|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1-603 |
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: 1132.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 1 MKGASTNICYNVLDRNVHekKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVV 80
Cdd:cd05966 47 FEGGKLNISYNCLDRHLK--ERGDKVAIIWEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 81 AMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekdFPVRCCIVVKHLGR 160
Cdd:cd05966 125 AMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 161 AelgmgdspsqsppikrscpdvqgklkekskrvqpqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGK 240
Cdd:cd05966 201 E-----------------------------------VPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 241 PKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYK 320
Cdd:cd05966 246 PKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 321 VTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLPGAT 400
Cdd:cd05966 326 VTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGAT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 401 PMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYY 480
Cdd:cd05966 406 PLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYY 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 481 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPI 560
Cdd:cd05966 486 WITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPI 565
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1622836714 561 ATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVAD 603
Cdd:cd05966 566 ATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
3-610 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1066.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 3 GASTNICYNVLDRNVHEKklGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM 82
Cdd:PRK00174 63 DGELNVSYNCLDRHLKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 83 LACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQekdfPVRCCIVVKHLGrae 162
Cdd:PRK00174 141 LACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG--- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 163 lgmGDspsqsppikrscpdvqgklkekskrvqpqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPK 242
Cdd:PRK00174 214 ---GD-----------------------------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 243 GVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVT 322
Cdd:PRK00174 262 GVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 KFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLPGATPM 402
Cdd:PRK00174 342 IFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 403 KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYWI 482
Cdd:PRK00174 422 KPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWI 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 483 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIAT 562
Cdd:PRK00174 502 TGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAK 581
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622836714 563 PDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVADPSVISHL 610
Cdd:PRK00174 582 PDVIQFAPGLPKTRSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
2-610 |
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: 1007.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRnvHEKKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:TIGR02188 52 VGGELNVSYNCVDR--HLEARPDKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKdfpVRCCIVVKHLGra 161
Cdd:TIGR02188 130 MLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 elgmgdspsqsppikrscpdvqgklkekskrvQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKP 241
Cdd:TIGR02188 205 --------------------------------NPVVPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 321
Cdd:TIGR02188 253 KGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLPGATP 401
Cdd:TIGR02188 333 TIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGSATFPFFGVAPAILNES-GEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYY 480
Cdd:TIGR02188 413 TKPGSATLPFFGIEPAVVDEEgNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYI 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 481 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPI 560
Cdd:TIGR02188 493 WITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPI 572
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 561 ATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD-LGDTSTVADPSVISHL 610
Cdd:TIGR02188 573 AKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEiLGDTSTLEDPSVVEEL 623
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
3-610 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 872.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 3 GASTNICYNVLDRNVHEKklGDKVAFYWEGnEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM 82
Cdd:COG0365 5 GGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 83 LACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEkdfpVRCCIVVKHLGrAE 162
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRTG-AD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 163 LGMGDspsqsppikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPK 242
Cdd:COG0365 157 VPMEG------------------------------------DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 243 GVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVT 322
Cdd:COG0365 201 GVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 KFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTETGGHMLTPLPGaTPM 402
Cdd:COG0365 281 VFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 403 KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYWI 482
Cdd:COG0365 357 KPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 483 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIAT 562
Cdd:COG0365 437 LGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAY 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622836714 563 PDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDTSTVADPSVISHL 610
Cdd:COG0365 517 PREIEFVDELPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2-610 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 825.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRNVhEKKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:PLN02654 83 KGGKTNICYNCLDRNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKDFPVRCCIVVkhlgra 161
Cdd:PLN02654 162 MLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTY------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 elgmgdspsqsppikrscpDVQGKLKEKSKRvqpqisWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKP 241
Cdd:PLN02654 236 -------------------ENQLAMKREDTK------WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 321
Cdd:PLN02654 291 KGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLPGATP 401
Cdd:PLN02654 371 TIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWP 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYW 481
Cdd:PLN02654 451 QKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYW 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIA 561
Cdd:PLN02654 531 LTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFA 610
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1622836714 562 TPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD-LGDTSTVADPSVISHL 610
Cdd:PLN02654 611 APDKIHWAPGLPKTRSGKIMRRILRKIASRQLDeLGDTSTLADPGVVDQL 660
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2-581 |
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: 682.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRNVHEKklGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:cd17634 48 EDATLNLAANALDRHLREN--GDRTAIIYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKcqeKDFPVRCCIVVKhlgra 161
Cdd:cd17634 126 MLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLK----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 elgmgdspsqsppikrscpdvqgklkekskRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKP 241
Cdd:cd17634 198 ------------------------------RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 321
Cdd:cd17634 248 KGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLPGATP 401
Cdd:cd17634 328 NILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYW 481
Cdd:cd17634 408 LKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYW 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIA 561
Cdd:cd17634 488 ITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLA 567
|
570 580
....*....|....*....|
gi 1622836714 562 TPDYIQNAPGLPKTRSGKIM 581
Cdd:cd17634 568 TPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2-610 |
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: 576.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRNVhEKKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:cd05967 45 VGGRLNTCYNALDRHV-EAGRGDQIALIYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKdfPVRCciVVKHLGRA 161
Cdd:cd05967 124 MLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHV--LVLNRPQV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 ELGMGDSpsqsppikrscpdvqgklkekskrvqpqiswnqGIDLWWHELMQEAGdECEPEWCDAEDPLFILYTSGSTGKP 241
Cdd:cd05967 200 PADLTKP---------------------------------GRDLDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPT-YPDVNRLWSIVDKYK 320
Cdd:cd05967 246 KGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 321 VTKFYTAPTAIRLLMKF--GDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTETGGHMLTPLPG 398
Cdd:cd05967 326 VNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 399 --ATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPW-PGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRD 475
Cdd:cd05967 403 lePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 476 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIR 554
Cdd:cd05967 483 EDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVR 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836714 555 EKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDTSTVADPSVISHL 610
Cdd:cd05967 563 EQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
2-607 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 532.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRnvHEKKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:PRK10524 48 VGGRTNLCHNAVDR--HLAKRPEQLALIAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKdfPVRCCIVVKHLGRA 161
Cdd:PRK10524 126 MLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGLAPM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 ElgmgdspsqsppikrscpdvqgklkekskrvqpqisWNQGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGK 240
Cdd:PRK10524 204 A------------------------------------RVAGRDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 241 PKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYK 320
Cdd:PRK10524 248 PKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 321 VTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTETGGHMLTPLPG-- 398
Cdd:PRK10524 328 VNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARGve 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 399 ATPMKPGSATFPFFGVAPAILNESGEELEGEAEG-YLVFKQPW-PGIMRTVYGNHERFETTYFKKF-PGYYVTGDGCRRD 475
Cdd:PRK10524 405 DRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKgVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 476 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-----PKLTEELK 550
Cdd:PRK10524 485 ADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIM 564
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836714 551 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDLGDTSTVADPSVI 607
Cdd:PRK10524 565 ALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAE-GRDPGDLTTIEDPAAL 620
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
7-603 |
1.17e-179 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 520.61 E-value: 1.17e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 7 NICYNVLDRNVHEKkLGDKVAFYWEGNEPGETtqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 86
Cdd:PRK04319 43 NIAYEAIDRHADGG-RKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 87 RIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELadealqkcqekdfpvrccivvKHLgraeLGMG 166
Cdd:PRK04319 120 KNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------------KHV----LLVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 167 DSPSQSPPIkrscpdvqgklkekskrvqpqiswnqgIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVH 246
Cdd:PRK04319 175 EDVEEGPGT---------------------------LDFN--ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 247 tVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDVNRLWSIVDKYKVTKFYT 326
Cdd:PRK04319 226 -VHNAMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 327 APTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTETGGHMLTPLPgATPMKPGS 406
Cdd:PRK04319 302 APTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 407 ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETtYFKkfPGYYVTGDGCRRDQDGYYWITGRI 486
Cdd:PRK04319 378 MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 487 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYI 566
Cdd:PRK04319 455 DDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREI 534
|
570 580 590
....*....|....*....|....*....|....*..
gi 1622836714 567 QNAPGLPKTRSGKIMRRVLrKIAQNDHDLGDTSTVAD 603
Cdd:PRK04319 535 EFKDKLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
3-604 |
2.70e-169 |
|
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: 495.86 E-value: 2.70e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 3 GASTNICYNVLDRnvHEKKLGDKVAFYWEGnEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM 82
Cdd:cd05968 57 GGRMNIVEQLLDK--WLADTRTRPALRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 83 LACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekdFPVRCCIVVKHLGRAE 162
Cdd:cd05968 134 LAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 163 LgmgdspsqsppikrscpdvqgklkekskrvqpqisWNQGIDLWWHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPK 242
Cdd:cd05968 210 T-----------------------------------PAKGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 243 GVVHTVGGYMLYVATTFKYVFDFHAED-VFWCTaDIGWITGhSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 321
Cdd:cd05968 253 GTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLPgATP 401
Cdd:cd05968 331 THLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYW 481
Cdd:cd05968 410 IKPSSFNGPVPGMKADVLDESGKPARPEVGE-LVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFY 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIA 561
Cdd:cd05968 489 ILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPL 568
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1622836714 562 TPDYIQNAPGLPKTRSGKIMRRVLRKiAQNDHDLGDTSTVADP 604
Cdd:cd05968 569 SPERILFVKDLPKTRNAKVMRRVIRA-AYLGKELGDLSSLENP 610
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
42-589 |
3.01e-140 |
|
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: 415.36 E-value: 3.01e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDa 121
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 fyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgKLKEKSkrvqpqiswnq 201
Cdd:cd05969 81 ---------------------------------------------------------------ELYERT----------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 202 gidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 281
Cdd:cd05969 87 ----------------------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVT 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 282 GHSYVTYGPLANGATSVLFEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPIN 361
Cdd:cd05969 144 GTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 362 PEAWLWYHQVVGAqrcPIVDTFWQTETGGHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 441
Cdd:cd05969 221 PEAIRWGMEVFGV---PIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 442 GIMRTVYGNHERFETtYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 521
Cdd:cd05969 297 SMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622836714 522 HPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 589
Cdd:cd05969 374 DPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
42-587 |
2.21e-108 |
|
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: 332.76 E-value: 2.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLIttda 121
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 fyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpqiswnq 201
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 202 gidlwwhelmqeagdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGgYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 281
Cdd:cd05972 78 ---------------------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 282 GHSYVTYGPLANGATSVLFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvtKHSRASLQVLGTVGEPIN 361
Cdd:cd05972 136 GAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 362 PEAWLWYHQVVGAqrcPIVDTFWQTETGgHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 441
Cdd:cd05972 211 PEVIEWWRAATGL---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 442 GIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 521
Cdd:cd05972 286 GLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP 362
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836714 522 HPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05972 363 DPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
13-493 |
2.41e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 332.35 E-value: 2.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 13 LDRNVheKKLGDKVAFywegnEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALH 92
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 93 SIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkelaDEALQKCQEKDFPVRCCIVVKHLGRAELGMGDSPSQS 172
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 173 PPIkrscpdvqgklkekskrvqpqiswnqgidlwwhelmqeagDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVgGYM 252
Cdd:pfam00501 142 ADV----------------------------------------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 253 LYVATTFKYV----FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDVNRLWSIVDKYKVTKFYTAP 328
Cdd:pfam00501 181 VANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 329 TAIRLLMKFGDEPVTKHSraSLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTETGGHMLTPLPGATPM-KPGSA 407
Cdd:pfam00501 260 TLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 408 TFPFFGVAPAILNESGEELEGEAEG-YLVFKQpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRI 486
Cdd:pfam00501 335 GRPLPGTEVKIVDDETGEPVPPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRK 410
|
....*..
gi 1622836714 487 DDMLNVS 493
Cdd:pfam00501 411 KDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
227-581 |
1.17e-87 |
|
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: 276.09 E-value: 1.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 227 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 306
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 307 PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQT 386
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 387 ETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRtVYGNHErfETTYFKKFPGYY 466
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MK-GYWNNP--EATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 467 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPklt 546
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 1622836714 547 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 581
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
12-593 |
7.39e-83 |
|
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: 267.45 E-value: 7.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 12 VLDRNVheKKLGDKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 91
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 92 HSIVFAGFSSESLcERIL-DSSCSLLITtdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdsps 170
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 171 qsppikrscpdvqgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaedpLFILYTSGSTGKPKGVVHTVGG 250
Cdd:COG0318 103 ----------------------------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 251 yMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTA 330
Cdd:COG0318 125 -LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTM 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 331 IRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFP 410
Cdd:COG0318 200 LARLLR--HPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 411 FFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFEttyfKKFP-GYYVTGDGCRRDQDGYYWITGRIDDM 489
Cdd:COG0318 275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 490 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNA 569
Cdd:COG0318 349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFV 425
|
570 580
....*....|....*....|....
gi 1622836714 570 PGLPKTRSGKIMRRVLRKIAQNDH 593
Cdd:COG0318 426 DELPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-587 |
3.14e-80 |
|
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: 260.14 E-value: 3.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERiLDSSCSLLITTD 120
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 AFYRgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpqiswn 200
Cdd:cd05973 80 AANR---------------------------------------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 qgidlwwHELmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWI 280
Cdd:cd05973 84 -------HKL--------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWA 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 281 TGHSYVTYGPLANGATSVLFEGIPTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPI 360
Cdd:cd05973 142 YGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 361 NPEAWLWYHQVVGAqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfKQPW 440
Cdd:cd05973 218 TPEVIRWFDAALGV---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG-------------DELG 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 441 PGIMRTVYGNHERFETTYFKKFP---------GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 511
Cdd:cd05973 282 PGEPGRLAIDIANSPLMWFRGYQlpdtpaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPA 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836714 512 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05973 362 VAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2-588 |
3.65e-77 |
|
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: 257.58 E-value: 3.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRNVHEkklgDKVAFYweGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:cd05943 66 PGARLNYAENLLRHADAD----DPAAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKEladealqKCQEkdfpvrcciVVKHLgra 161
Cdd:cd05943 140 MLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVRE-------KVAE---------LVKGL--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 elgmgdsPSQSPPIkrSCPDVQGklkekskRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKP 241
Cdd:cd05943 201 -------PSLLAVV--VVPYTVA-------AGQPDLSKIAKALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 321
Cdd:cd05943 265 KCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcpivDTFWQTETGGhmlTPLPGA-- 399
Cdd:cd05943 343 TVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfv 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 400 -----TPMKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDG 471
Cdd:cd05943 414 ggnplLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGE-LVCTKPFPS-MPVGFWNDPdgsRYRAAYFAKYPGVWAHGDW 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 472 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKK 551
Cdd:cd05943 492 IEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRS 571
|
570 580 590
....*....|....*....|....*....|....*..
gi 1622836714 552 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 588
Cdd:cd05943 572 TIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI 608
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
2-587 |
1.04e-74 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 251.58 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 2 KGASTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 81
Cdd:PTZ00237 54 KGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 82 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKdfpvrccivvkhlgra 161
Cdd:PTZ00237 134 MLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFK---------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 162 elgmgdsPSQSPPIKRSCPDVQGKLK--EKSKRVQPQISWNQGIDLWwHELMQEAGDECEPewCDAEDPLFILYTSGSTG 239
Cdd:PTZ00237 198 -------PSNVITLFRNDITSESDLKkiETIPTIPNTLSWYDEIKKI-KENNQSPFYEYVP--VESSHPLYILYTSGTTG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 240 KPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVtYGPLANGATSVLFEGIPTYPDV--NRLWSIVD 317
Cdd:PTZ00237 268 NSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHieDDLWNTIE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 318 KYKVTKFYTAPTAIRLLMKFGDEPVTKHSR---ASLQVLGTVGEPINPEAWLWYHQVVGAqRCPIVdtFWQTETGghMLT 394
Cdd:PTZ00237 347 KHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGGEVIEESIPEYIENKLKI-KSSRG--YGQTEIG--ITY 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 395 PLPGATPMKPGSAT-FPFFGVAPAILNESGEELEGEAEGYLVFKQPWP-GIMRTVYGNHERFETTyFKKFPGYYVTGDGC 472
Cdd:PTZ00237 422 LYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLG 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 473 RRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP----KLTEE 548
Cdd:PTZ00237 501 FKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNE 580
|
570 580 590
....*....|....*....|....*....|....*....
gi 1622836714 549 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PTZ00237 581 INNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
33-609 |
3.89e-70 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 239.31 E-value: 3.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 33 NEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSS 112
Cdd:PRK03584 107 GEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 113 CSLLITTDAFYRGEKLVN----LKELADeALQkcqekdfPVRCCIVVKHLGRAELGMGDSPSQSppikrscpdvqgklke 188
Cdd:PRK03584 187 PKVLIAVDGYRYGGKAFDrrakVAELRA-ALP-------SLEHVVVVPYLGPAAAAAALPGALL---------------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 189 kskrvqpqiswnqgidlwWHELMQEAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA 267
Cdd:PRK03584 243 ------------------WEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGP 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 268 ED-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 346
Cdd:PRK03584 305 GDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHD 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 347 RASLQVLGTVGEPINPEAWLWYHQVVGAqrcpivDTFWQTETGG-HMLTPLPGATPMKP---GSATFPFFGVAPAILNES 422
Cdd:PRK03584 382 LSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDED 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 423 GEELEGEAEGyLVFKQPWPGiMrTVY----GNHERFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 498
Cdd:PRK03584 456 GRPVVGEVGE-LVCTKPFPS-M-PLGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIG 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 499 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 578
Cdd:PRK03584 533 TAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSG 612
|
570 580 590
....*....|....*....|....*....|....*....
gi 1622836714 579 KIM----RRVLR----KIAQNdhdlgdTSTVADPSVISH 609
Cdd:PRK03584 613 KKVelpvKKLLHgrpvKKAVN------RDALANPEALDW 645
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
7-587 |
1.17e-66 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 226.96 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 7 NICYNVLDRNVHEKKLGDKV---AFYWEgNEPGETTQITYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAM 82
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 83 LACARIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladeaLQKCQEKdfpvrcCIVVKHLGRAE 162
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIVTSDELAPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 163 LgmgDSpsqsppIKRSCPDVQGKLkekskRVQPQiSWNQGIDLwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPK 242
Cdd:cd05928 128 V---DS------VASECPSLKTKL-----LVSEK-SRDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 243 GVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDVNRLWSIVDKYKVT 322
Cdd:cd05928 191 MAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPIT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 KFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAW-LWYHQVvGAQrcpIVDTFWQTETGghMLTPLPGATP 401
Cdd:cd05928 269 TFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLeKWKAQT-GLD---IYEGYGQTETG--LICANFKGMK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGS--ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVY-GNHERFETTYFKKFpgyYVTGDGCRRDQDG 478
Cdd:cd05928 340 IKPGSmgKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 479 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC-DGHTFSP-KLTEELKKQIREK 556
Cdd:cd05928 417 YFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApQFLSHDPeQLTKELQQHVKSV 496
|
570 580 590
....*....|....*....|....*....|.
gi 1622836714 557 IGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05928 497 TAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-586 |
1.82e-64 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 218.46 E-value: 1.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITtdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqp 195
Cdd:cd05971 82 LVT----------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 196 qiswnqgidlwwhelmqeagDEcepewcdAEDPLFILYTSGSTGKPKGVVHT-------VGGYMLYvattfkyvFDF--H 266
Cdd:cd05971 85 --------------------DG-------SDDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLfpR 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 267 AEDVFWCTADIGWItghsyvtyGPLANGATSVLFEGIP------TYPDVNRLWSIVDKYKVTKFYTAPTAIRLlMKFGDE 340
Cdd:cd05971 130 DGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGE 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 341 PVtKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTEtGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 420
Cdd:cd05971 201 QL-KHAQVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVD 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 421 ESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEttyfKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 499
Cdd:cd05971 276 DNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 500 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:cd05971 352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
....*..
gi 1622836714 580 IMRRVLR 586
Cdd:cd05971 432 IRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
10-586 |
7.31e-63 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 216.08 E-value: 7.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 10 YN---VLDRNVhEKKLGDKVAFYwegnepGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 86
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 87 RIGALhSIVFAGFSSESLCERIL-DSSCSLLITTDAFYrgeklvnlkELADEALqkcqEKDFPVRCCIVVkhlgraelgM 165
Cdd:cd05959 76 RAGIV-PVPVNTLLTPDDYAYYLeDSRARVVVVSGELA---------PVLAAAL----TKSEHTLVVLIV---------S 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 166 GDSPSQSPpikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVV 245
Cdd:cd05959 133 GGAGPEAG------------------------------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 246 HTVGGyMLYVATTF-KYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLWSIVDKYKVTKF 324
Cdd:cd05959 183 HLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 325 YTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTETGGHMLTPLPGAtpMKP 404
Cdd:cd05959 259 FGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 405 GSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTyfkkFPGYYV-TGDGCRRDQDGYYWIT 483
Cdd:cd05959 332 GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM--YWNNRDKTRDT----FQGEWTrTGDKYVRDDDGFYTYA 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 484 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATP 563
Cdd:cd05959 406 GRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYP 485
|
570 580
....*....|....*....|...
gi 1622836714 564 DYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05959 486 RWIVFVDELPKTATGKIQRFKLR 508
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
3-590 |
3.01e-62 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 217.83 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 3 GASTNICYNVLdrnvhEKKLGDKVAFYWegNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM 82
Cdd:TIGR01217 84 GARLNYAENLL-----RAAGTEPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 83 LACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKlvnlKELADEALQKCQEKDFPVRCCIVVKHLgrae 162
Cdd:TIGR01217 157 LATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVRKELPTLRAVVHIPYL---- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 163 lgmGDSPSQSPPIKRScpdvqgklkekskrvqpqiswnqgidLWWHELMQEAGD-ECEPEWCDAEDPLFILYTSGSTGKP 241
Cdd:TIGR01217 229 ---GPRETEAPKIDGA--------------------------LDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTygPLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 321
Cdd:TIGR01217 280 KCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHqvvgaqRCPIVDTFWQTETGG-HMLTPLPGAT 400
Cdd:TIGR01217 358 TLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY------DEIKADVWLASISGGtDICSCFAGAN 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 401 PMKP---GSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCRR 474
Cdd:TIGR01217 432 PTLPvhiGEIQAPGLGTAVQSWDPEGKPVTGEVGE-LVCTNPMPS-MPIRFWNDPdgsKYRDAYFDTYPGVWRHGDWITL 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 475 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIR 554
Cdd:TIGR01217 510 TPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIR 589
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622836714 555 EKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 590
Cdd:TIGR01217 590 AGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQ 625
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
7-592 |
7.96e-59 |
|
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: 205.81 E-value: 7.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 7 NICYNVLDRNVHEKKlgDKVAFYWeGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 86
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 87 RIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladealqkCQEKDFPVRCCIvvkhlgraelGMG 166
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYR-----------------IESADIKMIVAI----------AED 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 167 DSPSQSPPIKRSCPDvqgklkeKSKRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDA---EDPLFILYTSGSTGKPKG 243
Cdd:cd05970 130 NIPEEIEKAAPECPS-------KPKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKM 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 244 VVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTK 323
Cdd:cd05970 203 VEH-DFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 324 FYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQrcpIVDTFWQTETGGHMLTpLPGATPmK 403
Cdd:cd05970 280 FCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-K 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 404 PGSATFPFFGVAPAILNESGEELEGEAEGYLVF----KQPWpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGY 479
Cdd:cd05970 352 PGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGY 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 480 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGP 559
Cdd:cd05970 428 LWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAP 507
|
570 580 590
....*....|....*....|....*....|...
gi 1622836714 560 IATPDYIQNAPGLPKTRSGKImRRVlrKIAQND 592
Cdd:cd05970 508 YKYPRIVEFVDELPKTISGKI-RRV--EIRERD 537
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
10-586 |
1.31e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 196.95 E-value: 1.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 10 YNVLDRNVheKKLGDKVAFYWEGNEpgettqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 89
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDGRR------TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 90 A-LHSIVFagFSSESLCERIL-DSSCSLLITTDAFyrgEKLV-NLKELADEalqkcqekdfpVRCCIVvkhlgraelgMG 166
Cdd:PRK06187 81 AvLHPINI--RLKPEEIAYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------VRTVIV----------EG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 167 DSPSQSPPikrscPDVQGklkekskrvqpqiswnqgidlwWHELMQEAGDEcePEWCDAE--DPLFILYTSGSTGKPKGV 244
Cdd:PRK06187 135 DGPAAPLA-----PEVGE----------------------YEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGHPKGV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 245 V--------HTVGGymlyvattfKYVFDFHAEDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegIPT 305
Cdd:PRK06187 186 VlshrnlflHSLAV---------CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV----IPR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 306 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHQVVGaqrCPIVDTFWQ 385
Cdd:PRK06187 241 RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGM 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 386 TETGG--HMLTPLPGATPM--KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHERFETTYF 459
Cdd:PRK06187 316 TETSPvvSVLPPEDQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAETID 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 460 KkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGH 539
Cdd:PRK06187 394 G---GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGA 470
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1622836714 540 TFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK06187 471 TLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
23-582 |
1.27e-54 |
|
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: 192.05 E-value: 1.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 23 GDKVAFYWEGNEpgettqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 102
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 103 SLCERILDSSCSLLIttdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdv 182
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 183 qgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYV 262
Cdd:cd17631 98 -------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAA 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 263 FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPV 342
Cdd:cd17631 134 LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFAT 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 343 TKHSraSLQVLGTVGEPInPEAWLwyhQVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNES 422
Cdd:cd17631 210 TDLS--SLRAVIYGGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPD 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 423 GEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 502
Cdd:cd17631 284 GREVPPGEVGEIVVRGP--HVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEV 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 503 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 582
Cdd:cd17631 359 EDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
41-586 |
4.23e-54 |
|
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: 190.75 E-value: 4.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITtd 120
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 afyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpqiswn 200
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 qgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADI--G 278
Cdd:cd05919 89 -----------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffG 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 279 WITGHSyvTYGPLANGATSVLFegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGE 358
Cdd:cd05919 146 YGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 359 PInPEAwLWYhQVVGAQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQ 438
Cdd:cd05919 219 AL-PRG-LGE-RWMEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 439 PWPGIMrtvYGNheRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 518
Cdd:cd05919 294 PSAAVG---YWN--NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVV 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622836714 519 GHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05919 369 AVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
10-586 |
1.44e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 184.30 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 10 YNVLDRNVheKKLGDKVAFYWegnePGETtqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 89
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIF----MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 90 AlhsIVfagfsseslcerildsscsllITTDAFYRGEklvnlkELAdEALQKCQEKDfpvrccIVVkhlgraelgmgdsp 169
Cdd:cd05936 74 A---VV---------------------VPLNPLYTPR------ELE-HILNDSGAKA------LIV-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 170 sqsppikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVG 249
Cdd:cd05936 103 ----------------------------------AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 250 GYMLYVATTFKYVFDFH-AEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTyPDVNRLWSIVDKYKV 321
Cdd:cd05936 149 NLVANALQIKAWLEDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FRPIGVLKEIRKHRV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTETG--GHmLTPLPGa 399
Cdd:cd05936 218 TIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VNPLDG- 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 400 tPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTyFKKfpGYYVTGDGCRRDQDGY 479
Cdd:cd05936 291 -PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMKGYWNRPEETAEA-FVD--GWLRTGDIGYMDEDGY 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 480 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGP 559
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAG 441
|
570 580
....*....|....*....|....*..
gi 1622836714 560 IATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05936 442 YKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
35-587 |
1.73e-51 |
|
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: 184.82 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 35 PGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCS 114
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 LLITTDAFYRGEKLVNLKELAdealqkcqekdfpvrccivvkhLGRAELGMGDSPSQSPPIKRSCPDVQGKLKEKSKRVQ 194
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLG----------------------LAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 PQiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGV--VHT-VGGYMLYVATTFKYVFD------- 264
Cdd:cd05926 146 PL----------------------------PDDLALILHTSGTTGRPKGVplTHRnLAASATNITNTYKLTPDdrtlvvm 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 265 --FHaedvfwctadigwITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTkFYTA-PTAIRLLMKFgDEP 341
Cdd:cd05926 198 plFH-------------VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 342 VTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTETGGHM-LTPLPgATPMKPGSATFPFfGVAPAILN 420
Cdd:cd05926 259 NPESPPPKLRFIRSCSASLPPAVLEALEATFGA---PVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 421 ESGEELEGEAEGYLVFKQPwpGIMRTVYGNHE-RFEttYFKKFpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 499
Cdd:cd05926 334 EDGEILPPGVVGEICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISP 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 500 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHtfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:cd05926 409 LEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA---SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGK 485
|
....*...
gi 1622836714 580 IMRRVLRK 587
Cdd:cd05926 486 IQRRKVAE 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
225-586 |
7.05e-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: 176.51 E-value: 7.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 225 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 304
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 305 TYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFW 384
Cdd:cd05958 174 ATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 385 QTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVY-GNHERFETTYFKKfp 463
Cdd:cd05958 247 STEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQG-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 543
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622836714 544 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
225-589 |
1.17e-48 |
|
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: 175.83 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 225 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFkYVFDFHAEDVFWCTADIGWiTGHSYVT-YGPLANGATSVLFegi 303
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 304 pTYP--DVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTvGEPINPEAwlwYHQVVGAQRCPIVD 381
Cdd:cd05974 159 -NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQVRRAWGLTIRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 382 TFWQTETgghmlTPLPGATP---MKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWP-GIMRTVYGNHERfetT 457
Cdd:cd05974 231 GYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvGLMKGYAGDPDK---T 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 458 YFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 537
Cdd:cd05974 302 AHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRA 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622836714 538 GHTFSPKLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 589
Cdd:cd05974 382 GYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-586 |
1.44e-47 |
|
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: 172.48 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 39 TQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsscslLIT 118
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 119 TDAFYRGEKLvnlKELADEAlqkcqekdfpvRCCIVVKhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpqis 198
Cdd:cd05934 58 INTALRGDEL---AYIIDHS-----------GAQLVVV------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 199 wnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTAD 276
Cdd:cd05934 82 ----------------------------DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLP 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvlgTV 356
Cdd:cd05934 131 LFHINAQAVSVLAALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AY 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 357 GEPINPEAWLWYHQVVGaqrCPIVDTFWQTETGGHMLTPLPGATPmkPGSATFPFFGVAPAILNESGEELEGEAEGYLVF 436
Cdd:cd05934 203 GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVI 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 437 K-QPWPGIMRTVYGNHErfETTyfKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 514
Cdd:cd05934 278 RgLRGWGFFKGYYNMPE--ATA--EAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRE 353
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622836714 515 AAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05934 354 AAVVAVPDEVGEDEVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
24-587 |
1.41e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 172.04 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 103
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 LCeRILDSSCSLLITTDAfyrgeklvNLKELADEALQKCQEKDFPVRCcivvkhlgraELGMGDSPSqsppikrscpdvq 183
Cdd:PRK08316 100 LA-YILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSL----------VLGGREAPG------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 184 gklkekskrvqpqiSWnQGIDLWwhelmQEAGDECEPE-WCDAEDPLFILYTSGSTGKPKGVVHT----VGGYMLYVATT 258
Cdd:PRK08316 148 --------------GW-LDFADW-----AEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVAG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 259 fkyvfDFHAEDVFWCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTA-IRL 333
Cdd:PRK08316 208 -----DMSADDIPLHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 334 LmkfgdepvtKH---SRASLQVL--GTVGEPINPEAWLWYHQvvgaQRCPIVdTFW----QTETGghmltplPGATPM-- 402
Cdd:PRK08316 275 L---------RHpdfDTRDLSSLrkGYYGASIMPVEVLKELR----ERLPGL-RFYncygQTEIA-------PLATVLgp 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 403 -----KPGSATFPFFGVAPAILNESGEELEgeaegylvfkqpwPGIMRTVYGNHERFETTYFKKfP---------GYYVT 468
Cdd:PRK08316 334 eehlrRPGSAGRPVLNVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-PektaeafrgGWFHS 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 469 GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEE 548
Cdd:PRK08316 400 GDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DE 476
|
570 580 590
....*....|....*....|....*....|....*....
gi 1622836714 549 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
7-587 |
1.45e-44 |
|
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: 166.17 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 7 NICYNVLDRNVHEKKlGDKVAFYwegnepGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 86
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 87 RIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmg 166
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 167 dspsqsPPIKrscpDVQGKLKEKSKRVQPQISWNQGIDLwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVH 246
Cdd:TIGR02262 114 ------PVIK----AALGKSPHLEHRVVVGRPEAGEVQL--AELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 247 TVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLWSIVDKYKVTKFYT 326
Cdd:TIGR02262 182 THSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFDRLRRHQPTIFYG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 327 APTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQrcpIVDTFWQTETGGHMLTPLPGAtpMKPGS 406
Cdd:TIGR02262 259 VPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 407 ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRI 486
Cdd:TIGR02262 332 SGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 487 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHTfspKLTEELKKQIREKIGPIATP 563
Cdd:TIGR02262 407 DDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYP 480
|
570 580
....*....|....*....|....
gi 1622836714 564 DYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:TIGR02262 481 RWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-581 |
7.74e-43 |
|
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: 160.84 E-value: 7.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 116
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITTDAFYrgeklvnlkeladEALQKCQEKDFPVRCCIVvkhlgraelgMGDSPSQSPPIkrscpdvqgklkekskrvqpq 196
Cdd:cd05911 87 FTDPDGL-------------EKVKEAAKELGPKDKIIV----------LDDKPDGVLSI--------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 iswnqgIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVV--HTVGGYMLYVATTFKYVfDFHAEDVFWCT 274
Cdd:cd05911 123 ------EDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 275 ADIGWITG-HSYVTYgpLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVL 353
Cdd:cd05911 196 LPLYHIYGlFTTLAS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 354 GTVGEPINPEAWLWYHQVvgAQRCPIVDTFWQTETGGhMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEaegy 433
Cdd:cd05911 268 LSGGAPLSKELQELLAKR--FPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGP---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 434 lvfKQP---W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 507
Cdd:cd05911 340 ---NEPgeiCvrgPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 508 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsPKLTE-ELKKQIREKIgpiatPDY------IQNAPGLPKTRSGKI 580
Cdd:cd05911 415 EHPGVADAAVIGIPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPKSASGKI 485
|
.
gi 1622836714 581 M 581
Cdd:cd05911 486 L 486
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-585 |
1.45e-39 |
|
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: 150.76 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERIL----DSS 112
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 113 CSLLITtdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskr 192
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 193 vqpqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFW 272
Cdd:cd05930 91 -------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVL 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 273 CTADIGWItGHSYVTYGPLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVtkhsRASL 350
Cdd:cd05930 139 QFTSFSFD-VSVWEIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 351 QVLGTVGEPINPEAWLWYHQVVGAQR---------CPIVDTFWQTETGGHMLTPLPGATPMkPGSATFpffgvapaILNE 421
Cdd:cd05930 211 RLVLVGGEALPPDLVRRWRELLPGARlvnlygpteATVDATYYRVPPDDEEDGRVPIGRPI-PNTRVY--------VLDE 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 422 SGeelegeaegylvfkQPWP------------GIMRTVYGNHE----RFETTYFkkFPG--YYVTGDGCRRDQDG--YYw 481
Cdd:cd05930 282 NL--------------RPVPpgvpgelyiggaGLARGYLNRPEltaeRFVPNPF--GPGerMYRTGDLVRWLPDGnlEF- 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 iTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIA 561
Cdd:cd05930 345 -LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDYM 420
|
570 580
....*....|....*....|....
gi 1622836714 562 TPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd05930 421 VPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
41-605 |
2.29e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 153.19 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAcariGALHSIVFA---GFSSESLCErildsscsLLI 117
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 118 TTDAfyrgEKLVNLKELAD-EALQKCQEKdfpVRCCIVVKHLGRAELGMGDSPSQSPPIKRSCPDVQGKLkekskrvqpq 196
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGtDIWQKVAEV---LAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARI---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 ISWNQgidlwwhELMQEAGDECE-PEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTA 275
Cdd:PRK07529 190 LDFDA-------ELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 276 DIGWITGhSYVT-YGPLANGAtSVLFEGIPTYPD---VNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQ 351
Cdd:PRK07529 262 PLFHVNA-LLVTgLAPLARGA-HVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 352 VLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTE-TGGHMLTPLPGatPMKPGSA--TFPFFGVAPAILNESGEELEG 428
Cdd:PRK07529 337 YALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 429 EAEG---YLVFKQP--WPGIMRTVYGNHERFEttyfkkfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 503
Cdd:PRK07529 412 CAVDevgVLCIAGPnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 504 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIREkigPIATPDYIQNAPGLPKTRSGKI-- 580
Cdd:PRK07529 485 EALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEaELLAFARDHIAE---RAAVPKHVRILDALPKTAVGKIfk 561
|
570 580 590
....*....|....*....|....*....|...
gi 1622836714 581 -------MRRVLRK-IAQNDHDLGDTSTVADPS 605
Cdd:PRK07529 562 palrrdaIRRVLRAaLRDAGVEAEVVDVVEDGR 594
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
20-587 |
2.12e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 148.51 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAfYWEGNEpgettQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 99
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 100 SSESLCERILDSSCSLLITTDAFyrgeklvnlkeladealqkcqekdfpvrccivvkhLGRAELGMGDSPSQSppIKRSC 179
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLF-----------------------------------LGVDYSATTRLPALE--HVVIC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 180 PDVQGK-LKEKSKRvqpqiswnqgidlwWHELMQEA-GDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGG-YMLY-- 254
Cdd:PRK07656 133 ETEEDDpHTEKMKT--------------FTDFLAAGdPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSNAad 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 255 VATTFKYVFD---------FHaedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFY 325
Cdd:PRK07656 198 WAEYLGLTEGdrylaanpfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 326 TAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDT-FWQTETGGHM-LTPLPGATPMK 403
Cdd:PRK07656 261 GPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASMPVALLERFESELG---VDIVLTgYGLSEASGVTtFNRLDDDRKTV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 404 PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWIT 483
Cdd:PRK07656 336 AGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIV 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 484 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspkLTEE-LKKQIREKIGPIAT 562
Cdd:PRK07656 412 DRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE----LTEEeLIAYCREHLAKYKV 487
|
570 580
....*....|....*....|....*
gi 1622836714 563 PDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK07656 488 PRSIEFLDELPKNATGKVLKRALRE 512
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
40-590 |
2.01e-37 |
|
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: 146.06 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHsiVFAGFS---SE--SLCERildSSCS 114
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrrAEisHFAEQ---SEAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 LLITTDAfYRGeklVNLKELADEALQKCQEkdfpVRCCIVVkhlgraelgmGDSpsqsppikrscpdvqgklkekskrvQ 194
Cdd:COG1021 125 AYIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV----------GDA-------------------------G 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 PQISWNqgidlwwhELMQEAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCT 274
Cdd:COG1021 162 EFTSLD--------ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 275 ADIGwitgHSY-----VTYGPLANGATSVLfegIPTyPDVNRLWSIVDKYKVTkfYTA--PTAIRLLMKFGDEpvTKHSR 347
Cdd:COG1021 232 LPAA----HNFplsspGVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 348 ASLQVLGTVGEPINPEA----------WLwyHQVVG--------------------AQRCP--------IVDtfwqtETG 389
Cdd:COG1021 300 SSLRVLQVGGAKLSPELarrvrpalgcTL--QQVFGmaeglvnytrlddpeeviltTQGRPispddevrIVD-----EDG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 390 ghmlTPLPgatpmkPGSAtfpffGVapailnesgeelegeaegyLVFKQPWpgimrTVYGnherfettYFKKfP------ 463
Cdd:COG1021 373 ----NPVP------PGEV-----GE-------------------LLTRGPY-----TIRG--------YYRA-Pehnara 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 ----GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycFVTLcD 537
Cdd:COG1021 405 ftpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-R 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836714 538 GHTFSPKlteELKKQIREKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 590
Cdd:COG1021 482 GEPLTLA---ELRRFLRER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
72-586 |
4.12e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 141.88 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 72 MPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALqkcqekdfPVRC 151
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAA--------PAKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 152 cIVVKHLGRaelgmgdspsqsppikrscpDVQGKLKEKskrvqpqiswnqgiDLWWHELMQEA-------GDECEPEWCD 224
Cdd:PLN03051 73 -IVLPAAGE--------------------PVAVPLREQ--------------DLSWCDFLGVAaaqgsvgGNEYSPVYAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 225 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIP 304
Cdd:PLN03051 118 VESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 305 TYPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQRcPIVDTFW 384
Cdd:PLN03051 196 LGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 385 QTETGGHML--TPLpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTVYGNHERfetTYF 459
Cdd:PLN03051 272 GTELASGYIssTLL---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADHDK---VYY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 460 KKFPGYYVTGDGCRRDQD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPVKG-ECLY 530
Cdd:PLN03051 346 KGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpELLV 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 531 CFVTLCD-GHTFSPKLTEELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PLN03051 426 IFLVLGEeKKGFDQARPEALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
6-585 |
2.39e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 140.48 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 6 TNICYNVldrNVHEKKLGDKVAFYWEGNEpgettqITYHELLVQVCQFSNVL-RKQGIQKGDRVAIYMPMIPELVVAMLA 84
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 85 CARIGALHSIVFAGFSSESLCERILDSSCSLLITTDafyrgeklvnlkELADEALQkcQEKDFPVRCCIVVKhlgraelg 164
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS------------ELAPKVAP--AVGNLRLRHVIVAQ-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 165 MGDSPSQSPPIK-----RSCPDVQGKLKEKSkrvqpqISWNQGIDlwwhelmqeAGDECEPEWCDAEDPLFILYTSGSTG 239
Cdd:PRK08314 139 YSDYLPAEPEIAvpawlRAEPPLQALAPGGV------VAWKEALA---------AGLAPPPHTAGPDDLAVLPYTSGTTG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 240 KPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKY 319
Cdd:PRK08314 204 VPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DREAAARLIERY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 320 KVTKFYTAPT-AIRLLMKFGdepVTKHSRASLQVLGTVGEPInPEAwlwyhqvVgAQR------CPIVDTFWQTETGGHM 392
Cdd:PRK08314 279 RVTHWTNIPTmVVDFLASPG---LAERDLSSLRYIGGGGAAM-PEA-------V-AERlkeltgLDYVEGYGLTETMAQT 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 393 LTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTVYGNHERFETTyFKKFPG--YYVT 468
Cdd:PRK08314 347 HSNPPDRP--KLQCLGIPTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRT 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 469 GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlTEE 548
Cdd:PRK08314 421 GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEE 499
|
570 580 590
....*....|....*....|....*....|....*..
gi 1622836714 549 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK08314 500 IIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
224-585 |
3.74e-34 |
|
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: 135.13 E-value: 3.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVVHTVGGYM-LYVATTfkYVFDFHAEDVfwctadigWITGHSYV-------TYGPLANGA 295
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 296 TSVlfegIPTYpDVNR----LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPeAWL--WYh 369
Cdd:cd17643 161 RLV----VVPY-EVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEA-AMLrpWA- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 370 QVVGAQRCPIVDTFWQTETGGHM----LTP--LPGATpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGI 443
Cdd:cd17643 232 GRFGLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 444 MRTVYGNHERFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 521
Cdd:cd17643 311 LGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVRE 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 522 HPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVL 585
Cdd:cd17643 390 DEPGDTRLVAYVVADDGAAADI---AELRALLKELL-----PDYMVPAryvplDALPLTVNGKLDRAAL 450
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
3-587 |
3.31e-33 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 135.59 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 3 GASTNICYNVLDRNVHEKklGDKVAFYW--EGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVV 80
Cdd:PLN03052 171 GAVLNVAECCLTPKPSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 81 AMLAcarigalhsIVFAG---------FSSESLCERILDSSCSLLITTDAFYRGEKlvnlkeladealqkcqekDFPVRC 151
Cdd:PLN03052 249 IYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGK------------------SIPLYS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 152 CIVvkhlgraelgmgdsPSQSP-----PIKRSCPDVQgkLKEKskrvqpqiswnqgiDLWWHELMQEA-----GDECEPE 221
Cdd:PLN03052 302 RVV--------------EAKAPkaivlPADGKSVRVK--LREG--------------DMSWDDFLARAnglrrPDEYKAV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 222 WCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVF-WCTaDIGWITGHsYVTYGPLANGATSVLF 300
Cdd:PLN03052 352 EQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALY 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 301 EGIPTYPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGdePVTKHSRASLQVLGTVGEPINPEAWLWYhqVVGAQRCPIV 380
Cdd:PLN03052 429 NGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWL--MSRAGYKPII 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 381 DTFWQTETGGHMLTplpgATPMKPGS-ATF--PFFGVAPAILNESGeelegeaegylvfkQPWP---------------- 441
Cdd:PLN03052 502 EYCGGTELGGGFVT----GSLLQPQAfAAFstPAMGCKLFILDDSG--------------NPYPddapctgelalfplmf 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 442 GIMRTVY-GNHERfetTYFKKFPGYYVT-----GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE----SAlveHEA 511
Cdd:PLN03052 564 GASSTLLnADHYK---VYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DES 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 512 VAEAAVVGHPHPVKG-ECLYCFVTLCDGHTFSPKLtEELKK----QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PLN03052 638 VLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLR 716
|
.
gi 1622836714 587 K 587
Cdd:PLN03052 717 Q 717
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
20-587 |
1.84e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 131.70 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAFYWegnepGETTqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGf 99
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA----VWVP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 100 sseslcerildsscsllittdafyrgeklVNLKELADEalqkcqekdfpvrccivVKHLG-----RAELGMGDSPSQSPP 174
Cdd:PRK07470 87 -----------------------------TNFRQTPDE-----------------VAYLAeasgaRAMICHADFPEHAAA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 175 IKRSCPDVQGKLKEKSKRVQPQISwnqgidlwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLY 254
Cdd:PRK07470 121 VRAASPDLTHVVAIGGARAGLDYE---------ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 255 VATTfkyvfdfHAEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLfegIPTYP-DVNRLWSIVDKY 319
Cdd:PRK07470 191 VITN-------HLADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERH 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 320 KVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAQrcpIVDTFWQTETGGHMlTPLPGA 399
Cdd:PRK07470 254 RVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 400 ------TPM-KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEttyfKKF-PGYYVTGDG 471
Cdd:PRK07470 328 lhdaedGPDaRIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGP--AVFAGYYNNPEANA----KAFrDGWFRTGDL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 472 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKK 551
Cdd:PRK07470 402 GHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLA 478
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622836714 552 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK07470 479 WLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
233-589 |
2.36e-32 |
|
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: 128.37 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 233 YTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPD--- 308
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 309 VNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKhSRASLQVLGTVGEPINPEAwlwYHQVVGAQRCPIVDTFWQTE- 387
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 388 TGGHMLTPlPGaTPMKPGSA--TFPFFGVAPAILNESGEELEGEAEGYLvfkqpWPGIM--RTVYGNH---ERFETTYFK 460
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVglRLPYARVRIKVLDGVGRLLRDCAPDEV-----GEICVagPGVFGGYlytEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 461 kfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 540
Cdd:cd05944 232 --DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622836714 541 FSP-KLTEELKKQIREKigpIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 589
Cdd:cd05944 310 VEEeELLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
41-585 |
5.81e-32 |
|
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: 129.66 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 120
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 AfyrgeklvNLKELADEALQkcqekdfpvrccIVVkhLGRAElgmGDSPSQSPPIKRSCPDvqgklkeksKRVQPQISwn 200
Cdd:cd05904 113 E--------LAEKLASLALP------------VVL--LDSAE---FDSLSFSDLLFEADEA---------EPPVVVIK-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 qgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYmlyVATTFKYVFDF----HAEDVFWCTAD 276
Cdd:cd05904 157 ------------------------QDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTV 356
Cdd:cd05904 210 MFHIYGLSSFALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 357 GEPINPEawlwyHQVVGAQRCPIVDtFWQ----TETGG--HMlTPLPGATPMKPGSATFPFFGVAPAILNESGEELegea 430
Cdd:cd05904 284 AAPLGKE-----LIEAFRAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES---- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 431 egyLVFKQP---W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 504
Cdd:cd05904 353 ---LPPNQTgelWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 505 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGP------IATPDYIqnapglPKTRSG 578
Cdd:cd05904 428 LLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTED---EIMDFVAKQVAPykkvrkVAFVDAI------PKSPSG 498
|
....*..
gi 1622836714 579 KIMRRVL 585
Cdd:cd05904 499 KILRKEL 505
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
42-517 |
1.01e-30 |
|
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: 124.69 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLITT 119
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 120 DAFyrgeklvnlkeladealqkCQEKDFPVRCCIVVkhLGRAELGMGDSPSQSPPIKRSCPDvqgklkekskrvqpqisw 199
Cdd:TIGR01733 80 SAL-------------------ASRLAGLVLPVILL--DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 200 nqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVfwctadigW 279
Cdd:TIGR01733 121 ---------------------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------V 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 280 ITGHSYV-------TYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTkhSRASLQV 352
Cdd:TIGR01733 165 LQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 353 LGTVGEPINPEAWLWYHQVVGAQRcpIVDTFWQTETG---GHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelege 429
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPGAR--LINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 430 aegylvfkQPWP------------GIMRtvyGNHERFETT--YFKKFPGY-------YVTGDGCRRDQDGYYWITGRIDD 488
Cdd:TIGR01733 312 --------RPVPvgvvgelyiggpGVAR---GYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDD 380
|
490 500
....*....|....*....|....*....
gi 1622836714 489 MLNVSGHLLSTAEVESALVEHEAVAEAAV 517
Cdd:TIGR01733 381 QVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
24-590 |
1.40e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 126.31 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 103
Cdd:PRK06178 48 QRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 LCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKCqekdfPVRCCIVVkhlgraelGMGD----SPSQSPPIKRSC 179
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA---------PVVEQVRAET-----SLRHVIVT--------SLADvlpaEPTLPLPDSLRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 180 PdvqgklkekskRVQPQiswnqgidlWWHELMQEAGDECEP---EWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVA 256
Cdd:PRK06178 180 P-----------RLAAA---------GAIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHT-QRDMVYTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 257 TTFKYVFDFHAED-VFWCTADIGWITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTK-FYTAPTAIRLL 334
Cdd:PRK06178 239 AAAYAVAVVGGEDsVFLSFLPEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 335 mkfgDEP-VTKHSRASLQVLGTVG--EPINPEAWLWYHQVVGaqrCPIVDTFW-QTET------------GGHMLT---- 394
Cdd:PRK06178 315 ----DHPrFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTEThtcdtftagfqdDDFDLLsqpv 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 395 ----PLPGA----TPMKPGsATFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTVYGNHERFETTYF 459
Cdd:PRK06178 388 fvglPVPGTefkiCDFETG-ELLPL-GAegeivvrTPSLL--------------------------KGYWNKPEATAEAL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 460 KKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGH 539
Cdd:PRK06178 440 RD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA 517
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1622836714 540 TFSPkltEELKKQIREKIGPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 590
Cdd:PRK06178 518 DLTA---AALQAWCRENMAVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
24-586 |
1.62e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 125.87 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWegnepGETTqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM----LACARIGALHSIVfagf 99
Cdd:PRK06188 27 DRPALVL-----GDTR-LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIgaaqLAGLRRTALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 100 SSESLCERILDSSCSLLITTDAFYRgeklvnlkELADEALQKCQEkdfpvrccivVKHLgraeLGMGDSPSqsppikrsc 179
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPVPD--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 180 pdvqgklkekskrvqpqiswnqGIDLWwhelmqEAGDECEPE----WCDAEDPLFILYTSGSTGKPKGVVHTVGGYmlyv 255
Cdd:PRK06188 146 ----------------------GVDLL------AAAAKFGPAplvaAALPPDIAGLAYTGGTTGKPKGVMGTHRSI---- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 256 aTTFkyvfdfhaedVFWCTADIGWITGHSYVTYGPLANGATS----VLFEGIPTYP----DVNRLWSIVDKYKVTKFYTA 327
Cdd:PRK06188 194 -ATM----------AQIQLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGGTVIVlakfDPAEVLRAIEEQRITATFLV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 328 PTAIRLLMKFGDepVTKHSRASLQVLGTVGEPINP----EAwlwyHQVVGaqrcPI-VDTFWQTETGgHMLTPLP----- 397
Cdd:PRK06188 263 PTMIYALLDHPD--LRTRDLSSLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhd 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 398 GATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETT--YFKKfpGYYVTGDGCRRD 475
Cdd:PRK06188 332 PDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVARED 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 476 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIRE 555
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKE 481
|
570 580 590
....*....|....*....|....*....|.
gi 1622836714 556 KIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK06188 482 RKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
23-587 |
4.13e-30 |
|
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: 124.67 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 23 GDKVAFYWEGnePGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LHSI---VFAg 98
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 99 fsseslcERILdsscslLITTDAfyrGEKLVnlkeLADEALQKCQEkdfpvrccivvkhlgraelgmgdspsqspPIKRS 178
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLE-----------------------------AIAPR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 179 CPDVQGKLKEKSKRVQPQISWNQGIDlWWHELMQEAGDECEPEWcDAEDPLFILYTSGSTGKPKGVV--------HTVGG 250
Cdd:cd12119 118 LPTVEHVVVMTDDAAMPEPAGVGVLA-YEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVVyshrslvlHAMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 251 YMlyvattfKYVFDFHAEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdvnrLWSIVDKY 319
Cdd:cd12119 196 LL-------TDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIERE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 320 KVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhqVVGAQRCP----------IVDTF--W-QT 386
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 387 ETG--GHMLTPLPGATPMKPG-------SATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHErfe 455
Cdd:cd12119 315 ETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKNDE--- 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 456 TTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 535
Cdd:cd12119 390 ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVL 469
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1622836714 536 CDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd12119 470 KEGATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-586 |
1.42e-29 |
|
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: 122.45 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCSL 115
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITTDAFYRGEklvnlkeLADEAlqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqp 195
Cdd:cd17651 95 LVLTHPALAGE-------LAVEL--------------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 196 qiswnqGIDLWWHELMQEAGDECEPEW-CDAEDPLFILYTSGSTGKPKGVV------------HTVGGYMLYVATTFKYV 262
Cdd:cd17651 111 ------VAVTLLDQPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 263 ---FDFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegIPTY--PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF 337
Cdd:cd17651 185 glgFDVSVQEIF-----------------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 338 GDEPVTKHsrASLQVLGTVGEPINPEAWL--WYHQVVGAQrcpIVDTFWQTET---GGHMLTPLPGATPMKPGSATfPFF 412
Cdd:cd17651 245 GRPLGVRL--AALRYLLTGGEQLVLTEDLreFCAGLPGLR---LHNHYGPTEThvvTALSLPGDPAAWPAPPPIGR-PID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 413 GVAPAILNEsgeelegeaegylvFKQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCRRDQ 476
Cdd:cd17651 319 NTRVYVLDA--------------ALRPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLP 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 477 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREK 556
Cdd:cd17651 385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAALATH 461
|
570 580 590
....*....|....*....|....*....|
gi 1622836714 557 IGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
42-587 |
1.56e-29 |
|
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: 121.72 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsSCSLLittdA 121
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV--------------------TNPIL----P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 FYRGEKLVNLkeladeaLQKCQEKDFpvrccIVVKHLGRAE-LGMGDSPSQsppikrscpdvqgklkekskrvqpqiswn 200
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVF-----VVPERFRQFDpAAMPDAVAL----------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 qgidlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVHTVGGYMlyvATTFKYV--FDFHAEDVFWCTADIG 278
Cdd:cd05903 98 ------------------------------LLFTSGTTGEPKGVMHSHNTLS---ASIRQYAerLGLGPGDVFLVASPMA 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 279 WITGHSYVTYGPLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMK---FGDEPVtkhsrASLQVLGT 355
Cdd:cd05903 145 HQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVC 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 356 VGEPINP----EAWlwyhQVVGAQRCPIvdtFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAE 431
Cdd:cd05903 216 GGATVPRslarRAA----ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 432 GYLVFKQPwpgimRTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 511
Cdd:cd05903 289 GELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPG 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 512 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-PKLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05903 364 VIEAAVVALPDERLGERACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
24-588 |
1.87e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 121.99 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhSIVFAG--FSS 101
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 102 ESLCERILDSSCSLLITTDAFyrgeklvnlkeladealqkcQEKDFPvrccivvkhlgraelgmgdspsqsppikrscpd 181
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF--------------------EAKLIP--------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 182 vqgklkekskrvqpqiswnqGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFK 260
Cdd:PRK03640 116 --------------------GISVKFAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 261 YVFDFHAEDVFWCTADIGWITGHSYVTygplangaTSVLFeGIPTY-------PDVNRLwsIVDKyKVTKFYTAPTAI-R 332
Cdd:PRK03640 175 LNLGLTEDDCWLAAVPIFHISGLSILM--------RSVIY-GMRVVlvekfdaEKINKL--LQTG-GVTIISVVSTMLqR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 333 LLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhQVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFF 412
Cdd:PRK03640 243 LLERLGEGTYPSSFRCML--LG--GGPA-PKPLL---EQCKEKGIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLF 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 413 GVAPAILNESGEELEGEAEGYLVfKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCRRDQDGYYWITGRIDDML 490
Cdd:PRK03640 315 PCELKIEKDGVVVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 491 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSpklTEELKKQIREKIGPIATPDYIQNAP 570
Cdd:PRK03640 387 ISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT---EEELRHFCEEKLAKYKVPKRFYFVE 461
|
570
....*....|....*...
gi 1622836714 571 GLPKTRSGKIMRRVLRKI 588
Cdd:PRK03640 462 ELPRNASGKLLRHELKQL 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
42-586 |
3.47e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.45 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 121
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 FYRGE-KLVNLKELADEAlqKCQEkdfpvrccivvkhlgraelgmgdsPSQSPPIkrscpdvqgklkekskrvqpqiswn 200
Cdd:PRK09088 104 VAAGRtDVEDLAAFIASA--DALE------------------------PADTPSI------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 qgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTAD---- 276
Cdd:PRK09088 133 -----------------------PPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhi 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 IGWITGHSYVtygpLANGATSVLFEGIPTYPDVNRLWSIvdKYKVTKFYTAPtaiRLLMKFGDEPVTKHSR-ASLQVLGT 355
Cdd:PRK09088 189 IGLITSVRPV----LAVGGSILVSNGFEPKRTLGRLGDP--ALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFT 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 356 VGEPiNPE----AWLwyhqvvgAQRCPIVDTFWQTETGGHMLTPL-PGATPMKPGSATFPFFGVAPAILNESGEELEGEA 430
Cdd:PRK09088 260 GGAP-HAAedilGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 431 EGYLVFKQP--WPGIMRTVYGNHERFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 508
Cdd:PRK09088 332 PGELLLRGPnlSPGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLAD 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622836714 509 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK09088 406 HPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
41-585 |
5.53e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 121.68 E-value: 5.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 120
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 AFYrgEKLVNLKELAD-EALQKCQEKDF-PVrccivvkhlgraelgmgdspsqspPIKRSCPDVQgklkEKSKRVQPQIS 198
Cdd:PRK06710 130 LVF--PRVTNVQSATKiEHVIVTRIADFlPF------------------------PKNLLYPFVQ----KKQSNLVVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 199 WNQGIDLWwhELMQEAGDECEPEWCDAEDPLFIL-YTSGSTGKPKGVVHTVGGYMLYVATTFKYVFD-FHAEDVFWCTAD 276
Cdd:PRK06710 180 ESETIHLW--NSVEKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTK-HSRASLQVLGT 355
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 356 VGEPINPEAWLWYHQVVGAQrcpIVDTFWQTETgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAE 431
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 432 G-YLVFKQPwpGIMRTVYGNHErfETTYFKKfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 510
Cdd:PRK06710 403 IgEIVVKGP--QIMKGYWNKPE--ETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622836714 511 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK06710 478 KVQEVVTIGVPDPYRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
24-592 |
9.25e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 120.93 E-value: 9.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 103
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 LCERILDSSCSLLITTDAFyRG---EKLVNlkELADE--ALQKcqekdfpvrccIVVkhlgraeLGMGDSPS----QSPP 174
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF-RGfdhAAMAR--RLRPElpALRH-----------VVV-------VGGDGADSfealLITP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 175 IKRSCPDVQGKLKekskRVQPqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHT----VGG 250
Cdd:PRK13295 178 AWEQEPDAPAILA----RLRP----------------------------GPDDVTQLIYTSGTTGEPKGVMHTantlMAN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 251 YMLYVATtfkyvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDVNRLWSIVDKYKVTkFYTAPTA 330
Cdd:PRK13295 226 IVPYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 331 irLLMKFGDepVTKHSR---ASLQVLGTVGEPINP----EAWlwyhQVVGAQrcpIVDTFWQTETGGHMLTpLPGATPMK 403
Cdd:PRK13295 296 --FLTDLTR--AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDER 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 404 pGSAT--FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVYGNHERFETTYFKKFPGYYVTGDGCRRDQDGYYW 481
Cdd:PRK13295 364 -ASTTdgCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIR 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-PKLTEELKKQireKIGPI 560
Cdd:PRK13295 437 ISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQ 513
|
570 580 590
....*....|....*....|....*....|..
gi 1622836714 561 ATPDYIQNAPGLPKTRSGKIMRRVLRKIAQND 592
Cdd:PRK13295 514 YIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
501-579 |
1.28e-28 |
|
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: 108.79 E-value: 1.28e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 501 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
41-587 |
1.90e-28 |
|
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: 119.50 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 120
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 AFYRgeklvnlkeLADEALQKCqekdfpvrccivvkHLGRAELGMGDSPSQSPPIKRSCPdvqgklkekskrvqpqISWN 200
Cdd:TIGR03098 106 ERLD---------LLHPALPGC--------------HDLRTLIIVGDPAHASEGHPGEEP----------------ASWP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 QgidlwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT----VGGymlyvATTFKYVFDFHAEDVFWCTAD 276
Cdd:TIGR03098 147 K---------LLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLShrnlVAG-----AQSVATYLENRPDDRLLAVLP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 IGWITGHSYVTYGpLANGATSVLFEgiptYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTV 356
Cdd:TIGR03098 213 LSFDYGFNQLTTA-FYVGATVVLHD----YLLPRDVLKALEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 357 GEPINPEawlwyhqVVGAQRC--PIVDTFWQ---TETGGHMLTPlPGATPMKPGS--ATFPFFGVapAILNESGEELEGE 429
Cdd:TIGR03098 285 GGAMPRA-------TLSRLRSflPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEV--LVLREDGSECAPG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 430 AEGYLVFKQP------WPGIMRTVygnhERFE-TTYFK---KFPGYYV-TGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 498
Cdd:TIGR03098 355 EEGELVHRGAlvamgyWNDPEKTA----ERFRpLPPFPgelHLPELAVwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 499 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSG 578
Cdd:TIGR03098 431 PTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANG 507
|
....*....
gi 1622836714 579 KIMRRVLRK 587
Cdd:TIGR03098 508 KIDRKALAK 516
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
40-585 |
3.08e-28 |
|
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: 118.16 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 118
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 119 TDAfyrgeklvnlkeLADealqkcqekdfPVRCCIVVKHLGRAELGMGDSPSQSPPikrscpdvqgklkekskrvqpqis 198
Cdd:cd12116 91 DDA------------LPD-----------RLPAGLPVLLLALAAAAAAPAAPRTPV------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 199 wnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGY------------------MLYVATtfk 260
Cdd:cd12116 124 -------------------------SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnflhsmrerlglgpgdrLLAVTT--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 261 YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDE 340
Cdd:cd12116 176 YAFDISLLELLL-----------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 341 PvtkhsRASLQVL-GtvGEPINPEawlwyhqvVGAQRCPIVDTFWQ----TETgghmlTPLPGATPMKPGSATFPffgVA 415
Cdd:cd12116 238 G-----RAGLTALcG--GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 416 PAILNESGeelegeaegYLV--FKQPWP-GIMRTVY--------GNHERFETTyFKKF-------PG--YYVTGDGCRRD 475
Cdd:cd12116 295 RPLANTQV---------YVLdaALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRR 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 476 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSpklTEELKKQIRE 555
Cdd:cd12116 365 ADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRA 440
|
570 580 590
....*....|....*....|....*....|
gi 1622836714 556 KIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd12116 441 TLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
12-587 |
5.60e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 118.56 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 12 VLDRNVHEkkLGDKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA- 90
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 91 --LHSIVFAGFSSESLCErilDSSCSLLITTDafyrgeKLVN-LKELADealqkcqekDFPVRCCIVVkhlgraelgmgD 167
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFE---DHGARVAIVWD------KVAPtVERLRR---------TTPLETIVSV-----------N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 168 SPSQSPPIKRscpdVQGKL---KEKSKRVQPQISWNQGIDlwWHELMQEA----GDECEPEWCDAEDPLFILYTSGSTGK 240
Cdd:PRK05605 160 MIAAMPLLQR----LALRLpipALRKARAALTGPAPGTVP--WETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 241 PKGVVHTVGGYMLYVATTFKYVFD--------------FHAEDVFWCtadigwitghsyVTYGPLAnGATSVLFegiPTy 306
Cdd:PRK05605 234 PKGAQLTHRNLFANAAQGKAWVPGlgdgpervlaalpmFHAYGLTLC------------LTLAVSI-GGELVLL---PA- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 307 PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEP-VTKHS-RASLQvlgtvgepinpeawlwyhqvvGAQRCPiVDTF- 383
Cdd:PRK05605 297 PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS---------------------GAMALP-VSTVe 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 384 -WQTETGGHM-----LT---PLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTVY 448
Cdd:PRK05605 355 lWEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFK 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 449 GNHERFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 528
Cdd:PRK05605 430 GYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 529 LYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK05605 510 VVAAVVLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-586 |
1.24e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 116.39 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 226 EDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGi 303
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTND- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 304 pTYPDVNrLWSIVDKYKVTKFYTAPTAIRLL--MKFGDEPVtkhsrASLQVLGTVGEPInPEAWL--WYHQVVGAQrcpI 379
Cdd:cd05922 192 -GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIarLRELLPGAQ---V 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 380 VDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTvYGNHERFETTYf 459
Cdd:cd05922 261 YVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPYRRKE- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 460 KKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGH 539
Cdd:cd05922 337 GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKI 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622836714 540 TFSPklteeLKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05922 416 DPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
24-585 |
1.35e-27 |
|
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: 116.19 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 103
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 LcERILD-SSCSLLITTDAfyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdv 182
Cdd:cd05945 80 I-REILDaAKPALLIADGD------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 183 qgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYv 262
Cdd:cd05945 98 --------------------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 263 FDFHAEDVFWCTA---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdvnrlwsivdkykV 321
Cdd:cd05945 133 FPLGPGDVFLNQApfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------I 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMkfGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWyHQVvgAQRCPIVDTFWQTET----GGHMLTP 395
Cdd:cd05945 190 TVWVSTPSFAAMCL--LSPTFTPESLPSLrHFL-FCGEVLpHKTARAL-QQR--FPDARIYNTYGPTEAtvavTYIEVTP 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 396 LPGATpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRtVYGNHERFettyFKKFPGY--YVTGDG 471
Cdd:cd05945 264 EVLDG-YDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLN-NPEKTAAA----FFPDEGQraYRTGDL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 472 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFspKLTEELKK 551
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA--GLTKAIKA 415
|
570 580 590
....*....|....*....|....*....|....
gi 1622836714 552 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd05945 416 ELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
40-585 |
1.83e-27 |
|
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: 115.27 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 119
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 120 dafyrgeklvnlKELADEALqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpqisw 199
Cdd:cd05935 81 ------------SELDDLAL------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 200 nqgidlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGW 279
Cdd:cd05935 89 -------------------------------IPYTSGTTGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFH 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 280 ITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEP 359
Cdd:cd05935 137 VTGFVGSLNTAVYVGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 360 INPEAWLWYHQVVGAQrcpIVDTFWQTETgghmLTPLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEG-YLVF 436
Cdd:cd05935 211 MPPAVAEKLLKLTGLR---FVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDIETGRELPPNEVgEIVV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 437 KQPwpGIMRTvYGNHERFETTYFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 514
Cdd:cd05935 284 RGP--QIFKG-YWNRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622836714 515 AAVVGHPHPVKGECLYCFVTLCDGhtFSPKLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd05935 361 VCVISVPDERVGEEVKAFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
23-585 |
3.26e-27 |
|
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: 115.45 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 23 GDKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 102
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 103 SLCERILDSSCSLLITT-DAFYRGEKLVNLKELADEALqkcqekdfpvrccivvkhlgraelgmgDSPSQSPPIKRSCPD 181
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL---------------------------AAPPATPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 182 vqgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATT 258
Cdd:cd17646 139 ---------------------------------------------NLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQDE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 259 FK------------YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFE----GIPTYpdvnrLWSIVDKYKVT 322
Cdd:cd17646 174 YPlgpgdrvlqktpLSFDVSVWELFW-----------------PLVAGARLVVARpgghRDPAY-----LAALIREHGVT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 KFYTAPTAIRLlmkFGDEPvTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTET----------GGHM 392
Cdd:cd17646 232 TCHFVPSMLRV---FLAEP-AAGSCASLRRVFCSGEALPPELAARFLALPGA---ELHNLYGPTEAaidvthwpvrGPAE 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 393 LTPLPGATPMkPGSATFpffgVAPAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFETT 457
Cdd:cd17646 305 TPSVPIGRPV-PNTRLY----VLDDALRP----------------VP-VGVPGELYlggvqlarGYLgrpaltaERFVPD 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 458 YFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 537
Cdd:cd17646 363 PFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAA 442
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622836714 538 GHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd17646 443 GAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
231-587 |
6.28e-27 |
|
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: 113.60 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 231 ILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDVN 310
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 311 RLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhQVVGAQRCPIVDTFWQTETGG 390
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL---EQCKEKGIPVYQSYGMTETCS 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 391 HMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAegyLVFKQPwpGIMRTVYGNHER----FETTYFKkfpgyy 466
Cdd:cd05912 228 QIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--NVTKGYLNRPDAteesFENGWFK------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 467 vTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtfSPKLT 546
Cdd:cd05912 297 -TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS------ERPIS 369
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622836714 547 -EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05912 370 eEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
21-586 |
9.83e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 114.39 E-value: 9.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 21 KLGDKVAFYWEgNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFS 100
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 101 SESlCERILDSS-CSLLITTDAFYRgeklvnlkelADEALQkcQEKDFPVRCCIVvkhlgraelgmgdspsqsppikrsc 179
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFYP----------MYRQIQ--QEDATPLRHICL------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 180 pdvqgkLKEKSKRVQPQISWNQgidlwwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----VGGYmlY 254
Cdd:PRK08008 140 ------TRVALPADDGVSSFTQ-------LKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY--Y 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 255 ----VATTFKYVF-----DFHAEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDVNRLWSIVDKYKVTKFY 325
Cdd:PRK08008 205 sawqCALRDDDVYltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 326 TAPTAIRLLMKfgdEPVTKHSRASL--QVLGTVgePINPEAWLWYHQVVGAQrcpIVDTFWQTETGGHMLTPLPGATPMK 403
Cdd:PRK08008 268 CIPMMIRTLMV---QPPSANDRQHClrEVMFYL--NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGDKRRW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 404 PgSATFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWI 482
Cdd:PRK08008 340 P-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 483 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIAT 562
Cdd:PRK08008 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKV 493
|
570 580
....*....|....*....|....
gi 1622836714 563 PDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK08008 494 PSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
226-586 |
1.66e-26 |
|
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: 112.85 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 226 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVtYGPLANGAtSVLFEGIPT 305
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 306 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPINPE-AWLWYHQVV------GAQRCP 378
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRWLKAPVrlfnayGPTEAT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 379 IVDTFWQTETGghmLTPLPGATPMkpGSatfPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETTY 458
Cdd:cd17649 250 VTPLVWKCEAG---AARAGASMPI--GR---PLGGRSAYILDADLNPVPVGVTGELYIGGE--GLAR---GYLGRPELTA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 459 fKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECL 529
Cdd:cd17649 317 -ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836714 530 YCFVTLCDGHTfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd17649 395 VAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
227-587 |
2.25e-26 |
|
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: 112.38 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 227 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTY 306
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL----PK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 307 PDVNRLWSIVDKYKVTKFYTAPTA-IRLL--MKFGDEPVTKHSRAS-----LQVLGTVGEPInP--EAWlwyhQVVGAQR 376
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyYEAHFTDPQFARAAAaerlrLMVSGSAALPV-PtlEEW----EAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 377 cpIVDTFWQTETGGHMLTPLPGatPMKPGSATFPFFGVAPAIL-NESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFE 455
Cdd:cd05941 240 --LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGP--SVFKEYWNKPEATK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 456 ttyfKKFP--GYYVTGDGCRRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 532
Cdd:cd05941 314 ----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAV 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622836714 533 VTLCDGHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05941 390 VVLRAGAA--ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
20-585 |
7.60e-26 |
|
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: 111.14 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGF 99
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA----AYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 100 SSESLCERIL----DSSCSLLITtdafyrgeklvnLKELADEAlqkcqekdfPVRCCIVVkhlgraeLGMGDSPSQSPPI 175
Cdd:cd12117 78 DPELPAERLAfmlaDAGAKVLLT------------DRSLAGRA---------GGLEVAVV-------IDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 176 KRSCpdvqgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYV 255
Cdd:cd12117 130 AVPV--------------------------------------------SPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 256 ATTFKYVfDFHAEDVFWCTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTK-FYTAPTaIRLL 334
Cdd:cd12117 165 VKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAL-FNQL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 335 MKFGDEpvtkhSRASLQVLGTVGEPINPEawlWYHQVVgaQRCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGS 406
Cdd:cd12117 241 ADEDPE-----CFAGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 407 atfPFFGVAPAILNesgeelegeaegylVFKQPWP------------GIMRTvYGNH-----ERFETTYFkkFPG--YYV 467
Cdd:cd12117 311 ---PIANTRVYVLD--------------EDGRPVPpgvpgelyvggdGLALG-YLNRpaltaERFVADPF--GPGerLYR 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 468 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSPkltE 547
Cdd:cd12117 371 TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA--EGALDA---A 445
|
570 580 590
....*....|....*....|....*....|....*...
gi 1622836714 548 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
17-586 |
1.13e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.94 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 17 VHEKKLGDKVAFYWegnePGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVF 96
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 97 AGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKCqekdfP-VRCCIVVkhlgraelgmgDSPSQSPPI 175
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQC-----PgVRHRLVL-----------DGDGELEGF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 176 KRscpdvqgklkekskrvqpqiswnqgidlwwhelMQEAGDECePEWCDAEDPL--FILYTSGSTGKPKGVV----HTVG 249
Cdd:PRK13391 136 VG---------------------------------YAEAVAGL-PATPIADESLgtDMLYSSGTTGRPKGIKrplpEQPP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 250 GYMLYVATTFKYVFDFHAEDVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDVNRLWSIVDKYKVT 322
Cdd:PRK13391 182 DTPLPLTAFLQRLWGFRSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 KFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPE------AWlWyhqvvgaqrCPIVDTFWQTETGGhmltpl 396
Cdd:PRK13391 250 HTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL------ 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 397 pGATPM-------KPGSATFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTVYGNHER-FEttYFK------- 460
Cdd:PRK13391 314 -GFTACdseewlaHPGTVGRAMFGD-LHILDDDG--------------AELPpGEPGTIWFEGGRpFE--YLNdpaktae 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 461 ---KFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 537
Cdd:PRK13391 376 arhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVD 455
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622836714 538 GHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK13391 456 GVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
24-587 |
1.23e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.41 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGNEpgettqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 103
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 LCERILDSSCSLLITTDAfyrgeklvnLKELADEALQkcqekDFPVRCCIVVkhlgraelgMGDSPsqsppikrscpdvq 183
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA---------LAPVATAVRD-----IVPLLSTVVV---------AGGSS-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 184 gklkekskrvqpqiswnQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvggYMLYVATTFKYVF 263
Cdd:PRK07786 149 -----------------DDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 264 DFHA---EDVFWCTADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DVNRLWSIVDKYKVTKFYTAPTAIRLL 334
Cdd:PRK07786 209 TNGAdinSDVGFVGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 335 MkfgDEPVTKHSRASLQVLGTVGEPiNPEAWL--WYHQVVGAQrcpIVDTFWQTEtgghmLTPLpgaTPM--------KP 404
Cdd:PRK07786 280 C---AEQQARPRDLALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMllgedairKL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 405 GSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGN----HERFETtyfkkfpGYYVTGDGCRRDQDGYY 480
Cdd:PRK07786 345 GSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP--TLMSGYWNNpeatAEAFAG-------GWFHSGDLVRQDEEGYV 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 481 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLT-EELKKQIREKIGP 559
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLAR 492
|
570 580
....*....|....*....|....*...
gi 1622836714 560 IATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK07786 493 YKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
37-523 |
2.10e-25 |
|
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: 112.26 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsivfA------GFSSESLcERIL- 109
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 110 DSSCSLLITTDAFyrgeklvnLKELADEALQkcqekdfpvrcCIVVkhlgrAELGMGDSPSQSPPIKRScpdvqgklkek 189
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLAL-----DALALAAEPATNPPVPVT----------- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 190 skrvqpqiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATTFK------ 260
Cdd:COG1020 616 -----------------------------------PDDLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMQRRYGlgpgdr 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 261 ------YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLF--EGIptyPDVNRLWSIVDKYKVTKFYTAPTAIR 332
Cdd:COG1020 661 vlqfasLSFDASVWEIFG-----------------ALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTPSLLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 333 LLMKFGDEPVtkhsrASLQVLGTVGEPINPEAWLWYHQVVGAQR---------CPIVDTFWQTETGGHMLTPLP-GaTPM 402
Cdd:COG1020 721 ALLDAAPEAL-----PSLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPiG-RPI 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 403 kPGSATFpffgvapaILNEsgeelegeaegylvFKQPWP-GIM-------------------RTVygnhERFETTYFkKF 462
Cdd:COG1020 795 -ANTRVY--------VLDA--------------HLQPVPvGVPgelyiggaglargylnrpeLTA----ERFVADPF-GF 846
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622836714 463 PG--YYVTGDGCRRDQDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 523
Cdd:COG1020 847 PGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDA 909
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
207-586 |
4.29e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 109.35 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 207 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgyMLYV---ATTFKYvfDFHAEDVFWCTADIGwitgH 283
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 284 S---YVTYGP-LANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQV-LGT 355
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYILATPERP--DDADNPLRVaFGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 356 VGEPINPEAWlwyhqvvgAQR--CPIVDTFWQTETGGhMLTPLPGaTPmkPGSATFPFFGVApaILNESGEelegeaegy 433
Cdd:PRK13388 274 EASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVA--IYNPETL--------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 434 lvfkQPWPgimRTVYGNH-----------ERFETTYFKKFPGYYV---------------TGDGCRRDQDGYYWITGRID 487
Cdd:PRK13388 331 ----TECA---VARFDAHgallnadeaigELVNTAGAGFFEGYYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 488 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPIATPDYI 566
Cdd:PRK13388 404 DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYV 481
|
410 420
....*....|....*....|
gi 1622836714 567 QNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK13388 482 RIAADLPSTATNKVLKRELI 501
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
36-519 |
6.62e-25 |
|
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: 108.07 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESlCERIL-DSSCS 114
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 LLITTDAfyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvq 194
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 pqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCT 274
Cdd:cd05907 87 -------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSF 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 275 ADIGWITGHSYVTYGPLANGATSVLFEGI-----------PTY-PDVNRLWSIVdkYKVTKFYTAPTAIRLLMKFgdepv 342
Cdd:cd05907 135 LPLAHVFERRAGLYVPLLAGARIYFASSAetllddlsevrPTVfLAVPRVWEKV--YAAIKVKAVPGLKRKLFDL----- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 343 tkHSRASLQVLGTVGEPINPEAWLWYHQvVGaqrCPIVDTFWQTETGG-HMLTPLPGATPMKPGSATFPF-FGVAPA--I 418
Cdd:cd05907 208 --AVGGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTETSAvVTLNPPGDNRIGTVGKPLPGVeVRIADDgeI 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 419 LnesgeelegeaegylvFKQpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDML-NVSGHLL 497
Cdd:cd05907 282 L----------------VRG--PNVMLGYYKNPE--ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNI 341
|
490 500
....*....|....*....|..
gi 1622836714 498 STAEVESALVEHEAVAEAAVVG 519
Cdd:cd05907 342 SPEPIENALKASPLISQAVVIG 363
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
206-587 |
1.54e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.84 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 206 WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVG-----GYMLyvATTFkyvfDFHAEDVFWCTADI--- 277
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVML--AQRF----GLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 278 -----GWITGhsyvtygpLANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKF--------YTAPTAIR-------LL 334
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnyvgkplsYVLATPERpddadnpLR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 335 MKFGDEpvtkhsraslqvlgtvGEPINPEAWlwyhqvvgAQR--CPIVDTFWQTEtGGHMLTPLPGaTPmkPGSATFPFF 412
Cdd:PRK07867 271 IVYGNE----------------GAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 413 GVA-----------PAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHErfeTTYFKKFPGYYVTGDGCRRDQDGYYW 481
Cdd:PRK07867 323 GVAivdpdtgtecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAY 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPI 560
Cdd:PRK07867 399 FAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGPK 476
|
410 420
....*....|....*....|....*..
gi 1622836714 561 ATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
37-585 |
3.61e-24 |
|
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: 105.86 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 116
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITtdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpq 196
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 iswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTF------------KY 261
Cdd:cd12115 103 ---------------------------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 262 VFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGIPTYPDVNRLwsivdkYKVTKFYTAPTAIRLLMKFGDEP 341
Cdd:cd12115 156 CFDLSVFELF-----------------GPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 342 vtkhsrASLQVLGTVGEPINPEAWLWYHQVVGAQRC-----PIVDTFWQTetgGHMLTPLPGATPmkpgSATFPFFGVAP 416
Cdd:cd12115 213 ------ASVRVVNLAGEPLPRDLVQRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 417 AILNEsgeelegeaegylvFKQPWP------------GIMRTVYGN----HERFETTYFkkFPG--YYVTGDGCRRDQDG 478
Cdd:cd12115 280 YVLDR--------------ALQPVPlgvpgelyiggaGVARGYLGRpgltAERFLPDPF--GPGarLYRTGDLVRWRPDG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 479 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIG 558
Cdd:cd12115 344 LLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLP 420
|
570 580
....*....|....*....|....*..
gi 1622836714 559 PIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
209-587 |
6.26e-24 |
|
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: 105.46 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 209 ELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMLyVATTFKYVFDFHAEDVFWCTADI----GWItgh 283
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 284 syVTYGPLANGATSVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPE 363
Cdd:cd12118 191 --FPWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVM-TAGAP-PPA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 364 AWLWYHQVVGAQrcpIVDTFWQTETGGhmltplPGAT-PMKPGSATFPffGVAPAILNESGEELEGEAEGYLVFKQ---- 438
Cdd:cd12118 262 AVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPetmk 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 439 --PWPG------------IMRTVYGNHERFETTyFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 504
Cdd:cd12118 331 pvPRDGktigeivfrgniVMKGYLKNPEATAEA-FRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 505 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRV 584
Cdd:cd12118 408 VLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFV 483
|
...
gi 1622836714 585 LRK 587
Cdd:cd12118 484 LRD 486
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
36-586 |
9.38e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 104.99 E-value: 9.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITTDAFyrgeklvnlKELADEALQKCQEkdfpvrccivvkHLGRAELGMGDSPSQSPpikrscpdvqgklkekskrvqp 195
Cdd:PRK08276 87 LIVSAAL---------ADTAAELAAELPA------------GVPLLLVVAGPVPGFRS---------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 196 qiswnqgidlwWHELM-QEAGDECEPEWCDAEdplfILYTSGSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFH 266
Cdd:PRK08276 124 -----------YEEALaAQPDTPIADETAGAD----MLYSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 267 AEDVFWCTADIGwitgHSYVT-YG--PLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVT 343
Cdd:PRK08276 186 PDSVYLSPAPLY----HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 344 KHSRASLQVLGTVGEPINPE------AWlWyhqvvGaqrcPIVD-TFWQTETGGHMLtplpgATP----MKPGSATFPFF 412
Cdd:PRK08276 258 RYDVSSLRVAIHAAAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSedwlAHPGSVGKAVL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 413 GVApAILNESGEELEGEAEGYLVFKQPWPGImrTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLnV 492
Cdd:PRK08276 323 GEV-RILDEDGNELPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-I 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 493 SGHL-LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPG 571
Cdd:PRK08276 397 SGGVnIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDE 476
|
570
....*....|....*
gi 1622836714 572 LPKTRSGKIMRRVLR 586
Cdd:PRK08276 477 LPRTPTGKLYKRRLR 491
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
12-520 |
2.91e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 104.41 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 12 VLDRNVheKKLGDKVAFYWEGNepGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 91
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 92 HSIVFAGfSSESLCERIL-DSSCSLLITTDAfyrgEKLVNLKELADE--ALQKcqekdfpvrccIVVkhlgraelgmgds 168
Cdd:COG1022 92 TVPIYPT-SSAEEVAYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 169 psqsppikrscpdvqgkLKEKSKRVQPQIswnqgidLWWHELMQEAGDECEPEW-------CDAEDPLFILYTSGSTGKP 241
Cdd:COG1022 143 -----------------LDPRGLRDDPRL-------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGRP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 242 KGVVHTVGGyMLYVATTFKYVFDFHAEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGIPTYPD-------- 308
Cdd:COG1022 199 KGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPDTLAEdlrevkpt 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 309 ----VNRLW-----SIVDK------YKVTKFYTA-----------------PTAIRLLMKFGDEPVTKHSRASL----QV 352
Cdd:COG1022 272 fmlaVPRVWekvyaGIQAKaeeaggLKRKLFRWAlavgrryararlagkspSLLLRLKHALADKLVFSKLREALggrlRF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 353 LGTVGEPINPEAWLWYHqVVGAqrcPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAI-----Lnesgeele 427
Cdd:COG1022 352 AVSGGAALGPELARFFR-ALGI---PVLEGYGLTETSPVITVNRPGD--NRIGTVGPPLPGVEVKIaedgeI-------- 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 428 geaegyLVfKQpwPGIMRTVYGNHErfETTyfKKFP--GYYVTGD-GcRRDQDGYYWITGRIDDMLNVS-GHLLSTAEVE 503
Cdd:COG1022 418 ------LV-RG--PNVMKGYYKNPE--ATA--EAFDadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVAPQPIE 483
|
570
....*....|....*..
gi 1622836714 504 SALVEHEAVAEAAVVGH 520
Cdd:COG1022 484 NALKASPLIEQAVVVGD 500
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-590 |
3.11e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 103.67 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITTDAFyRGEKLVN-LKELADEALQkcqekdfPVRCCIVVkhlgraelgmgDSPSQSPPIKRSCpdvqgklkekskrvq 194
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV-----------DDAADATPAPAPG--------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 pqiSWNQGIDLWWHELMQEAGDECEPEwcdaeDPLFILYT-SGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWC 273
Cdd:PRK06164 157 ---ARVQLFALPDPAPPAAAGERAADP-----DAGALLFTtSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 274 TADIGWITGHSYVTyGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtkHSRASLQVL 353
Cdd:PRK06164 228 ALPFCGVFGFSTLL-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 354 GTVGepINPeAWLWYHQVVGAQRCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSATFPFFGVAPAILNESG 423
Cdd:PRK06164 300 GFAS--FAP-ALGELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 424 EELEGEAEgylvfkqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 503
Cdd:PRK06164 377 SGEIEIRA---------PSLMRGYLDNPD--ATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 504 SALVEHEAVAEAAVVGHPHPVKGEClYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG---KI 580
Cdd:PRK06164 446 HALEALPGVAAAQVVGATRDGKTVP-VAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKI 521
|
570
....*....|
gi 1622836714 581 MRRVLRKIAQ 590
Cdd:PRK06164 522 QKHRLREMAQ 531
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
42-589 |
6.46e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.93 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 121
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 FyRGEKLVN-----LKELADEALQKCQEKDFPvrccivvkHLgRAELGMGDSPsqsPPikrscpdvqgklkekskrvqpq 196
Cdd:PRK12583 127 F-KTSDYHAmlqelLPGLAEGQPGALACERLP--------EL-RGVVSLAPAP---PP---------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 iswnqGIdLWWHELmQEAGDECEPE-------WCDAEDPLFILYTSGSTGKPKGVV---HTV--GGYMLYVAttfkyvFD 264
Cdd:PRK12583 172 -----GF-LAWHEL-QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 265 FHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYPDVNrlWSIVDKYKVTKFYTAPTairLLMKFGDEPvtK 344
Cdd:PRK12583 239 LTEHDRLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELDHP--Q 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 345 HSRASLQVLGT---VGEPINPEAwlwYHQVVGAQRCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSATF----PFFGVA 415
Cdd:PRK12583 311 RGNFDLSSLRTgimAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 416 paILNESGEELEGEAEGYLVFKqpwpG--IMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 493
Cdd:PRK12583 386 --VVDPDGATVPRGEIGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 494 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLP 573
Cdd:PRK12583 458 GENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVDEFP 534
|
570
....*....|....*.
gi 1622836714 574 KTRSGKIMRRVLRKIA 589
Cdd:PRK12583 535 MTVTGKVQKFRMREIS 550
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
39-585 |
1.41e-22 |
|
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: 101.25 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 39 TQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsIVFAGFSseslcerildsscsllit 118
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 119 tdafYRGEKLVNLKELADEALqkcqekdfpvrcCIVvkhlgraelgmgdspsqsppikrscPDVQGklkekskRVQPQis 198
Cdd:cd05920 99 ----HRRSELSAFCAHAEAVA------------YIV-------------------------PDRHA-------GFDHR-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 199 wnqgidlwwhELMQEAGDECEpewcdaeDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIG 278
Cdd:cd05920 129 ----------ALARELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 279 witgHSYVTYGP-----LANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVL 353
Cdd:cd05920 191 ----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 354 GTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSAtf 409
Cdd:cd05920 261 QVGGARLSPALARRVPPVLG---CTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEE-- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 410 pffgvapailnesgeelegeaeGYLVFKQPWP--GIMRTVYGNHERFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRID 487
Cdd:cd05920 336 ----------------------GELLTRGPYTirGYYRAPEHNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 488 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSPKLTEELKKQIREKigPIAT---PD 564
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--GLAAyklPD 461
|
570 580
....*....|....*....|.
gi 1622836714 565 YIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd05920 462 RIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
36-588 |
1.56e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 101.48 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsscs 114
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI----------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 llittdafyrgekLVNLKELADEALQKCQEKDFPVRCCIVVKHLGRAELGMGDSPSQSPPIKRSCPDvqgklkekskrvq 194
Cdd:PRK06839 80 -------------AVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLK------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 pqiswnqgidlwwhELMQEAGDECEPEwcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCT 274
Cdd:PRK06839 134 --------------EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 275 ADIGWITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTKFYTAPT---AIRLLMKFgdepvTKHSRASLQ 351
Cdd:PRK06839 197 LPLFHIGGIGLFAFPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 352 VLGTVGEPInPEAWLWYHQVVGAqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAE 431
Cdd:PRK06839 268 WFYNGGAPC-PEELMREFIDRGF---LFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 432 GYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 511
Cdd:PRK06839 344 GELLIRGP--NVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSD 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836714 512 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 588
Cdd:PRK06839 419 VYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
35-585 |
2.71e-22 |
|
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: 100.66 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 35 PGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERI-LDSSC 113
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 114 SLLITTDAF-YRGEKLVNLKELAdealqkcqekdfpvrccivvkhLGrAELGMGDSPSQSPPIkrscpdvqgklkekskr 192
Cdd:cd05923 103 AAVIAVDAQvMDAIFQSGVRVLA----------------------LS-DLVGLGEPESAGPLI----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 193 vqpqiswnqgidlwwhelmqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKYVFDFHaeD 269
Cdd:cd05923 143 --------------------------EDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--N 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 270 VFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRAS 349
Cdd:cd05923 195 VVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 350 LQVLGTVGEPInPEAWLwyHQVVGAQRCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsatfpFFG---VAPaILNESGEE 425
Cdd:cd05923 269 LRHVTFAGATM-PDAVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 426 LEGEAEGYLVFKQP----WPGIMRtvygnheRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 501
Cdd:cd05923 340 LANGEEGELIVAAAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 502 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfspKLTEELKKQ--IREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:cd05923 413 IERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLDELPKNAMNK 487
|
....*.
gi 1622836714 580 IMRRVL 585
Cdd:cd05923 488 VLRRQL 493
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
22-588 |
8.91e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 99.45 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 22 LGDKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 101
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 102 ESLcERILDSSCSLLITTDAFYRgeklvnlkeladEALQKCQEKDFPvrccivvkhlgRAELGMGDSPsqsppikrscpd 181
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEAALL------------AALEAADPGDLP-----------LPAVWLLDAP------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 182 vqgklkekskrvqPQISWNQGidlwWHELMQEAGDECEPEwcdAE----DPLFILYTSGSTGKPKGVVHTvggymlyvat 257
Cdd:PRK06155 152 -------------ASVSVPAG----WSTAPLPPLDAPAPA---AAvqpgDTAAILYTSGTTGPSKGVCCP---------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 258 tfkyvfdfHAEDVFW---CTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIptypDVNRLWSIVDKYKV 321
Cdd:PRK06155 202 --------HAQFYWWgrnSAEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRF----SASGFWPAVRRHGA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMKfgdEPVTKHSRAS-LQVLGTVGEPINpeawlwYHQVVGAqRC--PIVDTFWQTETGGHMLTPLPG 398
Cdd:PRK06155 270 TVTYLLGAMVSILLS---QPARESDRAHrVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 399 AtpmKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNH-----ERFETTYFKkfpgyyvTGDGCR 473
Cdd:PRK06155 340 Q---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMpektvEAWRNLWFH-------TGDRVV 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 474 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQI 553
Cdd:PRK06155 410 RDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHC 486
|
570 580 590
....*....|....*....|....*....|....*
gi 1622836714 554 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 588
Cdd:PRK06155 487 EPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-585 |
5.69e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITTDAFyrGEKLvnlkeladealqkcqekdfPVRCCIVVKHLGRAELGMgDSPSQSPPIKRSCPdvqgklkekskrvqp 195
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PLAAGVQVLDLDRPAAWL-EGYSEENPGTELNP--------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 196 qiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHT------------------VGGYMLYVaT 257
Cdd:PRK12316 655 ------------------------------ENLAYVIYTSGSTGKPKGAGNRhralsnrlcwmqqayglgVGDTVLQK-T 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 258 TFKyvFDFHAEDVFWctadigwitghsyvtygPLANGATSVLF-EGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMK 336
Cdd:PRK12316 704 PFS--FDVSVWEFFW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQ 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 337 FGDEPvtkhSRASLQVLGTVGEPINPEAwlwyHQVVGAQR--CPIVDTFWQTETGghmlTPLPGATPMKPGSATF----P 410
Cdd:PRK12316 763 DEDVA----SCTSLRRIVCSGEALPADA----QEQVFAKLpqAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrP 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 411 FFGVAPAILNESGeelegeaegylvfkQPWP------------GIMRTVYG----NHERFETTYFKKFPGYYVTGDGCRR 474
Cdd:PRK12316 831 IANLACYILDANL--------------EPVPvgvlgelylagrGLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARY 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 475 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIR 554
Cdd:PRK12316 897 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLA 969
|
570 580 590
....*....|....*....|....*....|.
gi 1622836714 555 EKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK12316 970 ASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
231-586 |
8.92e-21 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 95.52 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 231 ILYTSGSTGKPKGVVHTVGGYMLYVAT--TFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 308
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 309 VNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP---EAWL-WYHqvvgaqrcPIVDTFW 384
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 385 Q-TETGGhmLTPLPGATPMK-PGSATFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTVY--GN-----HERFE 455
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfaNGpgfeyTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 456 TTYFKKFPGYYVT-GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 534
Cdd:cd05929 341 KTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622836714 535 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
37-588 |
9.45e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 96.15 E-value: 9.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 116
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITTDAFyrgeklvnlkelaDEALQKCQEKdfpvrccivvkhLGRAeLGMGDSPSQSPPIKRSCPDVQGKLKEKSKRVQPQ 196
Cdd:PRK07788 151 VYDDEF-------------TDLLSALPPD------------LGRL-RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 ISWNQGIdlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVH-------TVGGYMLYVAttfkyvfdFHAED 269
Cdd:PRK07788 205 PPKPGGI---------------------------VILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 270 VFWCTADIGWITGHSYVTYGpLANGATSVL---FEGIPTYPDVnrlwsivDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 346
Cdd:PRK07788 250 TTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrFDPEATLEDI-------AKHKATALVVVPVMLSRILDLGPEVLAKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 347 RASLQVLGTVGEPINPEAWLWYHQVVGaqrcPIVDTFW-QTETGGHMLtplpgATP----MKPGSATFPFFGVAPAILNE 421
Cdd:PRK07788 322 TSSLKIIFVSGSALSPELATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 422 SGeelegeaegylvfkQPWPG--IMRTVYGNHERFETtYF-----KKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSG 494
Cdd:PRK07788 393 NG--------------NEVPRgvVGRIFVGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 495 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPK 574
Cdd:PRK07788 458 ENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE---DAIKDYVRDNLARYKVPRDVVFLDELPR 534
|
570
....*....|....
gi 1622836714 575 TRSGKIMRRVLRKI 588
Cdd:PRK07788 535 NPTGKVLKRELREM 548
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
227-589 |
1.20e-20 |
|
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: 93.16 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 227 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 306
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 307 PDVNRlwsivdkYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQVLGTVGEPINPEAwlwyHQVVGAQRCPIVDTFWQT 386
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 387 ETGGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTVYGNHERFETTYFKKfPGYY 466
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 467 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspklT 546
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-----P 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622836714 547 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 589
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
42-587 |
1.82e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 95.20 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsSCSLLITtda 121
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV--------------------SVPLLPS--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 fYRGEKLVnlkeladEALQKCQEKDFpvrCCIVVKHLGRAElgmgdspSQSPPIKRSCPDVQG-KLKEKSKRVQPQISWN 200
Cdd:PRK06087 108 -WREAELV-------WVLNKCQAKMF---FAPTLFKQTRPV-------DLILPLQNQLPQLQQiVGVDKLAPATSSLSLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 QGIDLwwHELMQEagdecePEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWI 280
Cdd:PRK06087 170 QIIAD--YEPLTT------AITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 281 TGHSYVTYGPLANGATSVLFEGIPtyPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVLGTVGEPI 360
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLLDIFT--PD--ACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 361 nPEAWLWYHQVVGAQRCPIvdtFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPw 440
Cdd:PRK06087 315 -PKKVARECQQRGIKLLSV---YGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGP- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 441 pGIMRTVYGNHERfeTTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGH 520
Cdd:PRK06087 390 -NVFMGYLDEPEL--TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836714 521 PHPVKGECLYCFVTLcDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK06087 467 PDERLGERSCAYVVL-KAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
227-582 |
3.61e-20 |
|
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: 91.70 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 227 DPLFILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDvfwctadigwitghSYVTYGPLA-----NGATSVLF 300
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIeSFVCN--EDLFNISGED--------------AILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 301 EG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKhsrasLQVLGTVGEPINPEAWLWYHQvvGAQR 376
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFESTKKKLKN--IFPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 377 CPIVDTFWQTETGghMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTVYGNHERFET 456
Cdd:cd17633 137 ANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMVFS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 457 TY----FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCF 532
Cdd:cd17633 197 GYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 533 VTLCDGHTFsPKLTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSGKIMR 582
Cdd:cd17633 276 LYSGDKLTY-KQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
41-586 |
1.59e-19 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 92.13 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 120
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 AFyrgeklvnlKELADEALQKCqekdfpvrccivvkhlgraelgmgdspsqsPPIKRScpdvqgklkekskrvqpqISWN 200
Cdd:PRK13382 149 EF---------SATVDRALADC------------------------------PQATRI------------------VAWT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 QGIDLWWHELMQEAGDECEPEWCDAEDPLfILYTSGSTGKPKGVVHT-VGGYMlyvatTFKYVFDfhaedvfwctaDIGW 279
Cdd:PRK13382 172 DEDHDLTVEVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILD-----------RTPW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 280 ITGHSYVTYGPL--ANGATSVLFEGIPTYPDVNR-------LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASL 350
Cdd:PRK13382 235 RAEEPTVIVAPMfhAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 351 QVLGTVGEPINPEAWLWYHQVVGAQrcpIVDTFWQTETGghMLTPlpgATP----MKPGSATFPFFGVAPAILNESgeel 426
Cdd:PRK13382 315 RFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQD---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 427 egeaegylvFKQPWPGIMRTVY-GNHERFE-----TTyfKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 499
Cdd:PRK13382 383 ---------FREVPTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 500 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:PRK13382 452 IEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
....*..
gi 1622836714 580 IMRRVLR 586
Cdd:PRK13382 529 ILRRELQ 535
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
442-586 |
4.41e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 88.87 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 442 GIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 521
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622836714 522 HPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTE---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
37-583 |
5.57e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 90.72 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsIVFAgfsseslceriLDSScslL 116
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITTDAFYRGEKLVNLKELADeALQKCQEKDFPVRCCIVVKHLGRAELGMGDSPSQSPpikrscpDVQGKLkekskrvQPQ 196
Cdd:PRK05852 103 PIAEQRVRSQAAGARVVLID-ADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHL-------DAATEP-------TPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 ISWNQGIdlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGymlyVATTFKYV---FDFHAEDVfwC 273
Cdd:PRK05852 168 TSTPEGL---------------------RPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 274 TADIGWITGHSYVT--YGPLANGATSVLfegiptyPDVNRL-----WSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 346
Cdd:PRK05852 221 VAVMPLYHGHGLIAalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 347 RASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSATFPFFGVA-- 415
Cdd:PRK05852 294 PAALRFIRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgs 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 416 ------PAILNesgeelegeaegylvfkQPW---PGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRI 486
Cdd:PRK05852 371 dglplpAGAVG-----------------EVWlrgTTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 487 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYI 566
Cdd:PRK05852 431 KELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---EELVQFCRERLAAFEIPASF 507
|
570
....*....|....*..
gi 1622836714 567 QNAPGLPKTRSGKIMRR 583
Cdd:PRK05852 508 QEASGLPHTAKGSLDRR 524
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
224-589 |
1.42e-18 |
|
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: 88.93 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGAtSVLFEGI 303
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 304 PTYPdvNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepVTKHSRASLQVLGTVGEPINP---EAWLWYHQVvgaqrcPIV 380
Cdd:cd05909 223 PLDY--KKIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGI------RIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 381 DTFWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHERFETTYFK 460
Cdd:cd05909 291 EGYGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEPELTSFAFGD 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 461 kfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVGHPHPVKGECLYCFVTlcdGH 539
Cdd:cd05909 369 ---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTT---TT 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 540 TFSPkltEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 589
Cdd:cd05909 443 DTDP---SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
36-591 |
2.49e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 88.50 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQI-TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCS 114
Cdd:PLN02246 45 GATGRVyTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 LLITTDAFYrgEKLVNLKeladealqkcQEKDFPVRCCivvkhlgraelgmgDSPsqsppiKRSCpdvqgklkekskrvq 194
Cdd:PLN02246 125 LIITQSCYV--DKLKGLA----------EDDGVTVVTI--------------DDP------PEGC--------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 pqiswnqgidLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAttfKYV------FDFHAE 268
Cdd:PLN02246 158 ----------LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 269 DVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTkfyTAPTAIRLLMKFGDEP-VTKHSR 347
Cdd:PLN02246 225 DVILCVLPMFHIYSLNSVLLCGLRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 348 ASLQVLGTVGEPINPEawlwYHQVVGAqRCP---IVDTFWQTETGGHMLTPLPGA---TPMKPGSAtfpffgvAPAILNE 421
Cdd:PLN02246 298 SSIRMVLSGAAPLGKE----LEDAFRA-KLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 422 SGEELEGEAEGYLVFKQPW------PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 495
Cdd:PLN02246 366 ELKIVDPETGASLPRNQPGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 496 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELK----KQI--REKIGPIATPDYIqna 569
Cdd:PLN02246 444 QVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKVFFVDSI--- 517
|
570 580
....*....|....*....|...
gi 1622836714 570 pglPKTRSGKIMRRVLR-KIAQN 591
Cdd:PLN02246 518 ---PKAPSGKILRKDLRaKLAAG 537
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
224-585 |
2.61e-18 |
|
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: 87.91 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVV-------HTVGGY------------MLYVATtfkYVFDFHAEDvfWCTAdigwitghs 284
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWrreyeldsfpvrLLQMAS---FSFDVFAGD--FARS--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 285 yvtygpLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP 362
Cdd:cd17650 157 ------LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 363 EAWLwYHQVvgAQRCPIVDTFWQTET--------GGhmLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegyl 434
Cdd:cd17650 228 FKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERL----------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 435 vfkQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 498
Cdd:cd17650 289 ---QPQPvgvagelyiggaGVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 499 TAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdgHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKT 575
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA----ATLN---TAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
410
....*....|
gi 1622836714 576 RSGKIMRRVL 585
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
20-585 |
2.69e-18 |
|
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: 88.15 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAFYWEGNepgettQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 99
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 100 SSESLcERIL-DSSCSLLITTdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrs 178
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQ----------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 179 cpdvqgklkeksKRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGV----------VHTV 248
Cdd:cd17655 102 ------------SHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 249 GGYM-----LYVATTFKYVFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTK 323
Cdd:cd17655 170 NKVIyqgehLRVALFASISFDASVTEIF-----------------ASLLSGNTLYIVRK-ETVLDGQALTQYIRQNRITI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 324 FYTAPTAIRLLMKFGDEPvtkhsRASLQVLGTVGEPINPE-AWLWYHQVVGAqrCPIVDTFWQTETG-GHMLTPLpgaTP 401
Cdd:cd17655 232 IDLTPAHLKLLDAADDSE-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EP 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGSATFPffgVAPAILNESGeelegeaegYLVFK--QPWP------------GIMRTvYGNHErfETTYfKKF----- 462
Cdd:cd17655 302 ETDQQVSVP---IGKPLGNTRI---------YILDQygRPQPvgvagelyiggeGVARG-YLNRP--ELTA-EKFvddpf 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 463 -PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgh 539
Cdd:cd17655 366 vPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI------ 439
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1622836714 540 TFSPKLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd17655 440 VSEKELPvAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
18-586 |
3.03e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 88.02 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 18 HEKKLGDKVAFYWEGNEpgettqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFA 97
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA----VFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 98 GfsseslcerildsscsllittdafyrgeklVNLKELADEAlqkcqekdfpvrcCIVVKHLGrAELGMGDSPSQSPPIKR 177
Cdd:PRK06145 81 P------------------------------INYRLAADEV-------------AYILGDAG-AKLLLVDEEFDAIVALE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 178 SCPDVQGKLKEKSKRVqpqiswnqgidlwwhelMQEAGDECEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTVGgymlyva 256
Cdd:PRK06145 117 TPKIVIDAAAQADSRR-----------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 257 ttfkyvfdfhaeDVFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG----IPTYPDVNRLWSIVDKYKVT 322
Cdd:PRK06145 173 ------------NLHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRLT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 KFYTAPTAIRLLMKfgdepVTKHSRASLQVLgtvgepinpeAWLwyhqVVGAQRCP---------------IVDTFWQTE 387
Cdd:PRK06145 241 CAWMAPVMLSRVLT-----VPDRDRFDLDSL----------AWC----IGGGEKTPesrirdftrvftrarYIDAYGLTE 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 388 T-GGHMLTPlPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYY 466
Cdd:PRK06145 302 TcSGDTLME-AGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP--KVTKGYWKDPEKTAEAFYG---DWF 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 467 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklT 546
Cdd:PRK06145 376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---L 452
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622836714 547 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK06145 453 EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
37-591 |
5.86e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 87.14 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGiQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 116
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITtDAFYRGeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqspPIkrscPDVQGklkekskrvqPQ 196
Cdd:PRK07638 102 VT-ERYKLN------------------------------------------------DL----PDEEG----------RV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 ISWNQgidlwWHELMQEAGDECEPEwCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMlyvattfkYVFDFHAEDVFWCTA 275
Cdd:PRK07638 119 IEIDE-----WKRMIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKRE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 276 DIGWITG---HSYVTYGplangATSVLFEG-----IPTYPDVNRLWSIvDKYKVTKFYTAPTAIRLLMK---FGDEPVT- 343
Cdd:PRK07638 185 DSVLIAGtlvHSLFLYG-----AISTLYVGqtvhlMRKFIPNQVLDKL-ETENISVMYTVPTMLESLYKenrVIENKMKi 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 344 -----KHSRASLQVLGTvgepINPEAWLWyhQVVGAQRCPIVdTFWQTETgghmltplpgaTPMKPGSATFPFFGVAPAI 418
Cdd:PRK07638 259 issgaKWEAEAKEKIKN----IFPYAKLY--EFYGASELSFV-TALVDEE-----------SERRPNSVGRPFHNVQVRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 419 LNESGeelegeaegylvfKQPWPGIMRTVYGNHERFettyfkkFPGYYVTGDGCRR---------------DQDGYYWIT 483
Cdd:PRK07638 321 CNEAG-------------EEVQKGEIGTVYVKSPQF-------FMGYIIGGVLARElnadgwmtvrdvgyeDEEGFIYIV 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 484 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSpkltEELKKQIREKIGPIATP 563
Cdd:PRK07638 381 GREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQLKSFCLQRLSSFKIP 453
|
570 580
....*....|....*....|....*...
gi 1622836714 564 DYIQNAPGLPKTRSGKIMRRVLRKIAQN 591
Cdd:PRK07638 454 KEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
464-586 |
1.12e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 86.65 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 543
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622836714 544 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
34-586 |
1.28e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 86.22 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 34 EPGEttQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSC 113
Cdd:PRK13390 20 ETGE--QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 114 SLLITTDAfyrgeklvnLKELADEAlqkcqEKDFPVRccivVKHLGRAElGMGDspsqsppikrscpdvqgklkekskrv 193
Cdd:PRK13390 98 RVLVASAA---------LDGLAAKV-----GADLPLR----LSFGGEID-GFGS-------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 194 qpqiswnqgidlwWHELMQEAGDECEPEWCDAedplFILYTSGSTGKPKGV--------VHTVGGYMLYVATTFkyvFDF 265
Cdd:PRK13390 133 -------------FEAALAGAGPRLTEQPCGA----VMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 266 HAEDVFWCTADIGwitgHSyvtyGPL-------ANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFG 338
Cdd:PRK13390 193 SESDIYYSSAPIY----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 339 DEPVTKHSRASLQVLGTVGEPINPEA------WLWyhqvvgaqrcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSATFPF 411
Cdd:PRK13390 261 ADVRTRYDVSSLRAVIHAAAPCPVDVkhamidWLG----------PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 412 FGVA----------PAilnesgeelegeaegylvfkqpwpGIMRTVYGNHERFETTYFKK-----------FPGYYVTGD 470
Cdd:PRK13390 330 LGDLhicdddgnelPA------------------------GRIGTVYFERDRLPFRYLNDpektaaaqhpaHPFWTTVGD 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 471 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELK 550
Cdd:PRK13390 386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELI 465
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622836714 551 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK13390 466 DYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
210-602 |
1.37e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 210 LMQEAGDECEPEW-----CDAEDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAED 269
Cdd:PRK12316 3175 LDLDRGDENYAEAnpairTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVlqfttfsFDVFVEE 3254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 270 VFWctadigwitghsyvtygPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgdEPVTKHSRAS 349
Cdd:PRK12316 3255 LFW-----------------PLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTS 3312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 350 LQVLGTVGEPINPEAwlwyHQVVGAQRcPIVDTFWQTETgghmlTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGE 429
Cdd:PRK12316 3313 LKRIVCGGEALPADL----QQQVFAGL-PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLE 3382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 430 AEGYLVFKQPWPGIMRTVYGNH-------ERFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 502
Cdd:PRK12316 3383 PVPVGALGELYLGGEGLARGYHnrpgltaERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEI 3462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 503 ESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRS 577
Cdd:PRK12316 3463 EARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllflERMPLTPN 3530
|
410 420
....*....|....*....|....*
gi 1622836714 578 GKIMRRVLRKIaqnDHDLGDTSTVA 602
Cdd:PRK12316 3531 GKLDRKALPRP---DAALLQQDYVA 3552
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
224-590 |
1.74e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVV--HTvGGYMLYVATTFKY---VFDFH--AEDVFWCTadiGWItghsyVTYGPLANGAT 296
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWemgTCPVYlwTLPMFHCN---GWT-----FTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 297 SVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWLWYHQVVGAQr 376
Cdd:PLN03102 255 SVCMRHV-TAPEI---YKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 377 cpIVDTFWQTETGGHML--------TPLPGATPMK-PGSATFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwpGI 443
Cdd:PLN03102 327 --VMHAYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS--SI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 444 MRTvYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 523
Cdd:PLN03102 403 MKG-YLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622836714 524 VKGECLYCFVTLCDGHTFSPKLTEELK-------KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 590
Cdd:PLN03102 480 TWGETPCAFVVLEKGETTKEDRVDKLVtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
37-592 |
2.83e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 85.38 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LH---------SIVFagfsseslce 106
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 107 rILDSSCS-LLITTDAFyrgeklvnlKELADEALQKCqekdfPVRCCIVVkhlgraelgmgdspsqsppikrscpDVQGK 185
Cdd:PRK08162 110 -MLRHGEAkVLIVDTEF---------AEVAREALALL-----PGPKPLVI-------------------------DVDDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 186 LKEKSKRVQpqiswnqgiDLWWHELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVV-HTVGGYMLYVATTFKYVF 263
Cdd:PRK08162 150 EYPGGRFIG---------ALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 264 DFHAE-----DVFWCTadiGWitGHSY-VTygplANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMkf 337
Cdd:PRK08162 221 PKHPVylwtlPMFHCN---GW--CFPWtVA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALI-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 338 gdepvtkHSRASLQvlgtvgEPINpeawlwyHQVVG--AQRCPIVDTFWQTETGGHMLTPLPGATPM---------KPGS 406
Cdd:PRK08162 286 -------NAPAEWR------AGID-------HPVHAmvAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpatvcawQPEW 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 407 ATFPFF---------GV------APAILNESGEELEgeaegylvfkqPWPG-----IMrtVYGN-------------HER 453
Cdd:PRK08162 346 DALPLDeraqlkarqGVryplqeGVTVLDPDTMQPV-----------PADGetigeIM--FRGNivmkgylknpkatEEA 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 454 FETtyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 533
Cdd:PRK08162 413 FAG-------GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFV 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 534 TLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 592
Cdd:PRK08162 486 ELKDGASATE---EEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
208-588 |
3.36e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 208 HELMQEAGDEC-EPEWC-----DAEDPLFILYTSGSTGKPKGVVHTVGG-----------YMLYVATT----FKYVFDFH 266
Cdd:PRK12467 3213 TALTLDRLDLNgYSENNpstrvMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGA 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 267 AEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDepvtKHS 346
Cdd:PRK12467 3293 QERFLW-----------------TLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG----GAD 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 347 RASLQVLGTVGEPINPEAWLWY---------HQVVGAQRCPIVDTFWQTETGGhmlTPLPGATPMKPGSAtfpffGVAPA 417
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVkrklkprglTNGYGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIY 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 418 ILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCRRDQDGYY 480
Cdd:PRK12467 3422 VLDGQL--------------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVI 3487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 481 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSPKLTEELKKQIREKIgpi 560
Cdd:PRK12467 3488 EYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL--- 3560
|
410 420 430
....*....|....*....|....*....|...
gi 1622836714 561 atPDYIQNA-----PGLPKTRSGKIMRRVLRKI 588
Cdd:PRK12467 3561 --PDYMVPAqllvlAAMPLGPNGKVDRKALPDP 3591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
226-582 |
4.47e-17 |
|
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: 83.08 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 226 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 305
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 306 YpdvNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdepVTKHSRA---SLQVLGTVGE-PINPEA--WLWYHQVvgaqrcPI 379
Cdd:cd17635 80 Y---KSLFKILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLIGYGGSrAIAADVrfIEATGLT------NT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 380 VDTFWQTETGGHMLTPLpGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFETTYF 459
Cdd:cd17635 146 AQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 460 KkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdgh 539
Cdd:cd17635 223 D---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA---- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622836714 540 tfSPKLTEE----LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 582
Cdd:cd17635 296 --SAELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
12-586 |
6.57e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 84.70 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 12 VLDRNVHEKKLGDKVAFYwegnEPGETTQITYHELLVQVcqfSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 91
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY----AADVVTHGQIHDGAARL---GEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 92 HSIVFAGFSSESLCERILDSSCSLLITTDAF---YRGEKLVNLKELADEAlqkcqekdfpvrccivvkhlGRAElgmgds 168
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA--------------------ARVA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 169 PSQSPPIkrscpdvqgklkekskrvqpqiswnqgidlwwhelmqeAGDECEpewcdaedplFILYTSGSTGKPKGVVHTV 248
Cdd:PRK06060 136 PGGYEPM--------------------------------------GGDALA----------YATYTSGTTGPPKAAIHRH 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 249 ggymlyvATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG-------PLANGATSVLfEGIPTYPDVNRLWSIvdKYKV 321
Cdd:PRK06060 168 -------ADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAILSA--RFGP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 322 TKFYTAPTAIRLLMkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrCPIVDTFWQTETGGHMLTPlpGATP 401
Cdd:PRK06060 238 SVLYGVPNFFARVI----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGS--ATFPFFGVAPAILNESGEELEGEAEGYLvfkqPWPGIMRTVYGNHERFETTyfkkfPGYYVTGDGCRRDQDGY 479
Cdd:PRK06060 310 WRLGTlgRVLPPYEIRVVAPDGTTAGPGVEGDLWV----RGPAIAKGYWNRPDSPVAN-----EGWLDTRDRVCIDSDGW 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 480 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGP 559
Cdd:PRK06060 381 VTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSA 460
|
570 580
....*....|....*....|....*..
gi 1622836714 560 IATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK06060 461 FKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
40-585 |
1.08e-16 |
|
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: 83.09 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 118
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 119 TDAfyrgeklvnlkeladealqkCQEKDFPVRCCIVVkhlgraeLGMGDSPSQSPPikrscpdvqgklkekSKRVQPQis 198
Cdd:cd12114 91 DGP--------------------DAQLDVAVFDVLIL-------DLDALAAPAPPP---------------PVDVAPD-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 199 wnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYV--------------F 263
Cdd:cd12114 127 ----------------------------DLAYVIFTSGSTGTPKGVMISHRAALNTILdINRRFAvgpddrvlalsslsF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 264 DFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegiPTY---PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF-GD 339
Cdd:cd12114 179 DLSVYDIF-----------------GALSAGATLVL----PDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVlEA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 340 EPVTKHS-R--------------ASLQVLGTVGEPIN----PEAWLW--YHQVVGA---------------QRCPIVDTf 383
Cdd:cd12114 238 AQALLPSlRlvllsgdwipldlpARLRALAPDARLISlggaTEASIWsiYHPIDEVppdwrsipygrplanQRYRVLDP- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 384 wqtetgghMLTPLPGatpmkpgsatfpffGVAPAIlnesgeelegeaegylvfkqpW---PGIMRTVYGNHERFETTYFK 460
Cdd:cd12114 317 --------RGRDCPD--------------WVPGEL---------------------WiggRGVALGYLGDPELTAARFVT 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 461 KFPG--YYVTGD-GCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCD 537
Cdd:cd12114 354 HPDGerLYRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDN 431
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622836714 538 GHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd12114 432 DGT--PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
226-588 |
1.15e-16 |
|
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: 83.35 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 226 EDPLFILYTSGSTGKPKGVVHT--------------VGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITGhsyvtygpl 291
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC--------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 292 anGATSVLfegIPTYPDVNRLWSIVDkYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWlwyHQV 371
Cdd:cd17642 253 --GFRVVL---MYKFEEELFLRSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKEVG---EAV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 372 VGAQRCPIV-DTFWQTETGGHML-TPlpgATPMKPGSA--TFPFFGvAPAILNESGEELEGEAEGYLVFKQpwPGIMRTV 447
Cdd:cd17642 322 AKRFKLPGIrQGYGLTETTSAILiTP---EGDDKPGAVgkVVPFFY-AKVVDLDTGKTLGPNERGELCVKG--PMIMKGY 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 448 YGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 527
Cdd:cd17642 396 VNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGE 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622836714 528 CLYCFVTLCDGHTFSPKLTEEL-------KKQIRekiGPIATPDYIqnapglPKTRSGKIMRRVLRKI 588
Cdd:cd17642 474 LPAAVVVLEAGKTMTEKEVMDYvasqvstAKRLR---GGVKFVDEV------PKGLTGKIDRRKIREI 532
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
12-604 |
1.18e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.39 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 12 VLDRNVHekKLGDKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAl 91
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 92 hsivfagfsseslcerildssCSLLITTDAfyRGEKLVNLKELADEALqkcqekdfpvrccIVVKHlgraELgmgdspsq 171
Cdd:PRK08279 113 ---------------------VVALLNTQQ--RGAVLAHSLNLVDAKH-------------LIVGE----EL-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 172 SPPIKRSCPDVqgklkekskRVQPQISWNQGIDLW----WHELMQEAG--DECEPEWCD---AEDPLFILYTSGSTGKPK 242
Cdd:PRK08279 145 VEAFEEARADL---------ARPPRLWVAGGDTLDdpegYEDLAAAAAgaPTTNPASRSgvtAKDTAFYIYTSGTTGLPK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 243 GVVHTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKY 319
Cdd:PRK08279 216 AAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 320 KVTKFYtaptAI----RLLMkfgDEPVTKHSRA-SLQVLgtVGEPINPEAW--------------LW------------- 367
Cdd:PRK08279 288 RATAFQ----YIgelcRYLL---NQPPKPTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvf 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 368 -YHQVVGaqRCP--------IVDtfWQTETGghmlTPLPGA----TPMKPGSAtfpffGVAPAILNEsgeelegeaegyl 434
Cdd:PRK08279 359 nFDGTVG--RVPlwlahpyaIVK--YDVDTG----EPVRDAdgrcIKVKPGEV-----GLLIGRITD------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 435 vfKQPWPG----------IMRTVygnherfettyFKKFPGYYVTGDGCRRDQDGYYWITGRIDDML-----NVsghllST 499
Cdd:PRK08279 413 --RGPFDGytdpeasekkILRDV-----------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----AT 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 500 AEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSG 578
Cdd:PRK08279 475 TEVENALSGFPGVEEAVVYGVEVPgTDGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTF 551
|
650 660
....*....|....*....|....*.
gi 1622836714 579 KIMRRVLRKIAQNDHDLGDTSTVADP 604
Cdd:PRK08279 552 KYRKVDLRKEGFDPSKVDDPLYVLDP 577
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
216-587 |
3.34e-16 |
|
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: 81.71 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 216 DECepewcdaeDPLFILYTSGSTGKPKGVVHT-VGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVtYGPLANG 294
Cdd:cd05915 151 PER--------AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 295 ATSVLFEGIPTypDVNRLWSIVdKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPinPEAWL-----WYH 369
Cdd:cd05915 222 AKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSAA--PRSLIarferMGV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 370 QVVGAQRCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGI 443
Cdd:cd05915 296 EVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 444 MRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 523
Cdd:cd05915 371 TGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHP 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622836714 524 VKGECLYCFVTLCDGHTFSPKLTEELKKqireKIGPIAT-PDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05915 449 KWQERPLAVVVPRGEKPTPEELNEHLLK----AGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
22-579 |
5.36e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.08 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 22 LGDKVAFYWeGNEpgettQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 101
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 102 ESLCERILDSSCSLLITTDAFyrGEKLVNLKEladealqkcqekDFP-VRCCIVVkhlgraelGMGDSPSQSPPikrscp 180
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVLP------------RLPkLRTLVVV--------EDGSGNDLLPG------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 181 dvqgklkekskrvqpqiswnqGIDlwWHELMQEAGDECEPEWCDAEDpLFILYTSGSTGKPKGVVHT--------VGGYM 252
Cdd:PRK07798 142 ---------------------AVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRqedifrvlLGGRD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 253 LYVATTFKYVFDfHAEDVFWCTADIGWITG---H---SYVTYGPLANGATSVLfegiptYP----DVNRLWSIVDKYKVT 322
Cdd:PRK07798 198 FATGEPIEDEEE-LAKRAAAGPGMRRFPAPplmHgagQWAAFAALFSGQTVVL------LPdvrfDADEVWRTIEREKVN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 323 kfytaptairLLMKFGD---EPVTKHSRA-------SLQVLGTVGEPINP---EAWL-WYHQVVgaqrcpIVDTFWQTET 388
Cdd:PRK07798 271 ----------VITIVGDamaRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALLeLLPNVV------LTDSIGSSET 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 389 G-GHMLTPLPGATPmkPGSATF---PFFGVAPAILNEsgeelegeaegyLVFKQPWPG-IMRT------VYGNHERFETT 457
Cdd:PRK07798 335 GfGGSGTVAKGAVH--TGGPRFtigPRTVVLDEDGNP------------VEPGSGEIGwIARRghiplgYYKDPEKTAET 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 458 yFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 535
Cdd:PRK07798 401 -FPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQL 479
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1622836714 536 CDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:PRK07798 480 REGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
37-590 |
6.11e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 81.04 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 116
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITTDAFYrgeklvnlkELADEALQ---KCQEKDFPVRCCIVVkhlgraelgmGDsPSQSP-----PIKRSCPDVQGKLKE 188
Cdd:PLN02479 122 MVDQEFF---------TLAEEALKilaEKKKSSFKPPLLIVI----------GD-PTCDPkslqyALGKGAIEYEKFLET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 189 KSkrvqPQISWNQGIDLWwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV-HTVGGYMLyvATTFKYVFDFHA 267
Cdd:PLN02479 182 GD----PEFAWKPPADEW--------------------QSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 268 EDVFWCTADIGWITGHSYvTYGPLANGATSVLFEGIPTypdvNRLWSIVDKYKVTKFYTAPTAIRLL------------- 334
Cdd:PLN02479 236 GAVYLWTLPMFHCNGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 335 -----MKFGDEP----VTKHSRASLQVLGTVG--EPINPE---AWL--WYH---------------QVVGAQRCPIVDTf 383
Cdd:PLN02479 311 rvvhvMTAGAAPppsvLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 384 wqtetgghmltplpgaTPMKPGSATFPFFGVAPAILNesgeelegeaegyLVFKqpwpGIMRTVYGNHERFETtyfkkfp 463
Cdd:PLN02479 390 ----------------KTMKPVPADGKTMGEIVMRGN-------------MVMK----GYLKNPKANEEAFAN------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS- 542
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSd 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622836714 543 -PKLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 590
Cdd:PLN02479 510 eAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
20-586 |
6.67e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 80.96 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAFywegNEPGETtqITYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 98
Cdd:PRK05677 35 QRFADKPAF----SNLGKT--LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 99 FSSESLCERILDSSCSLLITtdafyrgekLVNLKELADEALQKCQekdfpvrccivVKHLGRAELGmgdspSQSPPIKRS 178
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 179 CpdVQGKLKEKSKRVqPQISWNQGIDLWwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---VGGYMLYV 255
Cdd:PRK05677 164 L--INAVVKHVKKMV-PAYHLPQAVKFN-DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 256 ATTFK-------------------YVFDFHaedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDVNRLWSIV 316
Cdd:PRK05677 240 RALMGsnlnegceiliaplplyhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKEL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 317 DKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHQVVGaqrCPIVDTFWQTETgghmlTPL 396
Cdd:PRK05677 297 GKWKFSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 397 PGATPMK---PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCR 473
Cdd:PRK05677 367 VSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--ATDEILDSDGWLKTGDIAL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 474 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQI 553
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHM 519
|
570 580 590
....*....|....*....|....*....|...
gi 1622836714 554 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK05677 520 RANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-587 |
6.96e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.93 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITtd 120
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT-- 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 121 afyrgeklvnlkelaDEALQKcqekDFPVRCCIVVKHLGRAElGMGDSPSQSPpikrscpdvqgklkekskrvQPQIswn 200
Cdd:PRK12316 2107 ---------------QRHLLE----RLPLPAGVARLPLDRDA-EWADYPDTAP--------------------AVQL--- 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 201 qgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKY---------------VFDF 265
Cdd:PRK12316 2144 -----------------------AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERyelspadcelqfmsfSFDG 2200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 266 HAEDVFWctadigwitghsyvtygPLANGATSVLFEGipTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKH 345
Cdd:PRK12316 2201 AHEQWFH-----------------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERDG 2258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 346 SRASLQVLGTVGEPINPEAWLWYHQVVGAQRcpIVDTFWQTETgghMLTPLP-GATPMKPGSATFPFFGVAPA-----IL 419
Cdd:PRK12316 2259 RPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayIL 2333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 420 NESGEELEGEAEGYLVFKQPwpGIMRTVYG----NHERFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSG 494
Cdd:PRK12316 2334 DADLNLLAPGMAGELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRG 2411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 495 HLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPK 574
Cdd:PRK12316 2412 FRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAAEDLL---AELRAWLAARLPAYMVPAHWVVLERLPL 2487
|
570
....*....|...
gi 1622836714 575 TRSGKIMRRVLRK 587
Cdd:PRK12316 2488 NPNGKLDRKALPK 2500
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
225-585 |
1.40e-15 |
|
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: 79.22 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 225 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLAnGATSVLFEGIP 304
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA-GATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 305 TYPDvNRLWSIVDKYKVTkFYTAPTAIRLLMKFGDEPvtkhsraSLQVLGTVGEPINPE-AWLWyhqvvgAQRCPIVDTF 383
Cdd:cd17652 170 LLPG-EPLADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW------APGRRMINAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 384 WQTET--GGHMLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegylvfkQPWP------------GIMRTvYG 449
Cdd:cd17652 235 GPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--------------RPVPpgvpgelyiagaGLARG-YL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 450 NH-----ERFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 522
Cdd:cd17652 297 NRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDD 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622836714 523 PVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd17652 376 RPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
207-588 |
1.62e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.89 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 207 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA----EDVFWCTADIGWITG 282
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAALPMFHIYG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 283 HSYVTYGPLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGTVGEPINP 362
Cdd:PLN02574 259 LSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPLSG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 363 EAWLWYHQVVgaqrcPIVDtFWQtetgGHMLTPLPGATPMKPGSATFPFFG----VAPAILNESGEELEGEAEGYLVFKQ 438
Cdd:PLN02574 334 KFIQDFVQTL-----PHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYSsvglLAPNMQAKVVDWSTGCLLPPGNCGE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 439 PW---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 515
Cdd:PLN02574 404 LWiqgPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDA 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622836714 516 AVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 588
Cdd:PLN02574 482 AVTAVPDKECGEIPVAFVVRRQGSTLS---QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
227-582 |
3.18e-15 |
|
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: 77.31 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 227 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 306
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 307 pDVNRLWSIVDKYKVTKFYT-APTAIRLLMKFGDEPVtkhSRASLQVLGTVGEPINPEAWlwyHQVVGAqrcpivdTFW- 384
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 385 ---QTETGGhMLTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEGY------LVFKQPWpgimrtvyGNHERFE 455
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEivvrgpLVFQGYW--------NLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 456 TTyFKKfpGYYVTGDGCRRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 533
Cdd:cd17637 211 YT-FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622836714 534 TLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 582
Cdd:cd17637 288 VLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
40-591 |
3.96e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 78.49 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhSIVFAGFS---SEsLCERILDSSCSLL 116
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFShqrSE-LNAYASQIEPALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITTdafyRGEKLVNLKELADEALQKCQekdfpvRCCIVVKHlgraelgmGDSPSQSppikrscpdvqgklkekskrvqpq 196
Cdd:PRK10946 125 IAD----RQHALFSDDDFLNTLVAEHS------SLRVVLLL--------NDDGEHS------------------------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 iswnqgIDLWwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVFWCTAD 276
Cdd:PRK10946 163 ------LDDA----INHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 igwiTGHSYVTYGPlanGATSVLFEG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQV 352
Cdd:PRK10946 232 ----AAHNYPMSSP---GALGVFLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 353 L--------GTVGEPINPEAWLWYHQVVG--------------------AQRCPIV--DTFWQTETGGHmltPLPGATP- 401
Cdd:PRK10946 305 LqvggarlsETLARRIPAELGCQLQQVFGmaeglvnytrlddsderiftTQGRPMSpdDEVWVADADGN---PLPQGEVg 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 --MKPGSATFPffgvapailnesgeelegeaegylvfkqpwpGIMRTVYGNHERFETTyfkkfpGYYVTGDGCRRDQDGY 479
Cdd:PRK10946 382 rlMTRGPYTFR-------------------------------GYYKSPQHNASAFDAN------GFYCSGDLVSIDPDGY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 480 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtfSPKLTEELKKQIREK- 556
Cdd:PRK10946 425 ITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK-------EPLKAVQLRRFLREQg 497
|
570 580 590
....*....|....*....|....*....|....*
gi 1622836714 557 IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 591
Cdd:PRK10946 498 IAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
226-585 |
4.53e-15 |
|
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: 77.86 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 226 EDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAEDVF--WCTadigwitghsyvty 288
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIYvtLLS-------------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 289 gplanGATSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWY 368
Cdd:cd17644 172 -----GATLVLRPE-EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVRQW 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 369 HQVVGaQRCPIVDTFWQTE----TGGHMLTPLPGATPMKPGSATfPFFGVAPAILNEsgeelegeaegylvFKQPWP-GI 443
Cdd:cd17644 245 QKNVG-NFIQLINVYGPTEatiaATVCRLTQLTERNITSVPIGR-PIANTQVYILDE--------------NLQPVPvGV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 444 MRTVY--------G-------NHERFETTYFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 506
Cdd:cd17644 309 PGELHiggvglarGylnrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVL 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 507 VEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd17644 389 SQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
464-587 |
8.07e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 77.48 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 543
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622836714 544 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
224-587 |
8.59e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.46 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTfkyvfdfhaEDVFWCTADIGWITGHSYV-------TYGPLANGAt 296
Cdd:PRK12316 4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLYHPLINGA- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 297 SVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGtvGEPINPEAW-LWY------- 368
Cdd:PRK12316 4762 SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFG--GEAVAQASYdLAWralkpvy 4837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 369 -HQVVGAQRCPIVDTFWQTETGghmltPLPGATPMKPGSatfPFFGVAPAILNESGEELEGEAEGYLVFKQpwPGIMRtv 447
Cdd:PRK12316 4838 lFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELYLGG--EGVAR-- 4905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 448 yGNH-------ERFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 518
Cdd:PRK12316 4906 -GYLerpaltaERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 519 GHPHPVkGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVLRK 587
Cdd:PRK12316 4984 AQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERL-----PEYMVPAhlvflARMPLTPNGKLDRKALPQ 5056
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
20-589 |
8.79e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.55 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAFywegNEPGETtqITYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 98
Cdd:PRK12492 35 KKFADRPAF----SNLGVT--LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 99 FSSESLCERILDSSCSLLITTDAFyrgEKLVNlKELADEALQkcqekdfpvrccivvkHLgrAELGMGDSpsqsppikrs 178
Cdd:PRK12492 109 YTAREMRHQFKDSGARALVYLNMF---GKLVQ-EVLPDTGIE----------------YL--IEAKMGDL---------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 179 CPDVQGKL----KEKSKRVQPQISWNQGIDlWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYmly 254
Cdd:PRK12492 157 LPAAKGWLvntvVDKVKKMVPAYHLPQAVP-FKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNL--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 255 VAttfkyvfdfHAEDVFWCTADIGwITGHS---------------YVTYGPLAN-------GATSVLFegipTYP-DVNR 311
Cdd:PRK12492 233 VA---------NMLQVRACLSQLG-PDGQPlmkegqevmiaplplYHIYAFTANcmcmmvsGNHNVLI----TNPrDIPG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 312 LWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRAS-LQVLGTVGEPI---NPEAWlwyHQVVGaqrCPIVDTFWQTE 387
Cdd:PRK12492 299 FIKELGKWRFSALLGLNTLFVALM---DHPGFKDLDFSaLKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 388 TgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFP 463
Cdd:PRK12492 370 T-----SPVASTNPYgelaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMKGYWQQPE--ATAEALDAE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 543
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD-----P 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1622836714 544 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 589
Cdd:PRK12492 516 GLSvEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
464-586 |
1.14e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.98 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 543
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----P 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622836714 544 KLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK07059 510 ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
216-587 |
1.91e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.51 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 216 DECEPEWCD--------AEDP---LFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHs 284
Cdd:PRK12467 635 DEPADLLCGysghnpevALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 285 YVTYGPLANGATsVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGtvGEPINPEA 364
Cdd:PRK12467 713 TELFGALASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GEALQVDL 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 365 WLWYHQVvgAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF--PFFGVAPAILNEsgeelegeaegYLvfkQPWP- 441
Cdd:PRK12467 788 LARVRAL--GPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIgqPLANLGLYILDH-----------YL---NPVPv 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 442 -----------GIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 504
Cdd:PRK12467 852 gvvgelyiggaGLARGYHRrpalTAERFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEA 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 505 ALVEHEAVAEAAVVGHPHPVKGECL-YCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRR 583
Cdd:PRK12467 931 RLLAQPGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
....
gi 1622836714 584 VLRK 587
Cdd:PRK12467 1011 ALPK 1014
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
39-589 |
2.18e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.07 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 39 TQITYHELLVQVCQF-SNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 117
Cdd:PRK08751 49 KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 118 TTDAFYRGEKLVnlkeLADEALQKCQEK------DFPVRCCI--VVKHlgraelgmgdspsqsppIKRSCPDVqgklkek 189
Cdd:PRK08751 129 VIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKY-----------------VKKLVPEY------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 190 skRVQPQISWNQGIDLWWHELMqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVvhtvggyMLYVATTFKYVFDFHAed 269
Cdd:PRK08751 181 --RINGAIRFREALALGRKHSM-------PTLQIEPDDIAFLQYTGGTTGVAKGA-------MLTHRNLVANMQQAHQ-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 270 vfWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGiptypdVNRLWS-------IVDKYKVTKFyTAPTAIRLL 334
Cdd:PRK08751 243 --WLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGG------CNHLISnprdmpgFVKELKKTRF-TAFTGVNTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 335 M-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHQVVGAqrcPIVDTFWQTETgghmlTPLPGATPMK----PGSAT 408
Cdd:PRK08751 314 FnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL---TLVEAYGLTET-----SPAACINPLTlkeyNGSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 409 FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDD 488
Cdd:PRK08751 386 LPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 489 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPKLT-EELKKQIREKIGPIATPDYIQ 567
Cdd:PRK08751 462 MILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaEDVKAHARANLTGYKQPRIIE 536
|
570 580
....*....|....*....|..
gi 1622836714 568 NAPGLPKTRSGKIMRRVLRKIA 589
Cdd:PRK08751 537 FRKELPKTNVGKILRRELRDAA 558
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
207-524 |
4.19e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 75.20 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 207 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMlYVATTFKYVFDFHAEDVFWCTADIGWITGHSYV 286
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 287 TYGPLANGATSVLFEGIPTYPD------------VNRLWS-----IVDKYKVTKfytaptaIRLLMK--FGDEPVTKHSR 347
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWTkfqqgVQDKIPQQK-------LNLLLKipVVNSLVKRKVL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 348 ASL-----QVLGTVGEPINPEAWLWYHQVvgaqRCPIVDTFWQTETGGHMLTPLPGATpmKPGSATFPFFGVAPAIlnes 422
Cdd:cd05932 270 KGLgldqcRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRI---- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 423 geelegEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS-GHLLSTAE 501
Cdd:cd05932 340 ------SEDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAP 409
|
330 340
....*....|....*....|....*
gi 1622836714 502 VESALVEHEAVAEAAVVGH--PHPV 524
Cdd:cd05932 410 IENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
464-582 |
4.88e-14 |
|
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: 73.69 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsp 543
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT--- 291
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622836714 544 kLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 582
Cdd:cd17638 292 -LTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
195-586 |
5.06e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 74.73 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 PQISWNQGIDLwwHELMQEAGDECEPEWCDAEDPL---------FILYTSGSTGKPKGVVHTVG------GYMLYVATTF 259
Cdd:PRK12406 114 PEIAAAYRISP--ALLTPPAGAIDWEGWLAQQEPYdgppvpqpqSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRALIY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 260 kyvfdfhaedvfwctadiGWITGHSYVTYGPLANGATSV-------LFEGIPTYP--DVNRLWSIVDKYKVTKFYTAPTA 330
Cdd:PRK12406 192 ------------------GLKPGIRALLTGPLYHSAPNAyglragrLGGVLVLQPrfDPEELLQLIERHRITHMHMVPTM 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 331 IRLLMKFGDEPVTKHSRASLQvlgtvgepinpeawlwyHQVVGAQRCP--------------IVDTFWQTETGGhmltpL 396
Cdd:PRK12406 254 FIRLLKLPEEVRAKYDVSSLR-----------------HVIHAAAPCPadvkramiewwgpvIYEYYGSTESGA-----V 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 397 PGATP----MKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGC 472
Cdd:PRK12406 312 TFATSedalSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 473 RRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQ 552
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE---ADIRAQ 464
|
410 420 430
....*....|....*....|....*....|....
gi 1622836714 553 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK12406 465 LKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
34-586 |
1.84e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 72.99 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 34 EPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVF----AGFSSESLCERIL 109
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 110 DSSCSLLITTDAfyrgeklvnlkelADEALQKcqekdfpvrccIVVKHLGRAELGMGDspsqsppikrscpDVQGKLKEk 189
Cdd:PRK07514 98 DAEPALVVCDPA-------------NFAWLSK-----------IAAAAGAPHVETLDA-------------DGTGSLLE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 190 skrvqpqiswnqgidlwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAED 269
Cdd:PRK07514 140 --------------------AAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 270 VFWCTADIGWITGHSYVTYGPLANGA------------------TSVLFEGIPTypdvnrlwsivdkykvtkFYTaptai 331
Cdd:PRK07514 199 VLIHALPIFHTHGLFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 332 RLLmkfgDEP-----VTKHSRasLQVLGTVgePINPE---AWlwyhqvvgAQRC--PIVDTFWQTETGghMLTPLPGATP 401
Cdd:PRK07514 256 RLL----QEPrltreAAAHMR--LFISGSA--PLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 402 MKPGSATFPFFGVAPAILNESGEELEGEAEGYL-------VFKQPW--PgimrtvygnherfETTY--FKKfPGYYVTGD 470
Cdd:PRK07514 318 RRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMievkgpnVFKGYWrmP-------------EKTAeeFRA-DGFFITGD 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 471 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELK 550
Cdd:PRK07514 384 LGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAIL 460
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622836714 551 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK07514 461 AALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
38-585 |
4.40e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 71.96 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 38 TTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVfagfsSESLCERILDSSCslli 117
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA-----DGNLPIAAIERFC---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 118 ttdafyrgeklvnlkELADEAlqkcqekdfpvrCCIVVKHLGRAELGMGDSPSQSPPIKRSCPDVQGKLKEKSKRVQPQI 197
Cdd:PRK05857 110 ---------------QITDPA------------AALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 198 SWNQGidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVvhtvggymLYVATTFKYVFD-FHAEDVFWctad 276
Cdd:PRK05857 163 NADQG----------------------SEDPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 277 IGWITGHSyvTYGPLAngATSV---------LFEG---IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLL---MKFGDEP 341
Cdd:PRK05857 209 VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 342 VtkhsrASLQVLGTVGEPInPEAWLWYHQVVGAQRCPIvdtFWQTETGGHMLTpLP----GATPMKPGSATFPFFGV--- 414
Cdd:PRK05857 285 V-----PSLRLVGYGGSRA-IAADVRFIEATGVRTAQV---YGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVdvy 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 415 -APAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 493
Cdd:PRK05857 355 lAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 494 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfspklTEELKKQI----REKIGPIATPDYI 566
Cdd:PRK05857 432 GVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIaarfRRESEPMARPSTI 506
|
570
....*....|....*....
gi 1622836714 567 QNAPGLPKTRSGKIMRRVL 585
Cdd:PRK05857 507 VIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
36-587 |
6.53e-13 |
|
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: 71.19 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSS-CS 114
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 LLITTDAfyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvq 194
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 pqiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATT---------------F 259
Cdd:cd17653 104 ------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 260 KYVFDFHAEDVFWCtadigwitghsyvtygpLANGATSVLFEGIPTYPDVNRlwsivdkyKVTKFYTAPTAIRLLmkfgd 339
Cdd:cd17653 154 SIAFDACIGEIFST-----------------LCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL----- 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 340 epvtkhSRASLQVLGTV---GEPINP---EAWL----WYHqVVGAQRCPIVDTFWQTETGghmlTPLPGATPMkPGSATF 409
Cdd:cd17653 204 ------SPQDFPNLKTIflgGEAVPPsllDRWSpgrrLYN-AYGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 410 pffgvapaILNESgeelegeaegylvfKQPWP------------GIMRTVYGNHERfETTYFKKFPGY-----YVTGDGC 472
Cdd:cd17653 272 --------ILDAD--------------LQPVPegvvgeicisgvQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYG 328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 473 RRDQDGYYWITGRIDDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTlcdghtfsPKL--TEEL 549
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVT--------PETvdVDGL 395
|
570 580 590
....*....|....*....|....*....|....*...
gi 1622836714 550 KKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd17653 396 RSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
36-585 |
7.99e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETtqITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITTDAFYRGeklvnLKELADEALQKCQEKDFPVRccivvkhlgraelgmgDSPSQSPPIKRSCPDVQGklkekskrvqp 195
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQHQA----------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 196 qiswnqgidlwwhelmqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDvfwCTA 275
Cdd:PRK05691 2337 ----------------------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CEL 2378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 276 DIGWIT--GHSYVTYGPLANGATSVL-FEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdePVTKHSRASLQV 352
Cdd:PRK05691 2379 HFYSINfdAASERLLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRM 2452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 353 LGTVGEPINPEAWLWYHQVVGAQRcpIVDTFWQTETgghMLTPLPGATP--MKPGSATFPFFGVAPA----ILNESGEEL 426
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALV 2527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 427 EGEAEGYLvfkqpWPGIMRTVYGNH-------ERFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 498
Cdd:PRK05691 2528 PQGATGEL-----YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIE 2602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 499 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPK--LTEELKKQIREKIgpiatPDYIQNA-----PG 571
Cdd:PRK05691 2603 LGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQaaLREALKAHLKQQL-----PDYMVPAhlillDS 2677
|
570
....*....|....
gi 1622836714 572 LPKTRSGKIMRRVL 585
Cdd:PRK05691 2678 LPLTANGKLDRRAL 2691
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
39-585 |
1.67e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 70.84 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 39 TQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLI 117
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 118 TTDAFyrgeklvnLKELADEALQKCQEKDFPvrccivvkhlgraelgmgDSPSQSPPIKRSCPDvqgklkekskrvqpqi 197
Cdd:PRK10252 561 TTADQ--------LPRFADVPDLTSLCYNAP------------------LAPQGAAPLQLSQPH---------------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 198 swnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV--HT-VGGYMLYVATTFKyvfdFHAEDVFW-- 272
Cdd:PRK10252 599 -----------------------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqk 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 273 --CTADIG-----WitghsyvtygPLANGATSVLFEgiptyPDVNR----LWSIVDKYKVTKFYTAPTairLLMKFGDEP 341
Cdd:PRK10252 646 tpCSFDVSvweffW----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 342 VTKHSRASLQVLGTV---GEPINPEAWLWYHQVVGAqrcPIVDTFWQTE---------TGGHMLTPLPGAtPMKPGsatF 409
Cdd:PRK10252 708 TPEGARQSCASLRQVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGS-SVPIG---Y 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 410 PFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKkfPG--YYVTGDG 471
Cdd:PRK10252 781 PVWNTGLRILDARM--------------RPVPpGVAGDLYltgiqlaqGYLgrpdltaSRFIADPFA--PGerMYRTGDV 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 472 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTLCDGhtfSPKL 545
Cdd:PRK10252 845 ARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQSG---LPLD 921
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622836714 546 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK10252 922 TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
464-586 |
1.68e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 70.02 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 542
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622836714 543 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 586
Cdd:PRK07787 428 ---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
24-587 |
3.30e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 69.24 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYwegnEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSS-- 101
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPta 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 102 -ESLCERILDSSCSLLITTDAFYRGEklvnlkeladealqkcqekdfpvrccivVKHLGRAELGMGDSpsqsppikrscp 180
Cdd:PLN02330 115 lESEIKKQAEAAGAKLIVTNDTNYGK----------------------------VKGLGLPVIVLGEE------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 181 dvqgklkekskRVQPQISWNQGIDLwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT------------- 247
Cdd:PLN02330 155 -----------KIEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLThrnlvanlcsslf 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 248 -VGGYMLYVATTFKYVFDFHaedvfwctadIGWITGHSYVTygpLANGATSVLfegiptypdVNR--LWSIVDKYKVTKF 324
Cdd:PLN02330 219 sVGPEMIGQVVTLGLIPFFH----------IYGITGICCAT---LRNKGKVVV---------MSRfeLRTFLNALITQEV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 325 YTAPTAIRLLMKFGDEPVTKH---SRASLQVLGTVGEPINPEAWLWYH-QVVGAQrcpIVDTFWQTETGGHMLT---PLP 397
Cdd:PLN02330 277 SFAPIVPPIILNLVKNPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdPEK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 398 GATPMKPGSATFPFFGVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTVYGNHERFETTYFKKfpGYYVTG 469
Cdd:PLN02330 354 GHGIAKKNSVGFILPNLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLHTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 470 DGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtfSPKLT--- 546
Cdd:PLN02330 423 DIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI------NPKAKese 496
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622836714 547 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PLN02330 497 EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
224-591 |
3.79e-12 |
|
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: 68.72 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKY-----VFDF--HAEDVfwCTADIgwitghsyvtYGPLAN 293
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVViehRALSTSALAHGRALGLtsesrVLQFasYTFDV--SILEI----------FTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 294 GATSVlfegIPTYPD-VNRLWSIVDKYKVTkfyTA---PTAIRLLmkfgdEPVTKhsrASLQVLGTVGEPINPEAW-LWY 368
Cdd:cd05918 172 GGCLC----IPSEEDrLNDLAGFINRLRVT---WAfltPSVARLL-----DPEDV---PSLRTLVLGGEALTQSDVdTWA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 369 HQV------------VGAQRCPIVD-------------TFWQTETGGH-MLTPLpGAT-------PMkpgsatfpffgVA 415
Cdd:cd05918 237 DRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI-----------LA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 416 PAILNESGEELEgeaegylVFKQPWPGIMRTVYGNHERFettyfkkfpgyYVTGDGCRRDQDG--YYwiTGRIDDMLNVS 493
Cdd:cd05918 305 RGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKDTQVKIR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 494 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSPKLTEELKKQIREKIGPIAT-------- 562
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGSGDGDSLFLEPSDEFRALVAelrsklrq 443
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622836714 563 --PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 591
Cdd:cd05918 444 rlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
468-589 |
6.10e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 68.30 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 468 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltE 547
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622836714 548 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 589
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
209-587 |
7.79e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 67.90 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 209 ELMQEAGDECEPEWCDA-EDPLFILYTSGSTGKPKGVvhTVGGYMLYVATTFKYVFDFHAE-DVFWCTADIGWITGHSYV 286
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIVGYGEdDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 287 tygpLAN---GATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL----GTVGEP 359
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 360 INPEAWLWYhqvvgaQRCPIVDTFWQTETGGHMltplpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP 439
Cdd:PLN02860 304 LLPDAKKLF------PNAKLFSAYGMTEACSSL-------TFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 440 ---------------------WPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 498
Cdd:PLN02860 371 phvelkigldessrvgriltrGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 499 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLT-----------EELKKQIREK-IGPIATPD-Y 565
Cdd:PLN02860 449 PEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlF 528
|
410 420
....*....|....*....|..
gi 1622836714 566 IQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PLN02860 529 VQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
40-585 |
8.08e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.03 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 119
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 120 DAFyrgeklvnLKELADEALQKCQEKDfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvQPQiSW 199
Cdd:PRK12467 1679 SHL--------QARLPLPDGLRSLVLD-----------------------------------------------QED-DW 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 200 nqgidlwwhelmQEAGDECEPEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDVfwctadi 277
Cdd:PRK12467 1703 ------------LEGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV------- 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 278 gWITGHSYV-------TYGPLANGAtSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKHSraSL 350
Cdd:PRK12467 1762 -VLQFTSFAfdvsvweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPL--SL 1836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 351 QVLGTVGEPINPEAW-LWYHQVVGAQrcpIVDTFWQTETGGHML------------TPLPGATPMkPGSATFpffgVAPA 417
Cdd:PRK12467 1837 RRVVCGGEALEVEALrPWLERLPDTG---LFNLYGPTETAVDVThwtcrrkdlegrDSVPIGQPI-ANLSTY----ILDA 1908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 418 ILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCRRDQDGYYW 481
Cdd:PRK12467 1909 SLNP----------------VP-IGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIE 1971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSPKLTEELKKQIREK 556
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKAS 2050
|
570 580 590
....*....|....*....|....*....|....
gi 1622836714 557 IgpiatPDYIQNA-----PGLPKTRSGKIMRRVL 585
Cdd:PRK12467 2051 L-----PEYMVPAhlvflARMPLTPNGKLDRKAL 2079
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-579 |
3.01e-11 |
|
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: 65.48 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 226 EDPLFILYTSGSTGKPKGVV---HTVGGYMLYVA--TTFKYVFDFHAEDVFWCTADIGW------ITGHSYVTYGPLANG 294
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGAdfGTGEFTPSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 295 ATSVLFEGIPTYPDvnRLWSIVDKYKVTKF------YTAPTaIRLLMKFGDEPVTkhsraSLQVLGTVGEPINPEawlwy 368
Cdd:cd05924 83 GQTVVLPDDRFDPE--EVWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS-----SLFAISSGGALLSPE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 369 hqvVGAQRCP------IVDTFWQTETGGHMLTPlpgATPMKPGSATFPFFGVAPAILNESgeelegeaegyLVFKQPWPG 442
Cdd:cd05924 150 ---VKQGLLElvpnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 443 IMRTV----------YGNHERFETTyFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 510
Cdd:cd05924 213 GVGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 511 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 579
Cdd:cd05924 292 AVYDVLVVGRPDERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-585 |
3.22e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGNepgettQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 103
Cdd:PRK05691 1146 ERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 LCERILDSSCSLLITTDAFYrgEKLVNLKELADEALqkcqekdfpvrccivvkhlgrAELGMGDSPSQSPpikrscpdvq 183
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLL--ERLPQAEGVSAIAL---------------------DSLHLDSWPSQAP---------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 184 gklkekskrvqpqiswnqGIDLWWHELMqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYV 262
Cdd:PRK05691 1267 ------------------GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNTHAALAERLQwMQATYA 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 263 FDfhAEDVFWCTADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPV 342
Cdd:PRK05691 1311 LD--DSDVLMQKAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPL 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 343 TKHSRaSLQVLGTVGEPINPE---------AWLWYHQVVGAQRCPIVDTFWQTETGGHMLTPLpgatpmkpGSatfPFFG 413
Cdd:PRK05691 1384 AAACT-SLRRLFSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI--------GR---PLGN 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 414 VAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRID 487
Cdd:PRK05691 1452 VLCRVLDAELNLLPPGVAGELCIGGA--GLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLGRLD 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 488 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQ 567
Cdd:PRK05691 1529 QQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAEL-----PEYMV 1599
|
570 580
....*....|....*....|...
gi 1622836714 568 NA-----PGLPKTRSGKIMRRVL 585
Cdd:PRK05691 1600 PAqlirlDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
224-585 |
4.91e-11 |
|
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: 65.11 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVVHTVGGYM--------LY---------VATTFKYVFDFHAEDVFwctadIGWITGHSYV 286
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 287 tygplangatsVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLmKFGdepvtkhSRASLQVLGTVGEPINPEAwl 366
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 367 wYHQVVGAQRCPIVDTFWQTETGGHML-TPLPGATPmKPGSATFPFFGVAPAILNESGeelegeaegylvfkQPWP---- 441
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM--------------KRVPvgav 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 442 --------GIMRTvYGNH-----ERFETTYFK--------KFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTA 500
Cdd:cd17648 288 gelylggdGVARG-YLNRpeltaERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 501 EVESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfspkLTE-ELKKQIREKIGPIATPDYIQNAPGLPK 574
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
410
....*....|.
gi 1622836714 575 TRSGKIMRRVL 585
Cdd:cd17648 442 TINGKLDVRAL 452
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
463-593 |
8.73e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.25 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 463 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFs 542
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 543 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 593
Cdd:PRK07445 402 ---LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
42-587 |
1.23e-10 |
|
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: 63.99 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLIT 118
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 119 TDafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppikrscpdvqgklkekskrvqpqis 198
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 199 wnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGgyMLYV-ATTFKYVFDFHAEDVFWCTADI 277
Cdd:cd05937 87 ---------------------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPL 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 278 GWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRaslqVLG 354
Cdd:cd05937 138 YHGTAAFLGACNCLMSGGTLALsrkFS-------ASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHK----VRV 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 355 TVGEPINPEAWLWYHQVVGAqrcPIVDTFWQ-TETGGHMLTPLPGAtpmkpgsatfpfFGvAPAILNESGEELEGEAEGY 433
Cdd:cd05937 207 AWGNGLRPDIWERFRERFNV---PEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQV 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 434 LVFK------QPW---------------PG--IMRTVYGNHERFETTY--------------FKKFPGYYVTGDGCRRDQ 476
Cdd:cd05937 271 VLVKmdpetdDPIrdpktgfcvrapvgePGemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDA 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 477 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDGHTF-SPKLTEELKKQ 552
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEESSAVpTEFTKSLLASL 428
|
570 580 590
....*....|....*....|....*....|....*
gi 1622836714 553 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
42-244 |
1.37e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 64.06 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LHSIVFAGFSSEslCERILDSS-CSLLITT 119
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAiLVTINPAYRLSE--LEYALNQSgCKALIAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 120 DAF----YRG--EKLVnlKELADEALQKCQEKDFP-VRCCIVvkhlgraeLGMGDSPsqsppikrscpdvqGKLKekskr 192
Cdd:PRK08315 123 DGFkdsdYVAmlYELA--PELATCEPGQLQSARLPeLRRVIF--------LGDEKHP--------------GMLN----- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836714 193 vqpqiswnqgidlwWHELMQEAGDEcEPEWCDA-------EDPLFILYTSGSTGKPKGV 244
Cdd:PRK08315 174 --------------FDELLALGRAV-DDAELAArqatldpDDPINIQYTSGTTGFPKGA 217
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
468-585 |
2.08e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 468 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSPkl 545
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEIDP-- 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622836714 546 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK08308 369 -VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
458-595 |
3.64e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 458 YFKK-----FPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 532
Cdd:PRK07008 398 YFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622836714 533 VTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDL 595
Cdd:PRK07008 478 VVKRPGAEVT---REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR-DYVL 536
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
20-587 |
3.87e-10 |
|
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: 62.64 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 20 KKLGDKVAFYWEGNEPGETTQITYHELLVQVCQFSNVLRKQGiQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 99
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 100 SSESLcERIL----DSSCSLLITTDAFyrgeklvnLKELADEALQKCQEKDFPVRCCivvkhlgraelgmgdspsqsppi 175
Cdd:cd05931 83 PGRHA-ERLAailaDAGPRVVLTTAAA--------LAAVRAFAASRPAAGTPRLLVV----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 176 krscpdvqgklkekskrvqpqiswnqgiDLwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 255
Cdd:cd05931 131 ----------------------------DL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 256 ATTFKyVFDFHAED--VFW--CTADIGWITGhsyvTYGPLANGATSVLFEgiPTY----PdvnRLW-SIVDKYKVTkFYT 326
Cdd:cd05931 179 RQIRR-AYGLDPGDvvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLMS--PAAflrrP---LRWlRLISRYRAT-ISA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 327 APTairllmkFG-DEPVTKHSRA--------SLQVLGTVGEPINPEAwlwyhqvvgaqrcpiVDTFwQTETGGHMLTP-- 395
Cdd:cd05931 248 APN-------FAyDLCVRRVRDEdlegldlsSWRVALNGAEPVRPAT---------------LRRF-AEAFAPFGFRPea 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 396 -LPG-----AT---PMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVF-------------------KQP-------- 439
Cdd:cd05931 305 fRPSyglaeATlfvSGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARELvscgrplpdqevrivdpetGRElpdgevge 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 440 -W---PGIMRTVYGNHERFETTYFKKFP----GYYVTGD-GCRRdqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 510
Cdd:cd05931 385 iWvrgPSVASGYWGRPEATAETFGALAAtdegGWLRTGDlGFLH--DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAH 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 511 AV---AEAAVVGHPHPVkGECLycFVTLCDGHTFSPKLTEELKKQIREKIGP---IATPDYIQNAPG-LPKTRSGKIMRR 583
Cdd:cd05931 463 PAlrpGCVAAFSVPDDG-EERL--VVVAEVERGADPADLAAIAAAIRAAVARehgVAPADVVLVRPGsIPRTSSGKIQRR 539
|
....
gi 1622836714 584 VLRK 587
Cdd:cd05931 540 ACRA 543
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
224-582 |
4.02e-10 |
|
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: 62.46 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGI 303
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 304 PT-------------YPDVNRLWSIVDKYKVTKFYTAPTAI---RLLMKFGDEPVTKHSRASLQ----------VLGtvG 357
Cdd:cd05914 166 PSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHeafggnikefVIG--G 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 358 EPINPEAWLWYHQVvgaqRCPIVDTFWQTETGghmltPLPGATP---MKPGSATFPFFGVAPAIlnesGEELEGEAEGYL 434
Cdd:cd05914 244 AKINPDVEEFLRTI----GFPYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRI----DSPDPATGEGEI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 435 VFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDM-LNVSGHLLSTAEVESALVEHEAVA 513
Cdd:cd05914 311 IVRGP--NVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 514 EAAVV---------GHPHP----VKGECLycfvtlcdghtfsPKLTEELKKQIREKIGpIATPDY-------IQNAPgLP 573
Cdd:cd05914 387 ESLVVvqekklvalAYIDPdfldVKALKQ-------------RNIIDAIKWEVRDKVN-QKVPNYkkiskvkIVKEE-FE 451
|
....*....
gi 1622836714 574 KTRSGKIMR 582
Cdd:cd05914 452 KTPKGKIKR 460
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
37-300 |
4.17e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 62.69 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 116
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 117 ITTdafyrGEKLVNLkeladeaLQKCQEKDFPvRCCIVvkHLGraelgmgdspsqsppikrSCPDvqgKLKEKSKRVqpq 196
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLD------------------SLPA---SVDTEGCRL--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 197 ISWNQGIDLWWHELMQEAGDECEpewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaeDVFWCTAD 276
Cdd:PTZ00216 239 VAWTDVVAKGHSAGSHHPLNIPE----NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLN-----DLIGPPEE 309
|
250 260
....*....|....*....|....*...
gi 1622836714 277 igwitGHSYVTYGPLAN----GATSVLF 300
Cdd:PTZ00216 310 -----DETYCSYLPLAHimefGVTNIFL 332
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
37-585 |
5.74e-10 |
|
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: 62.11 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 37 ETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERI----LDSS 112
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGG----AFVPIDPEYPEERRiyimLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 113 CSLLITtdafyrgeklvnlkeladealqkcqekdfpvrccivvkhlgraelgmgdspsqsppiKRSCPDVQGKLKEKSKR 192
Cdd:cd17656 86 VRVVLT---------------------------------------------------------QRHLKSKLSFNKSTILL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 193 VQPQISwnqgidlwwHELMQEAGDECEpewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFW 272
Cdd:cd17656 109 EDPSIS---------QEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 273 ---CTADIGWITGHSYVTYGplanGATSVLFEgiPTYPDVNRLWSIVDKYKVTKFYTaPTAIrLLMKFGDEPVTKHSRAS 349
Cdd:cd17656 175 fatCSFDVCYQEIFSTLLSG----GTLYIIRE--ETKRDVEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREFINRFPTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 350 LQVLGTVGEPI---NPeawlwYHQVVGAQRCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSATFPFfgvapa 417
Cdd:cd17656 247 VKHIITAGEQLvitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 418 ILNESgeelegeaegylvfKQPWP-GIMRTVY--------GNHERFETTYFKKFPG-------YYVTGDGCRRDQDGYYW 481
Cdd:cd17656 314 ILDQE--------------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIE 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 482 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSpklTEELKKQIREKIGPIA 561
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN---ISQLREYLAKQLPEYM 454
|
570 580
....*....|....*....|....
gi 1622836714 562 TPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
224-590 |
6.91e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 62.25 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATtfkyVFDFHAEDVfwctadigwITG-----HSY----VTYGPL 291
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 292 ANGATSVlFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLgtvgepinpeawlwyhqV 371
Cdd:PRK08633 847 LEGIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLV-----------------V 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 372 VGAQRCP--IVDTFWQ------------TETgghmlTP-----LPGA--------TPMKPGSATFPFFGVAPAILNESGe 424
Cdd:PRK08633 905 AGAEKLKpeVADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPET- 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 425 elegeaegYLVFKQPWPG--------IMRTVYGNHERF-ETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 495
Cdd:PRK08633 979 --------FEELPPGEDGliliggpqVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGE 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 496 LLSTAEVESALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgHTFSPKLTEELKKQIRE-KIGPIATPDYIQNAP 570
Cdd:PRK08633 1051 MVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVE 1122
|
410 420
....*....|....*....|
gi 1622836714 571 GLPKTRSGKIMRRVLRKIAQ 590
Cdd:PRK08633 1123 ALPLLGSGKLDLKGLKELAL 1142
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
463-587 |
7.36e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.83 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 463 PGYYVTGDGCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtLCDGHTfS 542
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGP-A 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622836714 543 PKLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK07824 310 PTL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
464-585 |
1.08e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.17 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSp 543
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD- 474
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622836714 544 klTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK13383 475 --AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
36-292 |
1.17e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.29 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 116 LITtdafyrGEKlvNLKELAD--EALQkcqekdfpvrcciVVKHLgraeLGMGDSPSQSPPikrSCPDVQGKLKEKSKRV 193
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDS---SLSGSSNWTVSSFSEV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 194 QpqiswnqgidlwwhELMQEAgdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVfwc 273
Cdd:PLN02387 234 E--------------KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--- 294
|
250
....*....|....*....
gi 1622836714 274 tadigwitghsYVTYGPLA 292
Cdd:PLN02387 295 -----------YLAYLPLA 302
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
38-587 |
2.03e-09 |
|
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: 60.13 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 38 TTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 117
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 118 TtdafyrgeklvNLKELADEALQKcqekdfpvrccivvkhlgraelgmgdspsqSPPikrSCPDVqgklkekskrvqpqi 197
Cdd:cd05939 81 F-----------NLLDPLLTQSST------------------------------EPP---SQDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 198 swnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADI 277
Cdd:cd05939 102 --------------------------NFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 278 gWITGHSYVTYGP-LANGATSVLFEGIptypDVNRLWSIVDKYKVTKF-YTAPTAIRLLMKFGDEPVTKHsraslQVLGT 355
Cdd:cd05939 155 -YHSAGGIMGVGQaLLHGSTVVIRKKF----SASNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 356 VGEPINPEAWlwyHQVVGAQRCPIVDTFWQTETGGHMLTPLPGatpmKPGSATF-PFFG--VAPAIL---NESGEELEGE 429
Cdd:cd05939 225 VGNGLRPQIW---EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLikvDEDTGELIRD 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 430 AEGYLVFKQPW-PGIM----------RTVYG------NHERFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNV 492
Cdd:cd05939 298 SDGLCIPCQPGePGLLvgkiiqndplRRFDGyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRW 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 493 SGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSPKLTEELKkqirekigPIATPDYIQ 567
Cdd:cd05939 378 KGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIR 449
|
570 580
....*....|....*....|
gi 1622836714 568 NAPGLPKTRSGKIMRRVLRK 587
Cdd:cd05939 450 LLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
464-587 |
2.06e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.18 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 543
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622836714 544 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 587
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
466-585 |
9.10e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 466 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSPKL 545
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622836714 546 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
40-123 |
3.70e-08 |
|
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: 56.21 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 40 QITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLI 117
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLahCLNV--SSAKHLV 80
|
....*.
gi 1622836714 118 TTDAFY 123
Cdd:cd05940 81 VDAALY 86
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
464-578 |
5.70e-08 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 55.00 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 464 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 543
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 1622836714 544 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 578
Cdd:cd17636 297 ---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
223-591 |
2.02e-07 |
|
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: 53.83 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 223 CDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVF--WCTADigWITGHSYVTYGPLANGATSVlf 300
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--HVGGLVELHLRAVYLGCQQV-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 301 eGIPT---YPDVNRLWSIVDKYKVTkfYT-APT-AIRLLMKFGDEPVTKH-SRASLQVLGTVGEPINP---EAWLWYHQV 371
Cdd:cd05906 239 -HVPTeeiLADPLRWLDLIDRYRVT--ITwAPNfAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAktiRRLLRLLEP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 372 VGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGvapailnesgeelegeaegylvfkQPWPGI-MRTVYGN 450
Cdd:cd05906 316 YGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLG------------------------RPIPGVsMRIVDDE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 451 HE--------RFETTYFKKFPGYY---------VTGDGCRRDQD------GYYWITGRIDDMLNVSGHLLSTAEVESALV 507
Cdd:cd05906 372 GQllpegevgRLQVRGPVVTKGYYnnpeanaeaFTEDGWFRTGDlgfldnGNLTITGRTKDTIIVNGVNYYSHEIEAAVE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 508 EHEAVAE--AAVVGHPHPVKGECLYCFVtlcdghtFSPKLTE-----ELKKQIR----EKIGpiATPDYI----QNApgL 572
Cdd:cd05906 452 EVPGVEPsfTAAFAVRDPGAETEELAIF-------FVPEYDLqdalsETLRAIRsvvsREVG--VSPAYLiplpKEE--I 520
|
410
....*....|....*....
gi 1622836714 573 PKTRSGKIMRRVLRKIAQN 591
Cdd:cd05906 521 PKTSLGKIQRSKLKAAFEA 539
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
219-371 |
5.49e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.59 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 219 EPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgymlyvattfkyvfDFHA------EDVFWCTADIGWITGHSYVTYGPlA 292
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHG--------------MFEAqiealrEDYGIEPGEIDLPTFPLFALFGP-A 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 293 NGATSVLFEGIPTYP-DVN--RLWSIVDKYKVTKFYTAPTAIrllmkfgdEPVTKHSRASLQVLGTV------GEPINPE 363
Cdd:PRK09274 232 LGMTSVIPDMDPTRPaTVDpaKLFAAIERYGVTNLFGSPALL--------ERLGRYGEANGIKLPSLrrvisaGAPVPIA 303
|
....*...
gi 1622836714 364 AWLWYHQV 371
Cdd:PRK09274 304 VIERFRAM 311
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
36-293 |
5.99e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 52.54 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILD-SSCS 114
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAV-EFIINhAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 115 LlittdAFYRGEKLvnlkeladEALQKCQEKdfpvrcCivVKHLgRAELGMGDspsqsppikrscpdVQGKLKEKSKrvq 194
Cdd:PLN02861 152 I-----AFVQESKI--------SSILSCLPK------C--SSNL-KTIVSFGD--------------VSSEQKEEAE--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 195 pqiswNQGIDLW-WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaedvfwc 273
Cdd:PLN02861 193 -----ELGVSCFsWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK---------- 257
|
250 260
....*....|....*....|
gi 1622836714 274 TADIGWITGHSYVTYGPLAN 293
Cdd:PLN02861 258 VTDRVATEEDSYFSYLPLAH 277
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-550 |
1.60e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.92 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 225 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 304
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 305 TYP---DVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDE----------------PVTKHSRASLQVLgtvgepINPEAW 365
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQhgitlpslrrvlsagaPVPIALAARLRKM------LSDEAE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 366 LWyhQVVGAQRC-PIvdtfwqTETGGHMLTPLPGATPmKPGSAT---FPFFGVAPAILNESGEELEGEAEGYLVfkQPW- 440
Cdd:cd05910 229 IL--TPYGATEAlPV------SSIGSRELLATTTAAT-SGGAGTcvgRPIPGVRVRIIEIDDEPIAEWDDTLEL--PRGe 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 441 --------PGIMRTVYGnheRFETTYFKKFPG-----YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 507
Cdd:cd05910 298 igeitvtgPTVTPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFN 374
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622836714 508 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELK 550
Cdd:cd05910 375 THPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
505-597 |
3.88e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 49.38 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 505 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSPKLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 584
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90
....*....|...
gi 1622836714 585 LRKIAQNDHDLGD 597
Cdd:PRK09188 322 LRLIAMNQIDELD 334
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
217-300 |
4.43e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.52 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 217 ECEPEWCD--AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDvfwctadigwitgHSYVTYGPLAN- 293
Cdd:cd17639 77 ECSAIFTDgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRYLAYLPLAHi 143
|
90
....*....|
gi 1622836714 294 ---GATSVLF 300
Cdd:cd17639 144 felAAENVCL 153
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
224-585 |
4.88e-06 |
|
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: 49.48 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVV---HTvggyMLYVATTFKYVFDFHAEDVFWCTADIGWiTGHSYVTYGPLANGAT-SVL 299
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMiehHN----LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAAlHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 300 FEGIPTypDVNRLWSIVDKYKVTKFYTaPTAIRllmkfgdEPVTKHSRASLQVLGTVGEPINpeawlwyhqVVGAQRCPI 379
Cdd:cd17645 177 PSERRL--DLDALNDYFNQEGITISFL-PTGAA-------EQFMQLDNQSLRVLLTGGDKLK---------KIERKGYKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 380 VDTFWQTETgghmlTPLPGATPMKPGSATFPFfGVAPA-----ILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERF 454
Cdd:cd17645 238 VNNYGPTEN-----TVVATSFEIDKPYANIPI-GKPIDntrvyILDEALQLQPIGVAGELCIAGE--GLAR---GYLNRP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 455 ETTYfKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKG 526
Cdd:cd17645 307 ELTA-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 527 ECLYCFVTlcdghtfSPKLT--EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 585
Cdd:cd17645 386 KYLVAYVT-------APEEIphEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
463-591 |
1.48e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 48.17 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 463 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 542
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 543 PKLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 591
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
36-118 |
2.57e-05 |
|
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: 47.21 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 36 GETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 115
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
...
gi 1622836714 116 LIT 118
Cdd:cd17639 81 IFT 83
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
42-255 |
2.57e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.12 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 42 TYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARigalHSIVfagfsseslcerildssCSLLITTda 121
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAA----HSLI-----------------CVPLYDT-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 122 fyRGEKLVNLkeLADEAlqkcqEKDFpvrccIVVKHLGRAELGMGDSPSQSpPIKRSCPDVQGKLKEKSKRVQPQI---S 198
Cdd:PLN02430 135 --LGPGAVDY--IVDHA-----EIDF-----VFVQDKKIKELLEPDCKSAK-RLKAIVSFTSVTEEESDKASQIGVktyS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836714 199 WNQgidlWWHELMQEAGDECEPEwcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 255
Cdd:PLN02430 200 WID----FLHMGKENPSETNPPK---PLDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
219-587 |
3.22e-05 |
|
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: 46.71 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 219 EPEWCDAEDPL-FILYTSGSTGKPKGVV---HTVGGYMLYVATTfkyvFDFHAEDVF--W--CTADIGWITGHsyvtYGP 290
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 291 LANGATSVLfegIPTYPDVNR--LW-SIVDKYKVTKFYTAPTAIRLLMK-FGDEPVTKHSRASLQVLGTVGEPINPE--- 363
Cdd:cd05908 170 LIAGMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYElch 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 364 AWLWYHQVVGAQRCPIVDTFWQTETGghmltplPGATPMKPGSATFPFF--------GV-APAILNESGEELEGEAEGY- 433
Cdd:cd05908 247 EFLDHMSKYGLKRNAILPVYGLAEAS-------VGASLPKAQSPFKTITlgrrhvthGEpEPEVDKKDSECLTFVEVGKp 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 434 LVFKQpwpgiMRTVYGNHERFETTYFKKF--------PGYY---------VTGDGCRR--DQ----DGYYWITGRIDDML 490
Cdd:cd05908 320 IDETD-----IRICDEDNKILPDGYIGHIqirgknvtPGYYnnpeatakvFTDDGWLKtgDLgfirNGRLVITGREKDII 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 491 NVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIG-------PI 560
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGwqinevlPI 474
|
410 420
....*....|....*....|....*..
gi 1622836714 561 ATpdyiqnapgLPKTRSGKIMRRVLRK 587
Cdd:cd05908 475 RR---------IPKTTSGKVKRYELAQ 492
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
18-292 |
1.08e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.48 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 18 HEKKLGDKVAfywEGNEPGETTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARigalHSIVfa 97
Cdd:PLN02736 59 DYKYLGTRIR---VDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSA----YSYV-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 98 gfsseslcerildsSCSLLIT--TDAFyrgEKLVNLKELAD--------EALQKCQEKDFPVRCCIVVkhlgraelGMGD 167
Cdd:PLN02736 130 --------------SVPLYDTlgPDAV---KFIVNHAEVAAifcvpqtlNTLLSCLSEIPSVRLIVVV--------GGAD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 168 SPSQSPPIKRSCPDVQGKLKEKSKRVQPQiswnqgidlwwhelmqeagDECEPEwcdAEDPLFILYTSGSTGKPKGVVHT 247
Cdd:PLN02736 185 EPLPSLPSGTGVEIVTYSKLLAQGRSSPQ-------------------PFRPPK---PEDVATICYTSGTTGTPKGVVLT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622836714 248 VGGYMLYVATTfkyvfdfhAEDVFWCTADIgwitghsYVTYGPLA 292
Cdd:PLN02736 243 HGNLIANVAGS--------SLSTKFYPSDV-------HISYLPLA 272
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
13-121 |
1.22e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 45.12 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 13 LDRNVHEkkLGDKVAFYW---EGNEPGETTQITYHELLVQVCQFSNVLrKQGIQKGDRVAIYMPMIPELVVAMLACARIG 89
Cdd:PRK12476 40 IERNIAN--VGDTVAYRYldhSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622836714 90 ALHSIVFA----GfSSESLCERILDSSCSLLITTDA 121
Cdd:PRK12476 117 TIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA 151
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
202-292 |
1.52e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. 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.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 44.51 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 202 GIDLW-WHELMQE-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFwctaDIgw 279
Cdd:cd05927 88 GVKVYsLEEFEKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPT----DV-- 161
|
90
....*....|...
gi 1622836714 280 itghsYVTYGPLA 292
Cdd:cd05927 162 -----YISYLPLA 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
224-306 |
2.93e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 301
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
....*
gi 1622836714 302 GIPTY 306
Cdd:PRK06814 860 GVKVF 864
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
224-520 |
4.48e-04 |
|
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: 43.12 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 224 DAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 300
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 301 EGIPTYPD------------VNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepvtkhsrasLQVLGTVGEPINpeawlwy 368
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGIS------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 369 hqvvGAQRCPI-VDTFWQ------------TETGghmltplPGATPMKP-----GSATFPFFGVAPAILNESGEELEGEA 430
Cdd:cd17640 221 ----GGGALPPhVDTFFEaigievlngyglTETS-------PVVSARRLkcnvrGSVGRPLPGTEIKIVDPEGNVVLPPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 431 EGYLVFKQPwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEH 509
Cdd:cd17640 290 EKGIVWVRG-PQVMKGYYKNPE--ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRS 366
|
330
....*....|.
gi 1622836714 510 EAVAEAAVVGH 520
Cdd:cd17640 367 PFIEQIMVVGQ 377
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
24-244 |
5.27e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.96 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 24 DKVAFYWEGnepgetTQITYHELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGalHSIVFAGFSSES 103
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 104 lcERILD----SSCSLLITTDAFyrGEKLVNLKELADEALQkcqekdfpvrccivvkhlgraelgmgDSPSQSPPIKRSC 179
Cdd:PRK04813 89 --ERIEMiievAKPSLIIATEEL--PLEILGIPVITLDELK--------------------------DIFATGNPYDFDH 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622836714 180 PdVQGklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGV 244
Cdd:PRK04813 139 A-VKG-----------------------------------------DDNYYIIFTSGTTGKPKGV 161
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
41-566 |
1.81e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.12 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 41 ITYHELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 119
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 120 DAfyrgeklvnLKELADEALQKCQEKDfpVRCCIVvkhlgraelgmgdSPSQSPPIKRScpdVQGKLKEKSKRVQPQiSW 199
Cdd:cd05938 86 PE---------LQEAVEEVLPALRADG--VSVWYL-------------SHTSNTEGVIS---LLDKVDAASDEPVPA-SL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 200 NQGIDLwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVhtVGGYMLYVATTFKYVFDFHAEDVFWCTA---- 275
Cdd:cd05938 138 RAHVTI--------------------KSPALYIYTSGTTGLPKAAR--ISHLRVLQCSGFLSLCGVTADDVIYITLplyh 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 276 DIGWITGHSyvtyGPLANGATSVLFEGIPTypdvNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvlgT 355
Cdd:cd05938 196 SSGFLLGIG----GCIELGATCVLKPKFSA----SQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRL----A 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 356 VGEPINPEAWLWYHQVVGAQRcpIVDTFWQTE--------TG-----------------------------------GHM 392
Cdd:cd05938 264 IGNGLRADVWREFLRRFGPIR--IREFYGSTEgnigffnyTGkigavgrvsylykllfpfelikfdvekeepvrdaqGFC 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 393 LTPLPGatpmKPG------SATFPFFGVAPAilnesgeelegeaegylvFKQPWPGIMRTVygnherfettyFKKFPGYY 466
Cdd:cd05938 342 IPVAKG----EPGllvakiTQQSPFLGYAGD------------------KEQTEKKLLRDV-----------FKKGDVYF 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 467 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSPKl 545
Cdd:cd05938 389 NTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLKPGHEFDGK- 467
|
570 580
....*....|....*....|.
gi 1622836714 546 teELKKQIREKIGPIATPDYI 566
Cdd:cd05938 468 --KLYQHVREYLPAYARPRFL 486
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
439-577 |
2.58e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.86 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836714 439 PWPGIMRTVYGNHERFETTyfkkfpGYYVtgdgcRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAavV 518
Cdd:PRK07868 822 PTASVKRGVFAPADTWIST------EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLA--V 888
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622836714 519 GHPHPVKGECL-YCFVTLCDGHTFSPK-LTEELkkqirEKIGPIATPDYIQNAPGLPKTRS 577
Cdd:PRK07868 889 TYGVEVGGRQLaVAAVTLRPGAAITAAdLTEAL-----ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| |
