwpgmmrTLYNNHERFE 506
Cdd:cd05903 233 gakVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP------SVFLGYLDRP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSKFP-GYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFIT 585
Cdd:cd05903 307 DLTADAAPeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24667955 586 PNENEVFDqklISDLKK-MVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05903 387 TKSGALLT---FDELVAyLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
98-637 |
5.41e-36 |
|
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: 141.71 E-value: 5.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPD 177
Cdd:cd17651 10 DAPALVAEG-------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 178 SLAERMFDCKAKLLITADgawrgekplylkalcdtalekveemghsvekcivvshlkRVTPCQPdhVEEEIPWTDDRDYW 257
Cdd:cd17651 83 RLAFMLADAGPVLVLTHP---------------------------------------ALAGELA--VELVAVTLLDQPGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 WHEEMEDKEPAcypewMDAEDPLFMLYTSGSTGKPKGVL--HTTAGYLLYAATTfkiVFDYKPGDiywCTGDVGWITGHT 335
Cdd:cd17651 122 AAGADAEPDPA-----LDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQAR---ASSLGPGA---RTLQFAGLGFDV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 YV--VYGPLANGATSVIfegtpffPGND------RYWSVIDKYKVTQFYTAPTAIRALmkFGEGPVLKHNLSGLKVLGSV 407
Cdd:cd17651 191 SVqeIFSTLCAGATLVL-------PPEEvrtdppALAAWLDEQRISRVFLPTVALRAL--AEHGRPLGVRLAALRYLLTG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 408 GEPINPEAWLWYYkYIGKEQCSIVDTFWQTETggHVIT----PLPGATPMKPGSASFPFFGVKPTLLDECG--IEIKGEG 481
Cdd:cd17651 262 GEQLVLTEDLREF-CAGLPGLRLHNHYGPTET--HVVTalslPGDPAAWPAPPPIGRPIDNTRVYVLDAALrpVPPGVPG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 482 EGYLVfsqpWPGMMRTLYNN----HERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVL 557
Cdd:cd17651 339 ELYIG----GAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAAL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 558 TEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd17651 415 ARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVD---AAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
117-568 |
5.66e-36 |
|
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: 140.09 E-value: 5.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKD-HGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAERM-F---DCKAKLL 191
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAA----YVPLDPAYPAERLaFileDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITaDGAWRGEKP-LYLKALCDTALEKVEEMGHSVEKcivvshlKRVTPCQPDHveeeipwtddrdywwheemedkePACY 270
Cdd:TIGR01733 77 LT-DSALASRLAgLVLPVILLDPLELAALDDAPAPP-------PPDAPSGPDD-----------------------LAYV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 271 pewmdaedplfmLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIywctgdvgWITGHTYV-------VYGPLA 343
Cdd:TIGR01733 126 ------------IYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 344 NGATSVIFEGTP--FFPGNDRYWsvIDKYKVTQFYTAPTAIRALMkfgegPVLKHNLSGLKVLGSVGEPINPEA---WLW 418
Cdd:TIGR01733 185 AGATLVVPPEDEerDDAALLAAL--IAEHPVTVLNLTPSLLALLA-----AALPPALASLRLVILGGEALTPALvdrWRA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 YYkyigkEQCSIVDTFWQTETGGHV---ITPLPGATPMKPGSASFPFFGVKPTLLDE----CGIEIKGE--------GEG 483
Cdd:TIGR01733 258 RG-----PGARLINLYGPTETTVWStatLVDPDDAPRESPVPIGRPLANTRLYVLDDdlrpVPVGVVGElyiggpgvARG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 484 YLvfsqpwpgmmrtlyN----NHERF-EDTYF-SKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVL 557
Cdd:TIGR01733 333 YL--------------NrpelTAERFvPDPFAgGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
|
490
....*....|.
gi 24667955 558 TEHPRVAESAV 568
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
114-638 |
1.33e-35 |
|
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: 141.07 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:TIGR03098 24 RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 AdgawrgekPLYLKALCDTALEkveemGHSVEKCIVVSHLKRVTPCQPDhvEEEIPWtddrdywwhEEMEDKEPACYPEW 273
Cdd:TIGR03098 104 S--------SERLDLLHPALPG-----CHDLRTLIIVGDPAHASEGHPG--EEPASW---------PKLLALGDADPPHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPLFMLYTSGSTGKPKGVL--HTT--------AGYL-------LYAATTFKivFDYKPGDIywctgDVGWITGHTY 336
Cdd:TIGR03098 160 VIDSDMAAILYTSGSTGRPKGVVlsHRNlvagaqsvATYLenrpddrLLAVLPLS--FDYGFNQL-----TTAFYVGATV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 337 VVYGPLA--NGATSVIFEGTPFFPGNDRYWSvidkyKVTQFYTAPTAIRALMKFGE--GPVLKHNLSGLKVLGSvgepiN 412
Cdd:TIGR03098 233 VLHDYLLprDVLKALEKHGITGLAAVPPLWA-----QLAQLDWPESAAPSLRYLTNsgGAMPRATLSRLRSFLP-----N 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 413 PEAWLWYykyigkeqcSIVDTFWQTetgghviTPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWP 492
Cdd:TIGR03098 303 ARLFLMY---------GLTEAFRST-------YLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 493 GMmrTLYNNHERFEDTyFSKFPGYYC----------TGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPR 562
Cdd:TIGR03098 367 AM--GYWNDPEKTAER-FRPLPPFPGelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGL 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 563 VAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:TIGR03098 444 VAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
98-637 |
1.91e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 140.89 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPD 177
Cdd:PRK06188 27 DRPALVLGD-------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 178 SLAERMFDCKAKLLITADGAWRgEKPLYLKALCDTaLEKVEEMGhsvekcivvshlkrvtpcqpdhveeeiPWTDDRDYW 257
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPAPFV-ERALALLARVPS-LKHVLTLG---------------------------PVPDGVDLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 whEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAAttfkivfdykpgdiyWCTGDVGWITGHTYV 337
Cdd:PRK06188 151 --AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWPADPRFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 338 VYGPLANGAtsvifeGTPFFPG--------------NDRYWSVIDKYKVTQFYTAPTAIRALMKfgEGPVLKHNLSGLKV 403
Cdd:PRK06188 214 MCTPLSHAG------GAFFLPTllrggtvivlakfdPAEVLRAIEEQRITATFLVPTMIYALLD--HPDLRTRDLSSLET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 404 LGSVGEPINP----EAwlwyYKYIGkeqcSI-VDTFWQTETGgHVITPLP-----GATPMKPGSASFPFFGVKPTLLDEC 473
Cdd:PRK06188 286 VYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 474 GIEIK-GE-GE----GYLVFSQPWpgmmrtlynnhERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHL 547
Cdd:PRK06188 357 GREVAqGEvGEicvrGPLVMDGYW-----------NRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 548 MSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTR 627
Cdd:PRK06188 426 VFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTA 502
|
570
....*....|
gi 24667955 628 SGKIMRRVLR 637
Cdd:PRK06188 503 LGKPDKKALR 512
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-638 |
2.83e-35 |
|
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: 140.07 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 87 LLDRNVRnGLGDQIAYYWegNHPDDYSRgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYM---PMILELpiaMLACARI 163
Cdd:cd12119 1 LLEHAAR-LHGDREIVSR--THEGEVHR-YTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLEL---YYAVPGM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 164 GAVHSIVFAGFSPDSLAERMFDCKAKLLITadgawrgekplylkalcDTALEKVeemghsvekcivvshLKRVTPcQPDH 243
Cdd:cd12119 74 GAVLHTINPRLFPEQIAYIINHAEDRVVFV-----------------DRDFLPL---------------LEAIAP-RLPT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 244 VEEEIPWTDDRDywwHEEMEDKEPACYPEWMDAEDPLF------------MLYTSGSTGKPKGVLHTTAGYLLYA-ATTF 310
Cdd:cd12119 121 VEHVVVMTDDAA---MPEPAGVGVLAYEELLAAESPEYdwpdfdentaaaICYTSGTTGNPKGVVYSHRSLVLHAmAALL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 311 KIVFDYKPGDIY-----------WCTGDVGWITGHTYVVYGPLANGATsvIFEgtpffpgndrywsVIDKYKVTQFYTAP 379
Cdd:cd12119 198 TDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS--LAE-------------LIEREGVTFAAGVP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 380 TAIRALMKFGEGPvlKHNLSGLKVLGSVGEPInPEAWLWYYKYIGkeqcsiVDTF--W-QTETG--GHVITPLPGATP-- 452
Cdd:cd12119 263 TVWQGLLDHLEAN--GRDLSSLRRVVIGGSAV-PRSLIEAFEERG------VRVIhaWgMTETSplGTVARPPSEHSNls 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 453 --------MKPGsasFPFFGVKPTLLDECGIEI--KGEGEGYLVFSQPWpgMMRTLYNNHER----FEDTYFSkfpgyyc 518
Cdd:cd12119 334 edeqlalrAKQG---RPVPGVELRIVDDDGRELpwDGKAVGELQVRGPW--VTKSYYKNDEEsealTEDGWLR------- 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 519 TGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlis 598
Cdd:cd12119 402 TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE--- 478
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 24667955 599 DLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-641 |
9.85e-35 |
|
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: 135.30 E-value: 9.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 284 YTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGAtSVIFEGTPFFPGN--- 360
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPAGYRNPglf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 361 DRYWSVIDKYKVTQFYTAPTAIRALMKFgegPVlKHNLSGLKVLGSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQTE-T 439
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQV---PV-NADISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEaT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 440 GGHVITPlPGaTPMKPGSAS--FPFFGVKPTLLDECGIEIK----GE-GEGYLVFSQPWPGMMRTLYNNHERFEDTYFSk 512
Cdd:cd05944 160 CLVAVNP-PD-GPKRPGSVGlrLPYARVRIKVLDGVGRLLRdcapDEvGEICVAGPGVFGGYLYTEGNKNAFVADGWLN- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 513 fpgyycTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGE--CLYCFITPNEnE 590
Cdd:cd05944 237 ------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGElpVAYVQLKPGA-V 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24667955 591 VFDQKLISDLKKMVRERIgpfAMPDVIQNAPGLPKTRSGKIMRRVLRKIAV 641
Cdd:cd05944 310 VEEEELLAWARDHVPERA---AVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
114-644 |
3.42e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 137.49 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIt 193
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADGAWRG-EKPLYLKALCDT--ALEKVEEMG----HSVEKcivvsHLkrvtpCQPdhveeeiPWTDDRDYwwHEEMEDKE 266
Cdd:PRK13295 133 VPKTFRGfDHAAMARRLRPElpALRHVVVVGgdgaDSFEA-----LL-----ITP-------AWEQEPDA--PAILARLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 267 PacypewmDAEDPLFMLYTSGSTGKPKGVLHTT----AGYLLYAATtfkivFDYKPGDIYWCTGDVGWITGHTYVVYGPL 342
Cdd:PRK13295 194 P-------GPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 ANGATSV---IFEgtpffpgNDRYWSVIDKYKVTqFYTAPTAIraLMKFGEGPVLK-HNLSGLKVLGSVGEPINP----E 414
Cdd:PRK13295 262 MLGATAVlqdIWD-------PARAAELIRTEGVT-FTMASTPF--LTDLTRAVKESgRPVSSLRTFLCAGAPIPGalveR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 415 AWlwyyKYIGkeqCSIVDTFWQTETGGhVITPLPGATPMKPG-SASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwpg 493
Cdd:PRK13295 332 AR----AALG---AKIVSAWGMTENGA-VTLTKLDDPDERAStTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC--- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 494 mmrTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPH 573
Cdd:PRK13295 401 ---SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 574 PVKGECLYCFITPNENEVFDQKLISDL---KKMVRERIgpfamPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDR 644
Cdd:PRK13295 478 ERLGERACAFVVPRPGQSLDFEEMVEFlkaQKVAKQYI-----PERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
98-636 |
5.37e-34 |
|
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: 135.45 E-value: 5.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPD 177
Cdd:cd05945 6 DRPAVVEGG-------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 178 SLAERMFDCKAKLLITAdgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqPDhveeeipwtddrdyw 257
Cdd:cd05945 79 RIREILDAAKPALLIAD----------------------------------------------GD--------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 wheemedkepacypewmdaeDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATtfkIV--FDYKPGDIYWCTG----DVGwi 331
Cdd:cd05945 98 --------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNW---MLsdFPLGPGDVFLNQApfsfDLS-- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 332 tghTYVVYGPLANGATSVIF--EGTPFFpgnDRYWSVIDKYKVTQFYTAPTAIRALMkfGEGPVLKHNLSGLKVLGSVGE 409
Cdd:cd05945 153 ---VMDLYPALASGATLVPVprDATADP---KQLFRFLAEHGITVWVSTPSFAAMCL--LSPTFTPESLPSLRHFLFCGE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 410 PI-NPEAWLWYYKYigkEQCSIVDTFWQTET----GGHVITPLPGATpMKPGSASFPFFGVKPTLLDECGIEIKGEGEGY 484
Cdd:cd05945 225 VLpHKTARALQQRF---PDARIYNTYGPTEAtvavTYIEVTPEVLDG-YDRLPIGYAKPGAKLVILDEDGRPVPPGEKGE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 485 LVFSQPwpGMMRTLYNNHERFEDTYFsKFPGY--YCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPR 562
Cdd:cd05945 301 LVISGP--SVSKGYLNNPEKTAAAFF-PDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPG 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 563 VAESAVVSRPHPVKGECLYCFITPNENEvfDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd05945 378 VKEAVVVPKYKGEKVTELIAFVVPKPGA--EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
112-631 |
6.71e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 136.71 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 112 YSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLL 191
Cdd:PRK06178 55 YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITADGAWrgekPLYLKALCDTALEKVeemghsvekcIVVShLKRVTPCQ-----PDHVEEEIPWTDDrdywWHEEME--D 264
Cdd:PRK06178 135 LALDQLA----PVVEQVRAETSLRHV----------IVTS-LADVLPAEptlplPDSLRAPRLAAAG----AIDLLPalR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 265 KEPACYPEWMDAEDPLFML-YTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLA 343
Cdd:PRK06178 196 ACTAPVPLPPPALDALAALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 344 NGATSVIFEgtpffpgndrYW------SVIDKYKVTQ-FYTAPTAIRaLMkfgEGPVLK-HNLSGLKVLGSVG--EPINP 413
Cdd:PRK06178 276 SGATLVLLA----------RWdavafmAAVERYRVTRtVMLVDNAVE-LM---DHPRFAeYDLSSLRQVRVVSfvKKLNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 414 EawlwyYKYIGKEQ--CSIVDTFW-QTETggHV---ITplpgaTPMKPGS---ASFPFFgvkptlldeCGI-----EIK- 478
Cdd:PRK06178 342 D-----YRQRWRALtgSVLAEAAWgMTET--HTcdtFT-----AGFQDDDfdlLSQPVF---------VGLpvpgtEFKi 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 479 -----GE-----GEGYLVFSQpwPGMMRTLYN----NHERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVS 544
Cdd:PRK06178 401 cdfetGEllplgAEGEIVVRT--PSLLKGYWNkpeaTAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 545 GhlMST--AEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDV-IQNAp 621
Cdd:PRK06178 472 G--MSVfpSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAVYKVPEIrIVDA- 545
|
570
....*....|
gi 24667955 622 gLPKTRSGKI 631
Cdd:PRK06178 546 -LPMTATGKV 554
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
111-636 |
6.74e-34 |
|
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: 135.50 E-value: 6.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 111 DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAER----MFDC 186
Cdd:cd12116 8 DDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAA----YVPLDPDYPADRlryiLEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 187 KAKLLITADgawRGEKPLylkALCDTALEKVEEMGHsvekcivVSHLKRVTPCQPDhveeeipwtddrdywwheemedke 266
Cdd:cd12116 84 EPALVLTDD---ALPDRL---PAGLPVLLLALAAAA-------AAPAAPRTPVSPD------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 267 pacypewmdaeDPLFMLYTSGSTGKPKGV-----------------LHTTAGYLLYAATTfkIVFDYKPGDIYWctgdvg 329
Cdd:cd12116 127 -----------DLAYVIYTSGSTGRPKGVvvshrnlvnflhsmrerLGLGPGDRLLAVTT--YAFDISLLELLL------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 330 witghtyvvygPLANGATSVIFEGTPFFPGND--RYwsvIDKYKVTQFYTAPTAIRALMKFGEGPvlkhnLSGLKVL-Gs 406
Cdd:cd12116 188 -----------PLLAGARVVIAPRETQRDPEAlaRL---IEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALcG- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 407 vGEPINPEawlwyykyIGKEQCSIVDTFWQ----TETgghviTPLPGATPMKPGSASF----PFFGVKPTLLDE------ 472
Cdd:cd12116 248 -GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIpigrPLANTQVYVLDAalrpvp 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 473 ---CG-IEIKGEG--EGYlvfsqpwpgmmrtlYNN----HERFEDTYFSKfPG--YYCTGDGARRDADGYLWITGRVDDM 540
Cdd:cd12116 314 pgvPGeLYIGGDGvaQGY--------------LGRpaltAERFVPDPFAG-PGsrLYRTGDLVRRRADGRLEYLGRADGQ 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 541 LNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGEcLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNA 620
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATLPAYMVPSAFVRL 454
|
570
....*....|....*.
gi 24667955 621 PGLPKTRSGKIMRRVL 636
Cdd:cd12116 455 DALPLTANGKLDRKAL 470
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
113-637 |
1.25e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 135.21 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 113 SRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLI 192
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 TADGAWRGEKPLYLKALCDTALEKVEEmghsvekcIVVSHlkRVTP--CQPDhveeeiPWTDDRDYWwheeMEDKEPACY 270
Cdd:PRK12406 89 AHADLLHGLASALPAGVTVLSVPTPPE--------IAAAY--RISPalLTPP------AGAIDWEGW----LAQQEPYDG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 271 PEwmdAEDPLFMLYTSGSTGKPKGVLHT--TAGYLLYAATTFKIVFDYKPGDIYWCTGDVGwitgHTYV-VYGPLANGAT 347
Cdd:PRK12406 149 PP---VPQPQSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLY----HSAPnAYGLRAGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 348 SVIFEGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPE------AWlW--- 418
Cdd:PRK12406 222 GVLVLQPRFDP--EELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADvkramiEW-Wgpv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 YYKYIGkeqcsivdtfwQTETGghVITplpGATP----MKPGSASFPFFGVKPTLLDECGIEIkGEGEGYLVFSQPwPGM 494
Cdd:PRK12406 299 IYEYYG-----------STESG--AVT---FATSedalSHPGTVGKAAPGAELRFVDEDGRPL-PQGEIGEIYSRI-AGN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 495 MRTLYNNHErfEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHP 574
Cdd:PRK12406 361 PDFTYHNKP--EKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDA 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 575 VKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK12406 439 EFGEALMAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
114-636 |
1.69e-33 |
|
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: 134.25 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAERMF----DCKAK 189
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAA----YVPLDPELPAERLAfmlaDAGAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 190 LLITAdgawrgekplylkalcdtalekveemghsvekcivvSHLKRVTPCQPDHVEEEIPWTddrdywwHEEMEDKEPAC 269
Cdd:cd12117 97 VLLTD------------------------------------RSLAGRAGGLEVAVVIDEALD-------AGPAGNPAVPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 270 ypewmDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDykPGDIYWCTGDVGWiTGHTYVVYGPLANGATSV 349
Cdd:cd12117 134 -----SPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVTLG--PDDRVLQTSPLAF-DASTFEIWGALLNGARLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 350 IFE-GTPFFPgnDRYWSVIDKYKVT-QFYTAPTairalmkFGEgpVLKHN---LSGLKVLGSVGEPINPE---AWLwyyk 421
Cdd:cd12117 206 LAPkGTLLDP--DALGALIAEEGVTvLWLTAAL-------FNQ--LADEDpecFAGLRELLTGGEVVSPPhvrRVL---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 422 yigkEQC---SIVDTFWQTETGG----HVITPL-PGATPMKPGSasfPFFGVKPTLLDE----CGIEIKGE----GEG-- 483
Cdd:cd12117 271 ----AACpglRLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR---PIANTRVYVLDEdgrpVPPGVPGElyvgGDGla 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 484 --YLvfsqpwpgmmrtlynNH-----ERF-EDTYFskfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEV 553
Cdd:cd12117 344 lgYL---------------NRpaltaERFvADPFG---PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEI 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 554 ESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNEnevfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd12117 406 EAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG-----ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
...
gi 24667955 634 RVL 636
Cdd:cd12117 481 RAL 483
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
114-651 |
2.23e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 134.90 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADgawrgekplylkALCDTALEkVEEMGHSVEKCIVVShlkrvtpcqpDHVEEEIPWTDDRdywWHEEMEDKEPACYPEw 273
Cdd:PRK07786 121 EA------------ALAPVATA-VRDIVPLLSTVVVAG----------GSSDDSVLGYEDL---LAEAGPAHAPVDIPN- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 mdaEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGpLANGATSVIFEG 353
Cdd:PRK07786 174 ---DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPG-LLLGAPTVIYPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 354 TPFFPGndRYWSVIDKYKVTQFYTAPTAIRALMkfGEGPVLKHNLSgLKVLGSVGEPINPEAWLWYYKYIGKEQcsIVDT 433
Cdd:PRK07786 250 GAFDPG--QLLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQ--ILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 434 FWQTETGGhVITPLPGATPM-KPGSASFPFFGVKPTLLDECGIEIkGEGE-GYLVFSQpwPGMMRTLYNNHERFEDTYFS 511
Cdd:PRK07786 323 FGQTEMSP-VTCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDV-PVGEvGEIVYRA--PTLMSGYWNNPEATAEAFAG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 512 kfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEv 591
Cdd:PRK07786 399 ---GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDD- 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667955 592 fDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKI--AVNDRNVGDTST 651
Cdd:PRK07786 475 -AALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERygACVNVERRSASA 535
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
116-637 |
2.40e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 134.43 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAd 195
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITS- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylKALCDTALEKVEEMGHsVEKCIVVSHlkrvtpcqpdhveeeipwTDDRDYWwheemEDKEPAC--YPEW 273
Cdd:PRK13391 104 -----------AAKLDVARALLKQCPG-VRHRLVLDG------------------DGELEGF-----VGYAEAVagLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPL--FMLYTSGSTGKPKGVLH--------TTAGYLLYaattFKIVFDYKPGDIYWCTGDVGwitgHTyvvyGPLA 343
Cdd:PRK13391 149 PIADESLgtDMLYSSGTTGRPKGIKRplpeqppdTPLPLTAF----LQRLWGFRSDMVYLSPAPLY----HS----APQR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 344 -------NGATSVIFEGtpFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAw 416
Cdd:PRK13391 217 avmlvirLGGTVIVMEH--FDA--EQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQV- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 417 lwyykyigKEQcsIVDtFWqtetgGHVITPLPGATP-------------MKPGSASFPFFGvKPTLLDECGIEI-KGEge 482
Cdd:PRK13391 292 --------KEQ--MID-WW-----GPIIHEYYAATEglgftacdseewlAHPGTVGRAMFG-DLHILDDDGAELpPGE-- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 483 gylvfsqpwPGmmrTLYNNHER-FEdtYF----------SKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTA 551
Cdd:PRK13391 353 ---------PG---TIWFEGGRpFE--YLndpaktaearHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQ 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 552 EVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKI 631
Cdd:PRK13391 419 EAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
|
....*.
gi 24667955 632 MRRVLR 637
Cdd:PRK13391 499 YKRLLR 504
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
125-637 |
4.40e-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: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 125 VCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMfdckakllitadgawrgekpL 204
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVL--------------------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 205 YLKALCDTALEKVEEMGhsvekcivVSHLKRVTPCQPDHVEeeipWTDDrDYWWHEEmeDKEPACYPEwmdAEDPLFMLY 284
Cdd:cd05922 63 YLVADAGGRIVLADAGA--------ADRLRDALPASPDPGT----VLDA-DGIRAAR--ASAPAHEVS---HEDLALLLY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 285 TSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGhTYVVYGPLANGATSVIfegTPFFPGNDRYW 364
Cdd:cd05922 125 TSGSTGSPKLVRLSHQN-LLANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVL---TNDGVLDDAFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 365 SVIDKYKVTQFYTAPT--AIRALMKFGEGPvlkhnLSGLKVLGSVGEPInPEAWLwyykyigKEQCS------IVDTFWQ 436
Cdd:cd05922 200 EDLREHGATGLAGVPStyAMLTRLGFDPAK-----LPSLRYLTQAGGRL-PQETI-------ARLREllpgaqVYVMYGQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 437 TETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWpGMMRtlYNNHERFeDTYFSKFPGY 516
Cdd:cd05922 267 TEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN-VMKG--YWNDPPY-RRKEGRGGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 517 YCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVkGECLYCFIT-PNENEVfdqk 595
Cdd:cd05922 343 LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTaPDKIDP---- 417
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24667955 596 liSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05922 418 --KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
87-591 |
6.65e-33 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 134.07 E-value: 6.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 87 LLDRNVRNgLGDQIAYYWEGNHPddySRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAV 166
Cdd:COG1022 16 LLRRRAAR-FPDRVALREKEDGI---WQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 167 HSIVFAGFSPDSLAERMFDCKAKLLITADgawrgekplylKALCDTALEKVEEMGHsVEKcIVVshlkrvtpcqpdhVEE 246
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVED-----------QEQLDKLLEVRDELPS-LRH-IVV-------------LDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 247 EIPWTDDRDYWWHEEMED----KEPACYPEWMDA---EDPLFMLYTSGSTGKPKGVLHtTAGYLLYAATTFKIVFDYKPG 319
Cdd:COG1022 146 RGLRDDPRLLSLDELLALgrevADPAELEARRAAvkpDDLATIIYTSGTTGRPKGVML-THRNLLSNARALLERLPLGPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 320 DIY-----WCtgdvgWITGHTYVVYGpLANGATSVIFEGTPFFPGNdrywsvIDKYKVTQFYTAP-------TAIRAlmK 387
Cdd:COG1022 225 DRTlsflpLA-----HVFERTVSYYA-LAAGATVAFAESPDTLAED------LREVKPTFMLAVPrvwekvyAGIQA--K 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 388 FGEGPVLKHNL--SGLKV------LGSVGEPINPEAWLWYY------------------KY-------IGKEqcsIVDTF 434
Cdd:COG1022 291 AEEAGGLKRKLfrWALAVgrryarARLAGKSPSLLLRLKHAladklvfsklrealggrlRFavsggaaLGPE---LARFF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 435 W-----------QTETGGhVIT-PLPGAtpMKPGSASFPFFG--VKptlLDECG-IEIKGegegylvfsqpwPGMMRTLY 499
Cdd:COG1022 368 RalgipvlegygLTETSP-VITvNRPGD--NRIGTVGPPLPGveVK---IAEDGeILVRG------------PNVMKGYY 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 500 NNHERFEDTyFSKfPGYYCTGDGARRDADGYLWITGRVDDMLNVS-GHLMSTAEVESVLTEHPRVAESAVV--SRPHPVk 576
Cdd:COG1022 430 KNPEATAEA-FDA-DGWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVgdGRPFLA- 506
|
570
....*....|....*
gi 24667955 577 geclyCFITPNENEV 591
Cdd:COG1022 507 -----ALIVPDFEAL 516
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
110-638 |
1.30e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 132.95 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 110 DDYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAK 189
Cdd:PRK06087 44 DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 190 LLItadgawrgekplylkalCDTALEKV--EEMGHSVEKciVVSHLKRVTpcqpdHVEEEIPWTDDRDYwwHEEMEDKEP 267
Cdd:PRK06087 124 MFF-----------------APTLFKQTrpVDLILPLQN--QLPQLQQIV-----GVDKLAPATSSLSL--SQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 268 ACYPEWMDAEDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGAT 347
Cdd:PRK06087 178 LTTAITTHGDELAAVLFTSGTEGLPKGVM-LTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 348 SVIFEgtPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSVGEPInPEAWLWYYKYIGKEQ 427
Cdd:PRK06087 257 SVLLD--IFTP--DACLALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PKKVARECQQRGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 CSIvdtFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDE------CGIEIKGEGEGylvfsqpwPGMMRTLYNN 501
Cdd:PRK06087 330 LSV---YGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEarktlpPGCEGEEASRG--------PNVFMGYLDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 502 HERF-----EDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVK 576
Cdd:PRK06087 399 PELTaraldEE-------GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERL 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 577 GE--CLYCFITPNENEVFDQKLISDLKkmvRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK06087 472 GErsCAYVVLKAPHHSLTLEEVVAFFS---RKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
86-638 |
1.36e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 132.47 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 86 NLLDRNVRNgLGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGA 165
Cdd:PRK07470 11 HFLRQAARR-FPDRIALVWGD-------RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 166 VhsIVFAGF--SPDSLAERMFDCKAKLLItADGAWRGEKPLyLKALCDTALEKVE----EMGHSVEKcIVVSHL-KRVTP 238
Cdd:PRK07470 83 V--WVPTNFrqTPDEVAYLAEASGARAMI-CHADFPEHAAA-VRAASPDLTHVVAiggaRAGLDYEA-LVARHLgARVAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 239 CQPDHveeeipwtddrdywwheemedkepacypewmdaEDPLFMLYTSGSTGKPK-GVLhtTAGYLLYAATTFkiVFDYK 317
Cdd:PRK07470 158 AAVDH---------------------------------DDPCWFFFTSGTTGRPKaAVL--THGQMAFVITNH--LADLM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 318 PGdiywctgdvgwiTGHTYV--VYGPL------------ANGATSVIFEGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIR 383
Cdd:PRK07470 201 PG------------TTEQDAslVVAPLshgagihqlcqvARGAATVLLPSERFDP--AEVWALVERHRVTNLFTVPTILK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 384 ALMkfgEGP-VLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGKeqcSIVDTFWQTETGGHvITPLPGA------TPM-KP 455
Cdd:PRK07470 267 MLV---EHPaVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGK---VLVQYFGLGEVTGN-ITVLPPAlhdaedGPDaRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 456 GSASFPFFGVKPTLLDECGIEIK-GE-GE----GYLVFSqpwpGMMRTLYNNHERFEDtyfskfpGYYCTGDGARRDADG 529
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDEGRELPpGEtGEicviGPAVFA----GYYNNPEANAKAFRD-------GWFRTGDLGHLDARG 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 530 YLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQkliSDLKKMVRERIG 609
Cdd:PRK07470 409 FLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLDGKVA 485
|
570 580
....*....|....*....|....*....
gi 24667955 610 PFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK07470 486 RYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
100-639 |
4.38e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 130.37 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 100 IAYYWEGN---HPDDYS-----RGLTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIV 170
Cdd:PRK06839 4 IAYWIEKRaylHPDRIAiiteeEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 171 FAGFSPDSLAERMFDCKAKLLItadgawrgekplylkalcdtALEKVEEMGHSVEKCIVVSHLKRVTPCQpdhveeeipw 250
Cdd:PRK06839 84 NIRLTENELIFQLKDSGTTVLF--------------------VEKTFQNMALSMQKVSYVQRVISITSLK---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 251 tddrdywwheEMEDKEPACYPEwMDAEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDI------YWC 324
Cdd:PRK06839 134 ----------EIEDRKIDNFVE-KNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRsivllpLFH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 325 TGDVGWITGHTYvvygpLANGATSVIFEGTPffpgnDRYWSVIDKYKVTQFYTAPT---AIRALMKFgegpvLKHNLSGL 401
Cdd:PRK06839 202 IGGIGLFAFPTL-----FAGGVIIVPRKFEP-----TKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 402 KVLGSVGEPInPEAWLWYYKYIGkeqCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEG 481
Cdd:PRK06839 267 RWFYNGGAPC-PEELMREFIDRG---FLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 482 EGYLVFSQPwpGMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHP 561
Cdd:PRK06839 343 VGELLIRGP--NVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLS 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 562 RVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKI 639
Cdd:PRK06839 418 DVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
114-593 |
8.37e-32 |
|
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: 128.87 E-value: 8.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIt 193
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 adgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhVEeeipwtddrdywwheemedkepacypew 273
Cdd:cd05907 83 --------------------------------------------------VE---------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 mDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVfDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEG 353
Cdd:cd05907 85 -DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 354 TPFFPGNdrywsvIDKYKVTQFYTAPT---AIRALMKFGEGPVLKHNLSGLKVLGSV------GEPINPEAWLWYYKyIG 424
Cdd:cd05907 163 AETLLDD------LSEVRPTVFLAVPRvweKVYAAIKVKAVPGLKRKLFDLAVGGRLrfaasgGAPLPAELLHFFRA-LG 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 keqCSIVDTFWQTETGGHVITPLPGATpmKPGSASFPFFGVkptlldECGIEIKGEgegyLVFSQPwpGMMRTLYNNHER 504
Cdd:cd05907 236 ---IPVYEGYGLTETSAVVTLNPPGDN--RIGTVGKPLPGV------EVRIADDGE----ILVRGP--NVMLGYYKNPEA 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 505 FEDTYFSkfPGYYCTGDGARRDADGYLWITGRVDDML-NVSGHLMSTAEVESVLTEHPRVAESAVV--SRPHPVkgecly 581
Cdd:cd05907 299 TAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIgdGRPFLV------ 370
|
490
....*....|..
gi 24667955 582 CFITPNENEVFD 593
Cdd:cd05907 371 ALIVPDPEALEA 382
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
278-638 |
5.10e-31 |
|
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: 126.25 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLYTSGSTGKPKGVLHTTAGYllyAATTFKIVFDYKpgdiyWCTGDV-----GWITGHTYVV--YGPLANGAtSVI 350
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANL---AANVRALVDAWR-----WTEDDVllhvlPLHHVHGLVNalLCPLFAGA-SVE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FegTPFFPGnDRYWSVIDKYKVTQFYTAPT--------------AIRALMKFGEGPVLkhnlsgLKVLGSVGEPInP--E 414
Cdd:cd05941 161 F--LPKFDP-KEVAISRLMPSITVFMGVPTiytrllqyyeahftDPQFARAAAAERLR------LMVSGSAALPV-PtlE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 415 AWlwyykyigkEQCS---IVDTFWQTETGGHVITPLPGatPMKPGSASFPFFGVKPTLLDECG-----------IEIKGE 480
Cdd:cd05941 231 EW---------EAITghtLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEETgeplprgevgeIQVRGP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 481 GegylVFSQPWpgmmrtlyNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRV-DDMLNVSGHLMSTAEVESVLTE 559
Cdd:cd05941 300 S----VFKEYW--------NKPEATKEEFTDD--GWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 560 HPRVAESAVVSRPHPVKGECLYCFITPNENEVfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05941 366 HPGVSECAVIGVPDPDWGERVVAVVVLRAGAA--ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
116-661 |
5.27e-31 |
|
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: 130.36 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAER---MF-DCKAKLL 191
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA----YVPLDPAYPAERlayMLeDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITaDGAWRGEKPlylkalcdtalekveemGHSVEkCIVVshlkrvtpcqpdhveEEIPWTDdrdywwheemedkEPACYP 271
Cdd:COG1020 578 LT-QSALAARLP-----------------ELGVP-VLAL---------------DALALAA-------------EPATNP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 EWM-DAEDPLFMLYTSGSTGKPKGVL--HTTAGYLLYAATTFkivFDYKPGD-IYWCTG---DVGwitghTYVVYGPLAN 344
Cdd:COG1020 611 PVPvTPDDLAYVIYTSGSTGRPKGVMveHRALVNLLAWMQRR---YGLGPGDrVLQFASlsfDAS-----VWEIFGALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 345 GATSVIFEGTPFFPGnDRYWSVIDKYKVTQFYTAPTAIRALMkfgegPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIG 424
Cdd:COG1020 683 GATLVLAPPEARRDP-AALAELLARHRVTVLNLTPSLLRALL-----DAAPEALPSLRLVLVGGEALPPELVRRWRARLP 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 keQCSIVDTFWQTETG----GHVITPLPGATPMKP-GSasfPFFGVKPTLLDE----CGIEIKGE--------GEGYLvf 487
Cdd:COG1020 757 --GARLVNLYGPTETTvdstYYEVTPPDADGGSVPiGR---PIANTRVYVLDAhlqpVPVGVPGElyiggaglARGYL-- 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 488 sqpwpgmmrtlyNNH----ERFEDTYFSkFPG--YYCTGDGARRDADG---YLwitGRVDDMLNVSGHLMSTAEVESVLT 558
Cdd:COG1020 830 ------------NRPeltaERFVADPFG-FPGarLYRTGDLARWLPDGnleFL---GRADDQVKIRGFRIELGEIEAALL 893
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 559 EHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRErigPFAMPDVIQNAPGLPKTRSGKImRRVLRK 638
Cdd:COG1020 894 QHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLP---PYMVPAAVVLLLPLPLTGNGKL-DRLALP 969
|
570 580
....*....|....*....|...
gi 24667955 639 IAVNDRNVGDTSTLADEQIVEQL 661
Cdd:COG1020 970 APAAAAAAAAAAPPAEEEEEEAA 992
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
108-636 |
7.54e-31 |
|
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: 126.62 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAER 182
Cdd:cd17646 11 TPDapavvDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDCKAKLLITADgawrgekplylkalcDTALEKVEEMGHSVekcivvshlkrVTPCQPDHVEEEIPWtddrdywwheem 262
Cdd:cd17646 91 LADAGPAVVLTTA---------------DLAARLPAGGDVAL-----------LGDEALAAPPATPPL------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 EDKEPAcypewmdaeDPLFMLYTSGSTGKPKGVLHTTAG---YLLYAATTFKIVfdykPGDIYW----CTGDV-GWitgh 334
Cdd:cd17646 133 VPPRPD---------NLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQDEYPLG----PGDRVLqktpLSFDVsVW---- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 335 tyVVYGPLANGATSVIFEgtpffPGNDR---YW-SVIDKYKVTQFYTAPTAIRAL---MKFGEGPVLKHNLSGlkvlgsv 407
Cdd:cd17646 196 --ELFWPLVAGARLVVAR-----PGGHRdpaYLaALIREHGVTTCHFVPSMLRVFlaePAAGSCASLRRVFCS------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 408 GEPINPE-AWLWY-------YKYIGKEQCSIVDTFWQTeTGGHVITPLPGATPMkPGSASFpffgvkptLLDECG----I 475
Cdd:cd17646 262 GEALPPElAARFLalpgaelHNLYGPTEAAIDVTHWPV-RGPAETPSVPIGRPV-PNTRLY--------VLDDALrpvpV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 476 EIKGE--------GEGYLvfsqPWPGMmrtlynNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHL 547
Cdd:cd17646 332 GVPGElylggvqlARGYL----GRPAL------TAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 548 MSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITP-NENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKT 626
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPaAGAAGPDT---AALRAHLAERLPEYMVPAAFVVLDALPLT 478
|
570
....*....|
gi 24667955 627 RSGKIMRRVL 636
Cdd:cd17646 479 ANGKLDRAAL 488
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
116-636 |
3.11e-29 |
|
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: 121.85 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAD 195
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 GAwrgekplylkalcdtalEKVEEMGHSVEKCIVVShlkrvtpcqpDHVEEEIPWTDDRDYwwheemedKEPACYPEwmd 275
Cdd:cd05923 109 DA-----------------QVMDAIFQSGVRVLALS----------DLVGLGEPESAGPLI--------EDPPREPE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aeDPLFMLYTSGSTGKPKGVL---HTTAGYLLYAATTFKIVFdykpgdiywctGDVGWITG-----HTYVVYGPLAngaT 347
Cdd:cd05923 151 --QPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRH-----------GRHNVVLGlmplyHVIGFFAVLV---A 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 348 SVIFEGT-----PFFPGNDRYWsvIDKYKVTQFYTAPTAIRALMKFGEGPVLKhnLSGLKVLGSVGEPInPEAWLwyYKY 422
Cdd:cd05923 215 ALALDGTyvvveEFDPADALKL--IEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGATM-PDAVL--ERV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 423 IGKEQCSIVDTFWQTETGGHVITPLPGA-TPMKPGsasfpFFG-VKPTLLDECGIEIKGEG-EGYLVF----SQPWPGMM 495
Cdd:cd05923 288 NQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSeVRIVRIGGSPDEALANGeEGELIVaaaaDAAFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 496 RtlynnheRFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPV 575
Cdd:cd05923 363 N-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADER 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 576 KGECLYCFITPNENEVFDQKL-----ISDLKKMVRERigpfamPDVIQNApgLPKTRSGKIMRRVL 636
Cdd:cd05923 436 WGQSVTACVVPREGTLSADELdqfcrASELADFKRPR------RYFFLDE--LPKNAMNKVLRRQL 493
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
116-637 |
3.45e-29 |
|
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: 121.32 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAER----MFDCKAKLL 191
Cdd:cd17649 13 LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGA----YVPLDPEYPAERlrymLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITADGawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacyp 271
Cdd:cd17649 89 LTHHP--------------------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewmdaEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKiVFDYKPGDIYWCTGDVGWITGHTYVvYGPLANGAtSVIF 351
Cdd:cd17649 94 -----RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE-RYGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 EGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKfgegpVLKHNLSG----LKVLGSVGEPINPE-AWLWyykyiGKE 426
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAE-----EADRTGDGrppsLRLYIFGGEALSPElLRRW-----LKA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 427 QCSIVDTFWQTETgghVITPL--PGATPMKPGSASFP----FFGVKPTLLDE----CGIEIKGE----GE----GYLvfs 488
Cdd:cd17649 236 PVRLFNAYGPTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDAdlnpVPVGVTGElyigGEglarGYL--- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 489 qPWPGMmrtlynNHERF-EDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESA 567
Cdd:cd17649 310 -GRPEL------TAERFvPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAA 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 568 VVSRPHPVkGECLYCFITPNENEVfDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd17649 383 VVALDGAG-GKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
108-636 |
1.65e-28 |
|
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: 119.74 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsIVFAGFSpdslaER 182
Cdd:cd05920 28 HPDriavvDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS-----HR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDckakllitadgawrgekplyLKALCDtalekveemgHSVEKCIVVShlkrvtpcqpdhveeeipwtDDRDYWWHEEM 262
Cdd:cd05920 101 RSE--------------------LSAFCA----------HAEAVAYIVP--------------------DRHAGFDHRAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 EDKEPACYPewmdaeDPLFMLYTSGSTGKPKGVLHTTAGYLlYAATTFKIVFDYKPGDIYWCTGDVGwitgHTYV----- 337
Cdd:cd05920 131 ARELAESIP------EVALFLLSGGTTGTPKLIPRTHNDYA-YNVRASAEVCGLDQDTVYLAVLPAA----HNFPlacpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 338 VYGPLANGATSVIfeGTPffPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSVGEPINPEAWL 417
Cdd:cd05920 200 VLGTLLAGGRVVL--APD--PSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 418 WYYKYIGkeqCSIVDTFWQTEtGGHVITPL--PGAT-------PMKPGSASfpffgvkpTLLDECGIEIkGEGE-GYLVF 487
Cdd:cd05920 274 RVPPVLG---CTLQQVFGMAE-GLLNYTRLddPDEViihtqgrPMSPDDEI--------RVVDEEGNPV-PPGEeGELLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 488 SQPWP--GMMRTLYNNHERFEDTyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAE 565
Cdd:cd05920 341 RGPYTirGYYRAPEHNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667955 566 SAVVSRPHPVKGECLYCFITPNENEVfdqkLISDLKKMVRER-IGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd05920 415 AAVVAMPDELLGERSCAFVVLRDPPP----SAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
116-636 |
1.70e-28 |
|
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: 118.96 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewmD 275
Cdd:cd12115 103 -------------------------------------------------------------------------------D 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVL--HTTAGYLL-YAATTF------------KIVFDYKpgdiywctgdvgwitghTYVVYG 340
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAieHRNAAAFLqWAAAAFsaeelagvlastSICFDLS-----------------VFELFG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 341 PLANGATSVIFEGTPFFPGNDRywsvidKYKVTQFYTAPTAIRALMKFGEGPvlkhnlSGLKVLGSVGEPINPEAWLWYY 420
Cdd:cd12115 167 PLATGGKVVLADNVLALPDLPA------AAEVTLINTVPSAAAELLRHDALP------ASVRVVNLAGEPLPRDLVQRLY 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 421 KYIGKEQcsIVDTFWQTETG----GHVITPLPGATPmkpgSASFPFFGVKPTLLDECG----------IEIKGEG--EGY 484
Cdd:cd12115 235 ARLQVER--VVNLYGPSEDTtystVAPVPPGASGEV----SIGRPLANTQAYVLDRALqpvplgvpgeLYIGGAGvaRGY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 485 LvfsqPWPGMmrtlynNHERFEDTYFskFPGYYC--TGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPR 562
Cdd:cd12115 309 L----GRPGL------TAERFLPDPF--GPGARLyrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPG 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 563 VAESAVVSRPHPVKGECLYCFITPNENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd12115 377 VREAVVVAIGDAAGERRLVAYIVAEPGA---AGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
282-637 |
5.66e-28 |
|
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: 117.86 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 282 MLYTSGSTGKPKGVLHTTAGYLLYAAT--TFKIVFDYKPGDIYWCTGDVGWITGHTyVVYGPLANGATSVIFEGtpFFPG 359
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEK--FDPE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 360 NdrYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINP---EAW-------LWYYkYIGKEQ-- 427
Cdd:cd05929 207 E--FLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWidwggpiIWEY-YGGTEGqg 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 -CSIVDTFWQTetggHvitplpgatpmkPGSASFPFFGvKPTLLDECGIEIKGEGEGYLVFSQPWPgmmrtlYNNHERFE 506
Cdd:cd05929 284 lTIINGEEWLT----H------------PGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSKFPGYYCT-GDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFIT 585
Cdd:cd05929 341 KTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24667955 586 PNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
114-630 |
1.66e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 117.29 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIt 193
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 adgawrgekplYLKALCDtaleKVEEMGHSVEKcivVSHLKRVtpcqPDHVEEEIPwTDDRDYwwhEEMEDKEPACYPEW 273
Cdd:PRK07798 106 -----------YEREFAP----RVAEVLPRLPK---LRTLVVV----EDGSGNDLL-PGAVDY---EDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPLFMLYTSGSTGKPKGVLHTTA--------GYLLY---------------AATTFKIVFDYKP---GDIYWctgd 327
Cdd:PRK07798 160 ERSPDDLYLLYTGGTTGMPKGVMWRQEdifrvllgGRDFAtgepiedeeelakraAAGPGMRRFPAPPlmhGAGQW---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 328 vgwitghtyVVYGPLANGATSVIFEGTPFFPgnDRYWSVIDKYKVTQF------YTAPTaIRALMKFGEGpvlkhNLSGL 401
Cdd:PRK07798 236 ---------AAFAALFSGQTVVLLPDVRFDA--DEVWRTIEREKVNVItivgdaMARPL-LDALEARGPY-----DLSSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 402 KVLGSVGEPINP---EAWLWYykyigKEQCSIVDTFWQTETG--GHVITPlPGATPmkpgsASFPFFGVKP--TLLDECG 474
Cdd:PRK07798 299 FAIASGGALFSPsvkEALLEL-----LPNVVLTDSIGSSETGfgGSGTVA-KGAVH-----TGGPRFTIGPrtVVLDEDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 475 IEIK-GEGE-GYLVFSQPWP-GMmrtlYNNHERFEDTYFSkFPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMS 549
Cdd:PRK07798 368 NPVEpGSGEiGWIARRGHIPlGY----YKDPEKTAETFPT-IDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 550 TAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSG 629
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAG 519
|
.
gi 24667955 630 K 630
Cdd:PRK07798 520 K 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
277-633 |
3.19e-27 |
|
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: 113.12 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFMLYTSGSTGKPKGVLhtTAGYLLYAATTFKIVfdykpGDIYWCTGDVGWITGHTYVVYGpLANGATSVIFEGT-P 355
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVL--LANKTFFAVPDILQK-----EGLNWVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 356 FFPGNDRYWSV---IDKYKVTQFYTAPTAIRALMKfgegpVLKHNLSGLKVLGSVG----EPINPEA--WLWYykyigkE 426
Cdd:cd17635 73 TGGENTTYKSLfkiLTTNAVTTTCLVPTLLSKLVS-----ELKSANATVPSLRLIGyggsRAIAADVrfIEAT------G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 427 QCSIVDTFWQTETGGHVITPLpGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWpgMMRTLYNNHERFE 506
Cdd:cd17635 142 LTNTAQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITp 586
Cdd:cd17635 219 EVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24667955 587 nENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd17635 295 -ASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
114-637 |
5.27e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 115.55 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADGAWrgekPLY--LKALCDTALEKVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPwtddrdywwheemedkepacyp 271
Cdd:PRK08008 116 SAQFY----PMYrqIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATLCYAPP---------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewMDAEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAA--TTFKIVFDYKpgDIYWCTGDVGWITGHTYVVYGPLANGATSV 349
Cdd:PRK08008 170 --LSTDDTAEILFTSGTTSRPKGVVITHYN-LRFAGyySAWQCALRDD--DVYLTVMPAFHIDCQCTAAMAAFSAGATFV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 350 IFEGTpffpGNDRYWSVIDKYKVTQFYTAPTAIRALMKfgegpvlkhnlsglkvlgsvgEPinPEAW--------LWYYK 421
Cdd:PRK08008 245 LLEKY----SARAFWGQVCKYRATITECIPMMIRTLMV---------------------QP--PSANdrqhclreVMFYL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 422 YIGKEQ---------CSIVDTFWQTETGGHVITPLPGATPMKPgSASFPFFGVKPTLLDECG----------IEIKGEge 482
Cdd:PRK08008 298 NLSDQEkdafeerfgVRLLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNrplpageigeICIKGV-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 483 gylvfsqpwPG--MMRTLYNNHERFEDTYfsKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEH 560
Cdd:PRK08008 375 ---------PGktIFKEYYLDPKATAKVL--EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24667955 561 PRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
113-642 |
1.40e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 113.72 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 113 SRGLTYRKLLEEVCRFANVLKDHGiRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLI 192
Cdd:PRK07638 24 DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 TADgawrgekpLYLKALCDtalekveemghsvEKCIVVShlkrvtpcqpdhVEEeipwtddrdywWHEEMEDKEPACYPE 272
Cdd:PRK07638 103 TER--------YKLNDLPD-------------EEGRVIE------------IDE-----------WKRMIEKYLPTYAPI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 273 WMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLY---AATTFKIVFDYK---PGDIYwctgdvgwitgHTYVVYGPLAN-- 344
Cdd:PRK07638 139 ENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSfdcNVHDFHMKREDSvliAGTLV-----------HSLFLYGAISTly 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 345 -GATSVIFEgtPFFPGNDRYWsvIDKYKVTQFYTAPTAIRALMKFGEGP--VLKHNLSGLK-VLGSVGE--PINPEAWLw 418
Cdd:PRK07638 208 vGQTVHLMR--KFIPNQVLDK--LETENISVMYTVPTMLESLYKENRVIenKMKIISSGAKwEAEAKEKikNIFPYAKL- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 yYKYIGKEQCSIVdTFWQTETgghvitplpgaTPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwpgMMRTL 498
Cdd:PRK07638 283 -YEFYGASELSFV-TALVDEE-----------SERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSP---QFFMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 499 YNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGE 578
Cdd:PRK07638 347 YIIGGVLARELNAD--GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 579 CLYCFITPNENEvfdqkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVN 642
Cdd:PRK07638 425 KPVAIIKGSATK-------QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
278-640 |
1.43e-26 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 110.88 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIfegtpff 357
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 358 pgnDRYWSV---IDKYKVTQFYTAPTAIRALMKFGEGPvlkHNLSGLKVLGSVGEPINPEAwlwyYKYIGKEQCSIVDTF 434
Cdd:cd17630 73 ---ERNQALaedLAPPGVTHVSLVPTQLQRLLDSGQGP---AALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 435 WQTETGGHVITPLPGATpmKPGSASFPFFGVKPTLLDECGIEIKGEG--EGYlvfsqpWPGMMRTLYNNherfedtyfsk 512
Cdd:cd17630 143 GMTETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEIWVGGASlaMGY------LRGQLVPEFNE----------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 513 fPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNenevf 592
Cdd:cd17630 204 -DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR----- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24667955 593 DQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIA 640
Cdd:cd17630 278 GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
87-638 |
1.49e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 114.71 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 87 LLDRNVRNgLGDQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAV 166
Cdd:PRK05605 37 LYDNAVAR-FGDRPALDFFG-------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 167 ---HSIVFagfSPDSLAERMFDCKAKLLItadgAWRGEKPLYLKALCDTALEKVeemgHSVEKCIVVSHLKRV------- 236
Cdd:PRK05605 109 vveHNPLY---TAHELEHPFEDHGARVAI----VWDKVAPTVERLRRTTPLETI----VSVNMIAAMPLLQRLalrlpip 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 237 ---------TPCQPDHVeeeiPWTDDRDywwHEEMEDKEPACYPEwMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAA 307
Cdd:PRK05605 178 alrkaraalTGPAPGTV----PWETLVD---AAIGGDGSDVSHPR-PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 308 TTFKIVFDYKPGD-----------IYwctgdvgwitGHTYVVYGPLANGATSVIFEGtpffPGNDRYWSVIDKYKVTQFY 376
Cdd:PRK05605 250 QGKAWVPGLGDGPervlaalpmfhAY----------GLTLCLTLAVSIGGELVLLPA----PDIDLILDAMKKHPPTWLP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 377 TAPTAIRALMKFGEgpvlKHN--LSGLKVLGSVGEPINPeawlwyykyigkeqcSIVDTfWQTETGGHVI--------TP 446
Cdd:PRK05605 316 GVPPLYEKIAEAAE----ERGvdLSGVRNAFSGAMALPV---------------STVEL-WEKLTGGLLVegygltetSP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 447 LPGATPM----KPGSASFPFFG-----VKPTLLDEcGIEIKGEGE----GYLVFSQPWpgmmrtlynnhERFEDTYFSKF 513
Cdd:PRK05605 376 IIVGNPMsddrRPGYVGVPFPDtevriVDPEDPDE-TMPDGEEGEllvrGPQVFKGYW-----------NRPEETAKSFL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 514 PGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFD 593
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALD 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 24667955 594 QKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK05605 524 PE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
114-636 |
2.43e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 113.97 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADGAWrgekPLYLKALCDTALEKVEEMGHS----VEKCIVVSHLKRVTPCQPDHVEEEipwtdDRDYWWHEEMEDKEPA- 268
Cdd:PRK06710 128 LDLVF----PRVTNVQSATKIEHVIVTRIAdflpFPKNLLYPFVQKKQSNLVVKVSES-----ETIHLWNSVEKEVNTGv 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 269 ---CYPEwmdaEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGD-IYWCTGDVGWITGHTYVVYGPLAN 344
Cdd:PRK06710 199 evpCDPE----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEeVVLGVLPFFHVYGMTAVMNLSIMQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 345 GATSVIFegtPFFpGNDRYWSVIDKYKVTQFYTAPTAIRALMKfgeGPVLK-HNLSGLKVLGSVGEPINPEAWLWYYKYI 423
Cdd:PRK06710 275 GYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN---SPLLKeYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 424 GKEqcsIVDTFWQTETgghviTPLPGATPM----KPGSASFPFFGVKPTLLDECGIEIKGEGE-GYLVFSQPwpGMMRTL 498
Cdd:PRK06710 348 GGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGEiGEIVVKGP--QIMKGY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 499 YNnheRFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGE 578
Cdd:PRK06710 418 WN---KPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGE 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 579 CLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK06710 495 TVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
113-638 |
2.67e-26 |
|
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: 112.78 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 113 SRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLI 192
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 tadgawrgekplylkalCDTALEKveemghsvekcivvshlkrvtpcqpdhveEEIPWTDDRDYWWhEEMEDkepacypE 272
Cdd:cd12118 107 -----------------VDREFEY-----------------------------EDLLAEGDPDFEW-IPPAD-------E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 273 WmdaeDPLFMLYTSGSTGKPKGVLHTTAG-YLlyAATTFKIVFDYKPGDIYWCTGDV----GWitghTYVvYGPLANGAT 347
Cdd:cd12118 133 W----DPIALNYTSGTTGRPKGVVYHHRGaYL--NALANILEWEMKQHPVYLWTLPMfhcnGW----CFP-WTVAAVGGT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 348 SVIF-EGTPffpgnDRYWSVIDKYKVTQFYTAPTAIRALMKfgEGPVLKHNLSGlKVLGSVGEPINPEAWLWYYKYIGke 426
Cdd:cd12118 202 NVCLrKVDA-----KAIYDLIEKHKVTHFCGAPTVLNMLAN--APPSDARPLPH-RVHVMTAGAPPPAAVLAKMEELG-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 427 qCSIVDTFWQTETGGHVItplpgATPMKPGSASFP--------------FFGVKP-TLLD-ECGIEIKGEGE--GYLVFS 488
Cdd:cd12118 272 -FDVTHVYGLTETYGPAT-----VCAWKPEWDELPteerarlkarqgvrYVGLEEvDVLDpETMKPVPRDGKtiGEIVFR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 489 qpwpG--MMRTLYNN----HERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPR 562
Cdd:cd12118 346 ----GniVMKGYLKNpeatAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 563 VAESAVVSRPHPVKGECLYCFITPNENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPgLPKTRSGKIMRRVLRK 638
Cdd:cd12118 415 VLEAAVVARPDEKWGEVPCAFVELKEGA---KVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
552-630 |
3.22e-26 |
|
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: 102.24 E-value: 3.22e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 552 EVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGK 630
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV---ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
116-636 |
3.70e-26 |
|
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: 112.42 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAER----MFDCKAKLL 191
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGA----YLPIDPDYPEERiqyiLEDSGADIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITAdgawrgekplylkalcdtalekveemghsvekcivvSHLKrvtpcQPDHVEEEIPWTDDRDYWwHEEMEDKEPACyp 271
Cdd:cd17655 99 LTQ------------------------------------SHLQ-----PPIAFIGLIDLLDEDTIY-HEESENLEPVS-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewmDAEDPLFMLYTSGSTGKPKGVLHTTAG-----------YLLYAATTF----KIVFDYKPGDIYwctgdVGWITGHTY 336
Cdd:cd17655 135 ---KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankvIYQGEHLRValfaSISFDASVTEIF-----ASLLSGNTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 337 VVYGplangaTSVIFEGTPFFpgndrywSVIDKYKVTQFYTAPTAIRAL--MKFGEGPVLKHNLSGlkvlgsvGEPINPE 414
Cdd:cd17655 207 YIVR------KETVLDGQALT-------QYIRQNRITIIDLTPAHLKLLdaADDSEGLSLKHLIVG-------GEALSTE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 415 -AWLWYYKYigKEQCSIVDTFWQTETGghVITPLPGATPMKPGSASFPFfGvKPT------LLDECG----------IEI 477
Cdd:cd17655 267 lAKKIIELF--GTNPTITNAYGPTETT--VDASIYQYEPETDQQVSVPI-G-KPLgntriyILDQYGrpqpvgvageLYI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 478 KGEG--EGYLvfSQPwpgmmrTLYNnhERFEDTYFSkfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEV 553
Cdd:cd17655 341 GGEGvaRGYL--NRP------ELTA--EKFVDDPFV--PGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 554 ESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENevFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd17655 409 EARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LP---VAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDR 483
|
...
gi 24667955 634 RVL 636
Cdd:cd17655 484 KAL 486
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
116-643 |
5.15e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 112.94 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAD 195
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gAWRGEKplYLkALCDTALEKVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPWTD---DRDYWWHEEMEDKEPAcype 272
Cdd:PRK12583 126 -AFKTSD--YH-AMLQELLPGLAEGQPGALACERLPELRGVVSLAPAPPPGFLAWHElqaRGETVSREALAERQAS---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 273 wMDAEDPLFMLYTSGSTGKPKGVLHT-----TAGYLLYAATTF----KIVFdykPGDIYWCTGDVgwitghtYVVYGPLA 343
Cdd:PRK12583 198 -LDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtehdRLCV---PVPLYHCFGMV-------LANLGCMT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 344 NGATsVIFEGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALM---KFGEgpvlkHNLSGLKVLGSVGEPINPEAwlwYY 420
Cdd:PRK12583 267 VGAC-LVYPNEAFDP--LATLQAVEEERCTALYGVPTMFIAELdhpQRGN-----FDLSSLRTGIMAGAPCPIEV---MR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 421 KYIGKEQCS-IVDTFWQTETGGhVITPLPGATPMKPGSASF----PFFGVKptLLDECGIEI-KGE-GE----GYLVfsq 489
Cdd:PRK12583 336 RVMDEMHMAeVQIAYGMTETSP-VSLQTTAADDLERRVETVgrtqPHLEVK--VVDPDGATVpRGEiGElctrGYSV--- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 490 pwpgmMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVV 569
Cdd:PRK12583 410 -----MKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 570 SRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVND 643
Cdd:PRK12583 483 GVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEE 553
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
110-639 |
9.55e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 111.94 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 110 DDysRG-LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKA 188
Cdd:PRK07788 70 DE--RGtLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 189 KLLITADgawrgEkplYLKALcdtalEKVEEmghSVEKCivvshlkRVTPCQPDHVEEEIPWTDDRDywwhEEMEDKEPA 268
Cdd:PRK07788 148 KALVYDD-----E---FTDLL-----SALPP---DLGRL-------RAWGGNPDDDEPSGSTDETLD----DLIAGSSTA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 269 CYPEWmdAEDPLFMLYTSGSTGKPKGVLHTTAGYLlyaaTTFKIVFDYKPgdiywctgdvgWITGHTYVVYGP------- 341
Cdd:PRK07788 201 PLPKP--PKPGGIVILTSGTTGTPKGAPRPEPSPL----APLAGLLSRVP-----------FRAGETTLLPAPmfhatgw 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 ------LANGATSVIFEgtPFFPGN---DrywsvIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPIN 412
Cdd:PRK07788 264 ahltlaMALGSTVVLRR--RFDPEAtleD-----IAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 413 PEawlwyykyigkeqcsIVDTFwqTETGGHVITPLPG---------ATP----MKPGSASFPFFGVKPTLLDECGIEIkG 479
Cdd:PRK07788 337 PE---------------LATRA--LEAFGPVLYNLYGstevafatiATPedlaEAPGTVGRPPKGVTVKILDENGNEV-P 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 480 EGEgylvfsqpwPGmmRTLYNNHERFEDTYFSKFP----GYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVES 555
Cdd:PRK07788 399 RGV---------VG--RIFVGNGFPFEGYTDGRDKqiidGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 556 VLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKlisDLKKMVRERIGPFAMP-DVIqNAPGLPKTRSGKIMRR 634
Cdd:PRK07788 468 LLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPrDVV-FLDELPRNPTGKVLKR 543
|
....*
gi 24667955 635 VLRKI 639
Cdd:PRK07788 544 ELREM 548
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
278-642 |
2.86e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 110.16 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLY-TSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIYWCTGD--------VGWITGhtyvvygpLANGATS 348
Cdd:PRK07867 152 DDLFMLIfTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA--------LAAGASI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 349 VI---FEGTPFFPGndrywsvIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNlsGLKVL-GSVGEPINPEAwlwYYKYIG 424
Cdd:PRK07867 223 ALrrkFSASGFLPD-------VRRYGATYANYVGKPLSYVLATPERPDDADN--PLRIVyGNEGAPGDIAR---FARRFG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 keqCSIVDTFWQTEtGGHVITPLPGaTPmkPGSASFPFFGVK-----------PTLLDECGIEIKGEGEGYLVFSQPwPG 493
Cdd:PRK07867 291 ---CVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGVAivdpdtgtecpPAEDADGRLLNADEAIGELVNTAG-PG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 494 MMRTLYNNHE----RFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVV 569
Cdd:PRK07867 363 GFEGYYNDPEadaeRMRG-------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVY 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 570 SRPHPVKGECLYCFITPNENEVFDQKLISDLKKmVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVN 642
Cdd:PRK07867 436 AVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
116-641 |
3.35e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 110.23 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT-A 194
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVeA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 195 DGAwrgekplylkalcdTALEKVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPWTddrdywwheemedkEPACYPEWM 274
Cdd:PRK06155 127 ALL--------------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLD--------------APAPAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 DAeDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKiVFDYKPGDIYWCTGDVGwitgHTYVV---YGPLANGATSVIf 351
Cdd:PRK06155 179 PG-DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLF----HTNALnafFQALLAGATYVL- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 egTPFFPGNdRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLGSVGEPINPEAWLwyykyigKEQCSI- 430
Cdd:PRK06155 252 --EPRFSAS-GFWPAVRRHGATVTYLLGAMVSILLSQPARE--SDRAHRVRVALGPGVPAALHAAF-------RERFGVd 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 431 -VDTFWQTETGGHVITPLPGAtpmKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNH-----ER 504
Cdd:PRK06155 320 lLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMpektvEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 505 FEDTYFSkfpgyycTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFI 584
Cdd:PRK06155 397 WRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAV 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24667955 585 TPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAV 641
Cdd:PRK06155 470 VLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
114-638 |
3.68e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 112.36 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT 4654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 adgawrgekplylkalcdtalekveemgHSvekcivvshlkrvtpcqpdHVEEEIPWTD-------DRDYWWhEEMEDKE 266
Cdd:PRK12316 4655 ----------------------------QS-------------------HLLQRLPIPDglaslalDRDEDW-EGFPAHD 4686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 267 PACYpewMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTfkivfdykpGDIYWCTGDVGWITGHTYV-------VY 339
Cdd:PRK12316 4687 PAVR---LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLY 4754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSVIFEGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMkfgEGPVLKHNLSGLKVLGSVGEPINPEAW-LW 418
Cdd:PRK12316 4755 HPLINGASVVIRDDSLWDP--ERLYAEIHEHRVTVLVFPPVYLQQLA---EHAERDGEPPSLRVYCFGGEAVAQASYdLA 4829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 YYKYigkEQCSIVDTFWQTETgghVITPLPGATP--MKPGSASFPFFGVKPT----LLDECG----------IEIKGEG- 481
Cdd:PRK12316 4830 WRAL---KPVYLFNGYGPTET---TVTVLLWKARdgDACGAAYMPIGTPLGNrsgyVLDGQLnplpvgvageLYLGGEGv 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 482 -EGYLvfsqPWPGMmrtlynNHERFEDTYFSKfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLT 558
Cdd:PRK12316 4904 aRGYL----ERPAL------TAERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLR 4972
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 559 EHPRVAESAVVSRPHPVkGECLYCFITPNENEVFDQ-----KLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:PRK12316 4973 EHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADAdeaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
....*
gi 24667955 634 RVLRK 638
Cdd:PRK12316 5052 KALPQ 5056
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
116-634 |
4.56e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 109.59 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAERMFDCKAKL----- 190
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV----VVPLDPALPIAEQRVRSQAAgarvv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 191 LITADGAwrgekplylkalCDTALEKVEEMGHSVekcivvshlkRVTPcqpDHVEEEIPWTDDRDywwhEEMEDKEPACY 270
Cdd:PRK05852 120 LIDADGP------------HDRAEPTTRWWPLTV----------NVGG---DSGPSGGTLSVHLD----AATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 271 PEWMDAEDPLFMlYTSGSTGKPKGVLHTTAGYllyAATTFKIVFDYKPGDiywctGDVGWITGHTYVVYGPLANGATSVI 350
Cdd:PRK05852 171 PEGLRPDDAMIM-FTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSP-----RDATVAVMPLYHGHGLIAALLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FEGTPFFPGNDRY-----WSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGk 425
Cdd:PRK05852 242 SGGAVLLPARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 426 eqCSIVDTFWQTETGGHVITPL---------PGATPMKPGSASFPFFGVKPTLLDECGIEIKGE--------GEGYLvfS 488
Cdd:PRK05852 321 --APVVCAFGMTEATHQVTTTQiegigqtenPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEvwlrgttvVRGYL--G 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 489 QPwpgmmrtlYNNHERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAV 568
Cdd:PRK05852 397 DP--------TITAANFTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 569 VSRPHPVKGECLYCFITPNENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRR 634
Cdd:PRK05852 462 FGVPDQLYGEAVAAVIVPRESA---PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
80-637 |
6.70e-25 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 110.12 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 80 STNLCYNLLDRNVRNGLGDQIAYYwegnHPDDYSRGltyrKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLA 159
Cdd:PRK06060 3 NGNLAGLLAEQASEAGWYDRPAFY----AADVVTHG----QIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 160 CARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADgawrgekplylkALCDTAlekveEMGHSVEKCIVVSHLKRVTPC 239
Cdd:PRK06060 75 CLARGVMAFLANPELHRDDHALAARNTEPALVVTSD------------ALRDRF-----QPSRVAEAAELMSEAARVAPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 240 qpdhveeeipwtddrDYwwheemedkepacypEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPG 319
Cdd:PRK06060 138 ---------------GY---------------EPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 320 DIYWCTGDVGWITGHTYVVYGPLANGATSVIfegTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMkfgeGPVLKHNLS 399
Cdd:PRK06060 188 DTGLCSARMYFAYGLGNSVWFPLATGGSAVI---NSAPVTPEAAAILSARFGPSVLYGVPNFFARVI----DSCSPDSFR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 400 GLKVLGSVGEPINPEAWLWYYKYIGKeqCSIVDTFWQTETGGHVITPlpGATPMKPGSAS--FPFFGVKPTLLDecGIEI 477
Cdd:PRK06060 261 SLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTLGrvLPPYEIRVVAPD--GTTA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 478 KGEGEGYLvfsqpW---PGMMRTLYNNHERF-EDTyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEV 553
Cdd:PRK06060 335 GPGVEGDL-----WvrgPAIAKGYWNRPDSPvANE------GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREV 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 554 ESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVR 483
|
....
gi 24667955 634 RVLR 637
Cdd:PRK06060 484 GALR 487
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
98-639 |
7.25e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 108.51 E-value: 7.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGnhpddysRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsIVFAG--FS 175
Cdd:PRK03640 17 DRTAIEFEE-------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLLNtrLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 176 PDSLAERMFDCKAKLLITADGawrgekplYLKALCDTALEKVEEMGHSVEKcivvshlkrvtpcqpdHVEEEIPWTDDrd 255
Cdd:PRK03640 88 REELLWQLDDAEVKCLITDDD--------FEAKLIPGISVKFAELMNGPKE----------------EAEIQEEFDLD-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 256 ywwheemedkepacypewmdaeDPLFMLYTSGSTGKPKGVLHTTAGYLlYAATTFKIVFDYKPGDIYWCTGDVGWITGHT 335
Cdd:PRK03640 142 ----------------------EVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 Y----VVYGplangaTSVIFEgtPFFPGNDRYWSVIDKyKVTQFYTAPTAI-RALMKFGEGPVLKHNLSGLkvLGsvGEP 410
Cdd:PRK03640 199 IlmrsVIYG------MRVVLV--EKFDAEKINKLLQTG-GVTIISVVSTMLqRLLERLGEGTYPSSFRCML--LG--GGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 411 InPEAWLwyykyigkEQCS-----IVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDEcGIEIKGEGEGYL 485
Cdd:PRK03640 266 A-PKPLL--------EQCKekgipVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 486 VFSQPwpGMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAE 565
Cdd:PRK03640 336 VVKGP--NVTKGYLNREDATRETFQD---GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAE 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667955 566 SAVVSRPHPVKGECLYCFItpneneVFDQKLISD-LKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKI 639
Cdd:PRK03640 411 AGVVGVPDDKWGQVPVAFV------VKSGEVTEEeLRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
116-637 |
2.17e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 107.83 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLlEEVCR-FANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAK-LLI 192
Cdd:PRK08974 49 MTFRKL-EERSRaFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaIVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 TADGAWRGEKPLYlkalcDTALEKV--EEMGH--SVEK----CIVVSHLKRVTPCQ--PDHVEEEIPWTDDRdywwheEM 262
Cdd:PRK08974 128 VSNFAHTLEKVVF-----KTPVKHVilTRMGDqlSTAKgtlvNFVVKYIKRLVPKYhlPDAISFRSALHKGR------RM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 EDKEPAcypewMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLlyaATTFKIVFDYKPGdiywctgdvgWITGHTYVVYG-P 341
Cdd:PRK08974 197 QYVKPE-----LVPEDLAFLQYTGGTTGVAKGAMLTHRNML---ANLEQAKAAYGPL----------LHPGKELVVTAlP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 L-------AN-------GATSVIFEGTPFFPGndrYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLkhNLSGLKVlgSV 407
Cdd:PRK08974 259 LyhifaltVNcllfielGGQNLLITNPRDIPG---FVKELKKYPFTAITGVNTLFNALLNNEEFQEL--DFSSLKL--SV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 408 GEpinpeawlwyykyiGKEQCSIVDTFWQTETGGHVI--------TPLPGATPMK----PGSASFPFFGVKPTLLDECGI 475
Cdd:PRK08974 332 GG--------------GMAVQQAVAERWVKLTGQYLLegygltecSPLVSVNPYDldyySGSIGLPVPSTEIKLVDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 476 EIKGEGEGYLvfsqpW---PGMMRTLYNnheRFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAE 552
Cdd:PRK08974 398 EVPPGEPGEL-----WvkgPQVMLGYWQ---RPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 553 VESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQklisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIM 632
Cdd:PRK08974 470 IEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKIL 545
|
....*
gi 24667955 633 RRVLR 637
Cdd:PRK08974 546 RRELR 550
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
116-640 |
8.16e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 106.06 E-value: 8.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIta 194
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALV-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 195 dgawrgekplYL--------KALCDTALEKVEE--MGHSVEKC------IVVSHLKRVTPcqPDHVEEEIPWTddrdyww 258
Cdd:PRK12492 128 ----------YLnmfgklvqEVLPDTGIEYLIEakMGDLLPAAkgwlvnTVVDKVKKMVP--AYHLPQAVPFK------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 259 HEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLhTTAGYLLyaATTFKIvfdykpgdiYWCTGDVGwITGHT--- 335
Cdd:PRK12492 189 QALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAM-LTHGNLV--ANMLQV---------RACLSQLG-PDGQPlmk 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 ------------YVVYGPLAN-------GATSVIFEGTPFFPGndrYWSVIDKYKVTQFYTAPTAIRALMkfgEGPVLKH 396
Cdd:PRK12492 256 egqevmiaplplYHIYAFTANcmcmmvsGNHNVLITNPRDIPG---FIKELGKWRFSALLGLNTLFVALM---DHPGFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 397 -NLSGLKVLGSVGEPI---NPEAWlwyykyigkEQ---CSIVDTFWQTETGGhVITPLPGATPMKPGSASFPFFGVKPTL 469
Cdd:PRK12492 330 lDFSALKLTNSGGTALvkaTAERW---------EQltgCTIVEGYGLTETSP-VASTNPYGELARLGTVGIPVPGTALKV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 470 LDECGIEIKGEGEGYLVFSQPwpGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMS 549
Cdd:PRK12492 400 IDDDGNELPLGERGELCIKGP--QVMKGYWQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 550 TAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVfdqkLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSG 629
Cdd:PRK12492 476 PNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGL----SVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVG 551
|
570
....*....|.
gi 24667955 630 KIMRRVLRKIA 640
Cdd:PRK12492 552 KILRRELRDIA 562
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
278-633 |
8.68e-24 |
|
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: 102.48 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLYTSGSTGKPKGVLHTTAGYLlyaaTTFKIVFDykpgDIYWCTGDvgwitghTYVVYGPLA-----NGATSVIFE 352
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI----ESFVCNED----LFNISGED-------AILAPGPLShslflYGAISALYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 353 GTPF-----FPGNdRYWSVIDKYKVTQFYTAPTAIRALMKFGEgPVLKhnlsgLKVLGSVGEPINPEAWLWYYKYIGKEQ 427
Cdd:cd17633 66 GGTFigqrkFNPK-SWIRKINQYNATVIYLVPTMLQALARTLE-PESK-----IKSIFSSGQKLFESTKKKLKNIFPKAN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 csIVDTFWQTETGghVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKgegegylvfsqpwpgmmrTLYNNHERFED 507
Cdd:cd17633 139 --LIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIG------------------KIFVKSEMVFS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 508 TY----FSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCF 583
Cdd:cd17633 197 GYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVAL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24667955 584 ITPneNEVFDQklisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd17633 277 YSG--DKLTYK----QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
116-640 |
1.01e-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: 105.11 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDhGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAD 195
Cdd:cd05909 8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 ------GAWRGEKPLYLKALcdTALEKVEEMGHSVEKCIVVSHLKrvtpCQPdhveeeiPWTDDRDYwwheemedkepaC 269
Cdd:cd05909 87 qfieklKLHHLFDVEYDARI--VYLEDLRAKISKADKCKAFLAGK----FPP-------KWLLRIFG------------V 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 270 YPEwmDAEDPLFMLYTSGSTGKPKGVLHTTAGYL--LYAATTfkiVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGAT 347
Cdd:cd05909 142 APV--QPDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 348 SVifegtpFFPGNDRYWSV---IDKYKVTQFYTAPTAIRALMKFGEgpvlKHNLSGLKVLGSVGEPINPEAwlwYYKYIG 424
Cdd:cd05909 217 VV------FHPNPLDYKKIpelIYDKKATILLGTPTFLRGYARAAH----PEDFSSLRLVVAGAEKLKDTL---RQEFQE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 KEQCSIVDTFWQTETGGhVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwPGMMRTLYNNHER 504
Cdd:cd05909 284 KFGIRILEGYGTTECSP-VISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEPEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 505 fedTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEH-PRVAESAVVSRPHPVKGECLYCF 583
Cdd:cd05909 362 ---TSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 584 ITPNENEVfdqkliSDLKKMVRE-RIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIA 640
Cdd:cd05909 439 TTTTDTDP------SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
116-638 |
2.27e-23 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 103.20 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsIVFAGfspdslaermfdckakllitad 195
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE--AVLLN---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlKRVTPcqpdhveEEIPWtddrdywwheEMEDKEPACypewmd 275
Cdd:cd05912 58 --------------------------------------TRLTP-------NELAF----------QLKDSDVKL------ 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aEDPLFMLYTSGSTGKPKGVLHTtAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGpLANGATSVIFEgtP 355
Cdd:cd05912 77 -DDIATIMYTSGTTGKPKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVD--K 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 356 FFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKfgEGPVLKHNLSGLKVLGsvGEPInPEAWLwyykyigkEQCS-----I 430
Cdd:cd05912 152 FDA--EQVLHLINSGKVTIISVVPTMLQRLLE--ILGEGYPNNLRCILLG--GGPA-PKPLL--------EQCKekgipV 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 431 VDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLDEcGIEIKGEGEGYLvfsqPWPGMMRTLYNNHER----FE 506
Cdd:cd05912 217 YQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDD-GQPPYEVGEILL----KGPNVTKGYLNRPDAteesFE 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSkfpgyycTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITP 586
Cdd:cd05912 292 NGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24667955 587 NEnEVFDQKLISDLkkmvRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05912 365 ER-PISEEELIAYC----SEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
116-636 |
2.38e-23 |
|
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: 103.49 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcQPDHveeeipwtddrdywwheemedkepacypewmd 275
Cdd:cd17652 91 --------------------------------------------TPDN-------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aedPLFMLYTSGSTGKPKGVL--HTTAGYLLYAATTFkivFDYKPGDIYWCTGDVGWiTGHTYVVYGPLANGATSVIFEG 353
Cdd:cd17652 95 ---LAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSF-DASVWELLMALLAGATLVLAPA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 354 TPFFPGNDrYWSVIDKYKVTqFYTAPTAIRALMKFGEGPvlkhnlsGLKVLGSVGEPINPE-AWLW-----YYKYIGKEQ 427
Cdd:cd17652 168 EELLPGEP-LADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRWapgrrMINAYGPTE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 CSIVDTFWQTETGGHVIT---PLPGAT---------PMKPGSASfpffgvkptlldECGIEIKGEGEGYLvfsqPWPGMM 495
Cdd:cd17652 239 TTVCATMAGPLPGGGVPPigrPVPGTRvyvldarlrPVPPGVPG------------ELYIAGAGLARGYL----NRPGLT 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 496 RtlynnhERFEDTYFSKfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPH 573
Cdd:cd17652 303 A------ERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDD 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 574 PVKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd17652 376 RPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
251-637 |
8.18e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.80 E-value: 8.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 251 TDDRDYwwhEEMEDKEPACYP-EWMDAEDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIYWCT---- 325
Cdd:PRK13388 126 VDTPAY---AELVAAAGALTPhREVDAMDPFMLIFTSGTTGAPKAVR-CSHGRLAFAGRALTERFGLTRDDVCYVSmplf 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 326 -GD---VGWitghtyvvyGP-LANGATSVI---FEGTPFFPGndrywsvIDKYKVTQFYTAPTAIRALMKFGEGPVLKHN 397
Cdd:PRK13388 202 hSNavmAGW---------APaVASGAAVALpakFSASGFLDD-------VRRYGATYFNYVGKPLAYILATPERPDDADN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 398 lsGLKVlgSVGEPINPEAWLWYYKYIGkeqCSIVDTFWQTETGGhVITPLPGaTPmkPGSASFPFFGV---KPTLLDECG 474
Cdd:PRK13388 266 --PLRV--AFGNEASPRDIAEFSRRFG---CQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVaiyNPETLTECA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 475 IEIKGE-----------GEgyLVFSQPwPGMMRTLYNNH----ERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDD 539
Cdd:PRK13388 335 VARFDAhgallnadeaiGE--LVNTAG-AGFFEGYYNNPeataERMRH-------GMYWSGDLAYRDADGWIYFAGRTAD 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 540 MLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKKmVRERIGPFAMPDVIQN 619
Cdd:PRK13388 405 WMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLA-AQPDLGTKAWPRYVRI 483
|
410
....*....|....*...
gi 24667955 620 APGLPKTRSGKIMRRVLR 637
Cdd:PRK13388 484 AADLPSTATNKVLKRELI 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
116-637 |
1.63e-22 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 101.76 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAd 195
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekvEEMGHSVEKCIvvshlkRVTPcqpdHVEEEIPWTDDRDYWWHEEMEDKEPACYPEWMD 275
Cdd:PRK13382 148 ----------------------EEFSATVDRAL------ADCP----QATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLyTSGSTGKPKGVLHTTAGyllyAATTFKIVFDYKPgdiyWCTGDVGWITGHTYVVYG----PLANGATSVIF 351
Cdd:PRK13382 196 RKGRVILL-TSGTTGTPKGARRSGPG----GIGTLKAILDRTP----WRAEEPTVIVAPMFHAWGfsqlVLAASLACTIV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 EGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYIGKeqcSIV 431
Cdd:PRK13382 267 TRRRFDP--EATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 432 DTFWQTETGGHVItplpgATP----MKPGSASFPFFGVKPTLLDECGIEI-KGEGEGYLVFSQpwpgmmrTLYNNHERFE 506
Cdd:PRK13382 342 NNYNATEAGMIAT-----ATPadlrAAPDTAGRPAEGTEIRILDQDFREVpTGEVGTIFVRND-------TQFDGYTSGS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITP 586
Cdd:PRK13382 410 TKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24667955 587 NENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK13382 488 KPGA---SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
275-636 |
1.82e-22 |
|
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: 101.00 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 DAEDPLFMLYTSGSTGKPKGVLHTTAGYLlYAATTFK-----------------IVFDYKPGDIYWCtgdvgwitghtyv 337
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVA-HAAHAWRreyeldsfpvrllqmasFSFDVFAGDFARS------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 338 vygpLANGATSVIF-EGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAW 416
Cdd:cd17650 157 ----LLNGGTLVICpDEVKLDP--AALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 417 LwyYKYIGKE----------QCSIVDTFWQTETGghvitPLPGATPMKPGSasfPFFGVKPTLLD------------ECG 474
Cdd:cd17650 231 L--AARFGQGmriinsygvtEATIDSTYYEEGRD-----PLGDSANVPIGR---PLPNTAMYVLDerlqpqpvgvagELY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 475 IEIKGEGEGYLvfSQPwpgmmrtlYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVE 554
Cdd:cd17650 301 IGGAGVARGYL--NRP--------ELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 555 SVLTEHPRVAESAVVSRpHPVKGE---CLYCFI--TPNENEvfdqklisdLKKMVRERIGPFAMPDVIQNAPGLPKTRSG 629
Cdd:cd17650 371 SQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAaaTLNTAE---------LRAFLAKELPSYMIPSYYVQLDALPLTPNG 440
|
....*..
gi 24667955 630 KIMRRVL 636
Cdd:cd17650 441 KVDRRAL 447
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
114-637 |
1.14e-21 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 99.32 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADG-AWRGEKplylkALCDTALEK--VEEMG-------HSVEkcIVVSHLKRVTPCQ--PDHVEEEIPWTDDRdywwheE 261
Cdd:PRK07059 127 LENfATTVQQ-----VLAKTAVKHvvVASMGdllgfkgHIVN--FVVRRVKKMVPAWslPGHVRFNDALAEGA------R 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 262 MEDKEPACYPEwmdaeDPLFMLYTSGSTGKPKGVLHTTAGYL---LYAATTFKIVFDYKPGD---IYWCTGDVGWITGHT 335
Cdd:PRK07059 194 QTFKPVKLGPD-----DVAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEKKPRPdqlNFVCALPLYHIFALT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 YVVYGPLANGATSVIFEGTPFFPGndrYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLkhNLSGLKV-LG---SVGEPI 411
Cdd:PRK07059 269 VCGLLGMRTGGRNILIPNPRDIPG---FIKELKKYQVHIFPAVNTLYNALLNNPDFDKL--DFSKLIVaNGggmAVQRPV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 412 nPEAWlwyYKYIGkeqCSIVDTFWQTETGGhVITPLPGATPMKPGSASFPFFGVKPTLLDECGIEIK-GE-GE----GYL 485
Cdd:PRK07059 344 -AERW---LEMTG---CPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPlGEpGEicirGPQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 486 VFSQPWpgmmrtlynnhERFEDTYFSKFP-GYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVA 564
Cdd:PRK07059 416 VMAGYW-----------NRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVL 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 565 ESAVVSRPHPVKGECLYCFITPNENEVFDQklisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK07059 485 EVAAVGVPDEHSGEAVKLFVVKKDPALTEE----DVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-636 |
1.15e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.80 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAd 195
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvSHLKRVTPcqpdhVEEEIPWTD-DRDYWWHEEMEDKEPACYpewM 274
Cdd:PRK12316 616 -----------------------------------SHLGRKLP-----LAAGVQVLDlDRPAAWLEGYSEENPGTE---L 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 DAEDPLFMLYTSGSTGKPKGVLHT---TAGYLLYAATTFKIvfdyKPGDIYWCTGDVGWITGHTyVVYGPLANGATSVIF 351
Cdd:PRK12316 653 NPENLAYVIYTSGSTGKPKGAGNRhraLSNRLCWMQQAYGL----GVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 -EGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlkhNLSGLKVLGSVGEPINPEAWLWYYKYigKEQCSI 430
Cdd:PRK12316 728 aPGDHRDP--AKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAK--LPQAGL 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 431 VDTFWQTETGGHVITplpgATPMKPGSASF----PFFGVKPTLLDE----CGIEIKGE--------GEGYLvfsqPWPGM 494
Cdd:PRK12316 800 YNLYGPTEAAIDVTH----WTCVEEGGDSVpigrPIANLACYILDAnlepVPVGVLGElylagrglARGYH----GRPGL 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 495 mrtlynNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSrphp 574
Cdd:PRK12316 872 ------TAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---- 941
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667955 575 VKGECLYCFITPnENEVFDqkLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK12316 942 VDGKQLVGYVVL-ESEGGD--WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
114-637 |
1.46e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 99.07 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAK-LL 191
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKaLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITADGAWRGEKPLYLKALCDTALEKVEEMGHSVEKCI---VVSHLKRVTPcqPDHVEEEIPWTDDRDYWWHEEMEDKEPA 268
Cdd:PRK05677 128 CLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLinaVVKHVKKMVP--AYHLPQAVKFNDALAKGAGQPVTEANPQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 269 cypewmdAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFD---------YKPGDIYWctgdvgwITGHTYVVY 339
Cdd:PRK05677 206 -------ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSnlnegceilIAPLPLYH-------IYAFTFHCM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSVIFEGTPFFPGndrYWSVIDKYKVTQFYTAPTAIRALMKfGEGpVLKHNLSGLKVLGSVGEPINPEAWLWY 419
Cdd:PRK05677 272 AMMLIGNHNILISNPRDLPA---MVKELGKWKFSGFVGLNTLFVALCN-NEA-FRKLDFSALKLTLSGGMALQLATAERW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 420 YKYIGkeqCSIVDTFWQTETgghviTPLPGATPMK---PGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwpGMMR 496
Cdd:PRK05677 347 KEVTG---CAICEGYGMTET-----SPVVSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 497 TLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVK 576
Cdd:PRK05677 417 GYWQRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKS 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667955 577 GECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK05677 495 GEAIKVFVVVKPGETLTK---EQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-644 |
3.69e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.47 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT 3198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 AdgawrgekplylkalcdtalekveemGHSVEKCIVVSHLKRVTPcqpdhveeeipwtdDRDYWWHEEmedkePACYPEW 273
Cdd:PRK12467 3199 Q--------------------------AHLLEQLPAPAGDTALTL--------------DRLDLNGYS-----ENNPSTR 3233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPLFMLYTSGSTGKPKGV--------LHTTAGYLLYAATTFKIVFDYKPGDIywctgdvgwiTGHTYVVYGPLANG 345
Cdd:PRK12467 3234 VMGENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSF----------DGAQERFLWTLICG 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 346 ATSVIFEGTPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGEG---PVLKHNLSGlkvlgsvGEPINPEAWLWYYKY 422
Cdd:PRK12467 3304 GCLVVRDNDLWDP--EELWQAIHAHRISIACFPPAYLQQFAEDAGGadcASLDIYVFG-------GEAVPPAAFEQVKRK 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 423 IgkEQCSIVDTFWQTETgghVITPLPGATPM--KPGSASFPF----FGVKPTLLD------------ECGIEIKGEGEGY 484
Cdd:PRK12467 3375 L--KPRGLTNGYGPTEA---VVTVTLWKCGGdaVCEAPYAPIgrpvAGRSIYVLDgqlnpvpvgvagELYIGGVGLARGY 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 485 lvFSQPwpGMmrtlynNHERFEDTYFSKFPG-YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRV 563
Cdd:PRK12467 3450 --HQRP--SL------TAERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 564 AESAVVSRPhPVKGECLYCFITPN-ENEVFDQKLISDLKKMVRErigpFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVN 642
Cdd:PRK12467 3520 REAVVLARD-GAGGKQLVAYVVPAdPQGDWRETLRDHLAASLPD----YMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK 3594
|
..
gi 24667955 643 DR 644
Cdd:PRK12467 3595 GS 3596
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
108-640 |
3.70e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 97.51 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAER 182
Cdd:PRK06164 23 RPDavaliDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDCKAKLLITADGaWRG-EKPLYLKALCDTALEKVEEMghsvekcIVVShlkRVTPCQPDhveeeiPWTDDRDYWWHEE 261
Cdd:PRK06164 103 LGRGRARWLVVWPG-FKGiDFAAILAAVPPDALPPLRAI-------AVVD---DAADATPA------PAPGARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 262 MEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKiVFDYKPGDIYWCTGDVGWITGHTYVVyGP 341
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-GA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 LANGATSV---IFEGTpffpgndRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlkHNLSGLKVLGsvgepinpeawlw 418
Cdd:PRK06164 244 LAGGAPLVcepVFDAA-------RTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLFG------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 yykyIGKEQCSIVDTFWQTETGGHVITPLPGAtpmkpgSASFPFFGVKPTLLDEC------GIEIKGEGEGYLVFSQP-- 490
Cdd:PRK06164 301 ----FASFAPALGELAALARARGVPLTGLYGS------SEVQALVALQPATDPVSvrieggGRPASPEARVRARDPQDga 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 491 -------------WPGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVL 557
Cdd:PRK06164 371 llpdgesgeieirAPSLMRGYLDNPDATARALTDD--GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 558 TEHPRVAESAVVSRPHPVKGEClYCFITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSG---KIMRR 634
Cdd:PRK06164 449 EALPGVAAAQVVGATRDGKTVP-VAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKH 524
|
....*.
gi 24667955 635 VLRKIA 640
Cdd:PRK06164 525 RLREMA 530
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
107-645 |
3.74e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.61 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 107 NHPD-----DYSRG--LTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDS 178
Cdd:PLN02574 51 NHNGdtaliDSSTGfsISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 179 LAERMFDCKAkllitadgawrgekplylkALCDTALEKVEEMGHSVEKCIVVshlkrvtPCQPDHVEEEIPWTDdrdywW 258
Cdd:PLN02574 131 IKKRVVDCSV-------------------GLAFTSPENVEKLSPLGVPVIGV-------PENYDFDSKRIEFPK-----F 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 259 HEEMEDKEPACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKI---VFDYKPGD-IYWCTGDVGWITGH 334
Cdd:PLN02574 180 YELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeasQYEYPGSDnVYLAALPMFHIYGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 335 TYVVYGPLANGATSVIFEGtpfFPGNDRYwSVIDKYKVTQFYTAPTAIRALMKFGEGpVLKHNLSGLKVLGSVGEPINPE 414
Cdd:PLN02574 260 SLFVVGLLSLGSTIVVMRR---FDASDMV-KVIDRFKVTHFPVVPPILMALTKKAKG-VCGEVLKSLKQVSCGAAPLSGK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 415 AWLWYYKYIgkEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASFPFFGVKPTLLD-ECGIEIKGEGEGYLvfsqpW-- 491
Cdd:PLN02574 335 FIQDFVQTL--PHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGEL-----Wiq 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 492 -PGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVS 570
Cdd:PLN02574 408 gPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667955 571 RPHPVKGECLYCFITPNENEVFDQKLISDlkkMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDRN 645
Cdd:PLN02574 486 VPDKECGEIPVAFVVRRQGSTLSQEAVIN---YVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVS 557
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
116-636 |
5.33e-21 |
|
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: 96.57 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVfagfSPDSLAERMF----DCKAKLL 191
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV----DIDQPAARREailaDAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITADGAWRGEkplylkALCDTALekveemghsvekcivvshlkrVTPCQPDHVEEEIPWTDdrdywwheemedkepacyp 271
Cdd:cd12114 89 LTDGPDAQLD------VAVFDVL---------------------ILDLDALAAPAPPPPVD------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewMDAEDPLFMLYTSGSTGKPKGVLHTTAGYL--------LYAATTFKIV-------FDYKpgdiywctgdvgwitghTY 336
Cdd:cd12114 123 --VAPDDLAYVIFTSGSTGTPKGVMISHRAALntildinrRFAVGPDDRVlalsslsFDLS-----------------VY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 337 VVYGPLANGATSVIfegtpffPGNDR-----YW-SVIDKYKVTQFYTAPtairALMKfgegpVLkhnlsgLKVLGSVGEP 410
Cdd:cd12114 184 DIFGALSAGATLVL-------PDEARrrdpaHWaELIERHGVTLWNSVP----ALLE-----ML------LDVLEAAQAL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 411 I-NPEAWLWYYKYIGKEQcsiVDTFWQTETGGHVITpLPGAT------------PMKPGSASFPF--------FGVKPTL 469
Cdd:cd12114 242 LpSLRLVLLSGDWIPLDL---PARLRALAPDARLIS-LGGATeasiwsiyhpidEVPPDWRSIPYgrplanqrYRVLDPR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 470 LDEC-----G-IEIKGEG--EGYlvfsqpwpgmmrtlYNNHERFEDTYFSKFPG--YYCTGDGARRDADGYLWITGRVDD 539
Cdd:cd12114 318 GRDCpdwvpGeLWIGGRGvaLGY--------------LGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 540 MLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPvKGECLYCFITPnenevfDQKLISDLKKMVRERIG---PFAM-PD 615
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVP------DNDGTPIAPDALRAFLAqtlPAYMiPS 456
|
570 580
....*....|....*....|.
gi 24667955 616 VIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd12114 457 RVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
108-638 |
5.62e-21 |
|
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: 96.22 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAER 182
Cdd:cd17653 10 HPDavaveSLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDCKAKLLITADGAwrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheem 262
Cdd:cd17653 90 LRTSGATLLLTTDSP----------------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 edkepacypewmdaEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATT---------------FKIVFDYkpgdiywCTGd 327
Cdd:cd17653 105 --------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvLSIAFDA-------CIG- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 328 vgwitghtyVVYGPLANGATSVifegtpfFPGNDRYWSVIDKyKVTQFYTAPTaIRALMKFGEGPVLKHNLSGlkvlgsv 407
Cdd:cd17653 163 ---------EIFSTLCNGGTLV-------LADPSDPFAHVAR-TVDALMSTPS-ILSTLSPQDFPNLKTIFLG------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 408 GEPINP---EAWL----WYYKYiGKEQCSIVDTFWQTETGGHVI--TPLPGATPmkpgsasfpffgvkpTLLDECGIE-- 476
Cdd:cd17653 218 GEAVPPsllDRWSpgrrLYNAY-GPTECTISSTMTELLPGQPVTigKPIPNSTC---------------YILDADLQPvp 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 477 IKGEGEGYLVfsqpWPGMMRTLYNNHERFEDTY-FSKF-PG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAE 552
Cdd:cd17653 282 EGVVGEICIS----GVQVARGYLGNPALTASKFvPDPFwPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEE 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 553 VES-VLTEHPRVAESAVVsrphpVKGECLYCFITPnenEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKI 631
Cdd:cd17653 358 IEEvVLQSQPEVTQAAAI-----VVNGRLVAFVTP---ETVD---VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
....*..
gi 24667955 632 MRRVLRK 638
Cdd:cd17653 427 DRKALRE 433
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
114-638 |
7.70e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 96.59 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAERMFD----CKAK 189
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESEIKKqaeaAGAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 190 LLITADgawrgekplylkalcdTALEKVEEMGHSVekcIVVSHLKrvtpcqpdhVEEEIPWTD-----DR--DYWWHEEM 262
Cdd:PLN02330 130 LIVTND----------------TNYGKVKGLGLPV---IVLGEEK---------IEGAVNWKElleaaDRagDTSDNEEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 EDKEPACYPewmdaedplfmlYTSGSTGKPKGVLHTTAGYLLYAATTfkiVFDYKPGDIYWCT--GDVGW--ITGHTYVV 338
Cdd:PLN02330 182 LQTDLCALP------------FSSGTTGISKGVMLTHRNLVANLCSS---LFSVGPEMIGQVVtlGLIPFfhIYGITGIC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 339 YGPLANGATSVI---FEGTPFFpgndrywSVIDKYKVTQFYTAPTAIRALMKfgeGPVLKH-NLSGLKV--LGSVGEPIN 412
Cdd:PLN02330 247 CATLRNKGKVVVmsrFELRTFL-------NALITQEVSFAPIVPPIILNLVK---NPIVEEfDLSKLKLqaIMTAAAPLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 413 PEAWLWYYKYIGKEQcsIVDTFWQTETGGHVIT---PLPGATPMKPGSASFPFFGVKPTLLD-ECGIEIKGEGEGYL-VF 487
Cdd:PLN02330 317 PELLTAFEAKFPGVQ--VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELcVR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 488 SQpwpGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESA 567
Cdd:PLN02330 395 SQ---CVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667955 568 VVSRPHPVKGE----CLYCFITPNENEvfdqkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PLN02330 470 VVPLPDEEAGEipaaCVVINPKAKESE-------EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
277-636 |
8.35e-21 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 95.96 E-value: 8.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIywctGDVGWITGHTYV--VYGPLANGATSVIFEGT 354
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRV----LQFASIAFDVAAeeIYVTLLSGATLVLRPEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 355 PFFPGNDrYWSVIDKYKVTQFYTAPTAIRALMKFGEgPVLKHNLSGLKVLGSVGEPINPEAW-LW---------YYKYIG 424
Cdd:cd17644 182 MRSSLED-FVQYIQQWQLTVLSLPPAYWHLLVLELL-LSTIDLPSSLRLVIVGGEAVQPELVrQWqknvgnfiqLINVYG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 KEQCSIVDTFwqtetggHVITPLPGATPMKPGSASfPFFGVKPTLLDE----CGIEIKGE--------GEGYLvfsqPWP 492
Cdd:cd17644 260 PTEATIAATV-------CRLTQLTERNITSVPIGR-PIANTQVYILDEnlqpVPVGVPGElhiggvglARGYL----NRP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 493 GMMRTLYNNHErFEDTYFSKFpgyYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRP 572
Cdd:cd17644 328 ELTAEKFISHP-FNSSESERL---YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRE 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 573 HPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd17644 404 DQPGNKRLVAYIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
113-640 |
9.71e-21 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 96.45 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 113 SRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLI 192
Cdd:PLN02479 43 SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 TADGAWrgekplylkALCDTALEKVEEMGHSVEK--CIVVSHLKRVTPCQPDH------VE-EEIPWTDDRDYWWheeme 263
Cdd:PLN02479 123 VDQEFF---------TLAEEALKILAEKKKSSFKppLLIVIGDPTCDPKSLQYalgkgaIEyEKFLETGDPEFAW----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 264 dKEPAcyPEWmdaeDPLFMLYTSGSTGKPKGV-LHTTAGYLLyaATTFKIVFDYKPGDIYWCTGDVGWITGHTYVvYGPL 342
Cdd:PLN02479 189 -KPPA--DEW----QSIALGYTSGTTASPKGVvLHHRGAYLM--ALSNALIWGMNEGAVYLWTLPMFHCNGWCFT-WTLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 ANGATSVIFEGTPffpgNDRYWSVIDKYKVTQFYTAPTAIRAL------------------MKFGEGP----VLKHNLSG 400
Cdd:PLN02479 259 ALCGTNICLRQVT----AKAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhvMTAGAAPppsvLFAMSEKG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 401 LKVLGSVG--EPINPE---AWL--W---------------YYKYIGKEQCSIVDTfwqtetgghvitplpgaTPMKPGSA 458
Cdd:PLN02479 335 FRVTHTYGlsETYGPStvcAWKpeWdslppeeqarlnarqGVRYIGLEGLDVVDT-----------------KTMKPVPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 459 SFPFFGvkptlldecgiEIKGEGEGYLvfsqpwPGMMRTLYNNHERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVD 538
Cdd:PLN02479 398 DGKTMG-----------EIVMRGNMVM------KGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 539 DMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNE--NEVFDQKLISDLKKMVRERIGPFAMPDV 616
Cdd:PLN02479 454 DIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPgvDKSDEAALAEDIMKFCRERLPAYWVPKS 533
|
570 580
....*....|....*....|....
gi 24667955 617 IQNAPgLPKTRSGKIMRRVLRKIA 640
Cdd:PLN02479 534 VVFGP-LPKTATGKIQKHVLRAKA 556
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
117-638 |
1.61e-20 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 95.58 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITadg 196
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 197 awrgekplylkalcDTALEKVEEMGHSVekcivvshLKRVTpcqpdhveeEIPwTDDRDYWWHEE-MEDKEPACYP-EWM 274
Cdd:cd05915 103 --------------DPNLLPLVEAIRGE--------LKTVQ---------HFV-VMDEKAPEGYLaYEEALGEEADpVRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 DAEDPLFMLYTSGSTGKPKGVLHTTAG-YLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEg 353
Cdd:cd05915 151 PERAACGMAYTTGTTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 354 tpfFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKfGEGPVLKHNLSGLKVLGSVGEPinPEAWL-----WYYKYIGKEQC 428
Cdd:cd05915 230 ---RLDPASLVELFDGEGVTFTAGVPTVWLALAD-YLESTGHRLKTLRRLVVGGSAA--PRSLIarferMGVEVRQGYGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 429 SIV-----DTFWQTETgghviTPLPGATPMK-PGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPWPGMMRTLYNNH 502
Cdd:cd05915 304 TETspvvvQNFVKSHL-----ESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 503 ERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYC 582
Cdd:cd05915 379 EATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24667955 583 FITPNENEVFDQKLIsdlkKMVRERIGPFAM-PDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05915 457 VVVPRGEKPTPEELN----EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
116-668 |
2.11e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 95.47 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gaWRGEKPLylkalcdtalekVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEeiPWTDDRDYWWHEEMEDKEPACYPEWM- 274
Cdd:PLN03102 118 --DRSFEPL------------AREVLHLLSSEDSNLNLPVIFIHEIDFPKR--PSSEELDYECLIQRGEPTPSLVARMFr 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 --DAEDPLFMLYTSGSTGKPKGVLHTTAGYLLyaaTTFKIVFDYKPG--DIYWCTGDVGWITGHTYVvYGPLANGATSVI 350
Cdd:PLN03102 182 iqDEHDPISLNYTSGTTADPKGVVISHRGAYL---STLSAIIGWEMGtcPVYLWTLPMFHCNGWTFT-WGTAARGGTSVC 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FE--GTPFFPGNdrywsvIDKYKVTQFYTAPTAIRALMKfGEGPVLKHNLSGLKVLGSVGEPinPEAWLWYYKYIGKEqc 428
Cdd:PLN03102 258 MRhvTAPEIYKN------IEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQ-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 429 sIVDTFWQTETGGHVI--------TPLPGATPMKPGSASfpffGVKPTLLDECGIEIK---------GEGEGYLVF--SQ 489
Cdd:PLN03102 327 -VMHAYGLTEATGPVLfcewqdewNRLPENQQMELKARQ----GVSILGLADVDVKNKetqesvprdGKTMGEIVIkgSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 490 PWPGMMRTLYNNHERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVV 569
Cdd:PLN03102 402 IMKGYLKNPKATSEAFKH-------GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 570 SRPHPVKGE--CLYCFITPNENEVFDQ--KLIS---DLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAvn 642
Cdd:PLN03102 475 AMPHPTWGEtpCAFVVLEKGETTKEDRvdKLVTrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIA-- 552
|
570 580
....*....|....*....|....*.
gi 24667955 643 drnvgDTSTLADEQIVEQLFANRPVE 668
Cdd:PLN03102 553 -----KGLVVEDEDNVIKKVHQRPVE 573
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
96-637 |
2.22e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.95 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 96 LGDQIAYyWEGNHPDDYS-----RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYM---PMILELpiaMLACARIGAVH 167
Cdd:PRK06145 4 LSASIAF-HARRTPDRAAlvyrdQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMknsAAFLEL---AFAASYLGAVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 168 SIVFAGFSPDSLAERMFDCKAKLLitadgawrgekplylkaLCDTALEKVEEMGHSveKCIVVSHlkrvtpCQPDHVEEE 247
Cdd:PRK06145 80 LPINYRLAADEVAYILGDAGAKLL-----------------LVDEEFDAIVALETP--KIVIDAA------AQADSRRLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 248 IPwtddrdywwHEEmedkepaCYPEWMDAEDPLF-MLYTSGSTGKPKGVLHTTagyllyaattfkivfdykpGDIYWCTG 326
Cdd:PRK06145 135 QG---------GLE-------IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSY-------------------GNLHWKSI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 327 D----VGWITGHTYVVYGPLAN-GA-----TSVIFEG------TPFFPgnDRYWSVIDKYKVTQFYTAPTAIRALMKFGE 390
Cdd:PRK06145 180 DhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrihREFDP--EAVLAAIERHRLTCAWMAPVMLSRVLTVPD 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 391 GPvlKHNLSGLKVLGSVGEPiNPEAWLWYYKYIGKeQCSIVDTFWQTETGGhvitplpGATPMKPGSaSFPFFGVKPTLL 470
Cdd:PRK06145 258 RD--RFDLDSLAWCIGGGEK-TPESRIRDFTRVFT-RARYIDAYGLTETCS-------GDTLMEAGR-EIEKIGSTGRAL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 471 DECGIEIKGEGEGYLVFSQPW------PGMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVS 544
Cdd:PRK06145 326 AHVEIRIADGAGRWLPPNMKGeicmrgPKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISG 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 545 GHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLP 624
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDELP 479
|
570
....*....|...
gi 24667955 625 KTRSGKIMRRVLR 637
Cdd:PRK06145 480 RNPSGKVLKRVLR 492
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
117-640 |
3.80e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 94.63 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITaDg 196
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV-D- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 197 awrgekplylKALCDTALEKVEEMGHSveKCIVVShlkrvtpcqpdhveeeipwTDDRDYWWHEEMEDKEpacYPEWMDA 276
Cdd:PRK08162 123 ----------TEFAEVAREALALLPGP--KPLVID-------------------VDDPEYPGGRFIGALD---YEAFLAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFML-------------YTSGSTGKPKGVL-HTTAGYLLYAATTfkIVFDYKPGDIY-W------CTGdvgWitGHT 335
Cdd:PRK08162 169 GDPDFAWtlpadewdaialnYTSGTTGNPKGVVyHHRGAYLNALSNI--LAWGMPKHPVYlWtlpmfhCNG---W--CFP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 YVVygpLANGATSV---------IFEgtpffpgndrywsVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGlKVLGS 406
Cdd:PRK08162 242 WTV---AARAGTNVclrkvdpklIFD-------------LIREHGVTHYCGAPIVLSALINAPAEW--RAGIDH-PVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 407 VGEPINPEAWLWYYKYIGKEqcsIVDTFWQTETGGHVIT----------PLPGATPMKP--GSASFPFFGVkpTLLD-EC 473
Cdd:PRK08162 303 VAGAAPPAAVIAKMEEIGFD---LTHVYGLTETYGPATVcawqpewdalPLDERAQLKArqGVRYPLQEGV--TVLDpDT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 474 GIEIKGEGE--GYLVFSqpwpG--MMRTLYNN----HERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSG 545
Cdd:PRK08162 378 MQPVPADGEtiGEIMFR----GniVMKGYLKNpkatEEAFAG-------GWFHTGDLAVLHPDGYIKIKDRSKDIIISGG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 546 HLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNEN-EVFDQKLISdlkkMVRERIGPFAMPDVIQNAPgLP 624
Cdd:PRK08162 447 ENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGaSATEEEIIA----HCREHLAGFKVPKAVVFGE-LP 521
|
570
....*....|....*.
gi 24667955 625 KTRSGKIMRRVLRKIA 640
Cdd:PRK08162 522 KTSTGKIQKFVLREQA 537
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
117-639 |
5.79e-20 |
|
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: 93.75 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAdg 196
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 197 awrgekplylKALCDTALeKVEEMGHSVEKCIVVSHLKRVTPCQPDH--VEEEIPWTDDrDYWWHEEMEDKEpacypewm 274
Cdd:cd17642 124 ----------KKGLQKVL-NVQKKLKIIKTIIILDSKEDYKGYQCLYtfITQNLPPGFN-EYDFKPPSFDRD-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 daEDPLFMLYTSGSTGKPKGVLHT--------------TAGYLLYAATTFKIVFDYKPGdiYWCTGDVGWITGHTYVVYG 340
Cdd:cd17642 184 --EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFHHG--FGMFTTLGYLICGFRVVLM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 341 PLangatsviFEGTPFFpgndrywSVIDKYKVTQFYTAPTairaLMKF-GEGPVL-KHNLSGLKVLGSVGEPINPEAWLW 418
Cdd:cd17642 260 YK--------FEEELFL-------RSLQDYKVQSALLVPT----LFAFfAKSTLVdKYDLSNLHEIASGGAPLSKEVGEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 419 YYKYIGKEqcSIVDTFWQTETGGHV-ITPlpgATPMKPGSAS--FPFFGVKPTLLDE---CGIEIKGEgegyLVFSQPwp 492
Cdd:cd17642 321 VAKRFKLP--GIRQGYGLTETTSAIlITP---EGDDKPGAVGkvVPFFYAKVVDLDTgktLGPNERGE----LCVKGP-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 493 GMMRTLYNNHERfEDTYFSKfPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRP 572
Cdd:cd17642 390 MIMKGYVNNPEA-TKALIDK-DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIP 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 573 HPVKGECLYCFI------TPNENEVFDQkLISDLKKMVRERIGPFAMPDViqnapglPKTRSGKIMRRVLRKI 639
Cdd:cd17642 468 DEDAGELPAAVVvleagkTMTEKEVMDY-VASQVSTAKRLRGGVKFVDEV-------PKGLTGKIDRRKIREI 532
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
269-638 |
1.14e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 92.89 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 269 CYPEWMDAEDPLF------------MLYTSGSTGKPKGVLHTTAGYLLYA-ATTFKIVFDYKPGDIY-----------WC 324
Cdd:PRK06018 157 AYEEWIAEADGDFawktfdentaagMCYTSGTTGDPKGVLYSHRSNVLHAlMANNGDALGTSAADTMlpvvplfhansWG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 325 TGDVGWITGHTYVVYGPLANGATsvIFEgtpffpgndrywsVIDKYKVTQFYTAPTAIRALMKFGEGPVLKhnLSGLKVL 404
Cdd:PRK06018 237 IAFSAPSMGTKLVMPGAKLDGAS--VYE-------------LLDTEKVTFTAGVPTVWLMLLQYMEKEGLK--LPHLKMV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 405 GSVGEPInPEAWLWYYKYIGKEqcsIVDTFWQTETG--GHVITpLPGATPMKPGSA--------SFPFFGVKPTLLDECG 474
Cdd:PRK06018 300 VCGGSAM-PRSMIKAFEDMGVE---VRHAWGMTEMSplGTLAA-LKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDAG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 475 IEIKGEGE--GYLVFSQPwpGMMRTLYnnheRFEDTYFSKfPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAE 552
Cdd:PRK06018 375 KELPWDGKtfGRLKVRGP--AVAAAYY----RVDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSID 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 553 VESVLTEHPRVAESAVVSRPHPVKGE--CLYCFITPNENEVFDQKLisdlkKMVRERIGPFAMPDVIQNAPGLPKTRSGK 630
Cdd:PRK06018 448 LENLAVGHPKVAEAAVIGVYHPKWDErpLLIVQLKPGETATREEIL-----KYMDGKIAKWWMPDDVAFVDAIPHTATGK 522
|
....*...
gi 24667955 631 IMRRVLRK 638
Cdd:PRK06018 523 ILKTALRE 530
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
111-636 |
1.27e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 92.76 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 111 DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKL 190
Cdd:PRK05857 37 DGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 191 LITADGawrgekplylkalCDTALEKVEEMGHSVEKCIV-VSHLKRVTPCQPDhveeeipwtddRDYwwheemedkePAC 269
Cdd:PRK05857 117 ALVAPG-------------SKMASSAVPEALHSIPVIAVdIAAVTRESEHSLD-----------AAS----------LAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 270 YPEwMDAEDPLFMLYTSGSTGKPKGVlhttagyLLYAATTFKIVFDYKPGDIYWctgdVGWITGHTyvVYGPLAngATSV 349
Cdd:PRK05857 163 NAD-QGSEDPLAMIFTSGTTGEPKAV-------LLANRTFFAVPDILQKEGLNW----VTWVVGET--TYSPLP--ATHI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 350 ---------IFEGTPFFPGNDRYWS---VIDKYKVTQFYTAPTAIRAL---MKFGEGPVlkhnlSGLKVLGSVGEpinpE 414
Cdd:PRK05857 227 gglwwiltcLMHGGLCVTGGENTTSlleILTTNAVATTCLVPTLLSKLvseLKSANATV-----PSLRLVGYGGS----R 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 415 AWLWYYKYIGKEQCSIVDTFWQTETGGHVITpLP----GATPMKPGSASFPFFGVKPTLLDECGIEIKGEGEG-YLVFSQ 489
Cdd:PRK05857 298 AIAADVRFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGpSASFGT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 490 PW---PGMMRTLYNNHERFEDTYFSkfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAES 566
Cdd:PRK05857 377 LWiksPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 567 AVVSRPHPVKGECLYCFITPNENevFDQKLISDLKKMV----RERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK05857 454 ACYEIPDEEFGALVGLAVVASAE--LDESAARALKHTIaarfRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
98-663 |
2.33e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGNHpddysrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPD 177
Cdd:PRK12316 3072 DAVALAFGEQR-------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEE 3144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 178 SLAERMFDCKAKLLITAdgawrgekplylkalcdtalekveemghsvekcivvSHLKRVtpcQPDHVEEEIPWTDDRDYW 257
Cdd:PRK12316 3145 RLAYMLEDSGAQLLLSQ------------------------------------SHLRLP---LAQGVQVLDLDRGDENYA 3185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 WHEEmedkepacyPEWMDAEDPLFMLYTSGSTGKPKGVL--------HTTAGYLLYAATTFKIVFDYKPGDIywctgdvg 329
Cdd:PRK12316 3186 EANP---------AIRTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVLQFTTFSF-------- 3248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 330 wiTGHTYVVYGPLANGATsVIFEGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKfgegPVLKHNLSGLKVLGSVGE 409
Cdd:PRK12316 3249 --DVFVEELFWPLMSGAR-VVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE----EEDAHRCTSLKRIVCGGE 3321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 410 PINPE------AWLWYYKYIGKEQCSIVDTFWQtetgghVITPLPGATPMKPgsasfPFFGVKPTLLDECG--IEIKGEG 481
Cdd:PRK12316 3322 ALPADlqqqvfAGLPLYNLYGPTEATITVTHWQ------CVEEGKDAVPIGR-----PIANRACYILDGSLepVPVGALG 3390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 482 EGYLVFSQPWPGMMRTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHP 561
Cdd:PRK12316 3391 ELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHP 3470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 562 RVAESAVVSrphpVKGECLYCFITPNENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIav 641
Cdd:PRK12316 3471 WVREAVVLA----VDGRQLVAYVVPEDEA---GDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP-- 3541
|
570 580
....*....|....*....|..
gi 24667955 642 nDRNVGDTSTLADEQIVEQLFA 663
Cdd:PRK12316 3542 -DAALLQQDYVAPVNELERRLA 3562
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
114-637 |
2.48e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 91.86 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:PRK07514 27 LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADGAWRGEKPLYLKAlcdtALEKVEEMGhsvekcivvshlkrvtpcqpdhveeeipwtDDRDYWWHEEMEDKEPACYPEW 273
Cdd:PRK07514 107 DPANFAWLSKIAAAA----GAPHVETLD------------------------------ADGTGSLLEAAAAAPDDFETVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 MDAEDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGD-------IYwctgdvgwitgHTYVVY----GPL 342
Cdd:PRK07514 153 RGADDLAAILYTSGTTGRSKGAM-LSHGNLLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvatnVAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 ANGAtSVIFegtpfFPGNDRYwSVIDKYK-------VTQFYTaptaiRALmkfgEGPVLKHNLSG---LKVLGSVgePIN 412
Cdd:PRK07514 221 LAGA-SMIF-----LPKFDPD-AVLALMPratvmmgVPTFYT-----RLL----QEPRLTREAAAhmrLFISGSA--PLL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 413 PEAWLWYYKYIGKeqcSIVDTFWQTETGGHVITPLPGATpmKPGSASFPFFGV----------KPTLLDECG-IEIKGEG 481
Cdd:PRK07514 283 AETHREFQERTGH---AILERYGMTETNMNTSNPYDGER--RAGTVGFPLPGVslrvtdpetgAELPPGEIGmIEVKGPN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 482 egylVFSQPW--PGMMRtlynnhERF-EDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLT 558
Cdd:PRK07514 358 ----VFKGYWrmPEKTA------EEFrAD-------GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEID 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 559 EHPRVAESAVVSRPHPVKGECLYCFITPNENEVFD-QKLISDLKkmvrERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK07514 421 ELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDeAAILAALK----GRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-644 |
4.04e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.71 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT-- 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgEKPLYLKALCDTALEKVEEmghsvekcivvshlkrvtpcqpdhveeeipwtdDRDYWWhEEMEDKEPACYpewMD 275
Cdd:PRK12316 2107 -----QRHLLERLPLPAGVARLPL---------------------------------DRDAEW-ADYPDTAPAVQ---LA 2144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGV----------LHTTAGYllYAATTFKIVFDYKPgdiYWCTGDV-GWITghtyvvygPLAN 344
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVavshgalvahCQAAGER--YELSPADCELQFMS---FSFDGAHeQWFH--------PLLN 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 345 GATSVIFEGTPFFPGndRYWSVIDKYKVTQFYTAPTAIRALMKFGEgpvLKHNLSGLKVLGSVGEPINPEAWLWYYKYIG 424
Cdd:PRK12316 2212 GARVLIRDDELWDPE--QLYDEMERHGVTILDFPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALR 2286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 KEqcSIVDTFWQTETgghVITPLP-GATPMKPGSASFPFFGV-----KPTLLDE---------CG-IEIKGEG--EGYLv 486
Cdd:PRK12316 2287 PV--YLFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRalgnrRAYILDAdlnllapgmAGeLYLGGEGlaRGYL- 2360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 487 fsqPWPGMmrtlynNHERFEDTYFSKFPG-YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAE 565
Cdd:PRK12316 2361 ---NRPGL------TAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 566 SAVVSRPHPvKGECLYCFITPNENEvfdQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDR 644
Cdd:PRK12316 2432 AVVVAQDGA-SGKQLVAYVVPDDAA---EDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
111-640 |
4.04e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.48 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 111 DYSRGLTYRKLLEEVCRFAN-VLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAK 189
Cdd:PRK08751 46 SFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGAS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 190 LLITADGAWRGEKplylKALCDTALEKV--EEMGHSVEKC------IVVSHLKRVTPcqpdhvEEEIPwtddRDYWWHEE 261
Cdd:PRK08751 126 VLVVIDNFGTTVQ----QVIADTPVKQVitTGLGDMLGFPkaalvnFVVKYVKKLVP------EYRIN----GAIRFREA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 262 MEDKEPACYPEW-MDAEDPLFMLYTSGSTGKPKGVLHTTAGYLL-------YAATTFKIvfdyKPGDiywctgDVGWITG 333
Cdd:PRK08751 192 LALGRKHSMPTLqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAnmqqahqWLAGTGKL----EEGC------EVVITAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 334 HTYVVYGPLANGATSVIFEGTPFFPGNDRYW-SVIDKYKVTQFyTAPTAIRALM-KFGEGPVL-KHNLSGLKVLGSVGEP 410
Cdd:PRK08751 262 PLYHIFALTANGLVFMKIGGCNHLISNPRDMpGFVKELKKTRF-TAFTGVNTLFnGLLNTPGFdQIDFSSLKMTLGGGMA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 411 INPEAWLWYYKYIGkeqCSIVDTFWQTETG-GHVITPLpgATPMKPGSASFPFFGVKPTLLDECGiEIKGEGE-GYLVFS 488
Cdd:PRK08751 341 VQRSVAERWKQVTG---LTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAG-TVLAIGEiGELCIK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 489 QPwpGMMRTLYNNHErfEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAV 568
Cdd:PRK08751 415 GP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 569 VSRPHPVKGECLYCFITPNenevfDQKLIS-DLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIA 640
Cdd:PRK08751 491 VGVPDEKSGEIVKVVIVKK-----DPALTAeDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
113-636 |
4.75e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.53 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 113 SRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLI 192
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 TAdgawrgekplylKALCD--TALEKVEemghsvekCIVVShlkrvtpcQPDHveeeipwtddrdywWHEEMEDKEPACY 270
Cdd:PRK12467 1677 TQ------------SHLQArlPLPDGLR--------SLVLD--------QEDD--------------WLEGYSDSNPAVN 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 271 PewmDAEDPLFMLYTSGSTGKPKGVL--HTTAGYLLYAAttfKIVFDYKPGDIywctgdvgWITGHTYV-------VYGP 341
Cdd:PRK12467 1715 L---APQNLAYVIYTSGSTGRPKGAGnrHGALVNRLCAT---QEAYQLSAADV--------VLQFTSFAfdvsvweLFWP 1780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 LANGATSVIFE-GTPFFPGndRYWSVIDKYKVTQFYTAPTAIRALMKFGegPVLKHNLSgLKVLGSVGEPINPEAWLWYY 420
Cdd:PRK12467 1781 LINGARLVIAPpGAHRDPE--QLIQLIERQQVTTLHFVPSMLQQLLQMD--EQVEHPLS-LRRVVCGGEALEVEALRPWL 1855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 421 KYIGKEQcsIVDTFWQTETGGHViTPLPGATPMKPGSASFPFfGV-----KPTLLDEC--GIEIKGEGEGYLVFSqpwpG 493
Cdd:PRK12467 1856 ERLPDTG--LFNLYGPTETAVDV-THWTCRRKDLEGRDSVPI-GQpianlSTYILDASlnPVPIGVAGELYLGGV----G 1927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 494 MMRTLYN----NHERFEDTYFSKFPG-YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAV 568
Cdd:PRK12467 1928 LARGYLNrpalTAERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV 2007
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 569 VSRPHPvKGECLYCFITPNENEVFD-----QKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK12467 2008 IAQDGA-NGKQLVAYVVPTDPGLVDddeaqVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
76-578 |
8.44e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 90.34 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 76 MEGASTNLCYNLLDrnVRNGLGDQIAYY----WEGNHPDDYSRgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMIL 151
Cdd:PRK09274 1 MMASMANIARHLPR--AAQERPDQLAVAvpggRGADGKLAYDE-LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 152 ELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITADGA-------WRGEKplylkalcdtalekveemghSV 224
Cdd:PRK09274 78 EFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAhlarrlfGWGKP--------------------SV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 225 EKCIVVshlkrvtpcqpdhveeeipwtdDRDYWW-----HEEMEDKEPACYP-EWMDAEDPLFMLYTSGSTGKPKGVLHt 298
Cdd:PRK09274 138 RRLVTV----------------------GGRLLWggttlATLLRDGAAAPFPmADLAPDDMAAILFTSGSTGTPKGVVY- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 299 TAGYLLYAATTFKIVFDYKPGDIYWCTGDVgwitghtYVVYGPlANGATSVIFEGTPFFPGN---DRYWSVIDKYKVTQF 375
Cdd:PRK09274 195 THGMFEAQIEALREDYGIEPGEIDLPTFPL-------FALFGP-ALGMTSVIPDMDPTRPATvdpAKLFAAIERYGVTNL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 376 YTAPTAIRALMKFGEGpvLKHNLSGLKVLGSVGEPINPEAWlwyykyigkEQCSIVdtfwqTETGGHVITPLpGATPMKP 455
Cdd:PRK09274 267 FGSPALLERLGRYGEA--NGIKLPSLRRVISAGAPVPIAVI---------ERFRAM-----LPPDAEILTPY-GATEALP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 456 ----GSAsfpffgvkpTLLDECGiEIKGEGEGYLVfSQPWPGM------------------------------------M 495
Cdd:PRK09274 330 issiESR---------EILFATR-AATDNGAGICV-GRPVDGVevriiaisdapipewddalrlatgeigeivvagpmvT 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 496 RTLYNNHerfEDTYFSKFPG-----YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVS 570
Cdd:PRK09274 399 RSYYNRP---EATRLAKIPDgqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG 475
|
....*...
gi 24667955 571 rpHPVKGE 578
Cdd:PRK09274 476 --VGVPGA 481
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
127-638 |
1.00e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 90.04 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 127 RFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITadgawrgeKPLYL 206
Cdd:PLN02246 62 RVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT--------QSCYV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 207 kalcdtalEKVEEMGHSVEKCIVvshlkrvtpCQPDHVEEEIPWTddrdywwhEEMEDKEPACYPEWMDAEDPLFMLYTS 286
Cdd:PLN02246 134 --------DKLKGLAEDDGVTVV---------TIDDPPEGCLHFS--------ELTQADENELPEVEISPDDVVALPYSS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 287 GSTGKPKGVLHTTAGYLlyaaTTFKIVFDYKPGDIYWCTGDVgwITG-----HTY----VVYGPLANGATSVI---FEGT 354
Cdd:PLN02246 189 GTTGLPKGVMLTHKGLV----TSVAQQVDGENPNLYFHSDDV--ILCvlpmfHIYslnsVLLCGLRVGAAILImpkFEIG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 355 PFFpgndrywSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLKVLGSVGEPInpeawlwyykyiGKEqcsIVDTF 434
Cdd:PLN02246 263 ALL-------ELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPL------------GKE---LEDAF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 435 wqtetgghvITPLPGAT--------------PMKPGSASFPFfGVKPtllDECGI-----EIK------GEGEGYlvfSQ 489
Cdd:PLN02246 319 ---------RAKLPNAVlgqgygmteagpvlAMCLAFAKEPF-PVKS---GSCGTvvrnaELKivdpetGASLPR---NQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 490 PW------PGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRV 563
Cdd:PLN02246 383 PGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 564 AESAVVSRPHPVKGECLYCFI------TPNENEVfdQKLISdlKKMV-RERIGPFAMPDVIqnapglPKTRSGKIMRRVL 636
Cdd:PLN02246 461 ADAAVVPMKDEVAGEVPVAFVvrsngsEITEDEI--KQFVA--KQVVfYKRIHKVFFVDSI------PKAPSGKILRKDL 530
|
..
gi 24667955 637 RK 638
Cdd:PLN02246 531 RA 532
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
97-638 |
1.99e-18 |
|
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: 89.22 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 97 GDQIAY-YWEgnHPDDYSRGLTYRKLLEEVCRFANVLKDHGiRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFS 175
Cdd:cd05931 7 PDRPAYtFLD--DEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 176 PDSlAERMF----DCKAKLLITADGAwrgekplylkalcdtaLEKVEEMGHSVEkcivvshlkrvTPCQPDHVEEEIPWT 251
Cdd:cd05931 84 GRH-AERLAailaDAGPRVVLTTAAA----------------LAAVRAFAASRP-----------AAGTPRLLVVDLLPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 252 DDRDYWwheemedkePACYPewmDAEDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIY--W--CTGD 327
Cdd:cd05931 136 TSAADW---------PPPSP---DPDDIAYLQYTSGSTGTPKGVV-VTHRNLLANVRQIRRAYGLDPGDVVvsWlpLYHD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 328 VGWITGhtyvVYGPLANGATSVIFegTPF-FPGNDRYW-SVIDKYKVTqFYTAPT-----AIRALMKFGEGPVlkhNLSG 400
Cdd:cd05931 203 MGLIGG----LLTPLYSGGPSVLM--SPAaFLRRPLRWlRLISRYRAT-ISAAPNfaydlCVRRVRDEDLEGL---DLSS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 401 LKVLGSVGEPINPEAwlwyykyigkeqcsiVDTFWQT------------------ETGGHVITPLPGATP----MKPGSA 458
Cdd:cd05931 273 WRVALNGAEPVRPAT---------------LRRFAEAfapfgfrpeafrpsyglaEATLFVSGGPPGTGPvvlrVDRDAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 459 SFPFFGVKP------------TLLDECGIEI-----------KGEGEgylvfsqPW---PGMMRTLYNNHERFEDTYFSK 512
Cdd:cd05931 338 AGRAVAVAAddpaarelvscgRPLPDQEVRIvdpetgrelpdGEVGE-------IWvrgPSVASGYWGRPEATAETFGAL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 513 FP----GYYCTGD-GARrdADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHP---RVAESAVVSRPHP-VKGECLYCF 583
Cdd:cd05931 411 AAtdegGWLRTGDlGFL--HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHpalRPGCVAAFSVPDDgEERLVVVAE 488
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 584 ITPNENEVFDQKLISDLKKMVRERIGpFAMPDVIQNAPG-LPKTRSGKIMRRVLRK 638
Cdd:cd05931 489 VERGADPADLAAIAAAIRAAVAREHG-VAPADVVLVRPGsIPRTSSGKIQRRACRA 543
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
270-637 |
2.99e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 88.12 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 270 YPEwMDAEDPLFMLYTSGSTGKPKGVL---HTTAGYLLYAATTFKivfdykpgdiyWCTGDV-----------GWITGht 335
Cdd:PRK07787 122 YPE-PDPDAPALIVYTSGTTGPPKGVVlsrRAIAADLDALAEAWQ-----------WTADDVlvhglplfhvhGLVLG-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 336 yvVYGPLANGAtSVIFEGTPffpgndrywsvidkykVTQFYTAPTAIRALMKFG---------EGPVLKHNLSG--LKVL 404
Cdd:PRK07787 188 --VLGPLRIGN-RFVHTGRP----------------TPEAYAQALSEGGTLYFGvptvwsriaADPEAARALRGarLLVS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 405 GS------VGEPINPEAwlwyykyiGKEqcsIVDTFWQTETgghVITPLPGAT-PMKPGSASFPFFGVKPTLLDECGIEI 477
Cdd:PRK07787 249 GSaalpvpVFDRLAALT--------GHR---PVERYGMTET---LITLSTRADgERRPGWVGLPLAGVETRLVDEDGGPV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 478 KGEGE--GYLVFSQPwpgMMRTLYNNheRFEDTYFSKFP-GYYCTGDGARRDADGYLWITGRVD-DMLNVSGHLMSTAEV 553
Cdd:PRK07787 315 PHDGEtvGELQVRGP---TLFDGYLN--RPDATAAAFTAdGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 554 ESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNEnEVFDQKLISdlkkMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:PRK07787 390 ETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD-DVAADELID----FVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
....
gi 24667955 634 RVLR 637
Cdd:PRK07787 465 KQLL 468
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
116-638 |
3.27e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.84 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAd 195
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvSHLKRVTPCqPDHVEEeIPWTDDRDYWWHEEMEDKEPACYPEWMd 275
Cdd:PRK12467 617 -----------------------------------SHLLAQLPV-PAGLRS-LCLDEPADLLCGYSGHNPEVALDPDNL- 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aedpLFMLYTSGSTGKPKGVL--HTT-AGYLLYAATTFKIVFDYKPGDIYWCTGDVGwitgHTyVVYGPLANGATSVIFE 352
Cdd:PRK12467 659 ----AYVIYTSGSTGQPKGVAisHGAlANYVCVIAERLQLAADDSMLMVSTFAFDLG----VT-ELFGALASGATLHLLP 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 353 GTPFFPGNDRYwSVIDKYKVTQFYTAPTAIRALMKFG--EGPVLKHNLsglkVLGsvGEPINPEAW-LWYYKyigKEQCS 429
Cdd:PRK12467 730 PDCARDAEAFA-ALMADQGVTVLKIVPSHLQALLQASrvALPRPQRAL----VCG--GEALQVDLLaRVRAL---GPGAR 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 430 IVDTFWQTETGGHVIT-PLPGATpmKPGSASF---PFFGVKPTLLDEC----------GIEIKGEG--EGYLvfsqPWPG 493
Cdd:PRK12467 800 LINHYGPTETTVGVSTyELSDEE--RDFGNVPigqPLANLGLYILDHYlnpvpvgvvgELYIGGAGlaRGYH----RRPA 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 494 MmrtlynNHERFEDTYFSKfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSR 571
Cdd:PRK12467 874 L------TAERFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ 946
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 572 PHPVKGECL-YCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK12467 947 PGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
103-633 |
9.35e-18 |
|
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: 86.34 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 103 YWEGNHpddysrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAER 182
Cdd:cd05914 2 YYGGEP-------LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDCKAKLLITADgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheem 262
Cdd:cd05914 75 LNHSEAKAIFVSD------------------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 edkepacypewmdAEDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPL 342
Cdd:cd05914 88 -------------EDDVALINYTSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 ANGATSVI--------------FEGTPFFpGNDRYWSVIDKYKVTqfyTAPTAIRALMKFG-EGPVL---KHNLSGLKVL 404
Cdd:cd05914 154 LNGAHVVFldkipsakiialafAQVTPTL-GVPVPLVIEKIFKMD---IIPKLTLKKFKFKlAKKINnrkIRKLAFKKVH 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 405 GSVG----------EPINPEAWLWYYKyIGkeqCSIVDTFWQTETGghvitPLPGATP---MKPGSASFPFFGVKPTLLD 471
Cdd:cd05914 230 EAFGgnikefviggAKINPDVEEFLRT-IG---FPYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRIDS 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 472 ECGIEIKGEgegYLVFSqpwPGMMRTLYNNHERFEDTyFSKfPGYYCTGDGARRDADGYLWITGRVDDM-LNVSGHLMST 550
Cdd:cd05914 301 PDPATGEGE---IIVRG---PNVMKGYYKNPEATAEA-FDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYP 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 551 AEVESVLTEHPRVAESAVVSRPhpvKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPF--AMPD-------VIQNAP 621
Cdd:cd05914 373 EEIEAKINNMPFVLESLVVVQE---KKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVnqKVPNykkiskvKIVKEE 449
|
570
....*....|..
gi 24667955 622 gLPKTRSGKIMR 633
Cdd:cd05914 450 -FEKTPKGKIKR 460
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
277-637 |
1.13e-17 |
|
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: 85.02 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFMLYTSGSTGKPKGVLHT-----TAGYLLYAATTF----KIVFdykPGDIYWCTGdvgwitghtyVVYGPLA---N 344
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLteqdRLCI---PVPLFHCFG----------SVLGVLAcltH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 345 GATsVIFEGTPFFPGNdrYWSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLK--VLGsvGEPINPEAWLWYYKY 422
Cdd:cd05917 69 GAT-MVFPSPSFDPLA--VLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRtgIMA--GAPCPPELMKRVIEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 423 IGKEQCSIVdtFWQTETGGHVITPLPGATPMKP----GSAsFPFFGVK---PTLLDECGIEIKGE--GEGYLVfsqpwpg 493
Cdd:cd05917 142 MNMKDVTIA--YGMTETSPVSTQTRTDDSIEKRvntvGRI-MPHTEAKivdPEGGIVPPVGVPGElcIRGYSV------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 494 mMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPH 573
Cdd:cd05917 212 -MKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPD 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24667955 574 PVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:cd05917 289 ERYGEEVCAWIRLKEGAELT---EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
515-642 |
1.17e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 86.58 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 515 GYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNEnevfDQ 594
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE----PL 484
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24667955 595 KLIsDLKKMVRER-IGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVN 642
Cdd:PRK10946 485 KAV-QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
282-633 |
1.23e-17 |
|
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: 84.47 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 282 MLYTSGSTGKPKGVLHTTAGYLLYAATtfkivfdykpgdiyWCtgDVGWIT-GHTYVVYGP--------------LANGA 346
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAA--------------WA--DCADLTeDDRYLIINPffhtfgykagivacLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 347 TSV---IFEGtpffpgnDRYWSVIDKYKVTQFYTAPTAIRALMkfGEGPVLKHNLSGLKVLGSVGEPINPEAWLWYYKYI 423
Cdd:cd17638 69 TVVpvaVFDV-------DAILEAIERERITVLPGPPTLFQSLL--DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 424 GKEqcSIVDTFWQTETGGhvitplpgATPMKPGSasfPFFGVKPTLLDEC-GIEIKGEGEGYLVFSQPwpGMMRTLYNNH 502
Cdd:cd17638 140 GFE--TVLTAYGLTEAGV--------ATMCRPGD---DAETVATTCGRACpGFEVRIADDGEVLVRGY--NVMQGYLDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 503 ERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYC 582
Cdd:cd17638 205 EATAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKA 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24667955 583 FITPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd17638 283 FVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
85-648 |
1.29e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.85 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 85 YNLLDRNVRNGLGDQIAYyWEGNHPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLA 159
Cdd:PRK08279 28 TALITPDSKRSLGDVFEE-AAARHPDrpallFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 160 CARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITAdgawrgekplylkalcdtalekvEEMGHSVEKciVVSHLKRVTPC 239
Cdd:PRK08279 107 LAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVG-----------------------EELVEAFEE--ARADLARPPRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 240 QPDHVEEEIPWTDDRDYwwhEEMEDKEPACYPEW---MDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAAtTFKIVFDY 316
Cdd:PRK08279 162 WVAGGDTLDDPEGYEDL---AAAAAGAPTTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 317 KPGDIYWCT--------GDVGWITGhtyvvygpLANGATSVI---FEGTPFfpgndryWSVIDKYKVTQFYtaptAI--- 382
Cdd:PRK08279 238 TPDDVLYCClplyhntgGTVAWSSV--------LAAGATLALrrkFSASRF-------WDDVRRYRATAFQ----YIgel 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 383 -RALMKFGEGPVLKHNlsglKVLGSVGEPINPEAWlwyykyigkEQcsivdtfWQTETGGHVITPLPGATPM-------- 453
Cdd:PRK08279 299 cRYLLNQPPKPTDRDH----RLRLMIGNGLRPDIW---------DE-------FQQRFGIPRILEFYAASEGnvgfinvf 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 454 -KPGSASF-PFFGVKPTLLDECGIE----IKGEgEGYLVFSQPW-PGMMRTLYNNHERFE-------------------- 506
Cdd:PRK08279 359 nFDGTVGRvPLWLAHPYAIVKYDVDtgepVRDA-DGRCIKVKPGeVGLLIGRITDRGPFDgytdpeasekkilrdvfkkg 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSkfpgyycTGDGARRDADGYLWITGRVDDML-----NVsghlmSTAEVESVLTEHPRVAESAV--VSRPHpVKGEC 579
Cdd:PRK08279 438 DAWFN-------TGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGFPGVEEAVVygVEVPG-TDGRA 504
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 580 LYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDRNVGD 648
Cdd:PRK08279 505 GMAAIVLADGAEFD---LAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDD 570
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
278-633 |
2.41e-17 |
|
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: 83.86 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGhTYVVYGPLANGATSVIFEgtPFF 357
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVME--KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 358 PgnDRYWSVIDKYKVTQFYT-APTAIRALMKFGEGPVlkhNLSGLKVLGSVGEPINPEAWLwyykyigkEQCSivDTFW- 435
Cdd:cd17637 77 P--AEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRFE--------ETTG--ATFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 436 ---QTETGGhVITPLPGATpmKPGSASFPFFGVKPTLLDECGIEIK-GE-GE----GYLVFSQPWpgmmrtlynNHErfE 506
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPaGEtGEivvrGPLVFQGYW---------NLP--E 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 507 DTYFSKFPGYYCTGDGARRDADGYLWITGRV--DDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFI 584
Cdd:cd17637 208 LTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24667955 585 TPNENEVFDQKlisDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMR 633
Cdd:cd17637 288 VLKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
203-604 |
6.59e-17 |
|
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: 84.06 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 203 PLYLKALCDTALEKVEemgHSVEKCIVVSHL------KRVTPCQPDHVEEEIPWTDDRDYWWHEEMEDKEPACYPEWMDA 276
Cdd:cd05932 60 PLYPTLNPDTIRYVLE---HSESKALFVGKLddwkamAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFMLYTSGSTGKPKGVLHTTAGYlLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVIFEGTPF 356
Cdd:cd05932 137 EQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 357 FPGNdrywsvIDKYKVTQFYTAPtaiRALMKFGEG-----PVLKHN----------------LSGL-----KVLGSVGEP 410
Cdd:cd05932 216 FVED------VQRARPTLFFSVP---RLWTKFQQGvqdkiPQQKLNlllkipvvnslvkrkvLKGLgldqcRLAGCGSAP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 411 INPEAWLWYYKyIGKEqcsIVDTFWQTETGGHVITPLPGATpmKPGSASFPFFGVKptlldecgIEIKGEGEgYLVFSqp 490
Cdd:cd05932 287 VPPALLEWYRS-LGLN---ILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVE--------VRISEDGE-ILVRS-- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 491 wPGMMRTLYNNHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVS-GHLMSTAEVESVLTEHPRVAESAVV 569
Cdd:cd05932 350 -PALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVI 426
|
410 420 430
....*....|....*....|....*....|....*..
gi 24667955 570 SR--PHPVKGECLYCFITPNENEVFDQKLISDLKKMV 604
Cdd:cd05932 427 GSglPAPLALVVLSEEARLRADAFARAELEASLRAHL 463
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
114-643 |
1.05e-16 |
|
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: 83.24 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAErmfdCkakllIT 193
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLH----C-----IT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 ADGAwrgekplylkalcdtalekveemghsveKCIVVSHLKRVTpcqpDHVEEEIPWTDDRDYwwheemedkepacypew 273
Cdd:cd05939 73 VSKA----------------------------KALIFNLLDPLL----TQSSTEPPSQDDVNF----------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 mdaEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKiVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVI--- 350
Cdd:cd05939 104 ---RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIrkk 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FEGTpffpgndRYWSVIDKYKVT--QF------YTAPTAIRALMKfgegpvlKHNLSGLkvlgsVGEPINPEAWLWYYKY 422
Cdd:cd05939 180 FSAS-------NFWDDCVKYNCTivQYigeicrYLLAQPPSEEEQ-------KHNVRLA-----VGNGLRPQIWEQFVRR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 423 IGKEQ-----------CSIVDTfwqtetGGHVitplpGATPMKP--GSASFPFFGVKptlLDECGIEIKGEGEGYLVFSQ 489
Cdd:cd05939 241 FGIPQigefygategnSSLVNI------DNHV-----GACGFNSriLPSVYPIRLIK---VDEDTGELIRDSDGLCIPCQ 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 490 PW-PGMM--RTLYNNHERFEDTY--------------FSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAE 552
Cdd:cd05939 307 PGePGLLvgKIIQNDPLRRFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 553 VESVLTEHPRVAESAV--VSRPHpVKGECLYCFITPNENEVFDQKLISDLKKmvreRIGPFAMPDVIQNAPGLPKTRSGK 630
Cdd:cd05939 387 VEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFK 461
|
570
....*....|...
gi 24667955 631 IMRRVLRKIAVND 643
Cdd:cd05939 462 LQKTDLQKEGYDP 474
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-639 |
1.42e-16 |
|
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: 83.10 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 87 LLDRNVRNGlGDQIAYYWEGNHPDDYsrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACarigav 166
Cdd:cd05906 15 LLLRAAERG-PTKGITYIDADGSEEF---QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 167 hsiVFAGFSPDSLAERMFDckakllitadgawrgekplylkALCDTALEKVEEMGHSVEKCIVVSHLKRVTPCQPdhVEE 246
Cdd:cd05906 85 ---VLAGFVPAPLTVPPTY----------------------DEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAG--LET 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 247 EIPWTDDRDywwHEEMEDKEPACYPEW--MDAEDPLFMLYTSGSTGKPKGVLHTTAGYLlyAATTFKIV-FDYKPGDIY- 322
Cdd:cd05906 138 LSGLPGIRV---LSIEELLDTAADHDLpqSRPDDLALLMLTSGSTGFPKAVPLTHRNIL--ARSAGKIQhNGLTPQDVFl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 323 -WCTGD-VGWITG-HTYVVYgpLA----NGATSVIFegtpffpGNDRYW-SVIDKYKVTqfYT-AP----TAIRALMKFG 389
Cdd:cd05906 213 nWVPLDhVGGLVElHLRAVY--LGcqqvHVPTEEIL-------ADPLRWlDLIDRYRVT--ITwAPnfafALLNDLLEEI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 390 EGPvlKHNLSGLKVLGSVGEPINP---EAWLWYYKYIGKEQCSIVDTFWQTETGGHVITPLPGATPMKPGSASF-----P 461
Cdd:cd05906 282 EDG--TWDLSSLRYLVNAGEAVVAktiRRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvslgrP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 462 FFGVKPTLLDECGiEIKGEGE-------GYLVFSQpwpgmmrtLYNNHERFEDTYFSKfpGYYCTGDGARRDaDGYLWIT 534
Cdd:cd05906 360 IPGVSMRIVDDEG-QLLPEGEvgrlqvrGPVVTKG--------YYNNPEANAEAFTED--GWFRTGDLGFLD-NGNLTIT 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 535 GRVDDMLNVSGHLMSTAEVESVLTEHPRVAES---AVVSRPHPVKGECLYCFITPNENEvFDQ--KLISDLKKMVRERIG 609
Cdd:cd05906 428 GRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftaAFAVRDPGAETEELAIFFVPEYDL-QDAlsETLRAIRSVVSREVG 506
|
570 580 590
....*....|....*....|....*....|.
gi 24667955 610 pFAMPDVIQNAPG-LPKTRSGKIMRRVLRKI 639
Cdd:cd05906 507 -VSPAYLIPLPKEeIPKTSLGKIQRSKLKAA 536
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
26-86 |
2.51e-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: 73.28 E-value: 2.51e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667955 26 YQKFYQESLDNPAEFWSRVAKQFHWETPADQdkflkyNFNISKGPiSIKWMEGASTNLCYN 86
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDK------VLDGSNGP-FAKWFVGGKLNVCYN 54
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
117-638 |
4.17e-16 |
|
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: 81.32 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 117 TYRKLLEEVCRFANVLKD-HGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLItad 195
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypewMD 275
Cdd:cd05937 84 ------------------------------------------------------------------------------VD 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTTaGYLLYAATTFKIVFDYKPGD-IYWC----------TGDVGWITGHTYVVYGP--- 341
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISW-RRTLVTSNLLSHDLNLKNGDrTYTCmplyhgtaafLGACNCLMSGGTLALSRkfs 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 342 --------LANGATSVIFEG--------TPFFPgNDRYWSVI------------DKYK-------VTQFYTAPTAIRALM 386
Cdd:cd05937 165 asqfwkdvRDSGATIIQYVGelcryllsTPPSP-YDRDHKVRvawgnglrpdiwERFRerfnvpeIGEFYAATEGVFALT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 387 KFGEGPVlkhnlsglkVLGSVGEpinpEAWLWYYKYIGKEQCSIVDTfwqtETGGHVITPLPGatpmkpgsasfpfFGVk 466
Cdd:cd05937 244 NHNVGDF---------GAGAIGH----HGLIRRWKFENQVVLVKMDP----ETDDPIRDPKTG-------------FCV- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 467 ptlldECGIEIKGEGEGYLVFS--QPWPGMmrtlYNNHE----RFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDM 540
Cdd:cd05937 293 -----RAPVGEPGEMLGRVPFKnrEAFQGY----LHNEDatesKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 541 LNVSGHLMSTAEVESVLTEHPRVAESAV--VSRP-HPVKGECLYCFITPNeNEVFDQKLISDLKKMVRERIGPFAMPDVI 617
Cdd:cd05937 364 FRWKSENVSTTEVADVLGAHPDIAEANVygVKVPgHDGRAGCAAITLEES-SAVPTEFTKSLLASLARKNLPSYAVPLFL 442
|
570 580
....*....|....*....|.
gi 24667955 618 QNAPGLPKTRSGKIMRRVLRK 638
Cdd:cd05937 443 RLTEEVATTDNHKQQKGVLRD 463
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
110-663 |
8.33e-16 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 81.63 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 110 DDYSrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAK 189
Cdd:PRK10252 480 ARYQ--FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPS 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 190 LLITADGawrgEKPLYlkalcdtalekveemghsvekcivvSHLKRVTPCQPDhveeeIPWTDDrdywwheemeDKEPAC 269
Cdd:PRK10252 558 LLITTAD----QLPRF-------------------------ADVPDLTSLCYN-----APLAPQ----------GAAPLQ 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 270 YPEwmdAEDPLFMLYTSGSTGKPKGVL--HTT-AGYLL-----YAATTFKIVFDYKPgdiywCTGDVG-WitghtyVVYG 340
Cdd:PRK10252 594 LSQ---PHHTAYIIFTSGSTGRPKGVMvgQTAiVNRLLwmqnhYPLTADDVVLQKTP-----CSFDVSvW------EFFW 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 341 PLANGATSVIFEgtpffPGNDR----YWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAW 416
Cdd:PRK10252 660 PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLC 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 417 LWYYKYIGKEQCSI-------VD-TFWqtetgghvitPLPGATPMKPGSASFPF-FGVKPT---LLDECGieikgegegy 484
Cdd:PRK10252 735 REWQQLTGAPLHNLygpteaaVDvSWY----------PAFGEELAAVRGSSVPIgYPVWNTglrILDARM---------- 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 485 lvfsQPWP-GMMRTLYN---------------NHERFEDTYFSkfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGH 546
Cdd:PRK10252 795 ----RPVPpGVAGDLYLtgiqlaqgylgrpdlTASRFIADPFA--PGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQ 868
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 547 LMSTAEVESVLTEHPRVAESAVVSR------PHPVKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNA 620
Cdd:PRK10252 869 RIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLD---TSALQAQLRERLPPHMVPVVLLQL 945
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 24667955 621 PGLPKTRSGKIMRRVLRKIAVNDRNVGDTSTLADEQIVEQLFA 663
Cdd:PRK10252 946 DQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFS 988
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
116-636 |
8.42e-16 |
|
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: 80.60 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAER----MFDCKAKLL 191
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGA----FVPIDPEYPEERriyiMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 192 ITadgawrgekplylKALCDTALekveemghSVEKCIVvshlkrvtpcqpdHVEEEIpwtddrdywwhEEMEDKEPACYP 271
Cdd:cd17656 90 LT-------------QRHLKSKL--------SFNKSTI-------------LLEDPS-----------ISQEDTSNIDYI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewMDAEDPLFMLYTSGSTGKPKGV-------------------LHTTAGYLLYAATTFKIVFDykpgDIY--WCTGdvgw 330
Cdd:cd17656 125 --NNSDDLLYIIYTSGTTGKPKGVqlehknmvnllhferektnINFSDKVLQFATCSFDVCYQ----EIFstLLSG---- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 331 itGHTYVVygplaNGATSVIFEGTPFFPGNDRywsvidkykvTQFYTAPTAIRALMkFGEGPVLKHNLSGLKVLGSVGEP 410
Cdd:cd17656 195 --GTLYII-----REETKRDVEQLFDLVKRHN----------IEVVFLPVAFLKFI-FSEREFINRFPTCVKHIITAGEQ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 411 I---NPeawlwYYKYIGKEQCSIVDTFWQTETggHVIT--------PLPGATPM-KPGSasfpffGVKPTLLDE------ 472
Cdd:cd17656 257 LvitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPIS------NTWIYILDQeqqlqp 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 473 CGIEikgeGEGYLVFSqpwpGMMRTLYNN----HERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLM 548
Cdd:cd17656 324 QGIV----GELYISGA----SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 549 STAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPnenevfDQKL-ISDLKKMVRERIGPFAMPDVIQNAPGLPKTR 627
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM------EQELnISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469
|
....*....
gi 24667955 628 SGKIMRRVL 636
Cdd:cd17656 470 NGKVDRKAL 478
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
104-640 |
1.70e-15 |
|
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: 79.51 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 104 WEGNhpddysrgLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAERM 183
Cdd:cd05918 21 WDGS--------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA----FVPLDPSHPLQRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 184 fdckaKLLITADGAwrgekplylkalcdtalekveemghsveKCIVVShlkrvtpcqpdhveeeipwtddrdywwheeme 263
Cdd:cd05918 89 -----QEILQDTGA----------------------------KVVLTS-------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 264 dkepacypewmDAEDPLFMLYTSGSTGKPKGVL------------HTTAG-------YLLYAATTFkivfdykpgdiywc 324
Cdd:cd05918 104 -----------SPSDAAYVIFTSGSTGKPKGVViehralstsalaHGRALgltsesrVLQFASYTF-------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 325 tgDVgwitgHTYVVYGPLANGATSVIfegtpffPGNDRYWS----VIDKYKVTQFYTAPTAIRALmkfgeGPvlkHNLSG 400
Cdd:cd05918 159 --DV-----SILEIFTTLAAGGCLCI-------PSEEDRLNdlagFINRLRVTWAFLTPSVARLL-----DP---EDVPS 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 401 LKVLGSVGEPINPeawlwyykyigkeqcSIVDTFWQ----------TETGGHVITPLPGATpMKPGSASFPFfGVKPTLL 470
Cdd:cd05918 217 LRTLVLGGEALTQ---------------SDVDTWADrvrlinaygpAECTIAATVSPVVPS-TDPRNIGRPL-GATCWVV 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 471 DECGIE----IKGEGE----------GYL--------VFSQPWPGMMRTLYNNHERFedtyfskfpgyYCTGDGARRDAD 528
Cdd:cd05918 280 DPDNHDrlvpIGAVGElliegpilarGYLndpektaaAFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPD 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 529 GYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGEC---LYCFITPNENEVFD------------ 593
Cdd:cd05918 349 GSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVLDGSSSGSgdgdslflepsd 428
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 24667955 594 --QKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIA 640
Cdd:cd05918 429 efRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
116-637 |
1.91e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 79.67 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLItAD 195
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV-AS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 GAWRGekplyLKALCDTALEKVEEMGHSVEKcivvshlkrvtpcqpdhveeeipwtddrdywwHEEMEDKEPACYPEWmd 275
Cdd:PRK13390 104 AALDG-----LAAKVGADLPLRLSFGGEIDG--------------------------------FGSFEAALAGAGPRL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPL--FMLYTSGSTGKPKGVLHTTAGYLLYA-----ATTFKIVFDYKPGDIYWCTGDVGwitgHTyvvyGPL------ 342
Cdd:PRK13390 145 TEQPCgaVMLYSSGTTGFPKGIQPDLPGRDVDApgdpiVAIARAFYDISESDIYYSSAPIY----HA----APLrwcsmv 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 343 -ANGATSVIFEGtpfFPGND--RYwsvIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNLSGLKVLGSVGEPINPEAWLWY 419
Cdd:PRK13390 217 hALGGTVVLAKR---FDAQAtlGH---VERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 420 YKYIGKeqcSIVDTFWQTETGGHVITPLPGATPmKPGSASFPFFGvKPTLLDECGIEIKGEGEGYLVFSQPwpGMMRTLY 499
Cdd:PRK13390 291 IDWLGP---IVYEYYSSTEAHGMTFIDSPDWLA-HPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERD--RLPFRYL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 500 NNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGEC 579
Cdd:PRK13390 364 NDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQ 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 580 LYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLR 637
Cdd:PRK13390 444 VKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
277-630 |
3.51e-15 |
|
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: 77.81 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 277 EDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDyKPGDIYWCTGDVGWITGHTYVVYGPLANGA------TSVI 350
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTgswtafGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FEGTPFFPGnDRY-----WSVIDKYKVTQF------YTAPTaIRALMKFGEgpvlkHNLSGLKVLGSVGEPINPEAwlwy 419
Cdd:cd05924 82 GGQTVVLPD-DRFdpeevWRTIEKHKVTSMtivgdaMARPL-IDALRDAGP-----YDLSSLFAISSGGALLSPEV---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 420 ykyigKEQ-------CSIVDTFWQTETGGhviTPLPGATPMKPGSASFPFFGVKPTLLDECG--IEIKGEGEGYLVFSQP 490
Cdd:cd05924 151 -----KQGllelvpnITLVDAFGSSETGF---TGSGHSAGSGPETGPFTRANPDTVVLDDDGrvVPPGSGGVGWIARRGH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 491 WP-GMmrtlYNNHERFEDTYFSKfPG--YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESA 567
Cdd:cd05924 223 IPlGY----YGDEAKTAETFPEV-DGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667955 568 VVSRPHPVKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGK 630
Cdd:cd05924 298 VVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
108-641 |
7.90e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 77.93 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGL--TYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSL- 179
Cdd:PRK08315 29 YPDrealvYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 180 -AERMFDCKAklLITADGaWRGEKplYLKALCDTALE-KVEEMGHSveKCIVVSHLKRVTpcqpdHVEEE-----IPWTD 252
Cdd:PRK08315 109 yALNQSGCKA--LIAADG-FKDSD--YVAMLYELAPElATCEPGQL--QSARLPELRRVI-----FLGDEkhpgmLNFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 253 drdywWHEEMEDKEPACYPEWM---DAEDPLFMLYTSGSTGKPKGVLHT-----TAGYLLYAATTFKivfdykPGD---- 320
Cdd:PRK08315 177 -----LLALGRAVDDAELAARQatlDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLT------EEDrlci 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 321 ---IYWCTGdvgwitghtyVVYGPLA---NGATSVIF-EGtpFFPGndRYWSVIDKYKVTQFYTAPT---AIRALMKFGE 390
Cdd:PRK08315 246 pvpLYHCFG----------MVLGNLAcvtHGATMVYPgEG--FDPL--ATLAAVEEERCTALYGVPTmfiAELDHPDFAR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 391 gpvlkHNLSGLK------------VLGSVGEPIN-PEAWLWYykyiGKEQCSIVDTfwQT----------ETGGHVitpl 447
Cdd:PRK08315 312 -----FDLSSLRtgimagspcpieVMKRVIDKMHmSEVTIAY----GMTETSPVST--QTrtddplekrvTTVGRA---- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 448 pgatpmkpgsasFPFFGVK---PTLLDECGIEIKGE--GEGYLVfsqpwpgmMRTLYNNHERFEDTYFSKfpGYYCTGDG 522
Cdd:PRK08315 377 ------------LPHLEVKivdPETGETVPRGEQGElcTRGYSV--------MKGYWNDPEKTAEAIDAD--GWMHTGDL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 523 ARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQkliSDLKK 602
Cdd:PRK08315 435 AVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---EDVRD 511
|
570 580 590
....*....|....*....|....*....|....*....
gi 24667955 603 MVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAV 641
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
278-629 |
1.76e-14 |
|
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: 75.03 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 278 DPLFMLYTSGSTGKPKGVLHTTAGyLLYAAttfkivfdykpgdiyWCTGDVGWITGHT-YVVYGPLAN------GATSVI 350
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA-LLAQA---------------LVLAVLQAIDEGTvFLNSGPLFHigtlmfTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FEGTP-FFPGND--RYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlKHNLSGLKVLgsvgepinPEAWLWyykyigkEQ 427
Cdd:cd17636 65 AGGTNvFVRRVDaeEVLELIEAERCTHAFLLPPTIDQIVELNADG--LYDLSSLRSS--------PAAPEW-------ND 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 CSIVDT---------FWQTETGGHVITPLPGATPMkpGSASFPFFGVKPTLLDECGIEI-KGE-GE----GYLVFSQPW- 491
Cdd:cd17636 128 MATVDTspwgrkpggYGQTEVMGLATFAALGGGAI--GGAGRPSPLVQVRILDEDGREVpDGEvGEivarGPTVMAGYWn 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 492 -PGMmrtlynNHERFEDtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVS 570
Cdd:cd17636 206 rPEV------NARRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIG 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 571 RPHPVKGECLYCFITPNENEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSG 629
Cdd:cd17636 273 VPDPRWAQSVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
275-636 |
1.45e-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: 73.20 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 DAEDPLFMLYTSGSTGKPKGVL--HTTagyLLYAATTFKIVFDYKpgdiywCTGDVGWITGHTYVvYGP--------LAN 344
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLveHGS---VVNLRTSLSERYFGR------DNGDEAVLFFSNYV-FDFfveqmtlaLLN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 345 GATSVIFEGTpFFPGNDRYWSVIDKYKVTQFYTAPTAIRaLMKFGegpvlkhNLSGLKVLGSVGEPINPEAwlwYYKYIG 424
Cdd:cd17648 162 GQKLVVPPDE-MRFDPDRFYAYINREKVTYLSGTPSVLQ-QYDLA-------RLPHLKRVDAAGEEFTAPV---FEKLRS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 425 KEQCSIVDTFWQTETG-GHVITPLPGATPmKPGSASFPFFGVKPTLLD------------ECGIEIKGEGEGYLvfSQPW 491
Cdd:cd17648 230 RFAGLIINAYGPTETTvTNHKRFFPGDQR-FDKSLGRPVRNTKCYVLNdamkrvpvgavgELYLGGDGVARGYL--NRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 492 PGMMRTLYNNHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSR 571
Cdd:cd17648 307 LTAERFLPNPFQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 572 PHPVKGEC-----LYCFITPNEnEVFDQkliSDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd17648 387 EDASQAQSriqkyLVGYYLPEP-GHVPE---SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
263-574 |
2.60e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 72.82 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 EDKEPA------CYPEWMDAED-----PLF-------MLYTSGSTGKPKGVLHTTAGYLLYA-ATTFKIVFDYKPGDIY- 322
Cdd:PRK07008 144 AAHLPAgstpllCYETLVGAQDgdydwPRFdenqassLCYTSGTTGNPKGALYSHRSTVLHAyGAALPDAMGLSARDAVl 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 323 ----------WCTGDVGWITGHTYVVYGPLANGATsvIFEgtpffpgndrywsVIDKYKVTqfYTA--PTAIRALMKFGE 390
Cdd:PRK07008 224 pvvpmfhvnaWGLPYSAPLTGAKLVLPGPDLDGKS--LYE-------------LIEAERVT--FSAgvPTVWLGLLNHMR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 391 GPVLKhnLSGLKvlgsvgepinpeawlwyYKYIGKEQC--SIVDTFwQTETGGHVITPLpGATPMKP-GSASF------- 460
Cdd:PRK07008 287 EAGLR--FSTLR-----------------RTVIGGSACppAMIRTF-EDEYGVEVIHAW-GMTEMSPlGTLCKlkwkhsq 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 461 ---------------PFFGVKPTLLDECGIEIKGEGEGY--LVFSQPWpgmmrtlynnherFEDTYFSK-----FPGYYC 518
Cdd:PRK07008 346 lpldeqrkllekqgrVIYGVDMKIVGDDGRELPWDGKAFgdLQVRGPW-------------VIDRYFRGdasplVDGWFP 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24667955 519 TGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHP 574
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
519-636 |
2.66e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 69.29 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 519 TGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGE--CL-YC---FITPNEnevf 592
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKAkVIsheEIDPVQ---- 370
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24667955 593 dqklisdLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK08308 371 -------LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
114-642 |
2.86e-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: 69.30 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLIT 193
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 adgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemedkepacypew 273
Cdd:cd05940 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 274 mdaeDPLFMLYTSGSTGKPKGVLhTTAGYLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGATSVI--- 350
Cdd:cd05940 82 ----DAALYIYTSGTTGLPKAAI-ISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkk 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 351 FEGTPFfpgndryWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKHNlsglKVLGSVGEPINPEAWLWYYKYIGKEQcsi 430
Cdd:cd05940 157 FSASNF-------WDDIRKYQATIFQYIGELCRYLLNQPPKPTERKH----KVRMIFGNGLRPDIWEEFKERFGVPR--- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 431 VDTFWQTETGGHVITPLPGatpmKPGSAsfpffGVKPTLL--------------------DECGIEIK-GEGE-GYLVFS 488
Cdd:cd05940 223 IAEFYAATEGNSGFINFFG----KPGAI-----GRNPSLLrkvaplalvkydlesgepirDAEGRCIKvPRGEpGLLISR 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 489 ----QPWPGMMRTLYNNHERFEDTyFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVA 564
Cdd:cd05940 294 inplEPFDGYTDPAATEKKILRDV-FKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVE 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 565 ESAVVSRPHP-VKGECLYCFITPNENEVFDqklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVN 642
Cdd:cd05940 373 EANVYGVQVPgTDGRAGMAAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
114-638 |
1.12e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 67.90 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYM---PMILELpiaMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKL 190
Cdd:PLN02860 31 RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAAlnsDLYLEW---LLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 191 LITADG--AWRGE------KPLYLKALCDTAlekveemghSVEKCIVVSHLKRvtpcqPDHVEEEIPWTDDRDYWWHeem 262
Cdd:PLN02860 108 LVTDETcsSWYEElqndrlPSLMWQVFLESP---------SSSVFIFLNSFLT-----TEMLKQRALGTTELDYAWA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 edkepacypewmdAEDPLFMLYTSGSTGKPKGVL--HTTagylLYAATTFKIVF-DYKPGDIYWCTGDVGWITGHTYVVy 339
Cdd:PLN02860 171 -------------PDDAVLICFTSGTTGRPKGVTisHSA----LIVQSLAKIAIvGYGEDDVYLHTAPLCHIGGLSSAL- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSVI---FEGTPFFpgndrywSVIDKYKVTQFYTAPTAIRALMKFG-------EGPVLKHNLSGLkvlGSVGE 409
Cdd:PLN02860 233 AMLMVGACHVLlpkFDAKAAL-------QAIKQHNVTSMITVPAMMADLISLTrksmtwkVFPSVRKILNGG---GSLSS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 410 PINPEAWLWYYK------YIGKEQCSIVdTFWQTETGGHVITPLPGATPMKPGSASFPFF-GV---KPTLLDECGIEIKG 479
Cdd:PLN02860 303 RLLPDAKKLFPNaklfsaYGMTEACSSL-TFMTLHDPTLESPKQTLQTVNQTKSSSVHQPqGVcvgKPAPHVELKIGLDE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 480 EGEGYLVFSQPWPGMMRTLYNNHERFEDtyfSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTE 559
Cdd:PLN02860 382 SSRVGRILTRGPHVMLGYWGQNSETASV---LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 560 HPRVAESAVVSRPHPVKGECLYCFI--------TPNENEVFDQKLI---SDLKKMVRER-IGPFAMPD-VIQNAPGLPKT 626
Cdd:PLN02860 459 HPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwSDNEKENAKKNLTlssETLRHHCREKnLSRFKIPKlFVQWRKPFPLT 538
|
570
....*....|..
gi 24667955 627 RSGKIMRRVLRK 638
Cdd:PLN02860 539 TTGKIRRDEVRR 550
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
108-636 |
1.21e-11 |
|
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: 67.19 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 108 HPD-----DYSRGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAER 182
Cdd:cd17645 11 TPDhvavvDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 183 MFDCKAKLLITadgawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheem 262
Cdd:cd17645 91 LADSSAKILLT--------------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 edkepacypewmDAEDPLFMLYTSGSTGKPKGVL--HTTagyLLYAATTFKIVFDYKPGDIYWCTGDVGWiTGHTYVVYG 340
Cdd:cd17645 102 ------------NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 341 PLANGAT-SVIFEGTPFfpGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGegpvlKHNLSGLKVLGSVGEPINPEAWLWY 419
Cdd:cd17645 166 HLTAGAAlHVVPSERRL--DLDALNDYFNQEGITISFLPTGAAEQFMQLD-----NQSLRVLLTGGDKLKKIERKGYKLV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 420 YKYiGKEQCSIVDTFWQtetgghvITPLPGATPMKPgsasfPFFGVKPTLLDE----CGIEIKGE----GEGylvfsqpw 491
Cdd:cd17645 239 NNY-GPTENTVVATSFE-------IDKPYANIPIGK-----PIDNTRVYILDEalqlQPIGVAGElciaGEG-------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 492 pgMMRTLYN----NHERFEDTYFSKFPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESA 567
Cdd:cd17645 298 --LARGYLNrpelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAA 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 568 VVSRPHPVKGECLYCFITPnENEVFDQKLISDLKKMVRErigpFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:cd17645 376 VLAKEDADGRKYLVAYVTA-PEEIPHEELREWLKNDLPD----YMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
515-636 |
5.18e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.40 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 515 GYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQ 594
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDA 475
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24667955 595 KLISDlkkMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK13383 476 AQLRD---YLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
116-322 |
3.23e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 63.21 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLItad 195
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVI--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalCDTA-LEKVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPWTDDRdyWWHEEMEDKEPACYPEWM 274
Cdd:PLN02387 184 --------------CDSKqLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSS--FSEVEKLGKENPVDPDLP 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24667955 275 DAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVFDYKPGDIY 322
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
116-631 |
3.39e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 62.87 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVhsivFAGFSPDSLAERmfdckakllitad 195
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQR------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtaleKVEEMGHSVEKCIVVSHLKRVTPcQPDHVEEEipwtddrdywwHEEMEDKEPACYpewmd 275
Cdd:cd17654 80 --------------------SLTVMKKCHVSYLLQNKELDNAP-LSFTPEHR-----------HFNIRTDECLAY----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aedplfMLYTSGSTGKPKGVlHTTAGYLLYAATTFKIVFDYKPGDIYWCTgdvGWITGHTYVV--YGPLANGATSVIFEg 353
Cdd:cd17654 123 ------VIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLT---SPLTFDPSVVeiFLSLSSGATLLIVP- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 354 TPFFPGNDRYWSVIDKYKVTQFYTAPTAIraLMKFGEGPVLKHNLSG---LKVLGSVGE--PINPEAWLWYYKYIGKEQC 428
Cdd:cd17654 192 TSVKVLPSKLADILFKRHRITVLQATPTL--FRRFGSQSIKSTVLSAtssLRVLALGGEpfPSLVILSSWRGKGNRTRIF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 429 SIVDTfwqTETGGHVIT--------PLPGATPMkpgsasfpfFGVKPTLLDECGIEIKGEgegylVFSQpwpGMMRTLYN 500
Cdd:cd17654 270 NIYGI---TEVSCWALAykvpeedsPVQLGSPL---------LGTVIEVRDQNGSEGTGQ-----VFLG---GLNRVCIL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 501 NHErfEDTYFSKFpgyYCTGDGARRDaDGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSrphpVKGECL 580
Cdd:cd17654 330 DDE--VTVPKGTM---RATGDFVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTL----SDQQRL 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24667955 581 YCFIT--PNENEVFDQKLISDLKkmvrerigPFAMPDVIQNAPGLPKTRSGKI 631
Cdd:cd17654 400 IAFIVgeSSSSRIHKELQLTLLS--------SHAIPDTFVQIDKLPLTSHGKV 444
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-575 |
4.62e-10 |
|
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: 62.48 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLH---TTAGYLLYAATTFKIVfdykpgdiywcTGDVGWITGHTYVVYGPlANGATSVIFE 352
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYrhgTFAAQIDALRQLYGIR-----------PGEVDLATFPLFALFGP-ALGLTSVIPD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 353 GTPFFPGN---DRYWSVIDKYKVTQFYTAPTAIRALMKFGEgpVLKHNLSGLKVLGSVGEPInPEAWLWYYKYIGKEQCS 429
Cdd:cd05910 152 MDPTRPARadpQKLVGAIRQYGVSIVFGSPALLERVARYCA--QHGITLPSLRRVLSAGAPV-PIALAARLRKMLSDEAE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 430 IVDTFWQTET------GGH-VITPLPGATPMKPGSA-SFPFFGVKPTLL--DECGI-------EIKGEGEGYLVFSQPwp 492
Cdd:cd05910 229 ILTPYGATEAlpvssiGSReLLATTTAATSGGAGTCvGRPIPGVRVRIIeiDDEPIaewddtlELPRGEIGEITVTGP-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 493 gMMRTLYnnHERFEDTYFSKFPG-----YYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESA 567
Cdd:cd05910 307 -TVTPTY--VNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
|
330
....*....|...
gi 24667955 568 VV-----SRPHPV 575
Cdd:cd05910 384 LVgvgkpGCQLPV 396
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
258-636 |
4.65e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 WHEEMEDKEPACYPEWMDAEDPL-FMLYTSGSTGKPKGVLHTTAG----------YLLYA-----ATTFKIVFDYKpgdi 321
Cdd:PRK05691 3849 WEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGmlnnqlskvpYLALSeadviAQTASQSFDIS---- 3924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 322 YWctgdvgwitghtYVVYGPLANGATSVIFEGTPFFPGNdrYWSVIDKYKVTQFYTAPTAIRALMKFGEGPvlkhnLSGL 401
Cdd:PRK05691 3925 VW------------QFLAAPLFGARVEIVPNAIAHDPQG--LLAHVQAQGITVLESVPSLIQGMLAEDRQA-----LDGL 3985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 402 KVLGSVGEPINPE---AWLWYYKYIG------KEQCSIVDTFWQTETGGHVITPLPGATP--------MKPGSASFPFFG 464
Cdd:PRK05691 3986 RWMLPTGEAMPPElarQWLQRYPQIGlvnaygPAECSDDVAFFRVDLASTRGSYLPIGSPtdnnrlylLDEALELVPLGA 4065
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 465 VkptllDECGIEIKGEGEGYLvfSQPwpgmMRTLynnhERFEDTYFSKfPG--YYCTGDGARRDADGYLWITGRVDDMLN 542
Cdd:PRK05691 4066 V-----GELCVAGTGVGRGYV--GDP----LRTA----LAFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQVK 4129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 543 VSGHLMSTAEVESVLTEHPRVAESAVVSRPHPvKGECLYCFITPNENEVFDQKLISDLKKMVRERIGPFAMPDVIQNAPG 622
Cdd:PRK05691 4130 IRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDR 4208
|
410
....*....|....
gi 24667955 623 LPKTRSGKIMRRVL 636
Cdd:PRK05691 4209 LPLNANGKLDRKAL 4222
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
514-647 |
1.06e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.16 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 514 PGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFd 593
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24667955 594 qklISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAVNDRNVG 647
Cdd:PRK07445 402 ---LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLGLP 452
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
116-352 |
2.68e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 60.38 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAE--RMFDCKA----- 188
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYalRETECKAivcng 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 189 ---KLLIT--ADGAWRGEKPLYLkalcDTALEKVEEMGHSVekcivvshlkrvtpcqpdhveeeIPWTDdrdywwHEEME 263
Cdd:PTZ00216 202 knvPNLLRlmKSGGMPNTTIIYL----DSLPASVDTEGCRL-----------------------VAWTD------VVAKG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 264 DKEPACY----PEwmDAEDPLFMLYTSGSTGKPKGVLHT----TAGYLLYAATTFKIVFDYKPGDiywctgdvgwitghT 335
Cdd:PTZ00216 249 HSAGSHHplniPE--NNDDLALIMYTSGTTGDPKGVMHThgslTAGILALEDRLNDLIGPPEEDE--------------T 312
|
250
....*....|....*..
gi 24667955 336 YVVYGPLANgatsvIFE 352
Cdd:PTZ00216 313 YCSYLPLAH-----IME 324
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
98-636 |
6.26e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.80 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 98 DQIAYYWEGNhpddysrGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPD 177
Cdd:PRK05691 1146 ERIALVWDGG-------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAE 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 178 SLAERMFDCKAKLLITADGAwrgekplylkalcdtaLEKVEEMGHSVEKCIVVSHLkrvtpcqpdhveeeipwtddrDYW 257
Cdd:PRK05691 1219 RLAYMLADSGVELLLTQSHL----------------LERLPQAEGVSAIALDSLHL---------------------DSW 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 258 wheemEDKEPACYpewMDAEDPLFMLYTSGSTGKPKGVLHTTAGY---LLYAATTFK------------IVFDYKPGDIY 322
Cdd:PRK05691 1262 -----PSQAPGLH---LHGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQATYAlddsdvlmqkapISFDVSVWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 323 WctgdvGWITGHTYVVYGPlangatsvifeGTPFFPgnDRYWSVIDKYKVTQFYTAPTAiraLMKFGEGPvLKHNLSGLK 402
Cdd:PRK05691 1334 W-----PLITGCRLVLAGP-----------GEHRDP--QRIAELVQQYGVTTLHFVPPL---LQLFIDEP-LAAACTSLR 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 403 VLGSVGEPINPE----------AWLWYYKYiGKEQCSIVDTFWQ--TETG---------GHVITPLPGA--TPMKPGSAS 459
Cdd:PRK05691 1392 RLFSGGEALPAElrnrvlqrlpQVQLHNRY-GPTETAINVTHWQcqAEDGerspigrplGNVLCRVLDAelNLLPPGVAG 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 460 fpffgvkptlldECGIEIKGEGEGYLvfsqPWPGMmrtlynNHERF-EDTYFSKFPGYYCTGDGARRDADGYLWITGRVD 538
Cdd:PRK05691 1471 ------------ELCIGGAGLARGYL----GRPAL------TAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLD 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 539 DMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFDQKLISDLKkmvrERIGPFAMPDVIQ 618
Cdd:PRK05691 1529 QQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALA----AELPEYMVPAQLI 1604
|
570
....*....|....*...
gi 24667955 619 NAPGLPKTRSGKIMRRVL 636
Cdd:PRK05691 1605 RLDQMPLGPSGKLDRRAL 1622
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
115-298 |
1.28e-08 |
|
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: 57.85 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 115 GLTYRKLLEEVCRFANVLK-DHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLL-I 192
Cdd:cd17632 67 TITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLaV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 193 TADgawrgekplYLkalcDTALEKVEEmGHSVEKCIVVSHLKRVTpcqpDH-----------VEEEIPWTDDRDYWWHEE 261
Cdd:cd17632 147 SAE---------HL----DLAVEAVLE-GGTPPRLVVFDHRPEVD----AHraalesarerlAAVGIPVTTLTLIAVRGR 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 24667955 262 MEDKEPACYPEwmDAEDPLFML-YTSGSTGKPKGVLHT 298
Cdd:cd17632 209 DLPPAPLFRPE--PDDDPLALLiYTSGSTGTPKGAMYT 244
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
514-638 |
1.45e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.98 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 514 PGYYCTGDGARRDaDGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVfd 593
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA-- 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24667955 594 qKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK07824 310 -PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
276-638 |
3.98e-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: 56.34 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIY--W--CTGDVGWITGHtyvvYGPLANGATSVIF 351
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGMNQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 EGTPFFPGNDRYWSVIDKYKVTQFYTAPTAIRALMKFGEGPVLKH-NLSGLKVLGSVGEPINPEAWLWYYKYIGK---EQ 427
Cdd:cd05908 180 PTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDwDLSSIRMILNGAEPIDYELCHEFLDHMSKyglKR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 428 CSIVDTFWQTETGGHVITPlPGATPMKPgsasfPFFGVKPTLLDECGIEI-KGEGEGYLVFSQPWP---GMMRTLYNNHE 503
Cdd:cd05908 260 NAILPVYGLAEASVGASLP-KAQSPFKT-----ITLGRRHVTHGEPEPEVdKKDSECLTFVEVGKPideTDIRICDEDNK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 504 RFEDTYF--------SKFPGYY---------CTGDGARRDAD------GYLWITGRVDDMLNVSGHLMSTAEVESVLTEH 560
Cdd:cd05908 334 ILPDGYIghiqirgkNVTPGYYnnpeatakvFTDDGWLKTGDlgfirnGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 561 PRVAESAVVS---RPHPVKGECLYCFITPNENEVFDQKLISDLKKMVRERIGpFAMPDV--IQNapgLPKTRSGKIMRRV 635
Cdd:cd05908 414 EGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGG-WQINEVlpIRR---IPKTTSGKVKRYE 489
|
...
gi 24667955 636 LRK 638
Cdd:cd05908 490 LAQ 492
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
110-640 |
5.16e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 56.51 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 110 DDYSRG-LTYRKLLEEvcrfANVLKD---HGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVfaGFSPdSLAERMFD 185
Cdd:PRK06814 652 EDPVNGpLTYRKLLTG----AFVLGRklkKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSA-GIANILSA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 186 CKA---KLLITAdgawrgekplylKALCDTAleKVEEMGHSVEKCIVVSHLkrvtpcqpDHVEEEIPWTDDRDYWWHEEM 262
Cdd:PRK06814 725 CKAaqvKTVLTS------------RAFIEKA--RLGPLIEALEFGIRIIYL--------EDVRAQIGLADKIKGLLAGRF 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 263 edkePACYPEWMDAEDPLFMLYTSGSTGKPKGVLHTTAGYLLYAATTFKIVfDYKPGDIYWCTGDV----GWITG----- 333
Cdd:PRK06814 783 ----PLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPVfhsfGLTGGlvlpl 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 334 ----HTYVVYGPL----------ANGATsVIFeGTPFF-PGNDRYWSVIDkykvtqFYTaptairalmkfgegpvlkhnl 398
Cdd:PRK06814 858 lsgvKVFLYPSPLhyriipeliyDTNAT-ILF-GTDTFlNGYARYAHPYD------FRS--------------------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 399 sgLKVLGSVGEPINPEAW-LWYYKYigkeQCSIVDTFWQTETGghvitP-LPGATPM--KPGSASFPFFGVKPTLLDECG 474
Cdd:PRK06814 909 --LRYVFAGAEKVKEETRqTWMEKF----GIRILEGYGVTETA-----PvIALNTPMhnKAGTVGRLLPGIEYRLEPVPG 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 475 IE------IKGEG--EGYLVFSQPwpGMMRTLYNnherfedtyfskfpGYYCTGDGARRDADGYLWITGRVDDMLNVSGH 546
Cdd:PRK06814 978 IDeggrlfVRGPNvmLGYLRAENP--GVLEPPAD--------------GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGE 1041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 547 LMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITpnenevfdQKLIS--DLKKMVRER-IGPFAMPDVIQNAPGL 623
Cdd:PRK06814 1042 MISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTT--------ASDATraAFLAHAKAAgASELMVPAEIITIDEI 1113
|
570
....*....|....*..
gi 24667955 624 PKTRSGKIMRRVLRKIA 640
Cdd:PRK06814 1114 PLLGTGKIDYVAVTKLA 1130
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
276-640 |
9.72e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.49 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 AEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVGWITGHTYVVYGPLANGA--------- 346
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAevflypspl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 347 -------------TSVIFeGTPFFPGN-DRYWSVIDKYKVtqfytaptaiRALMKFGEgpvlkhnlsglKVLGSVGEpin 412
Cdd:PRK08043 443 hyrivpelvydrnCTVLF-GTSTFLGNyARFANPYDFARL----------RYVVAGAE-----------KLQESTKQ--- 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 413 peawLWYYKYigkeQCSIVDTFWQTETGGHVITPLPGATpmKPGSASFPFFGVKPTLLDECGIE------IKGEG--EGY 484
Cdd:PRK08043 498 ----LWQDKF----GLRILEGYGVTECAPVVSINVPMAA--KPGTVGRILPGMDARLLSVPGIEqggrlqLKGPNimNGY 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 485 LVFSQPWPGMMRTLYNNHERFEdtyfskfPGYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVA 564
Cdd:PRK08043 568 LRVEKPGVLEVPTAENARGEME-------RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 565 ESAVVSRPHPVKGECLYCFITpnenevfDQKLISD-LKKMVRERIGP-FAMPDVIQNAPGLPKTRSGKIMRRVLRKIA 640
Cdd:PRK08043 641 QHATAIKSDASKGEALVLFTT-------DSELTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
116-591 |
1.16e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 54.91 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 116 LTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLITad 195
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 196 gawrgekplylkalcdtalekveemghsvekcivvshlkrvtpcqpdhveeeipwtddrdywwheemeDKEPacypewmd 275
Cdd:cd17639 84 --------------------------------------------------------------------DGKP-------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 276 aEDPLFMLYTSGSTGKPKGVLHT----TAGyllyaattfkivfdykpgdiywCTGDVGWITGH-----TYVVYGPLANga 346
Cdd:cd17639 88 -DDLACIMYTSGSTGNPKGVMLThgnlVAG----------------------IAGLGDRVPELlgpddRYLAYLPLAH-- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 347 tsvIFE----------------GTP---------------------FFPGNDRYWSVIDK-----------YKVTQFYTA 378
Cdd:cd17639 143 ---IFElaaenvclyrggtigyGSPrtltdkskrgckgdltefkptLMVGVPAIWDTIRKgvlaklnpmggLKRTLFWTA 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 379 PTAIRALMKFG-EGPVL--------KHNLSG-LKVLGSVGEPINPEAwlwyYKYIGKEQCSIVDTFWQTETGGHVITPLP 448
Cdd:cd17639 220 YQSKLKALKEGpGTPLLdelvfkkvRAALGGrLRYMLSGGAPLSADT----QEFLNIVLCPVIQGYGLTETCAGGTVQDP 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 449 GAtpMKPGSASFPFFGVKPTLLDecgIEikgEGeGYLVFSQP-----W---PGMMRTLYNNHERFEDTYFSKfpGYYCTG 520
Cdd:cd17639 296 GD--LETGRVGPPLPCCEIKLVD---WE---EG-GYSTDKPPprgeiLirgPNVFKGYYKNPEKTKEAFDGD--GWFHTG 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667955 521 DGARRDADGYLWITGRVDDML-NVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKgecLYCFITPNENEV 591
Cdd:cd17639 365 DIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNEKHL 433
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
97-638 |
1.33e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 54.79 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 97 GDQIAYYWEGNHPDDysrgLTYRKLLEEVCRFANVLKDH-GIRKGDRVSIYMPMILELPIAMLACARIGAVhsivfagFS 175
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ----TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAV-------FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 176 PdsLAERMFDCKAKLLITadgawRGEKPLylkALCDTALekVEEMGHSVEKCIVVSHLKRVTPCQPDHVEEEIPwtDDRD 255
Cdd:PRK05620 93 P--LNKQLMNDQIVHIIN-----HAEDEV---IVADPRL--AEQLGEILKECPCVRAVVFIGPSDADSAAAHMP--EGIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 256 YWWHEEMEDKEPACYPeWMDAE--DPLFMLYTSGSTGKPKGVLHT-TAGYL----LYAATTFKIVFDYK-----PgdIY- 322
Cdd:PRK05620 159 VYSYEALLDGRSTVYD-WPELDetTAAAICYSTGTTGAPKGVVYShRSLYLqslsLRTTDSLAVTHGESflccvP--IYh 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 323 ---WCTGDVGWITGHTYVVYGPLANGAT--SVIFEGTPffpgndrywsvidkykvTQFYTAPTAIRALM-KFGEGPVLKH 396
Cdd:PRK05620 236 vlsWGVPLAAFMSGTPLVFPGPDLSAPTlaKIIATAMP-----------------RVAHGVPTLWIQLMvHYLKNPPERM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 397 NLSGLKVLGSVGEPINPEAWLWYYKyigkeqCSIVDTFWQTETG--GHVITPLPGATpmkpGSASFPFF---GVKPTLL- 470
Cdd:PRK05620 299 SLQEIYVGGSAVPPILIKAWEERYG------VDVVHVWGMTETSpvGTVARPPSGVS----GEARWAYRvsqGRFPASLe 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 471 ---------------DECGIEIKGE---GEGYLVFSQPWPGMMRTLYNNHERFEDTYFSKfPGYYCTGDGARRDADGYLW 532
Cdd:PRK05620 369 yrivndgqvmestdrNEGEIQVRGNwvtASYYHSPTEEGGGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 533 ITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGE------CLYCFITPNENEVfdqkliSDLKKMVRE 606
Cdd:PRK05620 448 IHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGErplavtVLAPGIEPTRETA------ERLRDQLRD 521
|
570 580 590
....*....|....*....|....*....|..
gi 24667955 607 RIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRK 638
Cdd:PRK05620 522 RLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
517-631 |
5.35e-07 |
|
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: 52.52 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 517 YCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITPNENEVFD--- 593
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesf 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24667955 594 ---------------------QKLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKI 631
Cdd:cd17647 454 aqedvpkevstdpivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
114-636 |
6.98e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 114 RGLTYRKLLEEVCRFANVLKDHGIRKGDRVSIYMPMILELPIAMLACARIGAVHSIVFAGFSPDSLAERMFDCKAKLLit 193
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLL-- 2289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 194 adgawrgekplylkaLCDTALekVEEMGhsvekcivvshlkrvtpcqpdhveeEIPWTDDRdywWHeeMEDKEP--ACYP 271
Cdd:PRK05691 2290 ---------------LSDRAL--FEALG-------------------------ELPAGVAR---WC--LEDDAAalAAYS 2322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 272 ewmDAEDPL--------FMLYTSGSTGKPKGVLHTTAGYLLYAATTFKiVFDYKPGD----IYWCTGDVGwitghTYVVY 339
Cdd:PRK05691 2323 ---DAPLPFlslpqhqaYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDcelhFYSINFDAA-----SERLL 2393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 340 GPLANGATSV----------------------IFEGTPffpgndRYWSVIDKYKVTQFYTAPtaIRALMKFGEGPVLKHn 397
Cdd:PRK05691 2394 VPLLCGARVVlraqgqwgaeeicqlireqqvsILGFTP------SYGSQLAQWLAGQGEQLP--VRMCITGGEALTGEH- 2464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 398 lsglkvLGSVGEPINPEAWLwyykyigkeqcsivDTFWQTETgghVITPLPGATP--MKPGSASFPFFGV----KPTLLD 471
Cdd:PRK05691 2465 ------LQRIRQAFAPQLFF--------------NAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVvgarVAYILD 2521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 472 ------------ECGIEIKGEGEGYlvfsQPWPGMmrtlynNHERFEDTYFSKFPG-YYCTGDGARRDADGYLWITGRVD 538
Cdd:PRK05691 2522 adlalvpqgatgELYVGGAGLAQGY----HDRPGL------TAERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRID 2591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 539 DMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPvKGECLYCFI---TPNENEVFDQKLISDLKKMVRERIGPFAMPD 615
Cdd:PRK05691 2592 HQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPA 2670
|
570 580
....*....|....*....|.
gi 24667955 616 VIQNAPGLPKTRSGKIMRRVL 636
Cdd:PRK05691 2671 HLILLDSLPLTANGKLDRRAL 2691
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
275-569 |
3.09e-06 |
|
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: 50.05 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 275 DAEDPLFMLYTSGSTGKPKGVLHTTAGyLLYAATTFKIVFDYKPGDIYWCTGDVgWitgHTY---VVYGPLANGAtSVIF 351
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 352 EGTPFFPgNDrywsvIDKYKVTQFYTAPTAIRALM-----KFGEGPVLKHNLSGLKVLGSVGE-PIN-----PEAWLWYY 420
Cdd:cd17640 160 TSIRTLK-DD-----LKRVKPHYIVSVPRLWESLYsgiqkQVSKSSPIKQFLFLFFLSGGIFKfGISgggalPPHVDTFF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 421 KYIGKEqcsIVDTFWQTETGGHVITPLPGATpmKPGSASFPFFGVKPTLLDECGIEIKGEGEGYLVFSQPwPGMMRTLYN 500
Cdd:cd17640 234 EAIGIE---VLNGYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG-PQVMKGYYK 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 501 NHERFEDTYFSKfpGYYCTGDGARRDADGYLWITGRVDDMLNVS-GHLMSTAEVESVLTEHPRVAESAVV 569
Cdd:cd17640 308 NPEATSKVLDSD--GWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
464-636 |
1.52e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.97 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 464 GVKPTLLDECGIEIKGEGEGYLVFSQPwpGMMRTLYNNHERFEDTYFSkFPGY--YCTGDGARRDaDGYLWITGRVDDML 541
Cdd:PRK04813 326 DSPLLIIDEEGTKLPDGEQGEIVISGP--SVSKGYLNNPEKTAEAFFT-FDGQpaYHTGDAGYLE-DGLLFYQGRIDFQI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 542 NVSGHLMSTAEVESVLTEHPRVAESAVV--SRPHPVKGecLYCFITPNENEV-FDQKLISDLKKMVRERIGPFAMPD--V 616
Cdd:PRK04813 402 KLNGYRIELEEIEQNLRQSSYVESAVVVpyNKDHKVQY--LIAYVVPKEEDFeREFELTKAIKKELKERLMEYMIPRkfI 479
|
170 180
....*....|....*....|
gi 24667955 617 IQNApgLPKTRSGKIMRRVL 636
Cdd:PRK04813 480 YRDS--LPLTPNGKIDRKAL 497
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
515-641 |
2.94e-05 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 47.61 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 515 GYYCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLteHPRVAES----AVVSRPHPVKGECLYCFITPNENE 590
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKLVVLHTCGAED 1096
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24667955 591 VfdQKLisdLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKIMRRVLRKIAV 641
Cdd:PRK08633 1097 V--EEL---KRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELAL 1142
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
517-631 |
1.34e-04 |
|
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: 45.44 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 517 YCTGDGARRDADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAESAVVSRPHPVKGECLYCFITP---------- 586
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPqdksdeleef 759
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24667955 587 ----NENEVFDQ---------KLISDLKKMVRERIGPFAMPDVIQNAPGLPKTRSGKI 631
Cdd:TIGR03443 760 ksevDDEESSDPvvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
535-642 |
2.56e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 43.98 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 535 GRVDDMLNVSGHLMSTaevesvLTEHPRVAESAVVSRPHPVKGECLYCFITPNENeVFDQKLISDLKKMvreriGPFAMP 614
Cdd:PRK09188 233 GTGDRIDNEAPAIQAA------LKSDPAVSDVAIALFSLPAKGVGLYAFVEAELP-ADEKSLRARLAGA-----KPPKPP 300
|
90 100
....*....|....*....|....*...
gi 24667955 615 DVIQNAPGLPKTRSGKIMRRVLRKIAVN 642
Cdd:PRK09188 301 EHIQPVAALPRDADGTVRDDILRLIAMN 328
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
519-633 |
4.01e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 40.37 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 519 TGDGARRdADGYLWITGRVDDMLNVSGHLMSTAEVESVLTEHP--RVAESAVVSRPHPvKGE----CLYCFITPNENEvf 592
Cdd:PRK09192 443 TGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPelRSGDAAAFSIAQE-NGEkivlLVQCRISDEERR-- 518
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 24667955 593 dQKLISDLKKMVRERIGpfaMPDVIQNAP--GLPKTRSGKIMR 633
Cdd:PRK09192 519 -GQLIHALAALVRSEFG---VEAAVELVPphSLPRTSSGKLSR 557
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
533-638 |
8.79e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 38.98 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667955 533 ITGRVDDMLNVSGHLMSTAEVESVLTEHPRVAES--AVVSRPHP-----VKGEClycfitpnENEVFDQKLISDLKKMVR 605
Cdd:COG1541 322 ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREGGldeltVRVEL--------APGASLEALAEAIAAALK 393
|
90 100 110
....*....|....*....|....*....|....
gi 24667955 606 ERIGpfAMPDVIQNAPG-LPktRSGKIMRRVLRK 638
Cdd:COG1541 394 AVLG--LRAEVELVEPGsLP--RSEGKAKRVIDR 423
|
|
| |
